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Q9X450

- FABI_RHIML

UniProt

Q9X450 - FABI_RHIML

Protein

Enoyl-[acyl-carrier-protein] reductase [NADH] FabI

Gene

fabI

Organism
Rhizobium meliloti (Ensifer meliloti) (Sinorhizobium meliloti)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
  1. Functioni

    Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism By similarity.By similarity

    Catalytic activityi

    An acyl-[acyl-carrier protein] + NAD+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei20 – 201NAD; via carbonyl oxygenBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi26 – 272NADBy similarity

    GO - Molecular functioni

    1. enoyl-[acyl-carrier-protein] reductase (NADH) activity Source: UniProtKB

    GO - Biological processi

    1. fatty acid elongation Source: UniProtKB
    2. protein homotetramerization Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    UniPathwayiUPA00094.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Enoyl-[acyl-carrier-protein] reductase [NADH] FabI (EC:1.3.1.9)
    Short name:
    ENR
    Alternative name(s):
    NADH-dependent enoyl-ACP reductase
    Gene namesi
    Name:fabI
    OrganismiRhizobium meliloti (Ensifer meliloti) (Sinorhizobium meliloti)
    Taxonomic identifieri382 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeSinorhizobium/Ensifer groupSinorhizobium

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – ›55›55Enoyl-[acyl-carrier-protein] reductase [NADH] FabIPRO_0000054907Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.By similarity

    Family & Domainsi

    Sequence similaritiesi

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR016040. NAD(P)-bd_dom.
    [Graphical view]

    Sequencei

    Sequence statusi: Fragment.

    Q9X450-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSIPTVKAKL LQGRKGLIVG IANDRSIAWG RARAFRALGA EIAVTYLNDK   50
    ALPLV 55
    Length:55
    Mass (Da):5,905
    Last modified:November 1, 1999 - v1
    Checksum:i0FC6A58A8F0C3C50
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei55 – 551

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF095903 Genomic DNA. Translation: AAD24359.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF095903 Genomic DNA. Translation: AAD24359.1 .

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00094 .

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    InterProi IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Genes coding for phosphotransacetylase and acetate kinase in Sinorhizobium meliloti are in an operon that is inducible by phosphate stress and controlled by phoB."
      Summers M.L., Denton M.C., McDermott T.R.
      J. Bacteriol. 181:2217-2224(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 104A14.

    Entry informationi

    Entry nameiFABI_RHIML
    AccessioniPrimary (citable) accession number: Q9X450
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 70 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3