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Q2JV67

- RBL_SYNJA

UniProt

Q2JV67 - RBL_SYNJA

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Protein
Ribulose bisphosphate carboxylase large chain
Gene
cbbL, rbcL, CYA_1194
Organism
Synechococcus sp. (strain JA-3-3Ab) (Cyanobacteria bacterium Yellowstone A-Prime)
Status
Reviewed - Annotation score: 4 out of 5 - Protein inferred from homologyi

Functioni

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 in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site By similarity.UniRule annotation

Catalytic activityi

2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O.UniRule annotation
3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2.UniRule annotation

Cofactori

Binds 1 magnesium ion per subunit By similarity.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei122 – 1221Substrate; in homodimeric partner By similarity
Binding sitei172 – 1721Substrate By similarity
Active sitei174 – 1741Proton acceptor By similarity
Binding sitei176 – 1761Substrate By similarity
Metal bindingi200 – 2001Magnesium; via carbamate group By similarity
Metal bindingi202 – 2021Magnesium By similarity
Metal bindingi203 – 2031Magnesium By similarity
Active sitei293 – 2931Proton acceptor By similarity
Binding sitei294 – 2941Substrate By similarity
Binding sitei326 – 3261Substrate By similarity
Sitei333 – 3331Transition state stabilizer By similarity
Binding sitei378 – 3781Substrate By similarity

GO - Molecular functioni

  1. magnesium ion binding Source: UniProtKB-HAMAP
  2. monooxygenase activity Source: UniProtKB-KW
  3. ribulose-bisphosphate carboxylase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. photorespiration Source: UniProtKB-KW
  2. reductive pentose-phosphate cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Lyase, Monooxygenase, Oxidoreductase

Keywords - Biological processi

Calvin cycle, Carbon dioxide fixation, Photorespiration, Photosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciSSP321327:GHFX-1188-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylase large chain (EC:4.1.1.39)
Short name:
RuBisCO large subunit
Gene namesi
Name:cbbL
Synonyms:rbcL
Ordered Locus Names:CYA_1194
OrganismiSynechococcus sp. (strain JA-3-3Ab) (Cyanobacteria bacterium Yellowstone A-Prime)
Taxonomic identifieri321327 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus
ProteomesiUP000008818: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 474474Ribulose bisphosphate carboxylase large chainUniRule annotation
PRO_0000251461Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei200 – 2001N6-carboxylysine By similarity
Disulfide bondi246 – 246Interchain; in linked form By similarity

Post-translational modificationi

The disulfide bond which can form in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover By similarity.UniRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiQ2JV67.

Interactioni

Subunit structurei

Heterohexadecamer of 8 large chains and 8 small chains; disulfide-linked. The disulfide link is formed within the large subunit homodimers By similarity.

Protein-protein interaction databases

STRINGi321327.CYA_1194.

Structurei

3D structure databases

ProteinModelPortaliQ2JV67.
SMRiQ2JV67. Positions 11-474.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
KOiK01601.
OMAiFTQDWAS.
OrthoDBiEOG6ZKXMS.

Family and domain databases

Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPiMF_01338. RuBisCO_L_type1.
InterProiIPR020878. RuBisCo_large_chain_AS.
IPR020888. RuBisCO_lsu.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[Graphical view]
PfamiPF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view]
SUPFAMiSSF51649. SSF51649. 1 hit.
SSF54966. SSF54966. 1 hit.
PROSITEiPS00157. RUBISCO_LARGE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q2JV67-1 [UniParc]FASTAAdd to Basket

« Hide

MAYSATQTKK GYQAGVKDYR LTYYTPDYTP KDTDVLACFR VTPQPGVPPE    50
EAGAAVAAES STGTWTTVWT DLLTDLDRYK GRCYDIEPVP GEENQYFCFV 100
AYPLDLFEEG SVTNMLTSIV GNVFGFKALK ALRLEDVRIP VAYLKTFQGP 150
PHGIQVERDK LNKYGRPLLG CTIKPKLGLS AKNYGRAVYE ALRGGLDFTK 200
DDENINSQPF QRWRDRYLFV MEAVHKAQAE TGEIKGHYLN VTAPTCEEMF 250
KRAEFAKEIG APIIMHDYLT AGFTANTSLA KWCRDNGILL HIHRAMHAVI 300
DRQKNHGIHF RVLAKCLRMS GGDHLHAGTV VGKLEGDRAI TMGFVDLMRE 350
NYVEADRSRG IFFTQDWASM PGVMPVASGG IHVWHMPALV EIFGDDAVLQ 400
FGGGTLGHPW GNAPGATANR VALEACIQAR NEGRDLAREG NEIIREAAKW 450
SPELAAACEL WKEIKFEFKP VDTL 474
Length:474
Mass (Da):52,804
Last modified:March 7, 2006 - v1
Checksum:i55B14AF7F6EDCFD2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000239 Genomic DNA. Translation: ABC99380.1.
RefSeqiWP_011430061.1. NC_007775.1.
YP_474643.1. NC_007775.1.

Genome annotation databases

EnsemblBacteriaiABC99380; ABC99380; CYA_1194.
GeneIDi3898903.
KEGGicya:CYA_1194.
PATRICi23810659. VBISynSp90045_1183.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000239 Genomic DNA. Translation: ABC99380.1 .
RefSeqi WP_011430061.1. NC_007775.1.
YP_474643.1. NC_007775.1.

3D structure databases

ProteinModelPortali Q2JV67.
SMRi Q2JV67. Positions 11-474.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 321327.CYA_1194.

Proteomic databases

PRIDEi Q2JV67.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABC99380 ; ABC99380 ; CYA_1194 .
GeneIDi 3898903.
KEGGi cya:CYA_1194.
PATRICi 23810659. VBISynSp90045_1183.

Phylogenomic databases

eggNOGi COG1850.
HOGENOMi HOG000230831.
KOi K01601.
OMAi FTQDWAS.
OrthoDBi EOG6ZKXMS.

Enzyme and pathway databases

BioCyci SSP321327:GHFX-1188-MONOMER.

Family and domain databases

Gene3Di 3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPi MF_01338. RuBisCO_L_type1.
InterProi IPR020878. RuBisCo_large_chain_AS.
IPR020888. RuBisCO_lsu.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[Graphical view ]
Pfami PF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view ]
SUPFAMi SSF51649. SSF51649. 1 hit.
SSF54966. SSF54966. 1 hit.
PROSITEi PS00157. RUBISCO_LARGE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Population level functional diversity in a microbial community revealed by comparative genomic and metagenomic analyses."
    Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M., Hamamura N., Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.
    ISME J. 1:703-713(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: JA-3-3Ab.

Entry informationi

Entry nameiRBL_SYNJA
AccessioniPrimary (citable) accession number: Q2JV67
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: March 7, 2006
Last modified: September 3, 2014
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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