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D9SHP6 (D9SHP6_GALCS) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 18. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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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:Galf_0034
OrganismGallionella capsiferriformans (strain ES-2) (Gallionella ferruginea capsiferriformans (strain ES-2)) [Complete proteome] [HAMAP] EMBL ADL54079.1
Taxonomic identifier395494 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Gallionellales › Gallionellaceae › Gallionella ›

Protein attributes

Sequence length470 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 site1751Proton acceptor By similarity HAMAP-Rule MF_01339
Active site2981Proton acceptor By similarity HAMAP-Rule MF_01339
Metal binding2001Magnesium; via carbamate group By similarity HAMAP-Rule MF_01339
Metal binding2021Magnesium By similarity HAMAP-Rule MF_01339
Metal binding2031Magnesium By similarity HAMAP-Rule MF_01339
Binding site1201Substrate; in homodimeric partner By similarity HAMAP-Rule MF_01339
Binding site1771Substrate By similarity HAMAP-Rule MF_01339
Binding site2991Substrate By similarity HAMAP-Rule MF_01339
Binding site3321Substrate By similarity HAMAP-Rule MF_01339
Binding site3791Substrate By similarity HAMAP-Rule MF_01339
Site3401Transition state stabilizer By similarity HAMAP-Rule MF_01339

Amino acid modifications

Modified residue2001N6-carboxylysine By similarity HAMAP-Rule MF_01339

Sequences

Sequence LengthMass (Da)Tools
D9SHP6 [UniParc].

Last modified October 5, 2010. Version 1.
Checksum: 6CC37D30B388FDB6

FASTA47051,698
        10         20         30         40         50         60 
MDQSNRYANL NLKEEDLIKN GKHLLVAYKL IPAKGHGFLE VAAHVAAESS TGTNVEVSTT 

        70         80         90        100        110        120 
DDFTRGVDAL VYEIDETAFG DDIVKGGGLF KVAYPVELFD PNLTDGTYNI SHMWSLILGN 

       130        140        150        160        170        180 
NQGMGDHQGL RMLDFLVPEM MVRKFDGPSA NISNLWKVLG RSETDGGYIA GTIIKPKLGL 

       190        200        210        220        230        240 
RPEPFAKACY DFWLGGDFIK NDEPQANQPF CPMEVVMPKV AEAMDRAQQE TGQAKLFSAN 

       250        260        270        280        290        300 
ITADYYKEMI HRGDFVLETF AKYNSASHVA FLVDGFVTGP AGVTTCRREF PDTFLHFHRA 

       310        320        330        340        350        360 
GHGAVTSYKS PMGMDPLCYM KLVRLMGASG MHTGTMGYGK MEGHGKETVL AYMLERDECQ 

       370        380        390        400        410        420 
GPYFYQKWYG MKATTPIISG GMNALRLPGF FQNLGHGNVI NTCGGGAFGH IDSPAAGGIS 

       430        440        450        460        470 
LGQAYDCWKS GSDPIEYAKT HKEFARAFES FPKDGDKLFA GWREKLGVHK

« Hide

References

[1]"Complete sequence of Gallionella capsiferriformans ES-2."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., Pitluck S., Chertkov O., Davenport K.W., Detter J.C., Han C., Tapia R., Land M., Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N. expand/collapse author list , Mikhailova N., Shelobolina E.S., Picardal F., Roden E., Emerson D., Woyke T.
Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ES-2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP002159 Genomic DNA. Translation: ADL54079.1.
RefSeqYP_003845843.1. NC_014394.1.

3D structure databases

ProteinModelPortalD9SHP6.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADL54079; ADL54079; Galf_0034.
GeneID9611344.
KEGGgca:Galf_0034.
PATRIC42336609. VBIGalCap53152_0036.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000230831.
KOK01601.

Enzyme and pathway databases

BioCycGCAP395494:GHXI-34-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 nameD9SHP6_GALCS
AccessionPrimary (citable) accession number: D9SHP6
Entry history
Integrated into UniProtKB/TrEMBL: October 5, 2010
Last sequence update: October 5, 2010
Last modified: May 1, 2013
This is version 18 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info