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Q87TN9

- FADB_VIBPA

UniProt

Q87TN9 - FADB_VIBPA

Protein

Fatty acid oxidation complex subunit alpha

Gene

fadB

Organism
Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 82 (01 Oct 2014)
      Sequence version 1 (01 Jun 2003)
      Previous versions | rss
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    Functioni

    Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate.UniRule annotation

    Catalytic activityi

    (S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH.UniRule annotation
    (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O.UniRule annotation
    (S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA.UniRule annotation
    (3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-CoA.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei119 – 1191Important for catalytic activityUniRule annotation
    Sitei139 – 1391Important for catalytic activityUniRule annotation
    Binding sitei296 – 2961SubstrateUniRule annotation
    Binding sitei325 – 3251NAD; via amide nitrogenUniRule annotation
    Binding sitei344 – 3441NADUniRule annotation
    Binding sitei408 – 4081NADUniRule annotation
    Active sitei451 – 4511For 3-hydroxyacyl-CoA dehydrogenase activityUniRule annotation
    Binding sitei454 – 4541NADUniRule annotation
    Binding sitei501 – 5011SubstrateUniRule annotation
    Binding sitei661 – 6611SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi401 – 4033NADUniRule annotation
    Nucleotide bindingi428 – 4303NADUniRule annotation

    GO - Molecular functioni

    1. 3-hydroxyacyl-CoA dehydrogenase activity Source: UniProtKB-HAMAP
    2. 3-hydroxybutyryl-CoA epimerase activity Source: UniProtKB-HAMAP
    3. coenzyme binding Source: InterPro
    4. dodecenoyl-CoA delta-isomerase activity Source: UniProtKB-HAMAP
    5. enoyl-CoA hydratase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. fatty acid beta-oxidation Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Isomerase, Lyase, Oxidoreductase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid degradation, Lipid metabolism

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BioCyciVPAR223926:GHK4-30-MONOMER.
    UniPathwayiUPA00659.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fatty acid oxidation complex subunit alphaUniRule annotation
    Including the following 2 domains:
    Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimeraseUniRule annotation (EC:4.2.1.17UniRule annotation, EC:5.1.2.3UniRule annotation, EC:5.3.3.8UniRule annotation)
    3-hydroxyacyl-CoA dehydrogenaseUniRule annotation (EC:1.1.1.35UniRule annotation)
    Gene namesi
    Name:fadBUniRule annotation
    Ordered Locus Names:VP0030
    OrganismiVibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633)
    Taxonomic identifieri223926 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
    ProteomesiUP000002493: Chromosome 1

    Subcellular locationi

    GO - Cellular componenti

    1. fatty acid beta-oxidation multienzyme complex Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 723723Fatty acid oxidation complex subunit alphaPRO_0000109292Add
    BLAST

    Interactioni

    Subunit structurei

    Heterotetramer of two alpha chains (FadB) and two beta chains (FadA).UniRule annotation

    Protein-protein interaction databases

    STRINGi223926.VP0030.

    Structurei

    3D structure databases

    ProteinModelPortaliQ87TN9.
    SMRiQ87TN9. Positions 1-716.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 189189Enoyl-CoA hydratase/isomeraseUniRule annotationAdd
    BLAST
    Regioni311 – 7234133-hydroxyacyl-CoA dehydrogenaseUniRule annotationAdd
    BLAST

    Sequence similaritiesi

    In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.UniRule annotation
    In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG1250.
    HOGENOMiHOG000261344.
    KOiK01825.
    OMAiNPIVVND.
    OrthoDBiEOG6M9F0M.

    Family and domain databases

    Gene3Di1.10.1040.10. 2 hits.
    3.40.50.720. 1 hit.
    3.90.226.10. 2 hits.
    HAMAPiMF_01621. FadB.
    InterProiIPR006180. 3-OHacyl-CoA_DH_CS.
    IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
    IPR006108. 3HC_DH_C.
    IPR008927. 6-PGluconate_DH_C-like.
    IPR029045. ClpP/crotonase-like_dom.
    IPR001753. Crotonase_core_superfam.
    IPR013328. DH_multihelical.
    IPR012799. FadB.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF00725. 3HCDH. 2 hits.
    PF02737. 3HCDH_N. 1 hit.
    PF00378. ECH. 1 hit.
    [Graphical view]
    SUPFAMiSSF48179. SSF48179. 2 hits.
    SSF52096. SSF52096. 1 hit.
    TIGRFAMsiTIGR02437. FadB. 1 hit.
    PROSITEiPS00067. 3HCDH. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q87TN9-1 [UniParc]FASTAAdd to Basket

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    MIYQADTLQV KEIQDGIAEL SFCSPKSVNK LDLATLESLD KALDALTSHQ    50
    GLKGLMLTSD KDAFIVGADI TEFLGLFAKT DAELDQWLQF ANSIFNKLED 100
    LPVPTISVLK GHTLGGGCEC VLATDMRIGD KTTSIGLPET KLGIMPGFGG 150
    CVRLPRVIGA DSAMEIITQG KACRADEALK IGLLDAVVET DALYESALQT 200
    LTSAINEKID WQARRKQKTS PLTLSKLESM MSFTMAKGLV AQVAGPHYPA 250
    PMTAVITIEE GARFARNEAL DIERKYFVKL AKSEEAKALV GLFLNDQYIK 300
    GIAKKAAKSA SKDTERAAVL GAGIMGGGIA YQSALKGVPV LMKDIAQPSL 350
    DLGMTEASKL LNKRLAQGRI DGFKMAGILA SITPSLHYAG IENSDVIVEA 400
    VVENPKVKAT VLSEVESHVG EDTVITSNTS TIPINLLAQS LKRPENFCGM 450
    HFFNPVHRMP LVEIIRGEKT SDETINRVVA YAAKMGKSPI VVNDCPGFFV 500
    NRVLFPYFGG FSMLLRDGAD FTKVDKVMER KFGWPMGPAY LLDVVGIDTA 550
    HHAQAVMAEG FPERMGKQGR DAIDALFEAN KYGQKNGNGF YSYTIDKKGK 600
    PKKTFTEDIL PVLADVCADK QEFDEQTIIQ RMMIPMINEV VLCLQEGIIA 650
    TPQEADMALV YGLGFPPFRG GVFRYLDSVG IAEFVEMAKQ HADLGAMYHV 700
    PQMLIDMAAK GESFYGAQQQ GSI 723
    Length:723
    Mass (Da):78,556
    Last modified:June 1, 2003 - v1
    Checksum:iE4B650E43FE9BAA2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000031 Genomic DNA. Translation: BAC58293.1.
    RefSeqiNP_796409.1. NC_004603.1.

    Genome annotation databases

    EnsemblBacteriaiBAC58293; BAC58293; BAC58293.
    GeneIDi1187486.
    KEGGivpa:VP0030.
    PATRICi20138288. VBIVibPar50997_0030.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000031 Genomic DNA. Translation: BAC58293.1 .
    RefSeqi NP_796409.1. NC_004603.1.

    3D structure databases

    ProteinModelPortali Q87TN9.
    SMRi Q87TN9. Positions 1-716.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 223926.VP0030.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAC58293 ; BAC58293 ; BAC58293 .
    GeneIDi 1187486.
    KEGGi vpa:VP0030.
    PATRICi 20138288. VBIVibPar50997_0030.

    Phylogenomic databases

    eggNOGi COG1250.
    HOGENOMi HOG000261344.
    KOi K01825.
    OMAi NPIVVND.
    OrthoDBi EOG6M9F0M.

    Enzyme and pathway databases

    UniPathwayi UPA00659 .
    BioCyci VPAR223926:GHK4-30-MONOMER.

    Family and domain databases

    Gene3Di 1.10.1040.10. 2 hits.
    3.40.50.720. 1 hit.
    3.90.226.10. 2 hits.
    HAMAPi MF_01621. FadB.
    InterProi IPR006180. 3-OHacyl-CoA_DH_CS.
    IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
    IPR006108. 3HC_DH_C.
    IPR008927. 6-PGluconate_DH_C-like.
    IPR029045. ClpP/crotonase-like_dom.
    IPR001753. Crotonase_core_superfam.
    IPR013328. DH_multihelical.
    IPR012799. FadB.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    Pfami PF00725. 3HCDH. 2 hits.
    PF02737. 3HCDH_N. 1 hit.
    PF00378. ECH. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48179. SSF48179. 2 hits.
    SSF52096. SSF52096. 1 hit.
    TIGRFAMsi TIGR02437. FadB. 1 hit.
    PROSITEi PS00067. 3HCDH. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism distinct from that of V. cholerae."
      Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K., Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S., Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.
      Lancet 361:743-749(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: RIMD 2210633.

    Entry informationi

    Entry nameiFADB_VIBPA
    AccessioniPrimary (citable) accession number: Q87TN9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 6, 2005
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 82 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, Multifunctional enzyme, 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