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K9QNP0

- K9QNP0_NOSS7

UniProt

K9QNP0 - K9QNP0_NOSS7

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Protein
Ribulose bisphosphate carboxylase large chain
Gene
cbbL, rbcL, Nos7524_1120
Organism
Nostoc sp. (strain ATCC 29411 / PCC 7524)
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
Complete GO annotation...

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, PhotosynthesisUniRule 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
Ordered Locus Names:Nos7524_1120Imported
OrganismiNostoc sp. (strain ATCC 29411 / PCC 7524)Imported
Taxonomic identifieri28072 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaNostocalesNostocaceaeNostoc
ProteomesiUP000010378: 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.

K9QNP0-1 [UniParc]FASTAAdd to Basket

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MSYAQTKTQS KAGYQAGVKD YRLTYYTPDY TPKDTDILAA FRVTPQPGVP    50
PEEAGAAVAA ESSTGTWTTV WTDLLTDLDR YKGRCYDIEP VPGEDNQFIA 100
YIAYPLDLFE EGSVTNMFTS IVGNVFGFKA LRALRLEDLR IPVAYLKTFQ 150
GPPHGIQVER DKLNKYGRPL LGCTIKPKLG LSAKNYGRAV YECLRGGLDF 200
TKDDENINSA PFQRWRDRFL FVADAIHKSQ AETGEIKGHY LNVTAPTCEE 250
MLKRAEYAKE LGMPIIMHDY LTAGFTANTT LARWCRDNGL LLHIHRAMHA 300
VIDRQKNHGI HFRVLAKALR MSGGDHIHTG TVVGKLEGDR AITMGFVDLL 350
RENYVEQDKS RGIYFTQDWA SMPGVMAVAS GGIHVWHMPA LVEIFGDDSV 400
LQFGGGTLGH PWGNAPGATA NRVALEACIQ ARNEGRNLAR EGNDVIREAA 450
KWSPELAAAC ELWKEIKFEF EAMDTV 476
Length:476
Mass (Da):52,989
Last modified:March 6, 2013 - v1
Checksum:i45F3AE9780E3148A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP003552 Genomic DNA. Translation: AFY47013.1.
RefSeqiWP_015137469.1. NC_019684.1.
YP_007074610.1. NC_019684.1.

Genome annotation databases

EnsemblBacteriaiAFY47013; AFY47013; Nos7524_1120.
GeneIDi14089081.
KEGGinop:Nos7524_1120.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP003552 Genomic DNA. Translation: AFY47013.1 .
RefSeqi WP_015137469.1. NC_019684.1.
YP_007074610.1. NC_019684.1.

3D structure databases

ModBasei Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AFY47013 ; AFY47013 ; Nos7524_1120 .
GeneIDi 14089081.
KEGGi nop:Nos7524_1120.

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 [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 29411 / PCC 7524.

Entry informationi

Entry nameiK9QNP0_NOSS7
AccessioniPrimary (citable) accession number: K9QNP0
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