EC number:4.1.1.39

Enzyme

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EC Tree
     4. Lyases
        4.1 Carbon-carbon lyases
            4.1.1 Carboxy-lyases
ID:4.1.1.39
Description:Ribulose-bisphosphate carboxylase.
Alternative Name: RuBP carboxylase.
RuBisCO.
Ribulose diphosphate carboxylase/oxygenase.
Ribulose diphosphate carboxylase.
Ribulose bisphosphate carboxylase/oxygenase.
Ribulose 1,5-diphosphate carboxylase/oxygenase.
Ribulose 1,5-diphosphate carboxylase.
Ribulose 1,5-bisphosphate carboxylase/oxygenase.
Ribulose 1,5-bisphosphate carboxylase.
Diphosphoribulose carboxylase.
D-ribulose-1,5-bisphosphate carboxylase.
D-ribulose 1,5-diphosphate carboxylase.
Carboxydismutase.
Prosite: PDOC00142;
PDB:
PDBScop
1RSC 8023481; 8035861; 8023481; 8035861; 8023481; 8035861; 8023073; 8031323; 8035453; 8043701; 8023073; 8031323; 8035453; 8043701; 8023481; 8035861; 8023481; 8035861; 8023073; 8031323; 8035453; 8043701; 8023073; 8031323; 8035453; 8043701; 8023481; 8035861; 8023073; 8031323; 8035453; 8043701; 8023073; 8031323; 8035453; 8043701; 8023481; 8035861; 8023481; 8035861; 8023073; 8031323; 8035453; 8043701; 8023073; 8031323; 8035453; 8043701;
1RBO 8023429; 8035809; 8023025; 8031296; 8035405; 8043674; 8023429; 8035809; 8023025; 8031296; 8035405; 8043674; 8023429; 8035809; 8023429; 8035809; 8023025; 8031296; 8035405; 8043674; 8023025; 8031296; 8035405; 8043674;
1RLD 8023417; 8035797; 8023417; 8035797; 8023009; 8031292; 8035389; 8043670; 8023009; 8031292; 8035389; 8043670;
1RLC 8023417; 8035797; 8023009; 8031292; 8035389; 8043670;
1EJ7 8023417; 8035797; 8023009; 8031292; 8035389; 8043670;
 » show all
Cath: 3.20.20.110; 3.30.190.10; 3.30.70.150; 3.90.1410.10; 3.90.1420.10;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 4.1.1.39
BRENDA Enzyme Link: BRENDA 4.1.1.39
KEGG Enzyme Link: KEGG4.1.1.39
BioCyc Enzyme Link: BioCyc 4.1.1.39
ExPASy Enzyme Link: ExPASy4.1.1.39
EC2PDB Enzyme Link: EC2PDB 4.1.1.39
ExplorEnz Enzyme Link: ExplorEnz 4.1.1.39
PRIAM enzyme-specific profiles Link: PRIAM 4.1.1.39
IntEnz Enzyme Link: IntEnz 4.1.1.39
MEDLINE Enzyme Link: MEDLINE 4.1.1.39

EC number:4.1.1.39

MSA:

4.1.1.39;
Phylogenetic Tree:

4.1.1.39;
Uniprot:
M-CSA:
RHEA:23124 2 3-phospho-D-glycerate + 2 H(+) = CO2 + D-ribulose 1,5-bisphosphate + H2O
RULE(radius=1) [*:1]-[CH;+0:2](-[OH;+0:3])-[C;H0;+0:4](=[O;H0;+0:5])-[OH;+0:6].[*:7]=[C;H0;+0:8](-[OH;+0:9])-[CH;+0:10](-[*:11])-[*:12].[H+;H0:13].[H+;H0:14]>>[*:1]-[C;H0;+0:2](=[O;H0;+0:3])-[CH;+0:4](-[OH;+0:5])-[CH;+0:10](-[*:11])-[*:12].[*:7]=[C;H0;+0:8]=[O;H0;+0:9].[OH2;+0:6]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Presence of a structurally novel type ribulose-bisphosphate carboxylase/oxygenase in the hyperthermophilic archaeon, Pyrococcus kodakaraensis KOD1.Ezaki S, Maeda N, Kishimoto T, Atomi H, Imanaka T1999 Feb 199988755
Closely related form I ribulose bisphosphate carboxylase/oxygenase molecules that possess different CO2/O2 substrate specificities.Horken KM, Tabita FR1999 Jan 159882445
Structure of an effector-induced inactivated state of ribulose 1,5-bisphosphate carboxylase/oxygenase: the binary complex between enzyme and xylulose 1,5-bisphosphate.Newman J, Gutteridge S1994 Jun 157922027
A crystal form of ribulose-1,5-bisphosphate carboxylase/oxygenase from Nicotiana tabacum in the activated state.Suh SW, Cascio D, Chapman MS, Eisenberg D1987 Sep 203681999