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F2IXT6 (F2IXT6_POLGS) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 16. 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 large chain HAMAP-Rule MF_01338

Short name=RuBisCO large subunit HAMAP-Rule MF_01338
EC=4.1.1.39 HAMAP-Rule MF_01338
Gene names
Name:rbcL EMBL ADZ69417.1
Synonyms:cbbL HAMAP-Rule MF_01338
Ordered Locus Names:SL003B_0988 EMBL ADZ69417.1
OrganismPolymorphum gilvum (strain LMG 25793 / CGMCC 1.9160 / SL003B-26A1) [Complete proteome] [HAMAP] EMBL ADZ69417.1
Taxonomic identifier991905 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaPolymorphum

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. HAMAP-Rule MF_01338

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. HAMAP-Rule MF_01338

Sequence similarities

Belongs to the RuBisCO large chain family. Type I subfamily. HAMAP-Rule MF_01338

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site1771Proton acceptor By similarity HAMAP-Rule MF_01338
Active site2951Proton acceptor By similarity HAMAP-Rule MF_01338
Metal binding2031Magnesium; via carbamate group By similarity HAMAP-Rule MF_01338
Metal binding2051Magnesium By similarity HAMAP-Rule MF_01338
Metal binding2061Magnesium By similarity HAMAP-Rule MF_01338
Binding site1251Substrate; in homodimeric partner By similarity HAMAP-Rule MF_01338
Binding site1751Substrate By similarity HAMAP-Rule MF_01338
Binding site1791Substrate By similarity HAMAP-Rule MF_01338
Binding site2961Substrate By similarity HAMAP-Rule MF_01338
Binding site3281Substrate By similarity HAMAP-Rule MF_01338
Binding site3801Substrate By similarity HAMAP-Rule MF_01338
Site3351Transition state stabilizer By similarity HAMAP-Rule MF_01338

Amino acid modifications

Modified residue2031N6-carboxylysine By similarity HAMAP-Rule MF_01338

Sequences

Sequence LengthMass (Da)Tools
F2IXT6 [UniParc].

Last modified May 31, 2011. Version 1.
Checksum: 192F2CD7DC6C2F56

FASTA48553,685
        10         20         30         40         50         60 
MDAKMKEIKG KERYKAGVLK YAQMGYWDGD YEPKDTDVIA LFRITPQDGV DPIEAAAAVA 

        70         80         90        100        110        120 
GESSTATWTV VWTDRLTACD SYRAKAYRVD PVPGTPGQYF CYVAYDLILF EEGSIANLTA 

       130        140        150        160        170        180 
SIIGNVFSFK PLKAARLEDM RFPVAYVKTY KGPPTGIVVE RERLDKFGKP LLGATTKPKL 

       190        200        210        220        230        240 
GLSGKNYGRV VYEGLKGGLD FMKDDENINS QPFMHWRDRF LYCMEAVNKA SAETGEVKGH 

       250        260        270        280        290        300 
YLNITAGTME EMYRRAELAK ELGSVIVMVD LIIGWTAIQS ISEWCRQNDM ILHMHRAGHG 

       310        320        330        340        350        360 
TYTRQKNHGI SFRVIAKWLR LAGVDHLHCG TAVGKLEGDP LTVQGYYNVC RETRNAVDLP 

       370        380        390        400        410        420 
RGIFFEQDWA DLRKVMPVAS GGIHAGQMHQ LLDLFGDDVV LQFGGGTIGH PMGIQAGATA 

       430        440        450        460        470        480 
NRVALEAMVL ARNEGRDIVN EGPEILRAAA KWCKPLEAAL DTWGSITFNY TSTDTSDFVP 


TPAVA 

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References

[1]"Complete genome sequence of Polymorphum gilvum SL003B-26A1T, a crude oil-degrading bacterium from oil-polluted saline soil."
Li S.G., Tang Y.Q., Nie Y., Cai M., Wu X.L.
J. Bacteriol. 193:2894-2895(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LMG 25793 / CGMCC 1.9160 / SL003B-26A1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002568 Genomic DNA. Translation: ADZ69417.1.
RefSeqYP_004302717.1. NC_015259.1.

3D structure databases

ProteinModelPortalF2IXT6.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADZ69417; ADZ69417; SL003B_0988.
GeneID10418326.
KEGGpgv:SL003B_0988.
PATRIC47179816. VBIPolGil182274_1003.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01601.
OMAHRAMHAA.

Enzyme and pathway databases

BioCycPGIL991905:GJ0L-1006-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 nameF2IXT6_POLGS
AccessionPrimary (citable) accession number: F2IXT6
Entry history
Integrated into UniProtKB/TrEMBL: May 31, 2011
Last sequence update: May 31, 2011
Last modified: February 19, 2014
This is version 16 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)