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K9YHT3

- K9YHT3_HALP7

UniProt

K9YHT3 - K9YHT3_HALP7

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Protein
Ribulose bisphosphate carboxylase large chain
Gene
cbbL, rbcL, PCC7418_3537
Organism
Halothece sp. (strain PCC 7418) (Synechococcus sp. (strain PCC 7418))
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 sitei120 – 1201Substrate; in homodimeric partner By similarityUniRule annotation
Binding sitei170 – 1701Substrate By similarityUniRule annotation
Active sitei172 – 1721Proton acceptor By similarityUniRule annotation
Binding sitei174 – 1741Substrate By similarityUniRule annotation
Metal bindingi198 – 1981Magnesium; via carbamate group By similarityUniRule annotation
Metal bindingi200 – 2001Magnesium By similarityUniRule annotation
Metal bindingi201 – 2011Magnesium By similarityUniRule annotation
Active sitei291 – 2911Proton acceptor By similarityUniRule annotation
Binding sitei292 – 2921Substrate By similarityUniRule annotation
Binding sitei324 – 3241Substrate By similarityUniRule annotation
Sitei331 – 3311Transition state stabilizer By similarityUniRule annotation
Binding sitei376 – 3761Substrate 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, 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:PCC7418_3537Imported
OrganismiHalothece sp. (strain PCC 7418) (Synechococcus sp. (strain PCC 7418))Imported
Taxonomic identifieri65093 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesHalothece clusterHalothece
ProteomesiUP000010481: Chromosome

PTM / Processingi

Amino acid modifications

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

K9YHT3-1 [UniParc]FASTAAdd to Basket

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MVQAQQSSGF KAGVQDYALT YYTPDYTPKD TDVLAAFRVT PQPGVPPEEA    50
GAAVAAESST GTWTTVWTDN LTDLDRYKGR CYEIEAVPGE DNQYFMFVAY 100
PLDLFEEGSV TNMLTSIVGN VFGFKALRAL RLEDMRIPVA YLKTFQGPPH 150
GITVERDLLN KYGRPLLGCT IKPKLGLSAK NYGRAVYECL RGGLDFTKDD 200
ENINSQPFMR WRDRFLFVAE AVHKAQAETN EIKGHYLNVT APTCEQMLER 250
AEFVKELDMP ILMHDYLTGG FTANTTLSKW CRANGVLMHI HRAMHAVIDR 300
QKNHGIHFRV LAKCLRMSGG DHLHSGTVVG KLEGERAITL GFVDQMREDH 350
VEEDRSRGNF FTQDWASMGG VMPVASGGIH IWHMPALVDI FGDDSCLQFG 400
GGTLGHPWGN APGATANRVA LEACVQARNE GRNLAREGSE IIKEAARWSP 450
ELKVASELWK EIKFEYEAVD TL 472
Length:472
Mass (Da):52,605
Last modified:March 6, 2013 - v1
Checksum:i8FB36E8690FEECC1
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP003945 Genomic DNA. Translation: AFZ45648.1.
RefSeqiWP_015227520.1. NC_019779.1.
YP_007169862.1. NC_019779.1.

Genome annotation databases

EnsemblBacteriaiAFZ45648; AFZ45648; PCC7418_3537.
GeneIDi14200799.
KEGGihao:PCC7418_3537.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP003945 Genomic DNA. Translation: AFZ45648.1 .
RefSeqi WP_015227520.1. NC_019779.1.
YP_007169862.1. NC_019779.1.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AFZ45648 ; AFZ45648 ; PCC7418_3537 .
GeneIDi 14200799.
KEGGi hao:PCC7418_3537.

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: PCC 7418.

Entry informationi

Entry nameiK9YHT3_HALP7
AccessioniPrimary (citable) accession number: K9YHT3
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