D00871
type: Enzyme
active site residues resources: Structure of the complex between the antibiotic cerulenin and its target, beta-ketoacyl-acyl carrier protein synthase.
active site residues resources: A template search reveals mechanistic similarities and differences in beta-ketoacyl synthases (KAS) and related enzymes.
active site residues resources: The structural biology of type II fatty acid biosynthesis.
active site residues resources: Platensimycin is a selective FabF inhibitor with potent antibiotic properties.
active site residues resources: Structure of 3-oxoacyl-(acyl-carrier protein) synthase II from Thermus thermophilus HB8.
active site residues resources: Divergent evolution of the thiolase superfamily and chalcone synthase family.
active site residues resources: Synthesis and biological evaluation of platensimycin analogs.
active site residues resources: Isolation, enzyme-bound structure and antibacterial activity of platencin A1 from Streptomyces platensis.
active site residues resources: http://ezcatdb.cbrc.jp/EzCatDB/reference/D00871#21
active site residues resources: http://ezcatdb.cbrc.jp/EzCatDB/reference/D00871#25
active site residues resources: http://ezcatdb.cbrc.jp/EzCatDB/reference/D00871#31
active site residues resources: http://ezcatdb.cbrc.jp/EzCatDB/reference/D00871#32
active site residues resources: 1dd8
cath: Peroxisomal Thiolase; Chain A, domain 1
csa: 1kas
ec: https://purl.uniprot.org/enzyme/2.3.1.179
kegg enzyme: beta-ketoacyl-acyl-carrier-protein synthase II
kegg intermediate: Peptidyl-Cys-tetrahedral-(Z)-hexadec-11-enoyl-[acyl-carrier protein]
kegg intermediate: Peptidyl-Cys-S-(Z)-hexadec-11-enoyl
kegg intermediate: [Acyl-carrier protein]-tetrahedral-malonyl group
kegg intermediate: [Acyl-carrier protein]-decarboxylated malonyl group (Peptidyl-Ser-phosphopantetheine-S-enolate)
kegg intermediate: Peptidyl-Cys-tetrahedral-(Z)-hexadec-11-enoyl-keto-[acyl-carrier protein]
kegg pathway: Fatty acid biosynthesis
kegg product: Bicabonate(HCO3-)
kegg product: [acyl-carrier-protein]
kegg product: (Z)-3-oxooctadec-13-enoyl-[acyl-carrier protein]
kegg substrate: malonyl-[acyl-carrier-protein]
kegg substrate: (Z)-hexadec-11-enoyl-[acyl-carrier protein]
kegg substrate: H2O
pdb: 1b3nA01
pdb: 1kas001
pdb: 2gfvA01
pdb: 2gfwA01
pdb: 2gfxA01
pdb: 2gfyA01
pdb: 3g0yA01
pdb: 3g11A01
pdb: 3hnzA01
pdb: 3ho2A01
pdb: 3ho9A01
pdb: 3i8pA01
pdb: 3e60A01
pdb: 3e60B01
pdb: 3kzuA01
pdb: 3kzuB01
pdb: 3kzuC01
pdb: 4ddoA01
pdb: 4f32A01
pdb: 4f32B01
pdb: 1e5mA01
pdb: 1j3nA01
pdb: 1j3nB01
pdb: 2gqdA01
pdb: 2gqdB01
pdb: 3o04A01
pdb: 1ox0A01
pdb: 1oxhA01
pdb: 1oxhB01
pdb: 1oxhC01
pdb: 1oxhD01
pdb: 2almA01
pdb: 2rjtA01
pdb: 2rjtB01
pdb: 2rjtC01
pdb: 2rjtD01
pdb: 1b3nA02
pdb: 1kas002
pdb: 2gfvA02
pdb: 2gfwA02
pdb: 2gfxA02
pdb: 2gfyA02
pdb: 3g0yA02
pdb: 3g11A02
pdb: 3hnzA02
pdb: 3ho2A02
pdb: 3ho9A02
pdb: 3i8pA02
pdb: 3e60A02
pdb: 3e60B02

Analogue
compound: malonyl-[acyl-carrier-protein]
ligand het code: PMN
pdb: 2gfxA02

Analogue
compound: malonyl-[acyl-carrier-protein]
ligand het code: P9A
pdb: 3g0yA02

Analogue
compound: malonyl-[acyl-carrier-protein]
ligand het code: P9C
pdb: 3g11A02

Analogue
compound: malonyl-[acyl-carrier-protein]
ligand het code: PMN
pdb: 3hnzA02

Analogue
compound: malonyl-[acyl-carrier-protein]
ligand het code: N32
pdb: 3ho2A02

Analogue
compound: malonyl-[acyl-carrier-protein]
ligand het code: N3A
pdb: 3ho9A02

Analogue
compound: malonyl-[acyl-carrier-protein]
ligand het code: 840
pdb: 3i8pA02

Analogue
compound: malonyl-[acyl-carrier-protein]
ligand het code: N32
pdb: 4f32A02

Analogue
compound: malonyl-[acyl-carrier-protein]
ligand het code: N32
pdb: 4f32B02

IntermediateAnalogue
compound: Peptidyl-Cys-S-(Z)-hexadec-11-enoyl
ligand het code: DAO
pdb: 2gfyA01

TransitionStateAnalogue
compound: Peptidyl-Cys-tetrahedral-(Z)-hexadec-11-enoyl-keto-[acyl-carrier protein]
ligand het code: CER
pdb: 1b3nA01

ReferenceForCatalyticMechanism
reference index: 1
reference section: p.1186-1189

ReferenceForCatalyticMechanism
reference index: 3
reference section: Fig.1B, p.603-604

ReferenceForCatalyticMechanism
reference index: 5
reference section: p.9842-9844

ReferenceForCatalyticMechanism
reference index: 6
reference section: Table 4, p.496-498

ReferenceForCatalyticMechanism
reference index: 7
reference section: Fig.6, p.10883-10887

ReferenceForCatalyticMechanism
reference index: 8
reference section: p.4139-4141

ReferenceForCatalyticMechanism
reference index: 9
reference section: Fig.8, p.431-433

ReferenceForCatalyticMechanism
reference index: 11
reference section: Fig.7c, p.810-814

ReferenceForCatalyticMechanism
reference index: 13
reference section: Fig.6, p.17396-17398

ReferenceForCatalyticMechanism
reference index: 15
reference section: p.361-363

ReferenceForCatalyticMechanism
reference index: 16
reference section: Fig.5, p.696-697

Peroxisomal Thiolase; Chain A, domain 1
type: Cath
catalytic domain: index.html
references: http://www.cathdb.info/version/latest/superfamily/3.40.47.10

H2O
type: KeggSubstrate
compound type: H2O
references: KEGG:C00001
references: CHEBI:15377
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Fatty acid biosynthesis
type: KeggPathway
references: KEGG:MAP00061

Crystal structure of beta-ketoacyl-acyl carrier protein synthase II from E.coli reveals the molecular architecture of condensing enzymes.
type: BibliographicResource
authors:
  item: Huang W
  item: Jia J
  item: Edwards P
  item: Dehesh K
  item: Schneider G
  item: Lindqvist Y
journal: EMBO J
pages: 1183-91
published year: 1998
volume: 17
references: http://www.ncbi.nlm.nih.gov/pubmed/9482715
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P0AAI5
comment: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).

An antibiotic factory caught in action.
type: BibliographicResource
authors:
  item: Keatinge-Clay AT
  item: Maltby DA
  item: Medzihradszky KF
  item: Khosla C
  item: Stroud RM
journal: Nat Struct Mol Biol
pages: 888-93
published year: 2004
volume: 11
references: http://www.ncbi.nlm.nih.gov/pubmed/15286722
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

The thiolase superfamily: condensing enzymes with diverse reaction specificities.
type: BibliographicResource
authors:
  item: Haapalainen AM
  item: Merilainen G
  item: Wierenga RK
journal: Trends Biochem Sci
pages: 64-71
published year: 2005
volume: 31
references: http://www.ncbi.nlm.nih.gov/pubmed/16356722

Roles of the active site water, histidine 303, and phenylalanine 396 in the catalytic mechanism of the elongation condensing enzyme of Streptococcus pneumoniae.
type: BibliographicResource
authors:
  item: Zhang YM
  item: Hurlbert J
  item: White SW
  item: Rock CO
journal: J Biol Chem
pages: 17390-9
published year: 2006
volume: 281
references: http://www.ncbi.nlm.nih.gov/pubmed/16618705
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Molecular aspects of beta-ketoacyl synthase (KAS) catalysis.
type: BibliographicResource
authors:
  item: von Wettstein-Knowles P
  item: Olsen J
  item: Arnvig Mcguire K
  item: Larsen S
journal: Biochem Soc Trans
pages: 601-7
published year: 2000
volume: 28
references: http://www.ncbi.nlm.nih.gov/pubmed/11171140

The 1.8 A crystal structure and active-site architecture of beta-ketoacyl-acyl carrier protein synthase III (FabH) from escherichia coli.
type: BibliographicResource
authors:
  item: Davies C
  item: Heath RJ
  item: White SW
  item: Rock CO
journal: Structure
pages: 185-95
published year: 2000
volume: 8
references: http://www.ncbi.nlm.nih.gov/pubmed/10673437
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P0A6R0
comment: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).

beta-Ketoacyl-[acyl carrier protein] synthase I of Escherichia coli: aspects of the condensation mechanism revealed by analyses of mutations in the active site pocket.
type: BibliographicResource
authors:
  item: McGuire KA
  item: Siggaard-Andersen M
  item: Bangera MG
  item: Olsen JG
  item: von Wettstein-Knowles P
journal: Biochemistry
pages: 9836-45
published year: 2001
volume: 40
references: http://www.ncbi.nlm.nih.gov/pubmed/11502177

The crystal structure of beta-ketoacyl-acyl carrier protein synthase II from Synechocystis sp. at 1.54 A resolution and its relationship to other condensing enzymes.
type: BibliographicResource
authors:
  item: Moche M
  item: Dehesh K
  item: Edwards P
  item: Lindqvist Y
journal: J Mol Biol
pages: 491-503
published year: 2001
volume: 305
references: http://www.ncbi.nlm.nih.gov/pubmed/11152607
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P73283
comment: X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS).

Mechanism of the beta-ketoacyl synthase reaction catalyzed by the animal fatty acid synthase.
type: BibliographicResource
authors:
  item: Witkowski A
  item: Joshi AK
  item: Smith S
journal: Biochemistry
pages: 10877-87
published year: 2002
volume: 41
references: http://www.ncbi.nlm.nih.gov/pubmed/12196027

The 1.3-Angstrom-resolution crystal structure of beta-ketoacyl-acyl carrier protein synthase II from Streptococcus pneumoniae.
type: BibliographicResource
authors:
  item: Price AC
  item: Rock CO
  item: White SW
journal: J Bacteriol
pages: 4136-43
published year: 2003
volume: 185
references: http://www.ncbi.nlm.nih.gov/pubmed/12837788
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

The structural biology of type II fatty acid biosynthesis.
type: BibliographicResource
authors:
  item: White SW
  item: Zheng J
  item: Zhang YM
  item: Rock
journal: Annu Rev Biochem
pages: 791-831
published year: 2005
volume: 74
references: http://www.ncbi.nlm.nih.gov/pubmed/15952903

Platensimycin is a selective FabF inhibitor with potent antibiotic properties.
type: BibliographicResource
authors:
  item: Wang J
  item: Cummings R
  item: Ha S
  item: Dorso K
  item: Motyl M
  item: Jayasuriya H
  item: Ondeyka J
  item: Herath K
  item: Zhang C
  item: Hernandez L
  item: Allocco J
  item: Soisson SM
  item: Basilio A
  item: Tormo JR
  item: Genilloud O
  item: Vicente F
  item: Pelaez F
  item: Colwell L
  item: Lee SH
  item: Michael B
  item: Felcetto T
  item: Gill C
  item: Young K
  item: Silver LL
  item: Hermes JD
  item: Bartizal K
  item: Barrett J
  item: Schmatz D
  item: Becker JW
  item: Cully D
  item: Singh SB
  item: Shoop W
  item: Kodali S
  item: Galgoci A
  item: Painter R
  item: Parthasarathy G
  item: Tang YS
journal: Nature
pages: 358-61
published year: 2006
volume: 441
references: http://www.ncbi.nlm.nih.gov/pubmed/16710421
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Structure of 3-oxoacyl-(acyl-carrier protein) synthase II from Thermus thermophilus HB8.
type: BibliographicResource
authors:
  item: Bagautdinov B
  item: Ukita Y
  item: Miyano M
  item: Kunishima N
journal: Acta Crystallogr Sect F Struct Biol Cryst Commun
pages: 358-66
published year: 2008
volume: 64
references: http://www.ncbi.nlm.nih.gov/pubmed/18453702
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Divergent evolution of the thiolase superfamily and chalcone synthase family.
type: BibliographicResource
authors:
  item: Jiang C
  item: Kim SY
  item: Suh DY
journal: Mol Phylogenet Evol
pages: 691-701
published year: 2008
volume: 49
references: http://www.ncbi.nlm.nih.gov/pubmed/18824113

Synthesis and biological evaluation of platensimycin analogs.
type: BibliographicResource
authors:
  item: Shen HC
  item: Dorso K
  item: Tata JR
  item: Hammond ML
  item: Maccoss M
  item: Colletti SL
  item: Ding FX
  item: Singh SB
  item: Parthasarathy G
  item: Soisson SM
  item: Ha SN
  item: Chen X
  item: Kodali S
  item: Wang J
journal: Bioorg Med Chem Lett
pages: 1623-7
published year: 2009
volume: 19
references: http://www.ncbi.nlm.nih.gov/pubmed/19233644
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Isolation, enzyme-bound structure and antibacterial activity of platencin A1 from Streptomyces platensis.
type: BibliographicResource
authors:
  item: Singh SB
  item: Soisson SM
  item: Ondeyka JG
  item: Herath KB
  item: Zhang C
  item: Jayasuriya H
  item: Zink DL
  item: Parthasarathy G
  item: Becker JW
  item: Wang J
journal: Bioorg Med Chem Lett
pages: 4756-9
published year: 2009
volume: 19
references: http://www.ncbi.nlm.nih.gov/pubmed/19581087
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Structure of the complex between the antibiotic cerulenin and its target, beta-ketoacyl-acyl carrier protein synthase.
type: BibliographicResource
authors:
  item: Moche M
  item: Schneider G
  item: Edwards P
  item: Dehesh K
  item: Lindqvist Y
journal: J Biol Chem
pages: 6031-4
published year: 1999
volume: 274
references: http://www.ncbi.nlm.nih.gov/pubmed/10037680
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P0AAI5
comment: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS).

A template search reveals mechanistic similarities and differences in beta-ketoacyl synthases (KAS) and related enzymes.
type: BibliographicResource
authors:
  item: Dawe JH
  item: Porter CT
  item: Thornton JM
  item: Tabor AB
journal: Proteins
pages: 427-35
published year: 2003
volume: 52
references: http://www.ncbi.nlm.nih.gov/pubmed/12866053

1b3nA01
type: Pdb
catalytic residue: CYS 163
main chain in catalysis: CYS 163
references: 1b3n
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1b3n

1b3nA02
type: Pdb
catalytic residue: HIS 303;LYS 335;HIS 340
main chain in catalysis: PHE 400
references: 1b3n
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1b3n

1e5mA01
type: Pdb
catalytic residue: CYS 167
main chain in catalysis: CYS 167
references: 1e5m
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e5m

1e5mA02
type: Pdb
catalytic residue: HIS 307;LYS 339;HIS 344
main chain in catalysis: PHE 403
references: 1e5m
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e5m

1j3nA01
type: Pdb
catalytic residue: CYS 161
main chain in catalysis: CYS 161
references: 1j3n
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1j3n

1j3nA02
type: Pdb
catalytic residue: HIS 301;LYS 333;HIS 338
main chain in catalysis: PHE 396
references: 1j3n
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1j3n

1j3nB01
type: Pdb
catalytic residue: CYS 161
main chain in catalysis: CYS 161
references: 1j3n
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1j3n

1j3nB02
type: Pdb
catalytic residue: HIS 301;LYS 333;HIS 338
main chain in catalysis: PHE 396
references: 1j3n
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1j3n

1kas001
type: Pdb
catalytic residue: CYS 163
main chain in catalysis: CYS 163
references: 1kas
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kas

1kas002
type: Pdb
catalytic residue: HIS 303;LYS 335;HIS 340
main chain in catalysis: PHE 400
references: 1kas
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kas

1ox0A01
type: Pdb
catalytic residue: CYS 164
main chain in catalysis: CYS 164
references: 1ox0
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ox0

1ox0A02
type: Pdb
catalytic residue: HIS 303;LYS 332;HIS 337
main chain in catalysis: PHE 396
references: 1ox0
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ox0

1oxhA01
type: Pdb
catalytic residue: CYS 164
main chain in catalysis: CYS 164
references: 1oxh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1oxh

1oxhA02
type: Pdb
catalytic residue: HIS 303;LYS 332;HIS 337
main chain in catalysis: PHE 396
references: 1oxh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1oxh

1oxhB01
type: Pdb
catalytic residue: CYS 164
main chain in catalysis: CYS 164
references: 1oxh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1oxh

1oxhB02
type: Pdb
catalytic residue: HIS 303;LYS 332;HIS 337
main chain in catalysis: PHE 396
references: 1oxh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1oxh

1oxhC01
type: Pdb
catalytic residue: CYS 164
main chain in catalysis: CYS 164
references: 1oxh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1oxh

1oxhC02
type: Pdb
catalytic residue: HIS 303;LYS 332;HIS 337
main chain in catalysis: PHE 396
references: 1oxh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1oxh

1oxhD01
type: Pdb
catalytic residue: CYS 164
main chain in catalysis: CYS 164
references: 1oxh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1oxh

1oxhD02
type: Pdb
catalytic residue: HIS 303;LYS 332;HIS 337
main chain in catalysis: PHE 396
references: 1oxh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1oxh

2almA01
type: Pdb
catalytic residue: CYS 164
main chain in catalysis: CYS 164
references: 2alm
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2alm

2almA02
type: Pdb
catalytic residue: ;LYS 332;HIS 337
main chain in catalysis: PHE 396
references: 2alm
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2alm
comment: mutant H303A, G379A

2gfvA01
type: Pdb
references: 2gfv
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2gfv
comment: mutant C163Q

2gfvA02
type: Pdb
catalytic residue: HIS 303;LYS 335;HIS 340
main chain in catalysis: PHE 400
references: 2gfv
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2gfv

2gfwA01
type: Pdb
catalytic residue: CYS 163
main chain in catalysis: CYS 163
references: 2gfw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2gfw

2gfwA02
type: Pdb
catalytic residue: HIS 303;LYS 335;HIS 340
main chain in catalysis: PHE 400
references: 2gfw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2gfw

2gfxA01
type: Pdb
references: 2gfx
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2gfx
comment: mutant C163Q

2gfxA02
type: Pdb
catalytic residue: HIS 303;LYS 335;HIS 340
main chain in catalysis: PHE 400
references: 2gfx
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2gfx

2gfyA01
type: Pdb
catalytic residue: CYS 163
main chain in catalysis: CYS 163
references: 2gfy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2gfy

2gfyA02
type: Pdb
catalytic residue: HIS 303; ;HIS 340
main chain in catalysis: PHE 400
references: 2gfy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2gfy
comment: mutant K335A

2gqdA01
type: Pdb
catalytic residue: CYS 165
main chain in catalysis: CYS 165
references: 2gqd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2gqd

2gqdA02
type: Pdb
catalytic residue: HIS 304;LYS 336;HIS 341
main chain in catalysis: PHE 400
references: 2gqd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2gqd

2gqdB01
type: Pdb
catalytic residue: CYS 165
main chain in catalysis: CYS 165
references: 2gqd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2gqd

2gqdB02
type: Pdb
catalytic residue: HIS 304;LYS 336;HIS 341
main chain in catalysis: PHE 400
references: 2gqd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2gqd

2rjtA01
type: Pdb
catalytic residue: CYS 164
main chain in catalysis: CYS 164
references: 2rjt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2rjt

2rjtA02
type: Pdb
catalytic residue: HIS 303;LYS 332;HIS 337
main chain in catalysis: PHE 396
references: 2rjt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2rjt
comment: mutant E22A, E94A, E325A, E383A, E409A

2rjtB01
type: Pdb
catalytic residue: CYS 164
main chain in catalysis: CYS 164
references: 2rjt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2rjt

2rjtB02
type: Pdb
catalytic residue: HIS 303;LYS 332;HIS 337
main chain in catalysis: PHE 396
references: 2rjt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2rjt
comment: mutant E22A, E94A, E325A, E383A, E409A

2rjtC01
type: Pdb
catalytic residue: CYS 164
main chain in catalysis: CYS 164
references: 2rjt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2rjt

2rjtC02
type: Pdb
catalytic residue: HIS 303;LYS 332;HIS 337
main chain in catalysis: PHE 396
references: 2rjt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2rjt
comment: mutant E22A, E94A, E325A, E383A, E409A

2rjtD01
type: Pdb
catalytic residue: CYS 164
main chain in catalysis: CYS 164
references: 2rjt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2rjt

2rjtD02
type: Pdb
catalytic residue: HIS 303;LYS 332;HIS 337
main chain in catalysis: PHE 396
references: 2rjt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2rjt
comment: mutant E22A, E94A, E325A, E383A, E409A

3e60A01
type: Pdb
catalytic residue: CYS 170
main chain in catalysis: CYS 170
references: 3e60
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3e60

3e60A02
type: Pdb
catalytic residue: HIS 311;LYS 342;HIS 347
main chain in catalysis: PHE 406
references: 3e60
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3e60

3e60B01
type: Pdb
catalytic residue: CYS 170
main chain in catalysis: CYS 170
references: 3e60
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3e60

3e60B02
type: Pdb
catalytic residue: HIS 311;LYS 342;HIS 347
main chain in catalysis: PHE 406
references: 3e60
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3e60

3g0yA01
type: Pdb
references: 3g0y
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3g0y
comment: mutant C163Q

3g0yA02
type: Pdb
catalytic residue: HIS 303;LYS 335;HIS 340
main chain in catalysis: PHE 400
references: 3g0y
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3g0y

3g11A01
type: Pdb
references: 3g11
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3g11
comment: mutant C163Q

3g11A02
type: Pdb
catalytic residue: HIS 303;LYS 335;HIS 340
main chain in catalysis: PHE 400
references: 3g11
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3g11

3hnzA01
type: Pdb
references: 3hnz
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3hnz
comment: mutant C163A

3hnzA02
type: Pdb
catalytic residue: HIS 303;LYS 335;HIS 340
main chain in catalysis: PHE 400
references: 3hnz
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3hnz

3ho2A01
type: Pdb
references: 3ho2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3ho2
comment: mutant C163A

3ho2A02
type: Pdb
catalytic residue: HIS 303;LYS 335;HIS 340
main chain in catalysis: PHE 400
references: 3ho2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3ho2

3ho9A01
type: Pdb
references: 3ho9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3ho9
comment: mutant C163A

3ho9A02
type: Pdb
catalytic residue: HIS 303;LYS 335;HIS 340
main chain in catalysis: PHE 400
references: 3ho9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3ho9

3i8pA01
type: Pdb
references: 3i8p
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3i8p
comment: mutant C163A

3i8pA02
type: Pdb
catalytic residue: HIS 303;LYS 335;HIS 340
main chain in catalysis: PHE 400
references: 3i8p
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3i8p

3kzuA01
type: Pdb
catalytic residue: CYS 170
main chain in catalysis: CYS 170
references: 3kzu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3kzu

3kzuA02
type: Pdb
catalytic residue: HIS 311;LYS 342;HIS 347
main chain in catalysis: PHE 406
references: 3kzu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3kzu

3kzuB01
type: Pdb
catalytic residue: CYS 170
main chain in catalysis: CYS 170
references: 3kzu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3kzu

3kzuB02
type: Pdb
catalytic residue: HIS 311;LYS 342;HIS 347
main chain in catalysis: PHE 406
references: 3kzu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3kzu

3kzuC01
type: Pdb
catalytic residue: CYS 170
main chain in catalysis: CYS 170
references: 3kzu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3kzu

3kzuC02
type: Pdb
catalytic residue: HIS 311;LYS 342;HIS 347
main chain in catalysis: PHE 406
references: 3kzu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3kzu

3o04A01
type: Pdb
catalytic residue: CYS 164
main chain in catalysis: CYS 164
references: 3o04
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3o04

3o04A02
type: Pdb
catalytic residue: HIS 303;LYS 335;HIS 340
main chain in catalysis: PHE 399
references: 3o04
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3o04

4ddoA01
type: Pdb
catalytic residue: CYS 172
main chain in catalysis: CYS 172
references: 4ddo
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:4ddo

4ddoA02
type: Pdb
catalytic residue: HIS 313;LYS 344;HIS 349
main chain in catalysis: PHE 409
references: 4ddo
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:4ddo

4f32A01
type: Pdb
main chain in catalysis: CSU 172
modified residue: CSU 172(Cysteine-S-Sulfonic acid)
references: 4f32
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:4f32

4f32A02
type: Pdb
catalytic residue: HIS 313;LYS 344;HIS 349
main chain in catalysis: PHE 409
references: 4f32
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:4f32

4f32B01
type: Pdb
main chain in catalysis: CSU 172
modified residue: CSU 172(Cysteine-S-Sulfonic acid)
references: 4f32
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:4f32

4f32B02
type: Pdb
catalytic residue: HIS 313;LYS 344;HIS 349
main chain in catalysis: PHE 409
references: 4f32
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:4f32

[acyl-carrier-protein]
type: KeggProduct
compound type: carbohydrate
compound type: peptide/protein
compound type: phosphate group/phosphate ion
compound type: sulfhydryl group
references: KEGG:C00229

Bicabonate(HCO3-)
type: KeggProduct
compound type: carboxyl group
references: KEGG:C00288
references: CHEBI:17544
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

malonyl-[acyl-carrier-protein]
type: KeggSubstrate
compound type: carbohydrate
compound type: carboxyl group
compound type: peptide/protein
compound type: phosphate group/phosphate ion
compound type: sulfide group
references: KEGG:C01209

[Acyl-carrier protein]-decarboxylated malonyl group (Peptidyl-Ser-phosphopantetheine-S-enolate)
type: KeggIntermediate
references: KEGG:I00134

Peptidyl-Cys-tetrahedral-(Z)-hexadec-11-enoyl-[acyl-carrier protein]
type: KeggIntermediate
references: KEGG:I00138

Peptidyl-Cys-S-(Z)-hexadec-11-enoyl
type: KeggIntermediate
references: KEGG:I00139

[Acyl-carrier protein]-tetrahedral-malonyl group
type: KeggIntermediate
references: KEGG:I00140

Peptidyl-Cys-tetrahedral-(Z)-hexadec-11-enoyl-keto-[acyl-carrier protein]
type: KeggIntermediate
references: KEGG:I00141

(Z)-hexadec-11-enoyl-[acyl-carrier protein]
type: KeggSubstrate
compound type: carbohydrate
compound type: lipid
compound type: peptide/protein
compound type: phosphate group/phosphate ion
compound type: sulfide group
references: KEGG:L00039

(Z)-3-oxooctadec-13-enoyl-[acyl-carrier protein]
type: KeggProduct
compound type: carbohydrate
compound type: lipid
compound type: peptide/protein
compound type: phosphate group/phosphate ion
compound type: sulfide group
references: KEGG:L00040

KASII
type: KeggEnzyme

KAS II
type: KeggEnzyme

FabF
type: KeggEnzyme

3-oxoacyl-acyl carrier protein synthase I
type: KeggEnzyme

beta-ketoacyl-ACP synthase II
type: KeggEnzyme

(Z)-hexadec-11-enoyl-[acyl-carrier-protein]:malonyl-[acyl-carrier-protein] C-acyltransferase (decarboxylating)
type: KeggEnzyme