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A5CWB0 (A5CWB0_VESOH) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Protein attributes

Sequence length460 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 site1671Proton acceptor By similarity HAMAP-Rule MF_01339
Active site2881Proton acceptor By similarity HAMAP-Rule MF_01339
Metal binding1921Magnesium; via carbamate group By similarity HAMAP-Rule MF_01339
Metal binding1941Magnesium By similarity HAMAP-Rule MF_01339
Metal binding1951Magnesium By similarity HAMAP-Rule MF_01339
Binding site1121Substrate; in homodimeric partner By similarity HAMAP-Rule MF_01339
Binding site1691Substrate By similarity HAMAP-Rule MF_01339
Binding site2891Substrate By similarity HAMAP-Rule MF_01339
Binding site3221Substrate By similarity HAMAP-Rule MF_01339
Binding site3691Substrate By similarity HAMAP-Rule MF_01339
Site3301Transition state stabilizer By similarity HAMAP-Rule MF_01339

Amino acid modifications

Modified residue1921N6-carboxylysine By similarity HAMAP-Rule MF_01339

Sequences

Sequence LengthMass (Da)Tools
A5CWB0 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: ADFD0E4F9B87956D

FASTA46050,289
        10         20         30         40         50         60 
MDQSNRYADL SLDEDTLLAE GGHILVAYTM NIMPNFGGYL ETAAHFAAES STGTNVEVST 

        70         80         90        100        110        120 
TDDFTKDLDA MVYEIDEVKG IMKIAYPCGL FDRNLIDGRA MVVSFLTLAI GNNQGMGDVK 

       130        140        150        160        170        180 
CAQMIDFHVP KQMLDIFDGP SVDITDLWNL LGRDRKNGGY IAGTIIKPKL GLRPQPFAEA 

       190        200        210        220        230        240 
AYQFWLGGDF IKNDEPQGNQ VYARMKDVMP LVSDAMKRAQ DETGEAKIFS ANITADDYHE 

       250        260        270        280        290        300 
MIARGEYILE AFGENAHHVA FLVDGYVGGC GMVTTARRNF PGQYLHYHRA GHGAITSPSS 

       310        320        330        340        350        360 
VRGYTALVLA KLSRLMGASG IHVGTMGYGK MEGGADDRNI AYMIERDSAD GPVYHQEWFG 

       370        380        390        400        410        420 
MKPTTPIISG GMNALRLPGF FENLGHGNVI NTSGGGSYGH IDSPSAGAKS LRQAYDCWMA 

       430        440        450        460 
KADPIEFARD NNEFARAFES FPGDADSLYP GWRDKLGVHK

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References

[1]"Reduced genome of the thioautotrophic intracellular symbiont in a deep-sea clam, Calyptogena okutanii."
Kuwahara H., Yoshida T., Takaki Y., Shimamura S., Nishi S., Harada M., Matsuyama K., Takishita K., Kawato M., Uematsu K., Fujiwara Y., Sato T., Kato C., Kitagawa M., Kato I., Maruyama T.
Curr. Biol. 17:881-886(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HA.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AP009247 Genomic DNA. Translation: BAF61766.1.
RefSeqYP_001219490.1. NC_009465.1.

3D structure databases

ProteinModelPortalA5CWB0.
ModBaseSearch...

Protein-protein interaction databases

STRING412965.COSY_0653.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAF61766; BAF61766; COSY_0653.
GeneID5171911.
KEGGvok:COSY_0653.
PATRIC32021163. VBICanVes128383_0655.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1850.
HOGENOMHOG000230831.
KOK01601.
OMANQYLHYH.
ProtClustDBPRK13475.

Enzyme and pathway databases

BioCycCVES412965:GHZZ-630-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. RuBisCO_large. 1 hit.
SSF54966. RuBisCO_large. 1 hit.
PROSITEPS00157. RUBISCO_LARGE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameA5CWB0_VESOH
AccessionPrimary (citable) accession number: A5CWB0
Entry history
Integrated into UniProtKB/TrEMBL: June 12, 2007
Last sequence update: June 12, 2007
Last modified: May 1, 2013
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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