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A4WZQ9 (A4WZQ9_RHOS5) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Ribulose bisphosphate carboxylase HAMAP-Rule MF_01339

Short name=RuBisCO HAMAP-Rule MF_01339
EC=4.1.1.39 HAMAP-Rule MF_01339
Gene names
Name:cbbM HAMAP-Rule MF_01339
Ordered Locus Names:Rsph17025_4020 EMBL ABP72873.1
Encoded onPlasmid pRSPA02 Ref.1 EMBL ABP72873.1
OrganismRhodobacter sphaeroides (strain ATCC 17025 / ATH 2.4.3) [Complete proteome] [HAMAP] EMBL ABP72873.1
Taxonomic identifier349102 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter

Protein attributes

Sequence length461 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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. HAMAP-Rule MF_01339

Catalytic activity

2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O. HAMAP-Rule MF_01339

3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2. HAMAP-Rule MF_01339

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP-Rule MF_01339

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01339

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. HAMAP-Rule MF_01339

Sequence similarities

Belongs to the RuBisCO large chain family. Type II subfamily. HAMAP-Rule MF_01339

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site1661Proton acceptor By similarity HAMAP-Rule MF_01339
Active site2871Proton acceptor By similarity HAMAP-Rule MF_01339
Metal binding1911Magnesium; via carbamate group By similarity HAMAP-Rule MF_01339
Metal binding1931Magnesium By similarity HAMAP-Rule MF_01339
Metal binding1941Magnesium By similarity HAMAP-Rule MF_01339
Binding site1111Substrate; in homodimeric partner By similarity HAMAP-Rule MF_01339
Binding site1681Substrate By similarity HAMAP-Rule MF_01339
Binding site2881Substrate By similarity HAMAP-Rule MF_01339
Binding site3211Substrate By similarity HAMAP-Rule MF_01339
Binding site3681Substrate By similarity HAMAP-Rule MF_01339
Site3291Transition state stabilizer By similarity HAMAP-Rule MF_01339

Amino acid modifications

Modified residue1911N6-carboxylysine By similarity HAMAP-Rule MF_01339

Sequences

Sequence LengthMass (Da)Tools
A4WZQ9 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: E8F7E84A0EA6A01D

FASTA46150,518
        10         20         30         40         50         60 
MDQSNRYARL DLKEADLIAG GRHVLCAYVM KPKAGYGYLE TAAHFAAESS TGTNVEVSTT 

        70         80         90        100        110        120 
DDFTRGVDAL VYEIDEAREL MKIAYPVELF DRNIIDGRAM LCSFLTLTIG NNQGMGDVEY 

       130        140        150        160        170        180 
AKMHDFYVPP CYLRLFDGPS MNIADMWRVL GRSVTDGGMV VGTIIKPKLG LRPKPFADAC 

       190        200        210        220        230        240 
YEFWLGGDFI KNDEPQGNQT FAPLKETIRL VADAMKRAQD ETGEAKLFSA NITADDHYEM 

       250        260        270        280        290        300 
VARGEYILET FGENADHVAF LVDGYVTGPA AITTARRQFP RQFLHYHRAG HGAVTSPQSM 

       310        320        330        340        350        360 
RGYTAFVLSK MARLQGASGI HTGTMGFGKM EGEAADRIMA FMLTDDAAQG PFYPQDWLGM 

       370        380        390        400        410        420 
KATTPIISGG MNALRLPGFF DNLGHSNVIQ TSGGGAFGHL DGGTAGAKSL RQAHDAWKAG 

       430        440        450        460 
VDLVTYAREH RELARAFESF PADADRFHPG WREKLQLAGA A 

« Hide

References

[1]"Complete sequence of plasmid pRSPA02 of Rhodobacter sphaeroides ATCC 17025."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Richardson P., Mackenzie C., Choudhary M., Donohue T.J., Kaplan S.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17025 / ATH 2.4.3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000663 Genomic DNA. Translation: ABP72873.1.
RefSeqYP_001170178.1. NC_009430.1.

3D structure databases

ProteinModelPortalA4WZQ9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING349102.Rsph17025_4020.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABP72873; ABP72873; Rsph17025_4020.
GeneID5086194.
KEGGrsq:Rsph17025_4020.
PATRIC23166560. VBIRhoSph94549_4162.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1850.
HOGENOMHOG000230831.
KOK01601.
OMANQYLHYH.
OrthoDBEOG66QKT8.
ProtClustDBPRK13475.

Enzyme and pathway databases

BioCycRSPH349102:GHE1-213-MONOMER.

Family and domain databases

Gene3D3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPMF_01339. RuBisCO_L_type2.
InterProIPR020871. RuBisCO.
IPR020878. RuBisCo_large_chain_AS.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[Graphical view]
PfamPF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view]
SUPFAMSSF51649. SSF51649. 1 hit.
SSF54966. SSF54966. 1 hit.
PROSITEPS00157. RUBISCO_LARGE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameA4WZQ9_RHOS5
AccessionPrimary (citable) accession number: A4WZQ9
Entry history
Integrated into UniProtKB/TrEMBL: May 29, 2007
Last sequence update: May 29, 2007
Last modified: February 19, 2014
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)