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K9SU87

- K9SU87_9SYNE

UniProt

K9SU87 - K9SU87_9SYNE

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Protein
Ribulose bisphosphate carboxylase large chain
Gene
cbbL, rbcL, Syn7502_01669
Organism
Synechococcus sp. PCC 7502
Status
Unreviewed - Annotation score: 3 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 sitei124 – 1241Substrate; in homodimeric partner By similarityUniRule annotation
Binding sitei174 – 1741Substrate By similarityUniRule annotation
Active sitei176 – 1761Proton acceptor By similarityUniRule annotation
Binding sitei178 – 1781Substrate By similarityUniRule annotation
Metal bindingi202 – 2021Magnesium; via carbamate group By similarityUniRule annotation
Metal bindingi204 – 2041Magnesium By similarityUniRule annotation
Metal bindingi205 – 2051Magnesium By similarityUniRule annotation
Active sitei295 – 2951Proton acceptor By similarityUniRule annotation
Binding sitei296 – 2961Substrate By similarityUniRule annotation
Binding sitei328 – 3281Substrate By similarityUniRule annotation
Sitei335 – 3351Transition state stabilizer By similarityUniRule annotation
Binding sitei380 – 3801Substrate By similarityUniRule annotation

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

LyaseUniRule annotation, MonooxygenaseUniRule annotation, Oxidoreductase

Keywords - Biological processi

Calvin cycleUniRule annotation, Carbon dioxide fixationUniRule annotation, PhotorespirationUniRule annotation

Keywords - Ligandi

MagnesiumUniRule annotation, Metal-bindingUniRule annotation

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylase large chainUniRule annotation (EC:4.1.1.39UniRule annotation)
Short name:
RuBisCO large subunitUniRule annotation
Gene namesi
Name:cbbLUniRule annotation
Synonyms:rbcLUniRule annotation
ORF Names:Syn7502_01669Imported
OrganismiSynechococcus sp. PCC 7502Imported
Taxonomic identifieri1173263 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus
ProteomesiUP000010385: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei202 – 2021N6-carboxylysine By similarityUniRule annotation

Interactioni

Subunit structurei

Heterohexadecamer of 8 large chains and 8 small chains By similarity.UniRule annotation

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

KOiK01601.

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.

K9SU87-1 [UniParc]FASTAAdd to Basket

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MAYSQTKTQA KAGYKAGVQD YRLTYYTPDY TPKDTDILAA FRVTPQPGVP    50
FEEAAAAVAA ESSTGTWTTV WTDLLTDLDR YKGRCYDIEP VPGEDNQFIA 100
YIAYPLDLFE EGSVTNLLTS LVGNVFGFKA LKALRLEDLR IPVAYLKTFQ 150
GPPHGIQVER DKINKYGRPL LGCTIKPKLG LSAKNYGRAV YECLRGGLDF 200
TKDDENINSQ PFQRWRDRFL FVADAIHKAQ AETGEIKGHY LNVTAGTVEE 250
MLKRAEFAKE LNMPIIMHDF LTAGFTANTT LAHWCRDNGV LLHIHRAMHA 300
VIDRQKNHGI HFRVLAKCLR MSGGDHIHTG TVVGKLEGDK AITLGFVDLL 350
RENYVEQDKT RGIYFTQDWA SMPGVMAVAS GGIHIWHMPA LVEIFGDDSV 400
LQFGGGTLGH PWGNAPGATA NRVALEACVE ARNEGRDLYR EGGDIIREAA 450
KWSPELAVAC ELWKEIKFEF EAVDTV 476
Length:476
Mass (Da):52,993
Last modified:March 6, 2013 - v1
Checksum:i40A02D193CE6230C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP003594 Genomic DNA. Translation: AFY73725.1.
RefSeqiWP_015168382.1. NC_019702.1.
YP_007105860.1. NC_019702.1.

Genome annotation databases

EnsemblBacteriaiAFY73725; AFY73725; Syn7502_01669.
GeneIDi14132214.
KEGGisynp:Syn7502_01669.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP003594 Genomic DNA. Translation: AFY73725.1 .
RefSeqi WP_015168382.1. NC_019702.1.
YP_007105860.1. NC_019702.1.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AFY73725 ; AFY73725 ; Syn7502_01669 .
GeneIDi 14132214.
KEGGi synp:Syn7502_01669.

Phylogenomic databases

KOi K01601.

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. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: PCC 7502Imported.

Entry informationi

Entry nameiK9SU87_9SYNE
AccessioniPrimary (citable) accession number: K9SU87
Entry historyi
Integrated into UniProtKB/TrEMBL: March 6, 2013
Last sequence update: March 6, 2013
Last modified: September 3, 2014
This is version 11 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

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.UniRule annotation

Keywords - Technical termi

Complete proteome

External Data

Dasty 3

Similar proteinsi