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A1AWY1 (A1AWY1_RUTMC) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 44. 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:Rmag_0701 EMBL ABL02438.1
OrganismRuthia magnifica subsp. Calyptogena magnifica [Complete proteome] [HAMAP] EMBL ABL02438.1
Taxonomic identifier413404 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › sulfur-oxidizing symbionts ›

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
A1AWY1 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: 58A4E141FF56B3E6

FASTA46050,661
        10         20         30         40         50         60 
MDQSNRYADL LLDEETLIKE GNHFLVAYTM TPMPGFGGYL ETAAHFAAES STGTNVEVST 

        70         80         90        100        110        120 
TDDFTKDLDA MVYEIDEAKG TMKIAYPNNL FDRNLIDGRA MVVSLLTLII GNNQGMGDVQ 

       130        140        150        160        170        180 
CAQIQDFWIS RKFLEIFDGP SLDITDLWSI LGRSRTDGGY IAGTIIKPKL GLRPKPFSEA 

       190        200        210        220        230        240 
AYQFWLGGDF IKNDEPQGNQ VYARMKDVTP LVADAMRRAQ DETSEAKIFS ANITADDHHE 

       250        260        270        280        290        300 
MCARADYILE TFAENAHHVA FLVDGYVGGC GMITTARRNY PNQYLHYHRA GHGAITSPSS 

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

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

       430        440        450        460 
KADPIEFAKD HNEFARAFES FPNDADSLYP GWRDKLGIHK

« Hide

References

[1]"The Calyptogena magnifica chemoautotrophic symbiont genome."
Newton I.L., Woyke T., Auchtung T.A., Dilly G.F., Dutton R.J., Fisher M.C., Fontanez K.M., Lau E., Stewart F.J., Richardson P.M., Barry K.W., Saunders E., Detter J.C., Wu D., Eisen J.A., Cavanaugh C.M.
Science 315:998-1000(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Cm EMBL ABL02438.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000488 Genomic DNA. Translation: ABL02438.1.
RefSeqYP_903909.1. NC_008610.1.

3D structure databases

ProteinModelPortalA1AWY1.
SMRA1AWY1. Positions 2-458.
ModBaseSearch...

Protein-protein interaction databases

STRING413404.Rmag_0701.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABL02438; ABL02438; Rmag_0701.
GeneID4554715.
KEGGrma:Rmag_0701.
PATRIC32001125. VBICanRut45856_0775.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1850.
HOGENOMHOG000230831.
KOK01601.
OMANQYLHYH.
ProtClustDBPRK13475.

Enzyme and pathway databases

BioCycCRUT413404:GHM7-742-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 nameA1AWY1_RUTMC
AccessionPrimary (citable) accession number: A1AWY1
Entry history
Integrated into UniProtKB/TrEMBL: January 23, 2007
Last sequence update: January 23, 2007
Last modified: May 1, 2013
This is version 44 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