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F8GEW5

- F8GEW5_NITSI

UniProt

F8GEW5 - F8GEW5_NITSI

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Protein
Ribulose bisphosphate carboxylase large chain
Gene
cbbL, Nit79A3_1255
Organism
Nitrosomonas sp. (strain Is79A3)
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. 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 sitei116 – 1161Substrate; in homodimeric partner By similarityUniRule annotation
Binding sitei166 – 1661Substrate By similarityUniRule annotation
Active sitei168 – 1681Proton acceptor By similarityUniRule annotation
Binding sitei170 – 1701Substrate By similarityUniRule annotation
Metal bindingi194 – 1941Magnesium; via carbamate group By similarityUniRule annotation
Metal bindingi196 – 1961Magnesium By similarityUniRule annotation
Metal bindingi197 – 1971Magnesium By similarityUniRule annotation
Active sitei287 – 2871Proton acceptor By similarityUniRule annotation
Binding sitei288 – 2881Substrate By similarityUniRule annotation
Binding sitei320 – 3201Substrate By similarityUniRule annotation
Sitei327 – 3271Transition state stabilizer By similarityUniRule annotation
Binding sitei372 – 3721Substrate 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. 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

Keywords - Ligandi

MagnesiumUniRule annotation, Metal-bindingUniRule annotation

Enzyme and pathway databases

BioCyciNSP261292:GH7H-1274-MONOMER.

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
Ordered Locus Names:Nit79A3_1255Imported
OrganismiNitrosomonas sp. (strain Is79A3)Imported
Taxonomic identifieri261292 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNitrosomonadalesNitrosomonadaceaeNitrosomonas
ProteomesiUP000000501: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei194 – 1941N6-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.
InterProiIPR020888. 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.

Sequencei

Sequence statusi: Complete.

F8GEW5-1 [UniParc]FASTAAdd to Basket

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MAVKIYNAGV KEYRHTYWTP DYTPLDTDLL ACFKITPQAG VPREEVAAAV    50
AAESSTGTWT TVWTDLLTDL DYYKGRAYKI EDVPGDDTCF YAFVAYPIDL 100
FEEGSVVNVL TSLVGNVFGF KALRALRLED VRFPIAYVKT CGGPPAGIQV 150
ERDRLNKYGR ALLGCTIKPK LGLSAKNYGR AVYECLRGGL DLTKDDENVN 200
SQPFMRWRDR FEFVVEACQK AERETGERKG HYLNVTAPTP EEMYKRAEFA 250
KELGAPIIMH DYLTGGLTAN TGLANWCRNN GMLLHIHRAM HAVLDRNPHH 300
GIHFRVLTKV LRLSGGDHLH SGTVVGKLEG DRAATLGWID TMRDKFIKED 350
RSRGLFFDQD WGSMPGVFPV ASGGIHVWHM PALVAIFGDD ACLQFGGGTL 400
GHPWGNAAGA AANRVALEAC VEARNQGVEI EKEGKAILTK AAKSSPELKI 450
AMETWKEIKF EFDTVDKLDV AHK 473
Length:473
Mass (Da):52,459
Last modified:September 21, 2011 - v1
Checksum:i23F07A35161E6884
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP002876 Genomic DNA. Translation: AEJ01097.1.
RefSeqiWP_013965373.1. NC_015731.1.
YP_004694496.1. NC_015731.1.

Genome annotation databases

EnsemblBacteriaiAEJ01097; AEJ01097; Nit79A3_1255.
GeneIDi10933345.
KEGGinii:Nit79A3_1255.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP002876 Genomic DNA. Translation: AEJ01097.1 .
RefSeqi WP_013965373.1. NC_015731.1.
YP_004694496.1. NC_015731.1.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AEJ01097 ; AEJ01097 ; Nit79A3_1255 .
GeneIDi 10933345.
KEGGi nii:Nit79A3_1255.

Phylogenomic databases

KOi K01601.

Enzyme and pathway databases

BioCyci NSP261292:GH7H-1274-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 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.
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Is79A3Imported.

Entry informationi

Entry nameiF8GEW5_NITSI
AccessioniPrimary (citable) accession number: F8GEW5
Entry historyi
Integrated into UniProtKB/TrEMBL: September 21, 2011
Last sequence update: September 21, 2011
Last modified: September 3, 2014
This is version 19 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