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F0IX26 (F0IX26_ACIMA) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 20. Feed History...

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

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:cbbL HAMAP-Rule MF_01338 EMBL BAJ80436.1
Ordered Locus Names:ACMV_10890 EMBL BAJ80436.1
OrganismAcidiphilium multivorum (strain DSM 11245 / JCM 8867 / AIU301) [Complete proteome] [HAMAP] EMBL BAJ80436.1
Taxonomic identifier926570 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeAcidiphilium

Protein attributes

Sequence length493 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 site1841Proton acceptor By similarity HAMAP-Rule MF_01338
Active site3021Proton acceptor By similarity HAMAP-Rule MF_01338
Metal binding2101Magnesium; via carbamate group By similarity HAMAP-Rule MF_01338
Metal binding2121Magnesium By similarity HAMAP-Rule MF_01338
Metal binding2131Magnesium By similarity HAMAP-Rule MF_01338
Binding site1321Substrate; in homodimeric partner By similarity HAMAP-Rule MF_01338
Binding site1821Substrate By similarity HAMAP-Rule MF_01338
Binding site1861Substrate By similarity HAMAP-Rule MF_01338
Binding site3031Substrate By similarity HAMAP-Rule MF_01338
Binding site3351Substrate By similarity HAMAP-Rule MF_01338
Binding site3871Substrate By similarity HAMAP-Rule MF_01338
Site3421Transition state stabilizer By similarity HAMAP-Rule MF_01338

Amino acid modifications

Modified residue2101N6-carboxylysine By similarity HAMAP-Rule MF_01338

Sequences

Sequence LengthMass (Da)Tools
F0IX26 [UniParc].

Last modified May 3, 2011. Version 1.
Checksum: F3AEA66096D65998

FASTA49354,783
        10         20         30         40         50         60 
MDTPTPNITN EALTVRGKER YRSGVLEYRK MGYWEPDYEP KITDVISLFR ITPQDGVDPV 

        70         80         90        100        110        120 
EAAAAVAGES STATWTVVWT DRLTACEKYR AKAYRVDPVP NAPGQYFAYI AYDLALFEPG 

       130        140        150        160        170        180 
SIANLTASII GNVFGFKPLK ALRLEDMRLP VAYVKTFDGP ATGIVVERER LDKFGRPLLG 

       190        200        210        220        230        240 
ATVKPKLGLS GRNYGRVVYE ALKGGLDFTK DDENINSQPF MHWRDRFLYC MEAVNKAQAA 

       250        260        270        280        290        300 
TGEVKGTYLN VTAGTMEDMY ERASFAHELG STIIMIDLVI GYTAIQSMSK WARKHDMILH 

       310        320        330        340        350        360 
LHRAGHGTYT RHKTHGVSFR VISKWMRLAG VDHIHAGTVV GKLEGDPLTT RGFYDILRED 

       370        380        390        400        410        420 
YNETRYEHGI FFDQDWAGTR KVMPVASGGI HAGQMHQLLH HLGEDVVLQF GGGTIGHPQG 

       430        440        450        460        470        480 
IAAGAMANRV ALEAMILARN EGRDYLAEGP QILNDAARHC LPLRQALDTW GEVTFNYAST 

       490 
DTPDFAPTAM PAY 

« Hide

References

[1]"Whole genome sequence of Acidiphilium multivorum AIU301."
Narita-Yamada S., Nakamura S., Ito N., Takarada H., Katano Y., Nakazawa H., Hosoyama A., Yamada R., Fujita N.
Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 11245 / JCM 8867 / AIU301.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP012035 Genomic DNA. Translation: BAJ80436.1.
RefSeqYP_004283318.1. NC_015186.1.

3D structure databases

ProteinModelPortalF0IX26.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAJ80436; BAJ80436; ACMV_10890.
GeneID10320528.
KEGGamv:ACMV_10890.
PATRIC46810953. VBIAciMul178205_1458.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01601.

Enzyme and pathway databases

BioCycAMUL926570:GI8V-1104-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 nameF0IX26_ACIMA
AccessionPrimary (citable) accession number: F0IX26
Entry history
Integrated into UniProtKB/TrEMBL: May 3, 2011
Last sequence update: May 3, 2011
Last modified: June 11, 2014
This is version 20 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)