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C7M1Z0 (C7M1Z0_ACIFD) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 30. 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:Afer_0119
OrganismAcidimicrobium ferrooxidans (strain DSM 10331 / JCM 15462 / NBRC 103882 / ICP) [Complete proteome] [HAMAP]
Taxonomic identifier525909 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Acidimicrobidae › Acidimicrobiales › Acidimicrobineae › Acidimicrobiaceae › Acidimicrobium ›

Protein attributes

Sequence length473 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 site1681Proton acceptor By similarity HAMAP-Rule MF_01338
Active site2871Proton acceptor By similarity HAMAP-Rule MF_01338
Metal binding1941Magnesium; via carbamate group By similarity HAMAP-Rule MF_01338
Metal binding1961Magnesium By similarity HAMAP-Rule MF_01338
Metal binding1971Magnesium By similarity HAMAP-Rule MF_01338
Binding site1161Substrate; in homodimeric partner By similarity HAMAP-Rule MF_01338
Binding site1661Substrate By similarity HAMAP-Rule MF_01338
Binding site1701Substrate By similarity HAMAP-Rule MF_01338
Binding site2881Substrate By similarity HAMAP-Rule MF_01338
Binding site3201Substrate By similarity HAMAP-Rule MF_01338
Binding site3721Substrate By similarity HAMAP-Rule MF_01338
Site3271Transition state stabilizer By similarity HAMAP-Rule MF_01338

Amino acid modifications

Modified residue1941N6-carboxylysine By similarity HAMAP-Rule MF_01338

Sequences

Sequence LengthMass (Da)Tools
C7M1Z0 [UniParc].

Last modified October 13, 2009. Version 1.
Checksum: 1EE3DB0841FA345C

FASTA47352,903
        10         20         30         40         50         60 
MAGNRYEAGV KEYRKTYWAP DYVPLDSDLL AVFKIVPQPG VDREEAAAAV AAESSTGTWT 

        70         80         90        100        110        120 
TVWTDLLTDL DYYKGRAYRI EDVPGDDTAF YAFVAYPIDL FEEGSVVNVF TSLVGNVFGF 

       130        140        150        160        170        180 
KAVRSLRLED VRFPLAFVNT CNGPPHGIQV ERDKMNKYGR PLLGCTIKPK LGLSAKNYGR 

       190        200        210        220        230        240 
AVYEVLRGGL DFTKDDENVN SQPFMRWRDR FLFVAEAIHQ AEAETGERKG HYLNVTAPSP 

       250        260        270        280        290        300 
EEMYERAEFA KELGMPIIMH DFLTGGFTAN TGLARWCRRN GMLLHIHRAM HAVIDRNPYH 

       310        320        330        340        350        360 
GIHFRVLAKA LRLSGGDHLH TGTVVGKLEG DRAATQGWVD LLRESYIPED RSRGIFFDQD 

       370        380        390        400        410        420 
WGSMPGVFAV ASGGIHVWHM PSLLTIFGDD AVFQFGGGTL GHPWGNAPGA TANRVALEAC 

       430        440        450        460        470 
VQARNEGRDV EREGKDILQN AAKHSPELRV AMETWKEIKF EFDTVDKLDS VHR

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001631 Genomic DNA. Translation: ACU53088.1.
RefSeqYP_003108761.1. NC_013124.1.

3D structure databases

ProteinModelPortalC7M1Z0.
ModBaseSearch...

Protein-protein interaction databases

STRING525909.Afer_0119.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACU53088; ACU53088; Afer_0119.
GeneID8322172.
KEGGafo:Afer_0119.
PATRIC20639821. VBIAciFer34262_0126.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1850.
HOGENOMHOG000230831.
KOK01601.
OMAFTQDWAS.
ProtClustDBPRK04208.

Enzyme and pathway databases

BioCycAFER525909:GHMR-126-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 nameC7M1Z0_ACIFD
AccessionPrimary (citable) accession number: C7M1Z0
Entry history
Integrated into UniProtKB/TrEMBL: October 13, 2009
Last sequence update: October 13, 2009
Last modified: May 1, 2013
This is version 30 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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