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Q8K9J5

- FABG_BUCAP

UniProt

Q8K9J5 - FABG_BUCAP

Protein

3-oxoacyl-[acyl-carrier-protein] reductase FabG

Gene

fabG

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 84 (01 Oct 2014)
      Sequence version 1 (01 Oct 2002)
      Previous versions | rss
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    Functioni

    Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis.By similarity

    Catalytic activityi

    (3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP+ = 3-oxoacyl-[acyl-carrier-protein] + NADPH.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei37 – 371NADPBy similarity
    Metal bindingi50 – 501Calcium 1; via carbonyl oxygen; shared with dimeric partnerBy similarity
    Metal bindingi53 – 531Calcium 1; via carbonyl oxygen; shared with dimeric partnerBy similarity
    Binding sitei86 – 861NADP; via carbonyl oxygenBy similarity
    Binding sitei138 – 1381SubstrateBy similarity
    Metal bindingi145 – 1451Calcium 2By similarity
    Active sitei151 – 1511Proton acceptorPROSITE-ProRule annotation
    Binding sitei184 – 1841NADP; via amide nitrogen and carbonyl oxygenBy similarity
    Metal bindingi233 – 2331Calcium 3; shared with dimeric partnerBy similarity
    Metal bindingi234 – 2341Calcium 3; via carbonyl oxygen; shared with dimeric partnerBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi12 – 154NADPBy similarity
    Nucleotide bindingi59 – 602NADPBy similarity
    Nucleotide bindingi151 – 1555NADPBy similarity

    GO - Molecular functioni

    1. 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity Source: UniProtKB-EC
    2. metal ion binding Source: UniProtKB-KW
    3. NAD binding Source: InterPro

    GO - Biological processi

    1. fatty acid biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

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

    Keywords - Ligandi

    Calcium, Metal-binding, NADP

    Enzyme and pathway databases

    BioCyciBAPH198804:GHMG-356-MONOMER.
    UniPathwayiUPA00094.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    3-oxoacyl-[acyl-carrier-protein] reductase FabG (EC:1.1.1.100)
    Alternative name(s):
    3-ketoacyl-acyl carrier protein reductase
    Beta-Ketoacyl-acyl carrier protein reductase
    Beta-ketoacyl-ACP reductase
    Gene namesi
    Name:fabG
    Ordered Locus Names:BUsg_339
    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 – 2442443-oxoacyl-[acyl-carrier-protein] reductase FabGPRO_0000054667Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.By similarity

    Protein-protein interaction databases

    STRINGi198804.BUsg339.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8K9J5.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1028.
    KOiK00059.
    OMAiMARRPMV.
    OrthoDBiEOG6N3CR8.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR011284. 3oxo_ACP_reduc.
    IPR002198. DH_sc/Rdtase_SDR.
    IPR002347. Glc/ribitol_DH.
    IPR016040. NAD(P)-bd_dom.
    IPR020904. Sc_DH/Rdtase_CS.
    [Graphical view]
    PfamiPF00106. adh_short. 1 hit.
    [Graphical view]
    PRINTSiPR00081. GDHRDH.
    PR00080. SDRFAMILY.
    TIGRFAMsiTIGR01830. 3oxo_ACP_reduc. 1 hit.
    PROSITEiPS00061. ADH_SHORT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8K9J5-1 [UniParc]FASTAAdd to Basket

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    MKIEKKTALV TGANQGLGKE IAIKLSQKGI QVIGTSTTVD GVKTINKYLK    50
    KNGFGFILDL KDTDSILEKM KEICQKKYSI DILINNAGIT SDNLLVYMSN 100
    KEWENVIKIN LTSVFYMSKS VIRSMIKKRY GRIVTIGSVI GYLGNRGQIN 150
    YSASKSGLIG FHKSLALEVA QKGITVNIVS PGFIKTNLTK NLNVFQYKKH 200
    LSKIPMKRIG TAEEIANAVI FLSSEKASYI TGQTIHVNGG MYMT 244
    Length:244
    Mass (Da):26,939
    Last modified:October 1, 2002 - v1
    Checksum:i14526C91CDC54D5A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE013218 Genomic DNA. Translation: AAM67893.1.
    RefSeqiNP_660682.1. NC_004061.1.
    WP_011053860.1. NC_004061.1.

    Genome annotation databases

    EnsemblBacteriaiAAM67893; AAM67893; BUsg_339.
    GeneIDi1005569.
    KEGGibas:BUsg339.
    PATRICi21247493. VBIBucAph100086_0353.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE013218 Genomic DNA. Translation: AAM67893.1 .
    RefSeqi NP_660682.1. NC_004061.1.
    WP_011053860.1. NC_004061.1.

    3D structure databases

    ProteinModelPortali Q8K9J5.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 198804.BUsg339.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAM67893 ; AAM67893 ; BUsg_339 .
    GeneIDi 1005569.
    KEGGi bas:BUsg339.
    PATRICi 21247493. VBIBucAph100086_0353.

    Phylogenomic databases

    eggNOGi COG1028.
    KOi K00059.
    OMAi MARRPMV.
    OrthoDBi EOG6N3CR8.

    Enzyme and pathway databases

    UniPathwayi UPA00094 .
    BioCyci BAPH198804:GHMG-356-MONOMER.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    InterProi IPR011284. 3oxo_ACP_reduc.
    IPR002198. DH_sc/Rdtase_SDR.
    IPR002347. Glc/ribitol_DH.
    IPR016040. NAD(P)-bd_dom.
    IPR020904. Sc_DH/Rdtase_CS.
    [Graphical view ]
    Pfami PF00106. adh_short. 1 hit.
    [Graphical view ]
    PRINTSi PR00081. GDHRDH.
    PR00080. SDRFAMILY.
    TIGRFAMsi TIGR01830. 3oxo_ACP_reduc. 1 hit.
    PROSITEi PS00061. ADH_SHORT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

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

    Entry informationi

    Entry nameiFABG_BUCAP
    AccessioniPrimary (citable) accession number: Q8K9J5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 15, 2002
    Last sequence update: October 1, 2002
    Last modified: October 1, 2014
    This is version 84 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Calcium ions stabilize the structure, and may inhibit FabG activity by obstructing access to the active site.By similarity

    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