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A4WZQ9

- A4WZQ9_RHOS5

UniProt

A4WZQ9 - A4WZQ9_RHOS5

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Protein
Ribulose bisphosphate carboxylase
Gene
cbbM, Rsph17025_4020
Organism
Rhodobacter sphaeroides (strain ATCC 17025 / ATH 2.4.3)
Status
Unreviewed - 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 By similarity.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

Binds 1 magnesium ion per subunit By similarity.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei111 – 1111Substrate; in homodimeric partner By similarityUniRule annotation
Active sitei166 – 1661Proton acceptor By similarityUniRule annotation
Binding sitei168 – 1681Substrate By similarityUniRule annotation
Metal bindingi191 – 1911Magnesium; via carbamate group By similarityUniRule annotation
Metal bindingi193 – 1931Magnesium By similarityUniRule annotation
Metal bindingi194 – 1941Magnesium By similarityUniRule annotation
Active sitei287 – 2871Proton acceptor By similarityUniRule annotation
Binding sitei288 – 2881Substrate By similarityUniRule annotation
Binding sitei321 – 3211Substrate By similarityUniRule annotation
Sitei329 – 3291Transition state stabilizer By similarityUniRule annotation
Binding sitei368 – 3681Substrate By similarityUniRule 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: Plasmid pRSPA02

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei191 – 1911N6-carboxylysine By similarityUniRule annotation

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi349102.Rsph17025_4020.

Structurei

3D structure databases

ProteinModelPortaliA4WZQ9.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
KOiK01601.
OMAiAKEHREF.
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

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MDQSNRYARL DLKEADLIAG GRHVLCAYVM KPKAGYGYLE TAAHFAAESS    50
TGTNVEVSTT DDFTRGVDAL VYEIDEAREL MKIAYPVELF DRNIIDGRAM 100
LCSFLTLTIG NNQGMGDVEY AKMHDFYVPP CYLRLFDGPS MNIADMWRVL 150
GRSVTDGGMV VGTIIKPKLG LRPKPFADAC YEFWLGGDFI KNDEPQGNQT 200
FAPLKETIRL VADAMKRAQD ETGEAKLFSA NITADDHYEM VARGEYILET 250
FGENADHVAF LVDGYVTGPA AITTARRQFP RQFLHYHRAG HGAVTSPQSM 300
RGYTAFVLSK MARLQGASGI HTGTMGFGKM EGEAADRIMA FMLTDDAAQG 350
PFYPQDWLGM KATTPIISGG MNALRLPGFF DNLGHSNVIQ TSGGGAFGHL 400
DGGTAGAKSL RQAHDAWKAG VDLVTYAREH RELARAFESF PADADRFHPG 450
WREKLQLAGA A 461
Length:461
Mass (Da):50,518
Last modified:May 29, 2007 - v1
Checksum:iE8F7E84A0EA6A01D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000663 Genomic DNA. Translation: ABP72873.1.
RefSeqiYP_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:
EMBL
GenBank
DDBJ
Links Updated
CP000663 Genomic DNA. Translation: ABP72873.1 .
RefSeqi YP_001170178.1. NC_009430.1.

3D structure databases

ProteinModelPortali A4WZQ9.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 349102.Rsph17025_4020.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABP72873 ; ABP72873 ; Rsph17025_4020 .
GeneIDi 5086194.
KEGGi rsq:Rsph17025_4020.
PATRICi 23166560. VBIRhoSph94549_4162.

Phylogenomic databases

eggNOGi COG1850.
HOGENOMi HOG000230831.
KOi K01601.
OMAi AKEHREF.
OrthoDBi EOG66QKT8.

Enzyme and pathway databases

BioCyci RSPH349102:GHE1-213-MONOMER.

Family and domain databases

Gene3Di 3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPi MF_01339. RuBisCO_L_type2.
InterProi IPR020871. RuBisCO.
IPR020878. RuBisCo_large_chain_AS.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[Graphical view ]
Pfami PF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view ]
SUPFAMi SSF51649. SSF51649. 1 hit.
SSF54966. SSF54966. 1 hit.
PROSITEi PS00157. RUBISCO_LARGE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 17025 / ATH 2.4.3.
    Plasmid: pRSPA02

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: June 11, 2014
This is version 46 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 By similarity.UniRule annotation

Keywords - Technical termi

Complete proteome, PlasmidImported

External Data

Dasty 3

Similar proteinsi