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P51831

- FABG_BACSU

UniProt

P51831 - FABG_BACSU

Protein

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

Gene

fabG

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 3 (15 Dec 1998)
      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 sitei36 – 361NADPBy similarity
    Binding sitei89 – 891NADP; via carbonyl oxygenBy similarity
    Binding sitei141 – 1411SubstrateBy similarity
    Active sitei154 – 1541Proton acceptorBy similarity
    Binding sitei187 – 1871NADP; via amide nitrogen and carbonyl oxygenBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi11 – 144NADPBy similarity
    Nucleotide bindingi62 – 632NADPBy similarity
    Nucleotide bindingi154 – 1585NADPBy similarity

    GO - Molecular functioni

    1. 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity Source: UniProtKB-EC
    2. 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

    NADP

    Enzyme and pathway databases

    BioCyciBSUB:BSU15910-MONOMER.
    RETL1328306-WGS:GSTH-1078-MONOMER.
    RETL1328306-WGS:GSTH-2417-MONOMER.
    RETL1328306-WGS:GSTH-5994-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
    Synonyms:ylpF
    Ordered Locus Names:BSU15910
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU15910. [Micado]

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 2462463-oxoacyl-[acyl-carrier-protein] reductase FabGPRO_0000054665Add
    BLAST

    Proteomic databases

    PaxDbiP51831.
    PRIDEiP51831.

    Interactioni

    Subunit structurei

    Homotetramer.By similarity

    Protein-protein interaction databases

    IntActiP51831. 1 interaction.
    MINTiMINT-8365890.
    STRINGi224308.BSU15910.

    Structurei

    3D structure databases

    ProteinModelPortaliP51831.
    SMRiP51831. Positions 1-246.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1028.
    KOiK00059.
    OMAiDEFGAID.
    OrthoDBiEOG6N3CR8.
    PhylomeDBiP51831.

    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.
    [Graphical view]
    PfamiPF00106. adh_short. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000126. 11-beta-HSD1. 1 hit.
    PRINTSiPR00081. GDHRDH.
    PR00080. SDRFAMILY.
    TIGRFAMsiTIGR01830. 3oxo_ACP_reduc. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P51831-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLNDKTAIVT GASRGIGRSI ALDLAKSGAN VVVNYSGNEA KANEVVDEIK    50
    SMGRKAIAVK ADVSNPEDVQ NMIKETLSVF STIDILVNNA GITRDNLIMR 100
    MKEDEWDDVI NINLKGVFNC TKAVTRQMMK QRSGRIINVS SIVGVSGNPG 150
    QANYVAAKAG VIGLTKSSAK ELASRNITVN AIAPGFISTD MTDKLAKDVQ 200
    DEMLKQIPLA RFGEPSDVSS VVTFLASEGA RYMTGQTLHI DGGMVM 246
    Length:246
    Mass (Da):26,282
    Last modified:December 15, 1998 - v3
    Checksum:iC6A391167D3237DC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti23 – 231D → A in AAC44307. (PubMed:8759840)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U59433 Genomic DNA. Translation: AAC44307.1.
    AL009126 Genomic DNA. Translation: CAB13464.1.
    Y13937 Genomic DNA. Translation: CAA74250.1.
    D64116 Genomic DNA. Translation: BAA10974.1.
    PIRiA69621.
    RefSeqiNP_389473.1. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB13464; CAB13464; BSU15910.
    GeneIDi938113.
    KEGGibsu:BSU15910.
    PATRICi18974987. VBIBacSub10457_1685.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U59433 Genomic DNA. Translation: AAC44307.1 .
    AL009126 Genomic DNA. Translation: CAB13464.1 .
    Y13937 Genomic DNA. Translation: CAA74250.1 .
    D64116 Genomic DNA. Translation: BAA10974.1 .
    PIRi A69621.
    RefSeqi NP_389473.1. NC_000964.3.

    3D structure databases

    ProteinModelPortali P51831.
    SMRi P51831. Positions 1-246.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P51831. 1 interaction.
    MINTi MINT-8365890.
    STRINGi 224308.BSU15910.

    Proteomic databases

    PaxDbi P51831.
    PRIDEi P51831.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB13464 ; CAB13464 ; BSU15910 .
    GeneIDi 938113.
    KEGGi bsu:BSU15910.
    PATRICi 18974987. VBIBacSub10457_1685.

    Organism-specific databases

    GenoListi BSU15910. [Micado ]

    Phylogenomic databases

    eggNOGi COG1028.
    KOi K00059.
    OMAi DEFGAID.
    OrthoDBi EOG6N3CR8.
    PhylomeDBi P51831.

    Enzyme and pathway databases

    UniPathwayi UPA00094 .
    BioCyci BSUB:BSU15910-MONOMER.
    RETL1328306-WGS:GSTH-1078-MONOMER.
    RETL1328306-WGS:GSTH-2417-MONOMER.
    RETL1328306-WGS:GSTH-5994-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.
    [Graphical view ]
    Pfami PF00106. adh_short. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000126. 11-beta-HSD1. 1 hit.
    PRINTSi PR00081. GDHRDH.
    PR00080. SDRFAMILY.
    TIGRFAMsi TIGR01830. 3oxo_ACP_reduc. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Bacillus subtilis acyl carrier protein is encoded in a cluster of lipid biosynthesis genes."
      Morbidoni H.R., de Mendoza D., Cronan J.E. Jr.
      J. Bacteriol. 178:4794-4800(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168.
    2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
      Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
      , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
      Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 168.
    3. "A 28 kbp segment from the spoVM region of the Bacillus subtilis 168 genome."
      Foulger D., Errington J.
      Microbiology 144:801-805(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-172.
      Strain: 168.
    4. "The effect of Srb, a homologue of the mammalian SRP receptor alpha-subunit, on Bacillus subtilis growth and protein translocation."
      Oguro A., Kakeshita H., Takamatsu H., Nakamura K., Yamane K.
      Gene 172:17-24(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 230-246.
      Strain: 168.

    Entry informationi

    Entry nameiFABG_BACSU
    AccessioniPrimary (citable) accession number: P51831
    Secondary accession number(s): O31733
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: December 15, 1998
    Last modified: October 1, 2014
    This is version 107 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3