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P72383 (P72383_9FIRM) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 63. 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:cbbL HAMAP-Rule MF_01338
OrganismSulfobacillus acidophilus EMBL AAB17673.2
Taxonomic identifier53633 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Clostridiales › Clostridiales Family XVII. Incertae Sedis › Sulfobacillus

Protein attributes

Sequence length479 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 site1721Proton acceptor By similarity HAMAP-Rule MF_01338
Active site2901Proton acceptor By similarity HAMAP-Rule MF_01338
Metal binding1981Magnesium; via carbamate group By similarity HAMAP-Rule MF_01338
Metal binding2001Magnesium By similarity HAMAP-Rule MF_01338
Metal binding2011Magnesium By similarity HAMAP-Rule MF_01338
Binding site1201Substrate; in homodimeric partner By similarity HAMAP-Rule MF_01338
Binding site1701Substrate By similarity HAMAP-Rule MF_01338
Binding site1741Substrate By similarity HAMAP-Rule MF_01338
Binding site2911Substrate By similarity HAMAP-Rule MF_01338
Binding site3231Substrate By similarity HAMAP-Rule MF_01338
Binding site3751Substrate By similarity HAMAP-Rule MF_01338
Site3301Transition state stabilizer By similarity HAMAP-Rule MF_01338

Amino acid modifications

Modified residue1981N6-carboxylysine By similarity HAMAP-Rule MF_01338

Sequences

Sequence LengthMass (Da)Tools
P72383 [UniParc].

Last modified February 6, 2007. Version 2.
Checksum: 57040D702FF247F7

FASTA47953,094
        10         20         30         40         50         60 
MTTEENKNRW AAGVTPYSKM GYWQPDYQPK DTDILCAFRF VPQEGVDPEE AAAAVAGESS 

        70         80         90        100        110        120 
TATWTVVWTD RLTAHEHYQA KAYRVVPVPG TDQYIAYIAY DLDLFEEGSI ANLTASIIGN 

       130        140        150        160        170        180 
VFGFKALKSL RLEDMRIPPH YVKTFQGPAH GIVMEREYLN KYGRPLLGAT VKPKLGLSAR 

       190        200        210        220        230        240 
NYARVVYEAL RGGLDFTKDD ENINSQPFMR WRDRYLFVME AVNKATADTG EIKGHYLNVT 

       250        260        270        280        290        300 
AATMEDIYER ADFAKQIGSP IIMIDLIVGY TAIQSIAKWA RKNGVLLHLH RAGHSTYTRQ 

       310        320        330        340        350        360 
KTHGVSFRVI AKWMRLAGVD HIHAGTVLGK LEGDPRTTAG YYQTLRGMKY DADPTIGLYF 

       370        380        390        400        410        420 
EQDWASLPGV MPVASGGIHA GQMHQLIDLL GEDVVLQFGG GTFGHPHGIA AGAAANRIAC 

       430        440        450        460        470 
EAIIQARNEG RDYVNEGPEI LAEAAKWSPA LRAALDTWKD VTFNFESTDT PDVLPTPSF

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References

[1]"Partial sequence of the Rubisco large chain of two acidophilic Gram positive, mineral sulphide-oxidising bacteria."
Clark D.A., Norris P.R.
Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: NAL EMBL AAB17673.2.
[2]Caldwell P.E., Norris P.R.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: NAL EMBL AAB17673.2.
[3]"Ribulose bisphosphate carboxylase activity and a Calvin cycle gene cluster in Sulfobacillus species."
Caldwell P.E., McLean M.R., Norris P.R.
Microbiology 153:2231-2240(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: NAL EMBL AAB17673.2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U75301 Genomic DNA. Translation: AAB17673.2.
RefSeqYP_005257991.1. NC_016884.1.

3D structure databases

ProteinModelPortalP72383.
SMRP72383. Positions 8-472.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID11859639.
KEGGsap:Sulac_2858.

Phylogenomic databases

KOK01601.

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. RuBisCO_large. 1 hit.
SSF54966. RuBisCO_large. 1 hit.
PROSITEPS00157. RUBISCO_LARGE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameP72383_9FIRM
AccessionPrimary (citable) accession number: P72383
Entry history
Integrated into UniProtKB/TrEMBL: February 1, 1997
Last sequence update: February 6, 2007
Last modified: May 1, 2013
This is version 63 of the entry and version 2 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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