Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

A2SJJ7 (RBL1B_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 2

Short name=RuBisCO large subunit 2
EC=4.1.1.39
Gene names
Name:cbbL2
Ordered Locus Names:Mpe_A2782
OrganismMethylibium petroleiphilum (strain PM1) [Complete proteome] [HAMAP]
Taxonomic identifier420662 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesMethylibium

Protein attributes

Sequence length485 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 caution

The sequence ABM95736.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 485485Ribulose bisphosphate carboxylase large chain 2 HAMAP-Rule MF_01338
PRO_0000299965

Sites

Active site1771Proton acceptor By similarity
Active site2951Proton acceptor By similarity
Metal binding2031Magnesium; via carbamate group By similarity
Metal binding2051Magnesium By similarity
Metal binding2061Magnesium By similarity
Binding site1251Substrate; in homodimeric partner By similarity
Binding site1751Substrate By similarity
Binding site1791Substrate By similarity
Binding site2961Substrate By similarity
Binding site3281Substrate By similarity
Binding site3801Substrate By similarity
Site3351Transition state stabilizer By similarity

Amino acid modifications

Modified residue2031N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A2SJJ7 [UniParc].

Last modified September 11, 2007. Version 2.
Checksum: 3B36C71F79F2FCAD

FASTA48553,310
        10         20         30         40         50         60 
MNEPTQITDT KKRYAAGVLK YAQMGYWNGD YVPKDTDILA LFRITPQDGV DPIEAAAAVA 

        70         80         90        100        110        120 
GESSTATWTV VWTDRLTACD MYRAKAYKVE PVPNNPGQYF CYVAYDLSLF EEGSIANVTA 

       130        140        150        160        170        180 
SIIGNVFSFK PLKAARLEDM KFPVSYVKTF AGPPTGIVVE RERLDKFGRP LLGATTKPKL 

       190        200        210        220        230        240 
GLSGRNYGRV VYEGLKGGLD FMKDDENINS QPFMHWRDRF LFVMDAVNKA SAATGEVKGS 

       250        260        270        280        290        300 
YLNVTAGTME EMYRRAEFAK ELGSVIIMID LVVGYTAIQS MSNWARQNDM VLHMHRAGHG 

       310        320        330        340        350        360 
TYTRQKNHGV SFRVIAKWLR MAGVDHLHTG TAVGKLEGDP LTVQGYYNVC RDTHTKVDLP 

       370        380        390        400        410        420 
RGIFFDQDWG ALKKVMPVAS GGIHAGQMHQ LIDLFGDDVV LQFGGGTIGH PQGIQAGATA 

       430        440        450        460        470        480 
NRVALEAMVL ARNEGRDIKN EGPQILRDAA KSCTPLAAAL DTWGDITFNY TSTDTSDYVP 


TPSVA 

« 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: ABM95736.1. Different initiation.
RefSeqYP_001021971.1. NC_008825.1.

3D structure databases

ProteinModelPortalA2SJJ7.
SMRA2SJJ7. Positions 23-466.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING420662.Mpe_A2782.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM95736; ABM95736; Mpe_A2782.
GeneID4785032.
KEGGmpt:Mpe_A2782.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1850.
HOGENOMHOG000230831.
KOK01601.
OrthoDBEOG6ZKXMS.

Enzyme and pathway databases

BioCycMPET420662:GHBE-2816-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 nameRBL1B_METPP
AccessionPrimary (citable) accession number: A2SJJ7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: September 11, 2007
Last modified: May 14, 2014
This is version 47 of the entry and version 2 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