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P0A2C9

- FABG_SALTY

UniProt

P0A2C9 - FABG_SALTY

Protein

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

Gene

fabG

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 70 (01 Oct 2014)
      Sequence version 1 (15 Mar 2005)
      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.1 Publication

    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
    2. metal ion binding Source: UniProtKB-KW
    3. NAD binding Source: InterPro
    4. NADP binding Source: UniProtKB

    GO - Biological processi

    1. fatty acid elongation Source: UniProtKB

    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

    BioCyciSENT99287:GCTI-1204-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:STM1195
    OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
    Taxonomic identifieri99287 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
    ProteomesiUP000001014: Chromosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi125 – 1251M → I: Loss of the temperature-sensitive phenotype; when associated with T-223. 1 Publication
    Mutagenesisi223 – 2231A → T: Loss of the temperature-sensitive phenotype; when associated with I-125. 1 Publication
    Mutagenesisi224 – 2241S → F: Distorts the local conformation and prevent stacking around Phe-221. The S224F mutation would additionally disrupt the hydrogen bond formed between Ser-224 and Glu-226. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 2442443-oxoacyl-[acyl-carrier-protein] reductase FabGPRO_0000054681Add
    BLAST

    Proteomic databases

    PaxDbiP0A2C9.
    PRIDEiP0A2C9.

    Interactioni

    Subunit structurei

    Homotetramer.By similarity

    Protein-protein interaction databases

    STRINGi99287.STM1195.

    Structurei

    3D structure databases

    ProteinModelPortaliP0A2C9.
    SMRiP0A2C9. Positions 2-244.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1028.
    KOiK00059.
    OMAiDEFGAID.
    OrthoDBiEOG6N3CR8.
    PhylomeDBiP0A2C9.

    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.

    P0A2C9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSFEGKIALV TGASRGIGRA IAETLVARGA KVIGTATSEN GAKNISDYLG    50
    ANGKGLMLNV TDPASIESVL ENIRAEFGEV DILVNNAGIT RDNLLMRMKD 100
    DEWNDIIETN LSSVFRLSKA VMRAMMKKRC GRIITIGSVV GTMGNAGQAN 150
    YAAAKAGLIG FSKSLAREVA SRGITVNVVA PGFIETDMTR ALSDDQRAGI 200
    LAQVPAGRLG GAQEIASAVA FLASDEASYI TGETLHVNGG MYMV 244
    Length:244
    Mass (Da):25,545
    Last modified:March 15, 2005 - v1
    Checksum:i86D71DA3E9AF0363
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF044668 Genomic DNA. Translation: AAC38650.1.
    AE006468 Genomic DNA. Translation: AAL20124.1.
    RefSeqiNP_460165.1. NC_003197.1.

    Genome annotation databases

    EnsemblBacteriaiAAL20124; AAL20124; STM1195.
    GeneIDi1252713.
    KEGGistm:STM1195.
    PATRICi32380839. VBISalEnt20916_1264.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF044668 Genomic DNA. Translation: AAC38650.1 .
    AE006468 Genomic DNA. Translation: AAL20124.1 .
    RefSeqi NP_460165.1. NC_003197.1.

    3D structure databases

    ProteinModelPortali P0A2C9.
    SMRi P0A2C9. Positions 2-244.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 99287.STM1195.

    Proteomic databases

    PaxDbi P0A2C9.
    PRIDEi P0A2C9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAL20124 ; AAL20124 ; STM1195 .
    GeneIDi 1252713.
    KEGGi stm:STM1195.
    PATRICi 32380839. VBISalEnt20916_1264.

    Phylogenomic databases

    eggNOGi COG1028.
    KOi K00059.
    OMAi DEFGAID.
    OrthoDBi EOG6N3CR8.
    PhylomeDBi P0A2C9.

    Enzyme and pathway databases

    UniPathwayi UPA00094 .
    BioCyci SENT99287:GCTI-1204-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. "Transcriptional analysis of essential genes of the Escherichia coli fatty acid biosynthesis gene cluster by functional replacement with the analogous Salmonella typhimurium gene cluster."
      Zhang Y., Cronan J.E. Jr.
      J. Bacteriol. 180:3295-3303(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: LT2.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: LT2 / SGSC1412 / ATCC 700720.
    3. "Isolation and characterization of beta-ketoacyl-acyl carrier protein reductase (fabG) mutants of Escherichia coli and Salmonella enterica serovar Typhimurium."
      Lai C.Y., Cronan J.E.
      J. Bacteriol. 186:1869-1878(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN FATTY ACID BIOSYNTHESIS, MUTAGENESIS OF MET-125; ALA-223 AND SER-224.

    Entry informationi

    Entry nameiFABG_SALTY
    AccessioniPrimary (citable) accession number: P0A2C9
    Secondary accession number(s): O85141
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 15, 2005
    Last sequence update: March 15, 2005
    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

    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, Reference proteome

    Documents

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

    External Data

    Dasty 3