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A2SFV1 (RBL1A_METPP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribulose bisphosphate carboxylase large chain 1

Short name=RuBisCO large subunit 1
EC=4.1.1.39
Gene names
Name:cbbL1
Ordered Locus Names:Mpe_A1478
OrganismMethylibium petroleiphilum (strain PM1) [Complete proteome] [HAMAP]
Taxonomic identifier420662 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesMethylibium

Protein attributes

Sequence length488 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_01338

Catalytic activity

2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O. HAMAP-Rule MF_01338

3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2. HAMAP-Rule MF_01338

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP-Rule MF_01338

Subunit structure

Heterohexadecamer of 8 large chains and 8 small chains By similarity.

Miscellaneous

The basic functional RuBisCO is composed of a large chain homodimer in a "head-to-tail" conformation. In form I RuBisCO this homodimer is arranged in a barrel-like tetramer with the small subunits forming a tetrameric "cap" on each end of the "barrel" By similarity.

Sequence similarities

Belongs to the RuBisCO large chain family. Type I subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 488488Ribulose bisphosphate carboxylase large chain 1 HAMAP-Rule MF_01338
PRO_0000299964

Sites

Active site1801Proton acceptor By similarity
Active site2981Proton acceptor By similarity
Metal binding2061Magnesium; via carbamate group By similarity
Metal binding2081Magnesium By similarity
Metal binding2091Magnesium By similarity
Binding site1281Substrate; in homodimeric partner By similarity
Binding site1781Substrate By similarity
Binding site1821Substrate By similarity
Binding site2991Substrate By similarity
Binding site3311Substrate By similarity
Binding site3831Substrate By similarity
Site3381Transition state stabilizer By similarity

Amino acid modifications

Modified residue2061N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A2SFV1 [UniParc].

Last modified March 6, 2007. Version 1.
Checksum: D6FE45BF3D28E476

FASTA48853,929
        10         20         30         40         50         60 
MNKPMEDAAI TDVKKRYSAG VLKYRQMGYW MPDYVPKDTD TICLFRITPQ DGVDPVEAAA 

        70         80         90        100        110        120 
AVAGESSTAT WTVVWTDRLT ACDSYRAKAY KVEPVPGIPG QFFAWVAYDI ILFEEGSIAN 

       130        140        150        160        170        180 
MTASLIGNVF SFKPLKAARL EDIRIPVAYV KTFKGPPTGL VVERERLDKF GRPLLGATTK 

       190        200        210        220        230        240 
PKLGLSGRNY GRVVYEGLKG GLDFMKDDEN INSQPFMHWR DRYLYVMDAV NKASAATGEI 

       250        260        270        280        290        300 
KGSYLNVTAA TMEDMYERAE FAKELGSVIV MIDLVIGYTA IQSMSNWARR NDVILHLHRA 

       310        320        330        340        350        360 
GHGTYTRQKN HGVSFRVIAK WMRLAGVDHI HTGTAVGKLE GDPMTVQGYY NVCRDSVTKQ 

       370        380        390        400        410        420 
DLPRGLFFDQ DWADLKKVMP VASGGIHAGQ MHQLIDLFGD DVVLQFGGGT IGHPQGIQAG 

       430        440        450        460        470        480 
AVANRVALEC MVKARNEGRD IKNEGPEILR KAAQFCAPLK QALDTWGEIS FNYTPTDTSD 


YAVTPGVA 

« Hide

References

[1]"Whole-genome analysis of the methyl tert-butyl ether-degrading beta-proteobacterium Methylibium petroleiphilum PM1."
Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W., Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M., Hristova K.R.
J. Bacteriol. 189:1931-1945(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PM1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000555 Genomic DNA. Translation: ABM94440.1.
RefSeqYP_001020675.1. NC_008825.1.

3D structure databases

ProteinModelPortalA2SFV1.
SMRA2SFV1. Positions 26-469.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING420662.Mpe_A1478.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM94440; ABM94440; Mpe_A1478.
GeneID4784076.
KEGGmpt:Mpe_A1478.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1850.
HOGENOMHOG000230831.
KOK01601.
OMALDYYLEC.
OrthoDBEOG6ZKXMS.

Enzyme and pathway databases

BioCycMPET420662:GHBE-1499-MONOMER.

Family and domain databases

Gene3D3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPMF_01338. RuBisCO_L_type1.
InterProIPR020878. RuBisCo_large_chain_AS.
IPR020888. RuBisCO_lsu.
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 nameRBL1A_METPP
AccessionPrimary (citable) accession number: A2SFV1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: March 6, 2007
Last modified: May 14, 2014
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families