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F6EA14

- F6EA14_SINMK

UniProt

F6EA14 - F6EA14_SINMK

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Protein

Ribulose bisphosphate carboxylase large chain

Gene
cbbL, Sinme_3974
Organism
Sinorhizobium meliloti (strain AK83)
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 sitei126 – 1261Substrate; in homodimeric partner By similarityUniRule annotation
Binding sitei176 – 1761Substrate By similarityUniRule annotation
Active sitei178 – 1781Proton acceptor By similarityUniRule annotation
Binding sitei180 – 1801Substrate By similarityUniRule annotation
Metal bindingi204 – 2041Magnesium; via carbamate group By similarityUniRule annotation
Metal bindingi206 – 2061Magnesium By similarityUniRule annotation
Metal bindingi207 – 2071Magnesium By similarityUniRule annotation
Active sitei296 – 2961Proton acceptor By similarityUniRule annotation
Binding sitei297 – 2971Substrate By similarityUniRule annotation
Binding sitei329 – 3291Substrate By similarityUniRule annotation
Sitei336 – 3361Transition state stabilizer By similarityUniRule annotation
Binding sitei381 – 3811Substrate 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 annotationImported, MonooxygenaseUniRule annotation, Oxidoreductase

Keywords - Biological processi

Calvin cycleUniRule annotation, Carbon dioxide fixationUniRule annotation

Keywords - Ligandi

MagnesiumUniRule annotation, Metal-bindingUniRule annotation

Enzyme and pathway databases

BioCyciSMEL693982:GJDT-4039-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:Sinme_3974Imported
OrganismiSinorhizobium meliloti (strain AK83)Imported
Taxonomic identifieri693982 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeSinorhizobium/Ensifer groupSinorhizobium
ProteomesiUP000008705: Chromosome 2

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei204 – 2041N6-carboxylysine By similarityUniRule annotation

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliF6EA14.
SMRiF6EA14. Positions 7-480.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

KOiK01601.
OMAiFTQDWAS.

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.

F6EA14-1 [UniParc]FASTAAdd to Basket

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MNADAKTEIK GRERYKAGVL KYAQMGYWNG DYEPKDTDLI ALFRITPQDG    50
VDPIEAAAAV AGESSTATWT VVWTDRLTAC DQYRAKAYRV DPVPGTPGQY 100
FCYVAYDLIL FEEGSIANLT ASIIGNVFSF KPLKAARLED MRLPVAYVKT 150
FRGPPTGIVV ERERLDKFGK PLLGATTKPK LGLSGKNYGR VVYEGLKGGL 200
DFMKDDENIN SQPFMHWRDR YLYCMEAVNH ASAVTGEVKG HYLNITAGTM 250
EEMYRRAEFA KELGSVIVMV DLIVGWTAIQ SISEWCRQND MILHMHRAGH 300
GTYTRQKNHG ISFRVIAKWL RLAGVDHLHA GTAVGKLEGD PPTVQGYYNV 350
CREMKNEVDL PRGLFFEQDW ADLKKVMPVA SGGIHAGQMH QLLDLFGDDV 400
VLQFGGGTIG HPMGIQAGAT ANRVALEAMV LARNEGRDIA HEGPEILRAA 450
AKWCKPLEAA LDIWGNISFN YTPTDTSDFV PSVTAA 486
Length:486
Mass (Da):53,791
Last modified:July 27, 2011 - v1
Checksum:i4386CA656929EC5F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP002782 Genomic DNA. Translation: AEG55674.1.
RefSeqiYP_004556554.1. NC_015596.1.

Genome annotation databases

EnsemblBacteriaiAEG55674; AEG55674; Sinme_3974.
GeneIDi10730014.
KEGGismk:Sinme_3974.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP002782 Genomic DNA. Translation: AEG55674.1 .
RefSeqi YP_004556554.1. NC_015596.1.

3D structure databases

ProteinModelPortali F6EA14.
SMRi F6EA14. Positions 7-480.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AEG55674 ; AEG55674 ; Sinme_3974 .
GeneIDi 10730014.
KEGGi smk:Sinme_3974.

Phylogenomic databases

KOi K01601.
OMAi FTQDWAS.

Enzyme and pathway databases

BioCyci SMEL693982:GJDT-4039-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 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: AK83.

Entry informationi

Entry nameiF6EA14_SINMK
AccessioniPrimary (citable) accession number: F6EA14
Entry historyi
Integrated into UniProtKB/TrEMBL: July 27, 2011
Last sequence update: July 27, 2011
Last modified: June 11, 2014
This is version 20 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