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K9W672

- K9W672_9CYAN

UniProt

K9W672 - K9W672_9CYAN

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Protein

Ribulose bisphosphate carboxylase large chain

Gene
cbbL, rbcL, Cri9333_4173
Organism
Crinalium epipsammum PCC 9333
Status
Unreviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

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 annotationImported, 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:Cri9333_4173Imported
OrganismiCrinalium epipsammum PCC 9333Imported
Taxonomic identifieri1173022 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeOscillatorialesCrinalium
ProteomesiUP000010472: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei202 – 2021N6-carboxylysine By similarityUniRule annotation
Disulfide bondi248 – 248Interchain; in linked form By similarityUniRule annotation

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 bondUniRule annotation

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.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.

K9W672-1 [UniParc]FASTAAdd to Basket

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MAYSQTKTQS KTGYKAGVQD YRLTYYTPDY TPKDTDVLAA FRVTPQPGVP    50
PEEAGAAVAA ESSTGTWTTV WTDLLTDLDR YKGRCYDIEP VPGEDNQFIA 100
YIAYPLDLFE EGSVTNLLTS LVGNVFGFKA LRALRLEDLR IPVAYLKTFQ 150
GPPHGIQVER DKLNKYGRPL LGCTIKPKLG LSAKNYGRAV YEVLRGGLDF 200
TKDDENINSQ PFMRWRDRFL FVQEAIEKAQ AETGEIKGHY LNVTAPTCEE 250
MMERAEFAKE IGTPIIMHDY LTGGFTANTT LAKWCRRNGV LLHIHRAMHA 300
VIDRQKNHGI HFRVLAKCLR MSGGDHLHSG TVVGKLEGEK GITMGFVDLM 350
RENYVEQDRD RGIFFTQDWA SMPGVMPVAS GGIHVWHMPA LVEIFGDDSC 400
LQFGGGTLGH PWGNAPGATA NRVALEACVQ ARNEGRNLMR EGGDVIREAC 450
KWSPELAVAC ELWKEIKFEF EAMDTL 476
Length:476
Mass (Da):53,156
Last modified:March 6, 2013 - v1
Checksum:iA35A0D4ED351FCFE
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP003620 Genomic DNA. Translation: AFZ14965.1.
RefSeqiYP_007144475.1. NC_019753.1.

Genome annotation databases

EnsemblBacteriaiAFZ14965; AFZ14965; Cri9333_4173.
GeneIDi14170772.
KEGGicep:Cri9333_4173.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP003620 Genomic DNA. Translation: AFZ14965.1 .
RefSeqi YP_007144475.1. NC_019753.1.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AFZ14965 ; AFZ14965 ; Cri9333_4173 .
GeneIDi 14170772.
KEGGi cep:Cri9333_4173.

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 9333Imported.

Entry informationi

Entry nameiK9W672_9CYAN
AccessioniPrimary (citable) accession number: K9W672
Entry historyi
Integrated into UniProtKB/TrEMBL: March 6, 2013
Last sequence update: March 6, 2013
Last modified: July 9, 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