D00542
type: Enzyme
active site residues resources: Presence of a structurally novel type ribulose-bisphosphate carboxylase/oxygenase in the hyperthermophilic archaeon, Pyrococcus kodakaraensis KOD1.
cath: Alpha-Beta Plaits
cath: TIM Barrel
csa: 1rba
ec: https://purl.uniprot.org/enzyme/4.1.1.39
kegg cofactor: Magnesium
kegg enzyme: Ribulose-bisphosphate carboxylase
kegg intermediate: 2,3-cis-enediol-D-ribulose-1,5-bisphosphate
kegg intermediate: 2-carboxy-3,3-diol-D-arabinitol-1,5-bisphosphate
kegg intermediate: 2-peroxy-3,3-diol-D-arabinitol-1,5-bisphosphate
kegg pathway: Glyoxylate and dicarboxylate metabolism
kegg pathway: Carbon fixation
kegg product: 3-Phospho-D-glycerate
kegg product: 2-Phosphoglycolate
kegg substrate: D-Ribulose 1,5-bisphosphate
kegg substrate: CO2
kegg substrate: H2O
kegg substrate: O2
pdb: 2cwxA01
pdb: 2cwxE01
pdb: 2cxeA01
pdb: 2cxeB01
pdb: 2cxeC01
pdb: 2cxeD01
pdb: 2d69A01
pdb: 2d69B01
pdb: 2d69D01
pdb: 2d69E01
pdb: 1gehA01
pdb: 1gehB01
pdb: 1gehC01
pdb: 1gehD01
pdb: 1gehE01
pdb: 1rbaA01
pdb: 1rbaB01
pdb: 1rusA01
pdb: 1rusB01
pdb: 2rusA01
pdb: 2rusB01
pdb: 5rubA01
pdb: 5rubB01
pdb: 9rubA01
pdb: 9rubB01
pdb: 2cwxA02
pdb: 2cwxE02
pdb: 2cxeA02
pdb: 2cxeB02
pdb: 2cxeC02
pdb: 2cxeD02
pdb: 2d69A02
pdb: 2d69B02
pdb: 2d69D02
pdb: 2d69E02
pdb: 1gehA02
pdb: 1gehB02
pdb: 1gehC02
pdb: 1gehD02
pdb: 1gehE02
pdb: 1rbaA02
pdb: 1rbaB02
pdb: 1rusA02
pdb: 1rusB02
pdb: 2rusA02
pdb: 2rusB02
pdb: 5rubA02
pdb: 5rubB02
pdb: 9rubA02
pdb: 9rubB02
uniprot: O58677
uniprot: O93627
uniprot: P04718
references: Crystal structure of the ternary complex of ribulose-1,5-bisphosphate carboxylase, Mg(II), and activator CO2 at 2.3-A resolution.
references: Functional analysis of the putative catalytic bases His-321 and Ser-368 of Rhodospirillum rubrum ribulose bisphosphate carboxylase/oxygenase by site-directed mutagenesis.
references: Crystal structure of activated ribulose-1,5-bisphosphate carboxylase complexed with its substrate, ribulose-1,5-bisphosphate.
references: RUBISCO: structure and mechanism.
references: Substitution of ASP193 to ASN at the active site of ribulose-1,5-bisphosphate carboxylase results in conformational changes.
references: Role of asparagine-111 at the active site of ribulose-1,5-bisphosphate carboxylase/oxygenase from Rhodospirillum rubrum as explored by site-directed mutagenesis.
references: Chemical and genetic probes of the active site of D-ribulose-1,5-bisphosphate carboxylase/oxygenase: a retrospective based on the three-dimensional structure.
references: Perturbation of reaction-intermediate partitioning by a site-directed mutant of ribulose-bisphosphate carboxylase/oxygenase.

TIM Barrel
type: Cath
catalytic domain: index.html
references: http://www.cathdb.info/version/latest/superfamily/3.20.20.110

Alpha-Beta Plaits
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.30.70.150

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

Glyoxylate and dicarboxylate metabolism
type: KeggPathway
references: KEGG:MAP00630

Carbon fixation
type: KeggPathway
references: KEGG:MAP00710

The sites for catalysis and activation of ribulosebisphosphate carboxylase share a common domain.
type: BibliographicResource
authors:
  item: Pierce J
  item: Reddy GS
journal: Arch Biochem Biophys
pages: 483-93
published year: 1986
volume: 245
references: http://www.ncbi.nlm.nih.gov/pubmed/3082286

RUBISCO: structure and mechanism.
type: BibliographicResource
authors:
  item: Schneider G
  item: Lindqvist Y
  item: Branden CI
journal: Annu Rev Biophys Biomol Struct
pages: 119-43
published year: 1992
volume: 21
references: http://www.ncbi.nlm.nih.gov/pubmed/1525466

Substitution of ASP193 to ASN at the active site of ribulose-1,5-bisphosphate carboxylase results in conformational changes.
type: BibliographicResource
authors:
  item: Soderlind E
  item: Schneider G
  item: Gutteridge S
journal: Eur J Biochem
pages: 729-35
published year: 1992
volume: 206
references: http://www.ncbi.nlm.nih.gov/pubmed/1606957
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Role of asparagine-111 at the active site of ribulose-1,5-bisphosphate carboxylase/oxygenase from Rhodospirillum rubrum as explored by site-directed mutagenesis.
type: BibliographicResource
authors:
  item: Soper TS
  item: Larimer FW
  item: Mural RJ
  item: Lee EH
  item: Hartman FC
journal: J Biol Chem
pages: 8452-7
published year: 1992
volume: 267
references: http://www.ncbi.nlm.nih.gov/pubmed/1569095

Chemical and genetic probes of the active site of D-ribulose-1,5-bisphosphate carboxylase/oxygenase: a retrospective based on the three-dimensional structure.
type: BibliographicResource
authors:
  item: Hartman FC
  item: Harpel MR
journal: Adv Enzymol Relat Areas Mol Biol
pages: 1-75
published year: 1993
volume: 67
references: http://www.ncbi.nlm.nih.gov/pubmed/8322615

Perturbation of reaction-intermediate partitioning by a site-directed mutant of ribulose-bisphosphate carboxylase/oxygenase.
type: BibliographicResource
authors:
  item: Lee EH
  item: Harpel MR
  item: Chen YR
  item: Hartman FC
journal: J Biol Chem
pages: 26583-91
published year: 1993
volume: 268
references: http://www.ncbi.nlm.nih.gov/pubmed/8253788

The X-ray structure of Synechococcus ribulose-bisphosphate carboxylase/oxygenase-activated quaternary complex at 2.2-A resolution.
type: BibliographicResource
authors:
  item: Newman J
  item: Gutteridge S
journal: J Biol Chem
medline id: 94064666
pages: 25876-86
published year: 1993
volume: 268
references: http://www.ncbi.nlm.nih.gov/pubmed/8245022
references: P00880
references: P04716
comment: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).

Structure, function, regulation, and assembly of D-ribulose-1,5-bisphosphate carboxylase/oxygenase.
type: BibliographicResource
authors:
  item: Hartman FC
  item: Harpel MR
journal: Annu Rev Biochem
pages: 197-234
published year: 1994
volume: 63
references: http://www.ncbi.nlm.nih.gov/pubmed/7979237

Oxygenation mechanism of ribulose-bisphosphate carboxylase/oxygenase. Structure and origin of 2-carboxytetritol 1,4-bisphosphate, a novel O2-dependent side product generated by a site-directed mutant.
type: BibliographicResource
authors:
  item: Harpel MR
  item: Serpersu EH
  item: Lamerdin JA
  item: Huang ZH
  item: Gage DA
  item: Hartman FC
journal: Biochemistry
pages: 11296-306
published year: 1995
volume: 34
references: http://www.ncbi.nlm.nih.gov/pubmed/7669788

A signature of the oxygenase intermediate in catalysis by ribulose-bisphosphate carboxylase/oxygenase as provided by a site-directed mutant.
type: BibliographicResource
authors:
  item: Chen YR
  item: Hartman FC
journal: J Biol Chem
pages: 11741-4
published year: 1995
volume: 270
references: http://www.ncbi.nlm.nih.gov/pubmed/7744819

Large structures at high resolution: the 1.6 A crystal structure of spinach ribulose-1,5-bisphosphate carboxylase/oxygenase complexed with 2-carboxyarabinitol bisphosphate.
type: BibliographicResource
authors:
  item: Andersson I
journal: J Mol Biol
medline id: 96240687
pages: 160-74
published year: 1996
volume: 259
references: http://www.ncbi.nlm.nih.gov/pubmed/8648644
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00875
references: P00870
comment: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).

Three-dimensional structure of ribulose-1,5-bisphosphate carboxylase/oxygenase from Rhodospirillum rubrum at 2.9-A resolution.
type: BibliographicResource
authors:
  item: Schneider G
  item: Lindqvist Y
  item: Braenden CI.
  item: Lorimer G
journal: EMBO J
pages: 3409-15
published year: 1986
volume: 5
references: P04718
comment: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).

The structure of the complex between rubisco and its natural substrate ribulose 1,5-bisphosphate.
type: BibliographicResource
authors:
  item: Taylor TC
  item: Andersson I
journal: J Mol Biol
medline id: 97186746
pages: 432-44
published year: 1997
volume: 265
references: http://www.ncbi.nlm.nih.gov/pubmed/9034362
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00875
references: P00870
comment: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).

In situ measurements of ribulose-1,5-bisphosphate carboxylase activity by nuclear magnetic resonance.
type: BibliographicResource
authors:
  item: Wang ZY
  item: Luo S
  item: Sato K
  item: Kobayashi M
  item: Nozawa T
journal: Anal Biochem
pages: 26-32
published year: 1998
volume: 257
references: http://www.ncbi.nlm.nih.gov/pubmed/9512768

Multiple catalytic roles of His 287 of Rhodospirillum rubrum ribulose 1,5-bisphosphate carboxylase/oxygenase.
type: BibliographicResource
authors:
  item: Harpel MR
  item: Larimer FW
  item: Hartman FC
journal: Protein Sci
pages: 730-8
published year: 1998
volume: 7
references: http://www.ncbi.nlm.nih.gov/pubmed/9541405

Mechanism of Rubisco: The Carbamate as General Base.
type: BibliographicResource
authors:
  item: Cleland WW
  item: Andrews TJ
  item: Gutteridge S
  item: Hartman FC
  item: Lorimer GH
journal: Chem Rev
pages: 549-562
published year: 1998
volume: 98
references: http://www.ncbi.nlm.nih.gov/pubmed/11848907

Ribulose bisphosphate carboxylase/oxygenase from the hyperthermophilic archaeon Pyrococcus kodakaraensis KOD1 is composed solely of large subunits and forms a pentagonal structure.
type: BibliographicResource
authors:
  item: Maeda N
  item: Kitano K
  item: Fukui T
  item: Ezaki S
  item: Atomi H
  item: Miki K
  item: Imanaka T
journal: J Mol Biol
pages: 57-66
published year: 1999
volume: 293
references: http://www.ncbi.nlm.nih.gov/pubmed/10512715

Crystal structure of a novel-type archaeal rubisco with pentagonal symmetry.
type: BibliographicResource
authors:
  item: Kitano K
  item: Maeda N
  item: Fukui T
  item: Atomi H
  item: Imanaka T
  item: Miki K
journal: Structure (Camb)
pages: 473-81
published year: 2001
volume: 9
references: http://www.ncbi.nlm.nih.gov/pubmed/11435112
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Complete spectra of the far-red chemiluminescence of the oxygenase reaction of Mn2+-activated ribulose-bisphosphate carboxylase/oxygenase establish excited Mn2+ as the source.
type: BibliographicResource
authors:
  item: Lilley RM
  item: Wang X
  item: Krausz E
  item: Andrews TJ
journal: J Biol Chem
pages: 16488-93
published year: 2003
volume: 278
references: http://www.ncbi.nlm.nih.gov/pubmed/12604603

Despite slow catalysis and confused substrate specificity, all ribulose bisphosphate carboxylases may be nearly perfectly optimized.
type: BibliographicResource
authors:
  item: Tcherkez GG
  item: Farquhar GD
  item: Andrews TJ
journal: Proc Natl Acad Sci U S A
pages: 7246-51
published year: 2006
volume: 103
references: http://www.ncbi.nlm.nih.gov/pubmed/16641091

Distinct form I, II, III, and IV Rubisco proteins from the three kingdoms of life provide clues about Rubisco evolution and structure/function relationships.
type: BibliographicResource
authors:
  item: Tabita FR
  item: Satagopan S
  item: Hanson TE
  item: Kreel NE
  item: Scott SS
journal: J Exp Bot
pages: 1515-24
published year: 2008
volume: 59
references: http://www.ncbi.nlm.nih.gov/pubmed/18281717

Subtle alteration of the active site of ribulose bisphosphate carboxylase/oxygenase by concerted site-directed mutagenesis and chemical modification.
type: BibliographicResource
authors:
  item: Smith HB
  item: Larimer FW
  item: Hartman FC
journal: Biochem Biophys Res Commun
pages: 579-84
published year: 1988
volume: 152
references: http://www.ncbi.nlm.nih.gov/pubmed/2896501

Structure and function of Rubisco.
type: BibliographicResource
authors:
  item: Andersson I
  item: Backlund A
journal: Plant Physiol Biochem
pages: 275-91
published year: 2008
volume: 46
references: http://www.ncbi.nlm.nih.gov/pubmed/18294858

Catalysis and regulation in Rubisco.
type: BibliographicResource
authors:
  item: Andersson I
journal: J Exp Bot
pages: 1555-68
published year: 2008
volume: 59
references: http://www.ncbi.nlm.nih.gov/pubmed/18417482

Crystal structure of the binary complex of ribulose-1,5-bisphosphate carboxylase and its product, 3-phospho-D-glycerate.
type: BibliographicResource
authors:
  item: Lundqvist T
  item: Schneider G
journal: J Biol Chem
pages: 3643-6
published year: 1989
volume: 264
references: http://www.ncbi.nlm.nih.gov/pubmed/2492987
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Crystal structure of the active site of ribulose-bisphosphate carboxylase.
type: BibliographicResource
authors:
  item: Andersson I
  item: Knight S
  item: Schneider G
  item: Lindqvist Y
  item: Lundqvist T
  item: Braenden CI
  item: Lorimer GH
journal: Nature
pages: 229-34
published year: 1989
volume: 337
references: P04718
comment: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).

Crystallographic refinement and structure of ribulose-1,5-bisphosphate carboxylase from Rhodospirillum rubrum at 1.7 A resolution.
type: BibliographicResource
authors:
  item: Schneider G
  item: Lindqvist Y
  item: Lundqvist T
journal: J Mol Biol
medline id: 90189156
pages: 989-1008
published year: 1990
volume: 211
references: http://www.ncbi.nlm.nih.gov/pubmed/2107319
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P04718
comment: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).

Crystal structure of the ternary complex of ribulose-1,5-bisphosphate carboxylase, Mg(II), and activator CO2 at 2.3-A resolution.
type: BibliographicResource
authors:
  item: Lundqvist T
  item: Schneider G
journal: Biochemistry
medline id: 91113700
pages: 904-8
published year: 1991
volume: 30
references: http://www.ncbi.nlm.nih.gov/pubmed/1899197
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P04718
comment: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).

Functional analysis of the putative catalytic bases His-321 and Ser-368 of Rhodospirillum rubrum ribulose bisphosphate carboxylase/oxygenase by site-directed mutagenesis.
type: BibliographicResource
authors:
  item: Harpel MR
  item: Larimer FW
  item: Hartman FC
journal: J Biol Chem
pages: 24734-40
published year: 1991
volume: 266
references: http://www.ncbi.nlm.nih.gov/pubmed/1761567

Crystal structure of activated ribulose-1,5-bisphosphate carboxylase complexed with its substrate, ribulose-1,5-bisphosphate.
type: BibliographicResource
authors:
  item: Lundqvist T
  item: Schneider G
journal: J Biol Chem
pages: 12604-11
published year: 1991
volume: 266
references: http://www.ncbi.nlm.nih.gov/pubmed/1905726
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Presence of a structurally novel type ribulose-bisphosphate carboxylase/oxygenase in the hyperthermophilic archaeon, Pyrococcus kodakaraensis KOD1.
type: BibliographicResource
authors:
  item: Ezaki S
  item: Maeda N
  item: Kishimoto T
  item: Atomi H
  item: Imanaka T
journal: J Biol Chem
pages: 5078-82
published year: 1999
volume: 274
references: http://www.ncbi.nlm.nih.gov/pubmed/9988755

9rubA02
type: Pdb
catalytic residue: LYS 166;LYS 168;LYS 191;HIS 287;LYS 329
cofactor binding residue: LYS 191;ASP 193;GLU 194(Magnesium binding)
main chain in catalysis: ASN 192
modified residue: FMT 601
references: 9rub
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:9rub
comment: modified K191 (carbamated)

9rubB02
type: Pdb
catalytic residue: LYS 166;LYS 168;LYS 191;HIS 287;LYS 329
cofactor binding residue: LYS 191;ASP 193;GLU 194(Magnesium binding)
main chain in catalysis: ASN 192
modified residue: FMT 701
references: 9rub
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:9rub
comment: modified K191 (carbamated)

1rusA02
type: Pdb
catalytic residue: LYS 166;LYS 168;LYS 191;HIS 287;
cofactor binding residue: LYS 191;ASP 193;GLU 194(Magnesium binding)
main chain in catalysis: ASN 192
references: 1rus
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1rus
comment: invisible 326-333

1rusB02
type: Pdb
catalytic residue: LYS 166;LYS 168;LYS 191;HIS 287;
cofactor binding residue: LYS 191;ASP 193;GLU 194(Magnesium binding)
main chain in catalysis: ASN 192
references: 1rus
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1rus
comment: invisible 326-333

2rusA02
type: Pdb
catalytic residue: LYS 166;LYS 168;LYS 191;HIS 287;
cofactor binding residue: LYS 191;ASP 193;GLU 194(Magnesium binding)
main chain in catalysis: ASN 192
modified residue: FOR 501
references: 2rus
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2rus
comment: invisible 325-334, modified K191

2rusB02
type: Pdb
catalytic residue: LYS 166;LYS 168;LYS 191;HIS 287;LYS 329
cofactor binding residue: LYS 191;ASP 193;GLU 194(Magnesium binding)
main chain in catalysis: ASN 192
modified residue: FOR 501
references: 2rus
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2rus
comment: invisible 326-331, modified K191

1gehA02
type: Pdb
catalytic residue: LYS 163;LYS 165;LYS 189;HIS 281;
cofactor binding residue: LYS 189;ASP 191;GLU 192(Magnesium binding)
main chain in catalysis: ASP 190
references: 1geh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1geh
comment: invisible 319-323

1gehB02
type: Pdb
catalytic residue: LYS 163;LYS 165;LYS 189;HIS 281;
cofactor binding residue: LYS 189;ASP 191;GLU 192(Magnesium binding)
main chain in catalysis: ASP 190
references: 1geh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1geh
comment: invisible 319-323

1gehC02
type: Pdb
catalytic residue: LYS 163;LYS 165;LYS 189;HIS 281;
cofactor binding residue: LYS 189;ASP 191;GLU 192(Magnesium binding)
main chain in catalysis: ASP 190
references: 1geh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1geh
comment: invisible 319-323

1gehD02
type: Pdb
catalytic residue: LYS 163;LYS 165;LYS 189;HIS 281;
cofactor binding residue: LYS 189;ASP 191;GLU 192(Magnesium binding)
main chain in catalysis: ASP 190
references: 1geh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1geh
comment: invisible 319-323

1gehE02
type: Pdb
catalytic residue: LYS 163;LYS 165;LYS 189;HIS 281;
cofactor binding residue: LYS 189;ASP 191;GLU 192(Magnesium binding)
main chain in catalysis: ASP 190
references: 1geh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1geh
comment: invisible 319-323

1rbaA02
type: Pdb
catalytic residue: LYS 166;LYS 168;LYS 191;HIS 287;
cofactor binding residue: LYS 191; ;GLU 194(Magnesium binding)
main chain in catalysis: ASN 192
references: 1rba
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1rba
comment: mutant D193N, invisible 325-334

1rbaB02
type: Pdb
catalytic residue: LYS 166;LYS 168;LYS 191;HIS 287;
cofactor binding residue: LYS 191; ;GLU 194(Magnesium binding)
main chain in catalysis: ASN 192
references: 1rba
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1rba
comment: mutant D193N, invisible 325-334

2cwxA02
type: Pdb
catalytic residue: LYS 160;LYS 162;LYS 186;HIS 279;LYS 318
cofactor binding residue: LYS 186;ASP 188;GLU 189(Magnesium binding)
main chain in catalysis: ASP 187
references: 2cwx
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2cwx

2cwxE02
type: Pdb
catalytic residue: LYS 160;LYS 162;LYS 186;HIS 279;LYS 318
cofactor binding residue: LYS 186;ASP 188;GLU 189(Magnesium binding)
main chain in catalysis: ASP 187
references: 2cwx
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2cwx

2cxeA02
type: Pdb
catalytic residue: LYS 160;LYS 162;LYS 186;HIS 279;LYS 318
cofactor binding residue: LYS 186;ASP 188;GLU 189(Magnesium binding)
main chain in catalysis: ASP 187
references: 2cxe
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2cxe

2cxeB02
type: Pdb
catalytic residue: LYS 160;LYS 162;LYS 186;HIS 279;LYS 318
cofactor binding residue: LYS 186;ASP 188;GLU 189(Magnesium binding)
main chain in catalysis: ASP 187
references: 2cxe
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2cxe

2cxeC02
type: Pdb
catalytic residue: LYS 160;LYS 162;LYS 186;HIS 279;LYS 318
cofactor binding residue: LYS 186;ASP 188;GLU 189(Magnesium binding)
main chain in catalysis: ASP 187
references: 2cxe
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2cxe

2cxeD02
type: Pdb
catalytic residue: LYS 160;LYS 162;LYS 186;HIS 279;LYS 318
cofactor binding residue: LYS 186;ASP 188;GLU 189(Magnesium binding)
main chain in catalysis: ASP 187
references: 2cxe
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2cxe

2d69A02
type: Pdb
catalytic residue: LYS 160;LYS 162;LYS 186;HIS 279;LYS 318
cofactor binding residue: LYS 186;ASP 188;GLU 189(Magnesium binding)
main chain in catalysis: ASP 187
references: 2d69
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2d69

2d69B02
type: Pdb
catalytic residue: LYS 160;LYS 162;LYS 186;HIS 279;LYS 318
cofactor binding residue: LYS 186;ASP 188;GLU 189(Magnesium binding)
main chain in catalysis: ASP 187
references: 2d69
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2d69

2d69D02
type: Pdb
catalytic residue: LYS 160;LYS 162;LYS 186;HIS 279;LYS 318
cofactor binding residue: LYS 186;ASP 188;GLU 189(Magnesium binding)
main chain in catalysis: ASP 187
references: 2d69
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2d69

2d69E02
type: Pdb
catalytic residue: LYS 160;LYS 162;LYS 186;HIS 279;LYS 318
cofactor binding residue: LYS 186;ASP 188;GLU 189(Magnesium binding)
main chain in catalysis: ASP 187
references: 2d69
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2d69

5rubA02
type: Pdb
catalytic residue: LYS 166;LYS 168;LYS 191;HIS 287;
cofactor binding residue: LYS 191;ASP 193;GLU 194(Magnesium binding)
main chain in catalysis: ASN 192
references: 5rub
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:5rub
comment: invisible 325-333

5rubB02
type: Pdb
catalytic residue: LYS 166;LYS 168;LYS 191;HIS 287;
cofactor binding residue: LYS 191;ASP 193;GLU 194(Magnesium binding)
main chain in catalysis: ASN 192
references: 5rub
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:5rub
comment: invisible 324-335

Magnesium
type: KeggCofactor
compound type: divalent metal (Ca2+, Mg2+)
references: KEGG:C00305
references: CHEBI:18420
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

3-Phospho-D-glycerate
type: KeggProduct
compound type: carbohydrate
compound type: carboxyl group
compound type: phosphate group/phosphate ion
references: KEGG:C00197
references: CHEBI:17794
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

D-Ribulose 1,5-bisphosphate
type: KeggSubstrate
compound type: carbohydrate
compound type: phosphate group/phosphate ion
references: KEGG:C01182
references: CHEBI:16710
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

O2
type: KeggSubstrate
compound type: others
ec: (oxygenation)
references: KEGG:C00007
references: CHEBI:15379
references: CHEBI:26689
references: CHEBI:27140
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

CO2
type: KeggSubstrate
compound type: others
ec: (carboxylation)
references: KEGG:C00011
references: CHEBI:16526
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

2-Phosphoglycolate
type: KeggProduct
compound type: carboxyl group
compound type: phosphate group/phosphate ion
ec: (oxygenation)
references: KEGG:C00988
references: CHEBI:17150
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

2,3-cis-enediol-D-ribulose-1,5-bisphosphate
type: KeggIntermediate
references: KEGG:I00064

2-carboxy-3,3-diol-D-arabinitol-1,5-bisphosphate
type: KeggIntermediate
ec: (carboxylation)
references: KEGG:I00065

2-peroxy-3,3-diol-D-arabinitol-1,5-bisphosphate
type: KeggIntermediate
ec: (oxygenation)
references: KEGG:I00066

D-ribulose 1,5-diphosphate carboxylase
type: KeggEnzyme

D-ribulose-1,5-bisphosphate carboxylase
type: KeggEnzyme

RuBP carboxylase
type: KeggEnzyme

Carboxydismutase
type: KeggEnzyme

Diphosphoribulose carboxylase
type: KeggEnzyme

Ribulose 1,5-bisphosphate carboxylase
type: KeggEnzyme

Ribulose 1,5-bisphosphate carboxylase/oxygenase
type: KeggEnzyme

Ribulose 1,5-diphosphate carboxylase
type: KeggEnzyme

Ribulose 1,5-diphosphate carboxylase/oxygenase
type: KeggEnzyme

Ribulose bisphosphate carboxylase/oxygenase
type: KeggEnzyme

Ribulose diphosphate carboxylase
type: KeggEnzyme

Ribulose diphosphate carboxylase/oxygenase
type: KeggEnzyme

Rubisco
type: KeggEnzyme

ReferenceForCatalyticMechanism
reference index: 1
reference section: Scheme I, p.484
reference step: 3

ReferenceForCatalyticMechanism
reference index: 6
reference section: Scheme I, p.990
reference step: 5

ReferenceForCatalyticMechanism
reference index: 7
reference section: FIGURE 1, p.905
reference step: 3

ReferenceForCatalyticMechanism
reference index: 9
reference section: FIG. 1, p.12605
reference step: 5

ReferenceForCatalyticMechanism
reference index: 9
reference section: FIG. 8A, p.12609
reference step: 1

ReferenceForCatalyticMechanism
reference index: 10
reference section: Figure 1, p.124
reference step: 4

ReferenceForCatalyticMechanism
reference index: 13
reference section: Figure 2, p.6
reference step: 6

ReferenceForCatalyticMechanism
reference index: 13
reference section: Figure 10, p.38
reference step: 1

ReferenceForCatalyticMechanism
reference index: 15
reference section: FIG. 8, p.25884
reference step: 6

ReferenceForCatalyticMechanism
reference index: 16
reference section: Figure 1, p.209
reference step: 6

ReferenceForCatalyticMechanism
reference index: 17
reference section: FIGURE 10, p.11304
reference step: 2

ReferenceForCatalyticMechanism
reference index: 18
reference section: FIG. 1, p.11742
reference step: 5

ReferenceForCatalyticMechanism
reference index: 18
reference section: FIG. 5, p.11743
reference step: 3

ReferenceForCatalyticMechanism
reference index: 19
reference section: Figure 1, p.161
reference step: 5

ReferenceForCatalyticMechanism
reference index: 19
reference section: Figure 2A, p.162
reference step: 1

ReferenceForCatalyticMechanism
reference index: 19
reference section: Figure 2B, p.162
reference step: 1

ReferenceForCatalyticMechanism
reference index: 19
reference section: Figure 8, p.168
reference step: 5

ReferenceForCatalyticMechanism
reference index: 20
reference section: Figue 1, p.439
reference step: 7

ReferenceForCatalyticMechanism
reference index: 20
reference section: Figue 7, p.440
reference step: 8

ReferenceForCatalyticMechanism
reference index: 21
reference section: SCHEME 1, p.27
reference step: 3

ReferenceForCatalyticMechanism
reference index: 22
reference section: Fig. 6, p.734
reference step: 3