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G7ZAR7 (G7ZAR7_AZOL4) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 17. 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 EMBL CBS88950.1
Ordered Locus Names:AZOLI_p10724 EMBL CBS88950.1
Encoded onPlasmid AZO_p1 EMBL CBS88950.1
OrganismAzospirillum lipoferum (strain 4B) [Complete proteome] [HAMAP] EMBL CBS88950.1
Taxonomic identifier862719 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeAzospirillum

Protein attributes

Sequence length498 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 site1891Proton acceptor By similarity HAMAP-Rule MF_01338
Active site3071Proton acceptor By similarity HAMAP-Rule MF_01338
Metal binding2151Magnesium; via carbamate group By similarity HAMAP-Rule MF_01338
Metal binding2171Magnesium By similarity HAMAP-Rule MF_01338
Metal binding2181Magnesium By similarity HAMAP-Rule MF_01338
Binding site1371Substrate; in homodimeric partner By similarity HAMAP-Rule MF_01338
Binding site1871Substrate By similarity HAMAP-Rule MF_01338
Binding site1911Substrate By similarity HAMAP-Rule MF_01338
Binding site3081Substrate By similarity HAMAP-Rule MF_01338
Binding site3401Substrate By similarity HAMAP-Rule MF_01338
Binding site3921Substrate By similarity HAMAP-Rule MF_01338
Site3471Transition state stabilizer By similarity HAMAP-Rule MF_01338

Amino acid modifications

Modified residue2151N6-carboxylysine By similarity HAMAP-Rule MF_01338

Sequences

Sequence LengthMass (Da)Tools
G7ZAR7 [UniParc].

Last modified January 25, 2012. Version 1.
Checksum: D376615CBE745A2D

FASTA49855,364
        10         20         30         40         50         60 
MNYVSTTLPT DQKAADGVVS DPKARYRPGV LKYRQMGYWE PDYQPKDTDV LAVFRITPQD 

        70         80         90        100        110        120 
GVDPEEAAAA VAGESSTATW TVVWTDRLTD CERYRAKAFR VDPVPGAPGQ YFAYIAYELD 

       130        140        150        160        170        180 
LFEEGSIANL TASIIGNVFG FKPLKGLRLE DMRIPVAYLK TFQGPATGIV VERERLNNFG 

       190        200        210        220        230        240 
RPLLGATMKP KLGLSGRNYG RVVYEALKGG LDFTKDDENI NSQPFMHWRD RFLYCMEGVN 

       250        260        270        280        290        300 
RAIAETGEIK GTYLNVTAAT MEDMYERAEF AKELGSVIVM IDLVIGYTAI QSMAKWARRN 

       310        320        330        340        350        360 
DMILHLHRAG HSTYTRQKSH GVSFRVIAKW MRMAGVDHIH AGTVVGKLEG DPNVIRGIYD 

       370        380        390        400        410        420 
TCRETHVPQN LQHGIFFDQP WAGLKRVMPV ASGGIHAGQM HQLLTYLGED VILQFGGGTI 

       430        440        450        460        470        480 
GHPDGIQAGA TANRVALEVM VKARNEGRDI WNEGPEILRD AARWCAPLRA ALDTWKDVTF 

       490 
DYASTDSVDY VPTPTAAM 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FQ311869 Genomic DNA. Translation: CBS88950.1.
RefSeqYP_004974125.1. NC_016585.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCBS88950; CBS88950; AZOLI_p10724.
GeneID11622069.
KEGGali:AZOLI_p10724.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01601.
OMAHRAMHAA.

Enzyme and pathway databases

BioCycALIP862719:GJAA-3592-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 nameG7ZAR7_AZOL4
AccessionPrimary (citable) accession number: G7ZAR7
Entry history
Integrated into UniProtKB/TrEMBL: January 25, 2012
Last sequence update: January 25, 2012
Last modified: February 19, 2014
This is version 17 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)