M00145
type: Enzyme
cath: OB fold (Dihydrolipoamide Acetyltransferase, E2P)
cath: 2-enoyl-CoA Hydratase; Chain A, domain 1
cath: TIM Barrel
ec: https://purl.uniprot.org/enzyme/2.1.3.1
uniprot: P02904
uniprot: Q8GBW6
kegg enzyme: methylmalonyl-CoA carboxytransferase
kegg enzyme: transcarboxylase
kegg enzyme: methylmalonyl coenzyme A carboxyltransferase
kegg enzyme: methylmalonyl-CoA transcarboxylase
kegg enzyme: oxalacetic transcarboxylase
kegg enzyme: methylmalonyl-CoA carboxyltransferase
kegg enzyme: (S)-2-methyl-3-oxopropanoyl-CoA:pyruvate carboxyltransferase
kegg enzyme: (S)-2-methyl-3-oxopropanoyl-CoA:pyruvate carboxytransferasecarboxytransferase [incorrect]
kegg pathway: Propanoate metabolism
kegg cofactor: Biotin
kegg cofactor: Cobalt
kegg cofactor: Zinc
kegg substrate: (S)-2-Methyl-3-oxopropanoyl-CoA
kegg substrate: Pyruvate
kegg product: Propanoyl-CoA
kegg product: Oxaloacetate
pdb: 1dczA
pdb: 1dd2A
pdb: 1on3A01
pdb: 1on3B01
pdb: 1on3C01
pdb: 1on3D01
pdb: 1on3E01
pdb: 1on3F01
pdb: 1on9A01
pdb: 1on9B01
pdb: 1on9C01
pdb: 1on9D01
pdb: 1on9E01
pdb: 1on9F01
pdb: 1on3A02
pdb: 1on3B02
pdb: 1on3C02
pdb: 1on3D02
pdb: 1on3E02
pdb: 1on3F02
pdb: 1on9A02
pdb: 1on9B02
pdb: 1on9C02
pdb: 1on9D02
pdb: 1on9E02
pdb: 1on9F02
pdb bound state: Unbound
  compound: (S)-2-Methyl-3-oxopropanoyl-CoA
  pdb: 1dczA
pdb bound state: Unbound
  compound: (S)-2-Methyl-3-oxopropanoyl-CoA
  pdb: 1dd2A
pdb bound state: Analogue
  compound: (S)-2-Methyl-3-oxopropanoyl-CoA
  pdb: 1on9A01
  ligand het code: MCA
pdb bound state: Analogue
  compound: (S)-2-Methyl-3-oxopropanoyl-CoA
  pdb: 1on9B01
  ligand het code: MCA
pdb bound state: Analogue
  compound: (S)-2-Methyl-3-oxopropanoyl-CoA
  pdb: 1on9C01
  ligand het code: MCA
pdb bound state: Analogue
  compound: (S)-2-Methyl-3-oxopropanoyl-CoA
  pdb: 1on9D01
  ligand het code: MCA
pdb bound state: Analogue
  compound: (S)-2-Methyl-3-oxopropanoyl-CoA
  pdb: 1on9E01
  ligand het code: MCA
pdb bound state: Analogue
  compound: (S)-2-Methyl-3-oxopropanoyl-CoA
  pdb: 1on9F01
  ligand het code: MCA
pdb bound state: Unbound
  compound: (S)-2-Methyl-3-oxopropanoyl-CoA
  pdb: 1on3A02
pdb bound state: Unbound
  compound: (S)-2-Methyl-3-oxopropanoyl-CoA
  pdb: 1on3B02
pdb bound state: Unbound
  compound: (S)-2-Methyl-3-oxopropanoyl-CoA
  pdb: 1on3C02
pdb bound state: Unbound
  compound: (S)-2-Methyl-3-oxopropanoyl-CoA
  pdb: 1on3D02
pdb bound state: Unbound
  compound: (S)-2-Methyl-3-oxopropanoyl-CoA
  pdb: 1on3E02
pdb bound state: Unbound
  compound: (S)-2-Methyl-3-oxopropanoyl-CoA
  pdb: 1on3F02
references: Fluorine NMR studies on stereochemical aspects of reactions catalyzed by transcarboxylase, pyruvate kinase, and enzyme I
references: Preliminary crystallographic data and quaternary structural implications of the central subunit of the multi-subunit complex transcarboxylase
references: Carbon-13 labelled biotin--a new probe for the study of enzyme catalyzed carboxylation and decarboxylation reactions
references: The importance of methionine residues for the catalysis of the biotin enzyme, transcarboxylase. Analysis by site-directed mutagenesis
references: The conserved methionines of the 1.3 S biotinyl subunit of transcarboxylase: effect of mutations on conformation and activity
references: Dissection of the biotinyl subunit of transcarboxylase into regions essential for activity and assembly
references: Absence of observable biotin-protein interactions in the 1.3S subunit of transcarboxylase: an NMR study
references: The structure of the exocellular polysaccharide produced by the Archaeon Haloferax gibbonsii (ATCC 33959)
references: Structural characterization of the entire 1.3S subunit of transcarboxylase from Propionibacterium shermanii
references: http://ezcatdb.cbrc.jp/EzCatDB/reference/M00145#10
references: High resolution solution structure of the 1.3S subunit of transcarboxylase from Propionibacterium shermanii
references: New reactions in the crotonase superfamily: structure of methylmalonyl CoA decarboxylase from Escherichia coli.
references: Crystallization and preliminary X-ray analysis of the 12S central subunit of transcarboxylase from Propionibacterium shermanii
references: Characterization of the carboxylate delivery module of transcarboxylase: following spontaneous decarboxylation of the 1.3S-CO2- subunit by NMR and FTIR spectroscopies
references: Substrate binding induces a cooperative conformational change in the 12S subunit of transcarboxylase: Raman crystallographic evidence
references: Transcarboxylase 12S crystal structure: hexamer assembly and substrate binding to a multienzyme core.
comment: As annotated in Swiss-prot (P02904), this enzyme is a multienzyme, which is composed of three subunits, 1.3S, 5S, and 12S. The 1.3S subunit (PDB;1dcz, 1dd2) serves as a carrier of carboxyl group from the 12S subunit (PDB; 1on3, 1on9) to the 5S one (see [11]). The 12 subunit transfers a carboxyl group from the terminal of methyl-malonyl-CoA to the 1.3S subunit, whilst the 5S subunit transfers the carboxyl group from the carrier protein to pyruvate, producing oxalacetate (see [11]).

OB fold (Dihydrolipoamide Acetyltransferase, E2P)
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/2.40.50.100

2-enoyl-CoA Hydratase; Chain A, domain 1
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.90.226.10
catalytic domain: index.html

TIM Barrel
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.20.20.-

Propanoate metabolism
type: KeggPathway
references: KEGG:MAP00640

Biotin
type: KeggCofactor
references: KEGG:C00120
compound type: amide group
compound type: amine group
compound type: fatty acid
compound type: sulfide group
references: CHEBI:15956
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Cobalt
type: KeggCofactor
references: KEGG:C00175
compound type: heavy metal
references: CHEBI:48828
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Zinc
type: KeggCofactor
references: KEGG:C00038
compound type: heavy metal
references: CHEBI:29105
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

(S)-2-Methyl-3-oxopropanoyl-CoA
type: KeggSubstrate
references: KEGG:C00683
compound type: amine group
compound type: carbohydrate
compound type: carboxyl group
compound type: nucleotide
compound type: peptide/protein
compound type: sulfide group
references: CHEBI:15466
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Pyruvate
type: KeggSubstrate
references: KEGG:C00022
compound type: carbohydrate
compound type: carboxyl group
references: CHEBI:32816
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Propanoyl-CoA
type: KeggProduct
references: KEGG:C00100
compound type: amine group
compound type: carbohydrate
compound type: nucleotide
compound type: peptide/protein
compound type: sulfide group
references: CHEBI:15539
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Oxaloacetate
type: KeggProduct
references: KEGG:C00036
compound type: carbohydrate
compound type: carboxyl group
references: CHEBI:30744
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

1on3A01
type: Pdb
references: 1on3
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1on3
catalytic residue: TYR 185
main chain in catalysis: ALA 143;ALA 180;GLY 182;ALA 183

1on3B01
type: Pdb
references: 1on3
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1on3
catalytic residue: TYR 185
main chain in catalysis: ALA 143;ALA 180;GLY 182;ALA 183

1on3C01
type: Pdb
references: 1on3
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1on3
catalytic residue: TYR 185
main chain in catalysis: ALA 143;ALA 180;GLY 182;ALA 183

1on3D01
type: Pdb
references: 1on3
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1on3
catalytic residue: TYR 185
main chain in catalysis: ALA 143;ALA 180;GLY 182;ALA 183

1on3E01
type: Pdb
references: 1on3
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1on3
catalytic residue: TYR 185
main chain in catalysis: ALA 143;ALA 180;GLY 182;ALA 183

1on3F01
type: Pdb
references: 1on3
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1on3
catalytic residue: TYR 185
main chain in catalysis: ALA 143;ALA 180;GLY 182;ALA 183

1on9A01
type: Pdb
references: 1on9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1on9
catalytic residue: TYR 185
main chain in catalysis: ALA 143;ALA 180;GLY 182;ALA 183

1on9B01
type: Pdb
references: 1on9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1on9
catalytic residue: TYR 185
main chain in catalysis: ALA 143;ALA 180;GLY 182;ALA 183

1on9C01
type: Pdb
references: 1on9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1on9
catalytic residue: TYR 185
main chain in catalysis: ALA 143;ALA 180;GLY 182;ALA 183

1on9D01
type: Pdb
references: 1on9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1on9
catalytic residue: TYR 185
main chain in catalysis: ALA 143;ALA 180;GLY 182;ALA 183

1on9E01
type: Pdb
references: 1on9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1on9
catalytic residue: TYR 185
main chain in catalysis: ALA 143;ALA 180;GLY 182;ALA 183

1on9F01
type: Pdb
references: 1on9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1on9
catalytic residue: TYR 185
main chain in catalysis: ALA 143;ALA 180;GLY 182;ALA 183

1on3A02
type: Pdb
references: 1on3
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1on3
cofactor binding residue: HIS 388(metal binding)
main chain in catalysis: GLY 414

1on3B02
type: Pdb
references: 1on3
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1on3
cofactor binding residue: HIS 388(metal binding)
main chain in catalysis: GLY 414

1on3C02
type: Pdb
references: 1on3
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1on3
cofactor binding residue: HIS 388(metal binding)
main chain in catalysis: GLY 414

1on3D02
type: Pdb
references: 1on3
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1on3
cofactor binding residue: HIS 388(metal binding)
main chain in catalysis: GLY 414

1on3E02
type: Pdb
references: 1on3
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1on3
cofactor binding residue: HIS 388(metal binding)
main chain in catalysis: GLY 414

1on3F02
type: Pdb
references: 1on3
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1on3
cofactor binding residue: HIS 388(metal binding)
main chain in catalysis: GLY 414

1on9A02
type: Pdb
references: 1on9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1on9
cofactor binding residue: HIS 388(metal binding)
main chain in catalysis: GLY 414

1on9B02
type: Pdb
references: 1on9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1on9
cofactor binding residue: HIS 388(metal binding)
main chain in catalysis: GLY 414

1on9C02
type: Pdb
references: 1on9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1on9
cofactor binding residue: HIS 388(metal binding)
main chain in catalysis: GLY 414

1on9D02
type: Pdb
references: 1on9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1on9
cofactor binding residue: HIS 388(metal binding)
main chain in catalysis: GLY 414

1on9E02
type: Pdb
references: 1on9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1on9
cofactor binding residue: HIS 388(metal binding)
main chain in catalysis: GLY 414

1on9F02
type: Pdb
references: 1on9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1on9
cofactor binding residue: HIS 388(metal binding)
main chain in catalysis: GLY 414

Fluorine NMR studies on stereochemical aspects of reactions catalyzed by transcarboxylase, pyruvate kinase, and enzyme I
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/3910092
journal: Biochemistry
volume: 24
pages: 6163-9
published year: 1985
authors:
  item: Hoving H
  item: Crysell B
  item: Leadlay PF

Preliminary crystallographic data and quaternary structural implications of the central subunit of the multi-subunit complex transcarboxylase
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/3735431
journal: J Mol Biol
volume: 188
pages: 495-8
published year: 1986
authors:
  item: Skrzypczak-Jankun E
  item: Tulinsky A
  item: Fillers JP
  item: Kumar KG
  item: Wood HG

Carbon-13 labelled biotin--a new probe for the study of enzyme catalyzed carboxylation and decarboxylation reactions
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2269346
journal: FEBS Lett
volume: 277
pages: 156-8
published year: 1990
authors:
  item: Bendrat K
  item: Berger S
  item: Buckel W
  item: Etzel WA
  item: Rohm KH

The importance of methionine residues for the catalysis of the biotin enzyme, transcarboxylase. Analysis by site-directed mutagenesis
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1526981
journal: J Biol Chem
volume: 267
pages: 18407-12
published year: 1992
authors:
  item: Shenoy BC
  item: Xie Y
  item: Park VL
  item: Kumar GK
  item: Beegen H
  item: Wood HG
  item: Samols D

The conserved methionines of the 1.3 S biotinyl subunit of transcarboxylase: effect of mutations on conformation and activity
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8346913
journal: Arch Biochem Biophys
volume: 304
pages: 359-66
published year: 1993
authors:
  item: Shenoy BC
  item: Samols D
  item: Kumar GK

Dissection of the biotinyl subunit of transcarboxylase into regions essential for activity and assembly
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8420991
journal: J Biol Chem
volume: 268
pages: 2232-8
published year: 1993
authors:
  item: Shenoy BC
  item: Kumar GK
  item: Samols D

Absence of observable biotin-protein interactions in the 1.3S subunit of transcarboxylase: an NMR study
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9398186
journal: Biochemistry
volume: 36
pages: 14676-82
published year: 1997
authors:
  item: Reddy DV
  item: Shenoy BC
  item: Carey PR
  item: Sonnichsen FD
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

The structure of the exocellular polysaccharide produced by the Archaeon Haloferax gibbonsii (ATCC 33959)
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9720239
journal: Carbohydr Res
volume: 309
pages: 89-94
published year: 1998
authors:
  item: Paramonov NA
  item: Parolis LA
  item: Parolis H
  item: Boan IF
  item: Anton J
  item: Rodriguez-Valera F

Structural characterization of the entire 1.3S subunit of transcarboxylase from Propionibacterium shermanii
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9792103
journal: Protein Sci
volume: 7
pages: 2156-63
published year: 1998
authors:
  item: Reddy DV
  item: Rothemund S
  item: Shenoy BC
  item: Carey PR
  item: Sonnichsen FD
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

http://ezcatdb.cbrc.jp/EzCatDB/reference/M00145#10
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10542197
journal: J Biol Chem
volume: 274
pages: 31767-9
published year: 1999
authors:
  item: Blanchard CZ
  item: Chapman-Smith A
  item: Wallace JC
  item: Waldrop GL
title: The biotin domain peptide from the biotin carboxyl carrier protein of Escherichia coli acetyl-CoA carboxylase causes a marked increase in the catalytic efficiency of biotin carboxylase and carboxyltransferase relative to free biotin

High resolution solution structure of the 1.3S subunit of transcarboxylase from Propionibacterium shermanii
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10704200
journal: Biochemistry
volume: 39
pages: 2509-16
published year: 2000
authors:
  item: Reddy DV
  item: Shenoy BC
  item: Carey PR
  item: Sonnichsen FD
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

New reactions in the crotonase superfamily: structure of methylmalonyl CoA decarboxylase from Escherichia coli.
type: BibliographicResource
comment: Homologous enzyme
references: http://www.ncbi.nlm.nih.gov/pubmed/10769118
journal: Biochemistry
volume: 39
pages: 4630-9
published year: 2000
authors:
  item: Benning MM
  item: Haller T
  item: Gerlt JA
  item: Holden HM

Crystallization and preliminary X-ray analysis of the 12S central subunit of transcarboxylase from Propionibacterium shermanii
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11173475
journal: Acta Crystallogr D Biol Crystallogr
volume: 57
pages: 266-8
published year: 2001
authors:
  item: Wang YF
  item: Hyatt DC
  item: Rivera RE
  item: Carey PR
  item: Yee VC

Characterization of the carboxylate delivery module of transcarboxylase: following spontaneous decarboxylation of the 1.3S-CO2- subunit by NMR and FTIR spectroscopies
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11841210
journal: Biochemistry
volume: 41
pages: 2191-7
published year: 2002
authors:
  item: Rivera-Hainaj RE
  item: Pusztai-Carey M
  item: Venkat Reddy D
  item: Choowongkomon K
  item: Sonnichsen FD
  item: Carey PR

Substrate binding induces a cooperative conformational change in the 12S subunit of transcarboxylase: Raman crystallographic evidence
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12196011
journal: Biochemistry
volume: 41
pages: 10741-6
published year: 2002
authors:
  item: Zheng X
  item: Rivera-Hainaj RE
  item: Zheng Y
  item: Pusztai-Carey M
  item: Hall PR
  item: Yee VC
  item: Carey PR

Transcarboxylase 12S crystal structure: hexamer assembly and substrate binding to a multienzyme core.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12743028
journal: EMBO J
volume: 22
pages: 2334-47
published year: 2003
authors:
  item: Hall PR
  item: Wang YF
  item: Rivera-Hainaj RE
  item: Zheng X
  item: Pustai-Carey M
  item: Carey PR
  item: Yee VC

Analogue
compound: Pyruvate
pdb: 1on3A01
ligand het code: DXX

Analogue
compound: Pyruvate
pdb: 1on3B01
ligand het code: DXX

Analogue
compound: Pyruvate
pdb: 1on3C01
ligand het code: DXX

Analogue
compound: Pyruvate
pdb: 1on3D01
ligand het code: DXX

Analogue
compound: Pyruvate
pdb: 1on3E01
ligand het code: DXX

Analogue
compound: Pyruvate
pdb: 1on3F01
ligand het code: DXX

Analogue
compound: Cobalt
pdb: 1on3A02
ligand het code: _CD

Analogue
compound: Cobalt
pdb: 1on3C02
ligand het code: _CD

Analogue
compound: Cobalt
pdb: 1on3E02
ligand het code: _CD

Analogue
compound: Cobalt
pdb: 1on9A02
ligand het code: _CD

Analogue
compound: Cobalt
pdb: 1on9C02
ligand het code: _CD

Analogue
compound: Cobalt
pdb: 1on9E02
ligand het code: _CD

ReferenceForCatalyticMechanism
reference index: 12
reference section: Fig.7, p.4638-4639
reference step: 2

ReferenceForCatalyticMechanism
reference index: 16
reference section: Fig.6, p.2340-2341