1RBA
SUBSTITUTION OF ASP193 TO ASN AT THE ACTIVE SITE OF RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE RESULTS IN CONFORMATIONAL CHANGES
External Resource: Annotation
Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage
Domain Annotation: SCOP2 Classification SCOP2 Database Homepage
Chains | Type | Family Name | Domain Identifier | Family Identifier | Provenance Source (Version) |
---|---|---|---|---|---|
A | SCOP2B Superfamily | RuBisCo C-terminal domain | 8043704 | 3000552 | SCOP2B (2022-06-29) |
A | SCOP2B Superfamily | RuBisCO large subunit small (N-terminal) domain | 8035457 | 3001258 | SCOP2B (2022-06-29) |
B | SCOP2B Superfamily | RuBisCO large subunit small (N-terminal) domain | 8035457 | 3001258 | SCOP2B (2022-06-29) |
B | SCOP2B Superfamily | RuBisCo C-terminal domain | 8043704 | 3000552 | SCOP2B (2022-06-29) |
Domain Annotation: ECOD Classification ECOD Database Homepage
Chains | Family Name | Domain Identifier | Architecture | Possible Homology | Homology | Topology | Family | Provenance Source (Version) |
---|---|---|---|---|---|---|---|---|
A | PF02788 | e1rbaA1 | A: a+b two layers | X: Alpha-beta plaits | H: RuBisCO, large subunit, small (N-terminal) domain (From Topology) | T: RuBisCO, large subunit, small (N-terminal) domain | F: PF02788 | ECOD (1.6) |
A | PF00016 | e1rbaA2 | A: a/b barrels | X: TIM beta/alpha-barrel | H: TIM barrels (From Topology) | T: TIM barrels | F: PF00016 | ECOD (1.6) |
B | PF02788 | e1rbaB1 | A: a+b two layers | X: Alpha-beta plaits | H: RuBisCO, large subunit, small (N-terminal) domain (From Topology) | T: RuBisCO, large subunit, small (N-terminal) domain | F: PF02788 | ECOD (1.6) |
B | PF00016 | e1rbaB2 | A: a/b barrels | X: TIM beta/alpha-barrel | H: TIM barrels (From Topology) | T: TIM barrels | F: PF00016 | ECOD (1.6) |
Domain Annotation: CATH CATH Database Homepage
Chain | Domain | Class | Architecture | Topology | Homology | Provenance Source (Version) |
---|---|---|---|---|---|---|
A | 3.30.70.150 | Alpha Beta | 2-Layer Sandwich | Alpha-Beta Plaits | RuBisCO large subunit, N-terminal domain | CATH (4.3.0) |
A | 3.20.20.110 | Alpha Beta | Alpha-Beta Barrel | TIM Barrel | Ribulose bisphosphate carboxylase, large subunit, C-terminal domain | CATH (4.3.0) |
B | 3.30.70.150 | Alpha Beta | 2-Layer Sandwich | Alpha-Beta Plaits | RuBisCO large subunit, N-terminal domain | CATH (4.3.0) |
B | 3.20.20.110 | Alpha Beta | Alpha-Beta Barrel | TIM Barrel | Ribulose bisphosphate carboxylase, large subunit, C-terminal domain | CATH (4.3.0) |
Protein Family Annotation Pfam Database Homepage
Chains | Accession | Name | Description | Comments | Source |
---|---|---|---|---|---|
PF02788 | Ribulose bisphosphate carboxylase large chain, N-terminal domain (RuBisCO_large_N) | Ribulose bisphosphate carboxylase large chain, N-terminal domain | The N-terminal domain of RuBisCO large chain adopts a ferredoxin-like fold. | Domain | |
PF00016 | Ribulose bisphosphate carboxylase large chain, catalytic domain (RuBisCO_large) | Ribulose bisphosphate carboxylase large chain, catalytic domain | The C-terminal domain of RuBisCO large chain is the catalytic domain adopting a TIM barrel fold. | Domain |
Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage
InterPro: Protein Family Classification InterPro Database Homepage
Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage
Chains | Enzyme Name | Description | Catalytic Residues |
---|---|---|---|
ribulose-bisphosphate carboxylase (type II) M-CSA #797 | Ribulose-bisphosphate carboxylase/oxygenase (RuBisCO) is the enzyme responsible for the initial step of carbon fixation during photosynthesis. RuBisCO carboxylates one molecule of ribulose-bisphosphate (RuBP), yielding two molecules of 3-phosphoglycerate(PGA). The latter is subsequently used partly to regenerate RuBP in the Calvin cycle and partly to build up sugar compounds. RuBisCO also acts as an oxygenase with RuBP as substrate. The oxygenation of RuBP initiates photorespiration, a pathway in which energy initially accumulated through the light reactions is lost as heat, with no apparent benefit for the plant. In higher plants and the majority of photosynthetic microorganisms, RuBP-carboxylase is composed of eight large and eight small subunits, forming a hexadecameric structure, L8S8. In contrast, in some photosynthetic bacteria, RuBisCO is a dimer of only large subunits. | Defined by 8 residues: LYS:A-166LYS:A-191ASN:A-192ASN:A-193GLU:A-194HIS:A-287HIS:A-321LYS:A-329 EC: 4.1.1.39 (PDB Primary Data) |