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Protein

Ribulose bisphosphate carboxylase

Gene

cbbM

Organism
Rhodospirillum rubrum
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site.

Catalytic activityi

2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O.
3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2.

Cofactori

Mg2+2 PublicationsNote: Binds 1 Mg2+ ion per subunit.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei111Substrate; in homodimeric partner1
Active sitei166Proton acceptor1
Binding sitei168Substrate1
Metal bindingi191Magnesium; via carbamate group2 Publications1
Metal bindingi193Magnesium2 Publications1
Metal bindingi194Magnesium2 Publications1
Active sitei287Proton acceptor1
Binding sitei288Substrate1
Binding sitei321Substrate1
Sitei329Transition state stabilizer1
Binding sitei368Substrate1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase, Monooxygenase, Oxidoreductase

Keywords - Biological processi

Calvin cycle, Carbon dioxide fixation, Photosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13280.
BRENDAi4.1.1.39. 5420.
SABIO-RKP04718.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylase (EC:4.1.1.39)
Short name:
RuBisCO
Gene namesi
Name:cbbM
Synonyms:cbbL2, rbpL
OrganismiRhodospirillum rubrum
Taxonomic identifieri1085 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeRhodospirillum

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi193D → N: Loss of activity, decreased affinity for Mg(2+). Curated1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000626661 – 466Ribulose bisphosphate carboxylaseAdd BLAST466

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei191N6-carboxylysine1 Publication1

Interactioni

Subunit structurei

Homodimer.5 Publications

Protein-protein interaction databases

IntActiP04718. 1 interactor.
MINTiMINT-8090212.
STRINGi269796.Rru_A2400.

Structurei

Secondary structure

1466
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni4 – 6Combined sources3
Helixi14 – 20Combined sources7
Beta strandi23 – 32Combined sources10
Beta strandi34 – 36Combined sources3
Helixi38 – 48Combined sources11
Turni49 – 51Combined sources3
Beta strandi59 – 62Combined sources4
Beta strandi70 – 75Combined sources6
Turni76 – 79Combined sources4
Beta strandi80 – 86Combined sources7
Helixi87 – 89Combined sources3
Turni94 – 96Combined sources3
Helixi101 – 109Combined sources9
Helixi111 – 113Combined sources3
Beta strandi116 – 127Combined sources12
Helixi130 – 133Combined sources4
Helixi143 – 150Combined sources8
Beta strandi154 – 156Combined sources3
Beta strandi160 – 164Combined sources5
Beta strandi166 – 169Combined sources4
Helixi173 – 183Combined sources11
Turni184 – 186Combined sources3
Beta strandi188 – 191Combined sources4
Beta strandi197 – 199Combined sources3
Helixi204 – 222Combined sources19
Beta strandi227 – 231Combined sources5
Helixi237 – 251Combined sources15
Helixi252 – 257Combined sources6
Beta strandi258 – 263Combined sources6
Turni264 – 266Combined sources3
Helixi269 – 278Combined sources10
Beta strandi284 – 287Combined sources4
Turni289 – 291Combined sources3
Helixi292 – 295Combined sources4
Beta strandi301 – 303Combined sources3
Helixi305 – 315Combined sources11
Beta strandi318 – 321Combined sources4
Helixi336 – 344Combined sources9
Beta strandi346 – 349Combined sources4
Beta strandi354 – 356Combined sources3
Beta strandi364 – 369Combined sources6
Turni373 – 375Combined sources3
Helixi376 – 383Combined sources8
Beta strandi389 – 392Combined sources4
Turni394 – 397Combined sources4
Helixi403 – 419Combined sources17
Helixi423 – 428Combined sources6
Helixi431 – 439Combined sources9
Helixi441 – 447Combined sources7
Helixi451 – 455Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RBAX-ray2.60A/B1-466[»]
1RUSX-ray2.90A/B1-466[»]
2RUSX-ray2.30A/B1-466[»]
5RUBX-ray1.70A/B1-466[»]
9RUBX-ray2.60A/B1-466[»]
ProteinModelPortaliP04718.
SMRiP04718.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04718.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105DT1. Bacteria.
COG1850. LUCA.

Family and domain databases

CDDicd08211. RuBisCO_large_II. 1 hit.
Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPiMF_01339. RuBisCO_L_type2. 1 hit.
InterProiIPR033966. RuBisCO.
IPR020878. RuBisCo_large_chain_AS.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR020871. RuBisCO_lsuII.
[Graphical view]
PfamiPF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view]
SUPFAMiSSF51649. SSF51649. 1 hit.
SSF54966. SSF54966. 1 hit.
PROSITEiPS00157. RUBISCO_LARGE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P04718-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDQSSRYVNL ALKEEDLIAG GEHVLCAYIM KPKAGYGYVA TAAHFAAESS
60 70 80 90 100
TGTNVEVCTT DDFTRGVDAL VYEVDEAREL TKIAYPVALF HRNITDGKAM
110 120 130 140 150
IASFLTLTMG NNQGMGDVEY AKMHDFYVPE AYRALFDGPS VNISALWKVL
160 170 180 190 200
GRPEVDGGLV VGTIIKPKLG LRPKPFAEAC HAFWLGGDFI KNDEPQGNQP
210 220 230 240 250
FAPLRDTIAL VADAMRRAQD ETGEAKLFSA NITADDPFEI IARGEYVLET
260 270 280 290 300
FGENASHVAL LVDGYVAGAA AITTARRRFP DNFLHYHRAG HGAVTSPQSK
310 320 330 340 350
RGYTAFVHCK MARLQGASGI HTGTMGFGKM EGESSDRAIA YMLTQDEAQG
360 370 380 390 400
PFYRQSWGGM KACTPIISGG MNALRMPGFF ENLGNANVIL TAGGGAFGHI
410 420 430 440 450
DGPVAGARSL RQAWQAWRDG VPVLDYAREH KELARAFESF PGDADQIYPG
460
WRKALGVEDT RSALPA
Length:466
Mass (Da):50,504
Last modified:August 13, 1987 - v1
Checksum:i37D8C0076CAF7D54
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00286 Genomic DNA. Translation: CAA25080.1.
PIRiS07295.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00286 Genomic DNA. Translation: CAA25080.1.
PIRiS07295.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RBAX-ray2.60A/B1-466[»]
1RUSX-ray2.90A/B1-466[»]
2RUSX-ray2.30A/B1-466[»]
5RUBX-ray1.70A/B1-466[»]
9RUBX-ray2.60A/B1-466[»]
ProteinModelPortaliP04718.
SMRiP04718.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP04718. 1 interactor.
MINTiMINT-8090212.
STRINGi269796.Rru_A2400.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105DT1. Bacteria.
COG1850. LUCA.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13280.
BRENDAi4.1.1.39. 5420.
SABIO-RKP04718.

Miscellaneous databases

EvolutionaryTraceiP04718.

Family and domain databases

CDDicd08211. RuBisCO_large_II. 1 hit.
Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPiMF_01339. RuBisCO_L_type2. 1 hit.
InterProiIPR033966. RuBisCO.
IPR020878. RuBisCo_large_chain_AS.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR020871. RuBisCO_lsuII.
[Graphical view]
PfamiPF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view]
SUPFAMiSSF51649. SSF51649. 1 hit.
SSF54966. SSF54966. 1 hit.
PROSITEiPS00157. RUBISCO_LARGE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRBL2_RHORU
AccessioniPrimary (citable) accession number: P04718
Secondary accession number(s): P19365, P72313
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: November 30, 2016
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The basic functional RuBisCO is composed of a large chain homodimer in a "head-to-tail" conformation. In contrast to form I RuBisCO, the form II RuBisCO are composed solely of large subunits (By similarity).By similarity

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.