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Q8K9Q6

- FABI_BUCAP

UniProt

Q8K9Q6 - FABI_BUCAP

Protein

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

Gene

fabI

Organism
Buchnera aphidicola subsp. Schizaphis graminum (strain Sg)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 83 (01 Oct 2014)
      Sequence version 1 (01 Oct 2002)
      Previous versions | rss
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    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 and in the biotin biosynthesis 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 sitei13 – 131NAD; via carbonyl oxygenBy similarity
    Binding sitei40 – 401NADBy similarity
    Binding sitei92 – 921NAD; via carbonyl oxygenBy similarity
    Active sitei146 – 1461Proton acceptorBy similarity
    Active sitei156 – 1561Proton acceptorBy similarity
    Binding sitei163 – 1631NADBy similarity
    Sitei201 – 2011Involved in acyl-ACP bindingBy similarity
    Sitei204 – 2041Involved in acyl-ACP bindingBy similarity
    Sitei205 – 2051Involved in acyl-ACP bindingBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi19 – 202NADBy similarity
    Nucleotide bindingi64 – 652NADBy similarity
    Nucleotide bindingi192 – 1965NADBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. biotin biosynthetic process Source: UniProtKB
    2. fatty acid elongation Source: UniProtKB
    3. protein homotetramerization Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

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

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BioCyciBAPH198804:GHMG-269-MONOMER.
    UniPathwayiUPA00078.
    UPA00094.

    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
    Ordered Locus Names:BUsg_255
    OrganismiBuchnera aphidicola subsp. Schizaphis graminum (strain Sg)
    Taxonomic identifieri198804 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera
    ProteomesiUP000000416: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 260260Enoyl-[acyl-carrier-protein] reductase [NADH] FabIPRO_0000054897Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.By similarity

    Protein-protein interaction databases

    STRINGi198804.BUsg255.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8K9Q6.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0623.
    KOiK00208.
    OMAiGISGEIM.
    OrthoDBiEOG6HF644.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR014358. Enoyl-ACP_Rdtase_NADH.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PIRSFiPIRSF000094. Enoyl-ACP_rdct. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q8K9Q6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGILKGKKIL ITGILNEKSI AFGIAKSMYK QEAELIFVCQ NKKIINKIKY    50
    LIKSINYNTI FFCDVSHDEN IKELFFNIKK VWNNFDGLVH SIAYCPKKQM 100
    HEDFVESSSR KSFNICHEIS SYSFLSMARE CKNMLNKFSS LVTLSYLGSQ 150
    KIVSNYNMMG LAKSSLEANV RYMANSLGKN NIRVNAISSG PIKTTSSYQI 200
    KNFNKIQKIH KLFSLTKNHV SSEEIGNVAA FLCSDLSIGI TGSIINVDHG 250
    FNLNGINSII 260
    Length:260
    Mass (Da):29,268
    Last modified:October 1, 2002 - v1
    Checksum:iB97D1279FEFD3C71
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE013218 Genomic DNA. Translation: AAM67813.1.
    RefSeqiNP_660602.1. NC_004061.1.
    WP_011053780.1. NC_004061.1.

    Genome annotation databases

    EnsemblBacteriaiAAM67813; AAM67813; BUsg_255.
    GeneIDi1005457.
    KEGGibas:BUsg255.
    PATRICi21247315. VBIBucAph100086_0267.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE013218 Genomic DNA. Translation: AAM67813.1 .
    RefSeqi NP_660602.1. NC_004061.1.
    WP_011053780.1. NC_004061.1.

    3D structure databases

    ProteinModelPortali Q8K9Q6.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 198804.BUsg255.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAM67813 ; AAM67813 ; BUsg_255 .
    GeneIDi 1005457.
    KEGGi bas:BUsg255.
    PATRICi 21247315. VBIBucAph100086_0267.

    Phylogenomic databases

    eggNOGi COG0623.
    KOi K00208.
    OMAi GISGEIM.
    OrthoDBi EOG6HF644.

    Enzyme and pathway databases

    UniPathwayi UPA00078 .
    UPA00094 .
    BioCyci BAPH198804:GHMG-269-MONOMER.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    InterProi IPR014358. Enoyl-ACP_Rdtase_NADH.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    PIRSFi PIRSF000094. Enoyl-ACP_rdct. 1 hit.
    ProtoNeti Search...

    Publicationsi

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

    Entry informationi

    Entry nameiFABI_BUCAP
    AccessioniPrimary (citable) accession number: Q8K9Q6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 15, 2002
    Last sequence update: October 1, 2002
    Last modified: October 1, 2014
    This is version 83 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome

    Documents

    1. Buchnera aphidicola (subsp. Schizaphis graminum)
      Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3