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Q31NB3

- RBL_SYNE7

UniProt

Q31NB3 - RBL_SYNE7

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Protein
Ribulose bisphosphate carboxylase large chain
Gene
cbbL, rbcL, Synpcc7942_1426
Organism
Synechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2)
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 sitei120 – 1201Substrate; in homodimeric partner By similarity
Binding sitei170 – 1701Substrate By similarity
Active sitei172 – 1721Proton acceptor By similarity
Binding sitei174 – 1741Substrate By similarity
Metal bindingi198 – 1981Magnesium; via carbamate group By similarity
Metal bindingi200 – 2001Magnesium By similarity
Metal bindingi201 – 2011Magnesium By similarity
Active sitei291 – 2911Proton acceptor By similarity
Binding sitei292 – 2921Substrate By similarity
Binding sitei324 – 3241Substrate By similarity
Sitei331 – 3311Transition state stabilizer By similarity
Binding sitei376 – 3761Substrate 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

BioCyciSYNEL:SYNPCC7942_1426-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:Synpcc7942_1426
OrganismiSynechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2)
Taxonomic identifieri1140 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus
ProteomesiUP000002717: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 472472Ribulose bisphosphate carboxylase large chainUniRule annotation
PRO_0000251463Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei198 – 1981N6-carboxylysine By similarity
Disulfide bondi244 – 244Interchain; 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

PRIDEiQ31NB3.

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

STRINGi1140.Synpcc7942_1426.

Structurei

3D structure databases

ProteinModelPortaliQ31NB3.
SMRiQ31NB3. Positions 6-472.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
KOiK01601.
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.

Q31NB3-1 [UniParc]FASTAAdd to Basket

« Hide

MPKTQSAAGY KAGVKDYKLT YYTPDYTPKD TDLLAAFRFS PQPGVPADEA    50
GAAIAAESST GTWTTVWTDL LTDMDRYKGK CYHIEPVQGE ENSYFAFIAY 100
PLDLFEEGSV TNILTSIVGN VFGFKAIRSL RLEDIRFPVA LVKTFQGPPH 150
GIQVERDLLN KYGRPMLGCT IKPKLGLSAK NYGRAVYECL RGGLDFTKDD 200
ENINSQPFQR WRDRFLFVAD AIHKSQAETG EIKGHYLNVT APTCEEMMKR 250
AEFAKELGMP IIMHDFLTAG FTANTTLAKW CRDNGVLLHI HRAMHAVIDR 300
QRNHGIHFRV LAKCLRLSGG DHLHSGTVVG KLEGDKASTL GFVDLMREDH 350
IEADRSRGVF FTQDWASMPG VLPVASGGIH VWHMPALVEI FGDDSVLQFG 400
GGTLGHPWGN APGATANRVA LEACVQARNE GRDLYREGGD ILREAGKWSP 450
ELAAALDLWK EIKFEFETMD KL 472
Length:472
Mass (Da):52,448
Last modified:December 6, 2005 - v1
Checksum:iCDD8519AA9D493C9
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000100 Genomic DNA. Translation: ABB57456.1.
RefSeqiYP_400443.1. NC_007604.1.

Genome annotation databases

EnsemblBacteriaiABB57456; ABB57456; Synpcc7942_1426.
GeneIDi3773598.
KEGGisyf:Synpcc7942_1426.
PATRICi23788203. VBISynElo51371_1628.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000100 Genomic DNA. Translation: ABB57456.1 .
RefSeqi YP_400443.1. NC_007604.1.

3D structure databases

ProteinModelPortali Q31NB3.
SMRi Q31NB3. Positions 6-472.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 1140.Synpcc7942_1426.

Proteomic databases

PRIDEi Q31NB3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABB57456 ; ABB57456 ; Synpcc7942_1426 .
GeneIDi 3773598.
KEGGi syf:Synpcc7942_1426.
PATRICi 23788203. VBISynElo51371_1628.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci SYNEL:SYNPCC7942_1426-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. "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942."
    US DOE Joint Genome Institute
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PCC 7942.

Entry informationi

Entry nameiRBL_SYNE7
AccessioniPrimary (citable) accession number: Q31NB3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: December 6, 2005
Last modified: May 14, 2014
This is version 53 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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