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D5WV36 (D5WV36_BACT2) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 18. 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
Ordered Locus Names:Btus_2871
OrganismBacillus tusciae (strain DSM 2912 / NBRC 15312 / T2) [Complete proteome] [HAMAP] EMBL ADG07508.1
Taxonomic identifier562970 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Alicyclobacillaceae › Kyrpidia ›

Protein attributes

Sequence length478 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 site1711Proton acceptor By similarity HAMAP-Rule MF_01338
Active site2891Proton acceptor By similarity HAMAP-Rule MF_01338
Metal binding1971Magnesium; via carbamate group By similarity HAMAP-Rule MF_01338
Metal binding1991Magnesium By similarity HAMAP-Rule MF_01338
Metal binding2001Magnesium By similarity HAMAP-Rule MF_01338
Binding site1191Substrate; in homodimeric partner By similarity HAMAP-Rule MF_01338
Binding site1691Substrate By similarity HAMAP-Rule MF_01338
Binding site1731Substrate By similarity HAMAP-Rule MF_01338
Binding site2901Substrate By similarity HAMAP-Rule MF_01338
Binding site3221Substrate By similarity HAMAP-Rule MF_01338
Binding site3741Substrate By similarity HAMAP-Rule MF_01338
Site3291Transition state stabilizer By similarity HAMAP-Rule MF_01338

Amino acid modifications

Modified residue1971N6-carboxylysine By similarity HAMAP-Rule MF_01338

Sequences

Sequence LengthMass (Da)Tools
D5WV36 [UniParc].

Last modified July 13, 2010. Version 1.
Checksum: 7FA37074DA659678

FASTA47853,224
        10         20         30         40         50         60 
MEQDVKKRWA SGVIPYKEMG YWQPDYEVKD TDVIAAFRVV PQEGIDPEEA AAAVAGESST 

        70         80         90        100        110        120 
ATWTVVWTDR LTTYEHYQGK AFRVDPVPGT DQYIAYIAYD IDLFEEGSIA NLASSIIGNV 

       130        140        150        160        170        180 
FGFKALKSLR LEDMRIPLHY VKTFQGPAHG IVMEREMLNK YGRPLLGATT KPKLGLSARN 

       190        200        210        220        230        240 
YGRVVYEALR GGLDFVKDDE NINSQPFMRW RDRFLYAMEA VHRAMAETGE IKGHYLNVTG 

       250        260        270        280        290        300 
ATMEDIYERA EFAKELGSVI VMIDLTVGYS AIQSLAKWAR RNSVLLHLHR AGHSTFTRQK 

       310        320        330        340        350        360 
THGVSFRVIA KWMRLAGVDH LHAGTVVGKL EGDPNITKGY YQTLRGMKYD ADPRLGLLFE 

       370        380        390        400        410        420 
QDWGSMPAVM PVASGGIHAG QVHQLIDLFG EDVIFQFGGG TIGHPMGIAA GATANRVAIE 

       430        440        450        460        470 
AMIQARNEGR DILREGPEIL EKAAKWSPEL RAALEVWKDV TFNYASTDTP DVVATPTF

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP002017 Genomic DNA. Translation: ADG07508.1.
RefSeqYP_003590652.1. NC_014098.1.

3D structure databases

ProteinModelPortalD5WV36.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADG07508; ADG07508; Btus_2871.
GeneID9110849.
KEGGbts:Btus_2871.
PATRIC37248986. VBIBacTus29608_2993.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000230831.
KOK01601.

Enzyme and pathway databases

BioCycKTUS562970:GHUX-2942-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. RuBisCO_large. 1 hit.
SSF54966. RuBisCO_large. 1 hit.
PROSITEPS00157. RUBISCO_LARGE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameD5WV36_BACT2
AccessionPrimary (citable) accession number: D5WV36
Entry history
Integrated into UniProtKB/TrEMBL: July 13, 2010
Last sequence update: July 13, 2010
Last modified: May 1, 2013
This is version 18 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info