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P71019

- FABD_BACSU

UniProt

P71019 - FABD_BACSU

Protein

Malonyl CoA-acyl carrier protein transacylase

Gene

fabD

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 2 (30 May 2000)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Malonyl-CoA + an [acyl-carrier-protein] = CoA + a malonyl-[acyl-carrier-protein].

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei91 – 911By similarity
    Active sitei201 – 2011By similarity

    GO - Molecular functioni

    1. [acyl-carrier-protein] S-malonyltransferase activity Source: UniProtKB-EC

    GO - Biological processi

    1. fatty acid biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

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

    Enzyme and pathway databases

    BioCyciBSUB:BSU15900-MONOMER.
    UniPathwayiUPA00094.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Malonyl CoA-acyl carrier protein transacylase (EC:2.3.1.39)
    Short name:
    MCT
    Gene namesi
    Name:fabD
    Synonyms:ylpE
    Ordered Locus Names:BSU15900
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU15900. [Micado]

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 317317Malonyl CoA-acyl carrier protein transacylasePRO_0000194210Add
    BLAST

    Proteomic databases

    PaxDbiP71019.

    Interactioni

    Protein-protein interaction databases

    IntActiP71019. 1 interaction.
    MINTiMINT-8366726.
    STRINGi224308.BSU15900.

    Structurei

    3D structure databases

    ProteinModelPortaliP71019.
    SMRiP71019. Positions 1-311.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the FabD family.Curated

    Phylogenomic databases

    eggNOGiCOG0331.
    HOGENOMiHOG000036504.
    KOiK00645.
    OMAiIWRVWQE.
    OrthoDBiEOG6W19KW.
    PhylomeDBiP71019.

    Family and domain databases

    Gene3Di3.40.366.10. 2 hits.
    InterProiIPR001227. Ac_transferase_dom.
    IPR014043. Acyl_transferase.
    IPR016035. Acyl_Trfase/lysoPLipase.
    IPR024925. Malonyl_CoA-ACP_transAc.
    IPR004410. Malonyl_CoA-ACP_transAc_FabD.
    IPR016036. Malonyl_transacylase_ACP-bd.
    [Graphical view]
    PfamiPF00698. Acyl_transf_1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000446. Mct. 1 hit.
    SUPFAMiSSF52151. SSF52151. 2 hits.
    SSF55048. SSF55048. 1 hit.
    TIGRFAMsiTIGR00128. fabD. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P71019-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSKIAFLFPG QGSQFIGMGK ELYEQVPAAK RLFDEADETL ETKLSSLIFE    50
    GDAEELTLTY NAQPALLTTS IAVLEKFKES GITPDFTAGH SLGEYSALVA 100
    AGALSFKDAV YTVRKRGEFM NEAVPAGEGA MAAILGMDAE ALKQVTDKVT 150
    EEGNLVQLAN LNCPGQIVIS GTAKGVELAS ELAKENGAKR AIPLEVSGPF 200
    HSELMKPAAE KLKEVLDACD IKDADVPVIS NVSADVMTEK ADIKEKLIEQ 250
    LYSPVRFEES INKLIAEGVT TFIEIGPGKV LSGLVKKVNR RLKTIAVSDP 300
    ETIELAIQTL KEENDNA 317
    Length:317
    Mass (Da):34,035
    Last modified:May 30, 2000 - v2
    Checksum:i191AE828B1C91D7F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti124 – 1318VPAGEGAM → GCRLAKEQW(PubMed:8759840)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U59433 Genomic DNA. Translation: AAC44306.1.
    Y13937 Genomic DNA. Translation: CAA74249.1.
    AL009126 Genomic DNA. Translation: CAB13463.1.
    PIRiH69620.
    RefSeqiNP_389472.1. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB13463; CAB13463; BSU15900.
    GeneIDi938488.
    KEGGibsu:BSU15900.
    PATRICi18974985. VBIBacSub10457_1684.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U59433 Genomic DNA. Translation: AAC44306.1 .
    Y13937 Genomic DNA. Translation: CAA74249.1 .
    AL009126 Genomic DNA. Translation: CAB13463.1 .
    PIRi H69620.
    RefSeqi NP_389472.1. NC_000964.3.

    3D structure databases

    ProteinModelPortali P71019.
    SMRi P71019. Positions 1-311.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P71019. 1 interaction.
    MINTi MINT-8366726.
    STRINGi 224308.BSU15900.

    Proteomic databases

    PaxDbi P71019.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB13463 ; CAB13463 ; BSU15900 .
    GeneIDi 938488.
    KEGGi bsu:BSU15900.
    PATRICi 18974985. VBIBacSub10457_1684.

    Organism-specific databases

    GenoListi BSU15900. [Micado ]

    Phylogenomic databases

    eggNOGi COG0331.
    HOGENOMi HOG000036504.
    KOi K00645.
    OMAi IWRVWQE.
    OrthoDBi EOG6W19KW.
    PhylomeDBi P71019.

    Enzyme and pathway databases

    UniPathwayi UPA00094 .
    BioCyci BSUB:BSU15900-MONOMER.

    Family and domain databases

    Gene3Di 3.40.366.10. 2 hits.
    InterProi IPR001227. Ac_transferase_dom.
    IPR014043. Acyl_transferase.
    IPR016035. Acyl_Trfase/lysoPLipase.
    IPR024925. Malonyl_CoA-ACP_transAc.
    IPR004410. Malonyl_CoA-ACP_transAc_FabD.
    IPR016036. Malonyl_transacylase_ACP-bd.
    [Graphical view ]
    Pfami PF00698. Acyl_transf_1. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000446. Mct. 1 hit.
    SUPFAMi SSF52151. SSF52151. 2 hits.
    SSF55048. SSF55048. 1 hit.
    TIGRFAMsi TIGR00128. fabD. 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. "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].
      Strain: 168.
    3. "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.

    Entry informationi

    Entry nameiFABD_BACSU
    AccessioniPrimary (citable) accession number: P71019
    Secondary accession number(s): O34463
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: May 30, 2000
    Last modified: October 1, 2014
    This is version 97 of the entry and version 2 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