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Protein

Ribulose bisphosphate carboxylase

Gene

cbbM

Organism
Rhodobacter sphaeroides (strain ATCC 17025 / ATH 2.4.3)
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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.UniRule annotation

Catalytic activityi

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

Cofactori

Mg2+UniRule annotationNote: Binds 1 Mg2+ ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei111 – 1111Substrate; in homodimeric partnerUniRule annotation
Active sitei166 – 1661Proton acceptorUniRule annotation
Binding sitei168 – 1681SubstrateUniRule annotation
Metal bindingi191 – 1911Magnesium; via carbamate groupUniRule annotation
Metal bindingi193 – 1931MagnesiumUniRule annotation
Metal bindingi194 – 1941MagnesiumUniRule annotation
Active sitei287 – 2871Proton acceptorUniRule annotation
Binding sitei288 – 2881SubstrateUniRule annotation
Binding sitei321 – 3211SubstrateUniRule annotation
Sitei329 – 3291Transition state stabilizerUniRule annotation
Binding sitei368 – 3681SubstrateUniRule annotation

GO - Molecular functioni

  1. magnesium ion binding Source: UniProtKB-HAMAP
  2. monooxygenase activity Source: UniProtKB-KW
  3. ribulose-bisphosphate carboxylase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. reductive pentose-phosphate cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

LyaseUniRule annotationImported, MonooxygenaseUniRule annotation, Oxidoreductase

Keywords - Biological processi

Calvin cycleUniRule annotation, Carbon dioxide fixationUniRule annotation, PhotosynthesisUniRule annotation

Keywords - Ligandi

MagnesiumUniRule annotation, Metal-bindingUniRule annotation

Enzyme and pathway databases

BioCyciRSPH349102:GHE1-213-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylaseUniRule annotation (EC:4.1.1.39UniRule annotation)
Short name:
RuBisCOUniRule annotation
Gene namesi
Name:cbbMUniRule annotation
Ordered Locus Names:Rsph17025_4020Imported
Encoded oniPlasmid pRSPA02Imported
OrganismiRhodobacter sphaeroides (strain ATCC 17025 / ATH 2.4.3)Imported
Taxonomic identifieri349102 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter
ProteomesiUP000000234 Componenti: Plasmid pRSPA02

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei191 – 1911N6-carboxylysineUniRule annotation

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi349102.Rsph17025_4020.

Structurei

3D structure databases

ProteinModelPortaliA4WZQ9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the RuBisCO large chain family. Type II subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
KOiK01601.
OMAiNQYLHYH.
OrthoDBiEOG66QKT8.

Family and domain databases

Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPiMF_01339. RuBisCO_L_type2.
InterProiIPR020871. RuBisCO.
IPR020878. RuBisCo_large_chain_AS.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[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.

A4WZQ9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDQSNRYARL DLKEADLIAG GRHVLCAYVM KPKAGYGYLE TAAHFAAESS
60 70 80 90 100
TGTNVEVSTT DDFTRGVDAL VYEIDEAREL MKIAYPVELF DRNIIDGRAM
110 120 130 140 150
LCSFLTLTIG NNQGMGDVEY AKMHDFYVPP CYLRLFDGPS MNIADMWRVL
160 170 180 190 200
GRSVTDGGMV VGTIIKPKLG LRPKPFADAC YEFWLGGDFI KNDEPQGNQT
210 220 230 240 250
FAPLKETIRL VADAMKRAQD ETGEAKLFSA NITADDHYEM VARGEYILET
260 270 280 290 300
FGENADHVAF LVDGYVTGPA AITTARRQFP RQFLHYHRAG HGAVTSPQSM
310 320 330 340 350
RGYTAFVLSK MARLQGASGI HTGTMGFGKM EGEAADRIMA FMLTDDAAQG
360 370 380 390 400
PFYPQDWLGM KATTPIISGG MNALRLPGFF DNLGHSNVIQ TSGGGAFGHL
410 420 430 440 450
DGGTAGAKSL RQAHDAWKAG VDLVTYAREH RELARAFESF PADADRFHPG
460
WREKLQLAGA A
Length:461
Mass (Da):50,518
Last modified:May 29, 2007 - v1
Checksum:iE8F7E84A0EA6A01D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000663 Genomic DNA. Translation: ABP72873.1.
RefSeqiWP_011911067.1. NC_009430.1.
YP_001170178.1. NC_009430.1.

Genome annotation databases

EnsemblBacteriaiABP72873; ABP72873; Rsph17025_4020.
GeneIDi5086194.
KEGGirsq:Rsph17025_4020.
PATRICi23166560. VBIRhoSph94549_4162.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000663 Genomic DNA. Translation: ABP72873.1.
RefSeqiWP_011911067.1. NC_009430.1.
YP_001170178.1. NC_009430.1.

3D structure databases

ProteinModelPortaliA4WZQ9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi349102.Rsph17025_4020.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABP72873; ABP72873; Rsph17025_4020.
GeneIDi5086194.
KEGGirsq:Rsph17025_4020.
PATRICi23166560. VBIRhoSph94549_4162.

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
KOiK01601.
OMAiNQYLHYH.
OrthoDBiEOG66QKT8.

Enzyme and pathway databases

BioCyciRSPH349102:GHE1-213-MONOMER.

Family and domain databases

Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPiMF_01339. RuBisCO_L_type2.
InterProiIPR020871. RuBisCO.
IPR020878. RuBisCo_large_chain_AS.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[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...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 17025Imported.

Entry informationi

Entry nameiA4WZQ9_RHOS5
AccessioniPrimary (citable) accession number: A4WZQ9
Entry historyi
Integrated into UniProtKB/TrEMBL: May 29, 2007
Last sequence update: May 29, 2007
Last modified: April 1, 2015
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

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.UniRule annotation

Keywords - Technical termi

Complete proteomeImported, PlasmidImported

External Data

Dasty 3

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 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.