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B7VGL4

- FADB_VIBSL

UniProt

B7VGL4 - FADB_VIBSL

Protein

Fatty acid oxidation complex subunit alpha

Gene

fadB

Organism
Vibrio splendidus (strain LGP32) (Vibrio splendidus (strain Mel32))
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 46 (01 Oct 2014)
      Sequence version 1 (10 Feb 2009)
      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

    BioCyciVSPL575788:GH64-41-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:VS_0041
    OrganismiVibrio splendidus (strain LGP32) (Vibrio splendidus (strain Mel32))
    Taxonomic identifieri575788 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
    ProteomesiUP000009100: 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_1000186059Add
    BLAST

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    STRINGi575788.VS_0041.

    Structurei

    3D structure databases

    ProteinModelPortaliB7VGL4.
    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.
    IPR018376. Enoyl-CoA_hyd/isom_CS.
    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.
    PS00166. ENOYL_COA_HYDRATASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    B7VGL4-1 [UniParc]FASTAAdd to Basket

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    MIYQANTLQV KELQDGIAEL SFCAPASVNK LDLATLESLD KALDALNAHA    50
    GLRGLILTSN KDAFIVGADI TEFLGLFAKP EAELDEWLRF ANSIFSKLED 100
    LPVPTLSMMR GHALGGGCEC VLATDFRIGD KTTSIGLPET KLGIMPGFGG 150
    CVRLPRVIGA DSAMEIITQG KACRADEALK VGLLDAIVET DQLLESAINT 200
    VSLAANEKLD WQLRRKQKTS ALSLSKLEAM MSFTMAKGLV AQKAGPHYPA 250
    PITSVIAIEE AARSDRDAAL DIERKHFVKL AKSEEAKALV GLFLNDQYIK 300
    GLAKHAGKSA NKATERAAVL GAGIMGGGIA YQSALKGVPV MMKDIAQASL 350
    ELGMNEASKL LNKRLSRGRL DGFKMAGILS SITPSLHYAG VEQSDVIVEA 400
    VVENPKVKAA VLSEVEGLVG EDTVLTSNTS TIPINLLAKS LKRPENFCGM 450
    HFFNPVHRMP LVEIIRGEHT SEETINRVVA YAAKMGKSPI VVNDCPGFFV 500
    NRVLFPYFGG FSMLLRDGAD FTKIDKVMER KFGWPMGPAY LLDVVGLDTA 550
    HHAQAVMAQG FPERMGKEGR DAIDALYVAE KYGQKNGSGF YTYSVDKRGR 600
    PKKTFSEDIL PILADVCQQP QDFDDQTIIQ RVMIPMINEV VLCLEEGIIA 650
    TPQEADMALV YGLGFPPFRG GVFRYLDSVG IGNFVEMAKS YQDLGAMYQV 700
    PQLLLDMAAK GESFYDGQQA SSL 723
    Length:723
    Mass (Da):78,363
    Last modified:February 10, 2009 - v1
    Checksum:i9268B0DFE76F707D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    FM954972 Genomic DNA. Translation: CAV17097.1.
    RefSeqiWP_012602959.1. NC_011753.2.
    YP_002415749.1. NC_011753.2.

    Genome annotation databases

    EnsemblBacteriaiCAV17097; CAV17097; VS_0041.
    GeneIDi7159737.
    KEGGivsp:VS_0041.
    PATRICi20150830. VBIVibSpl48387_1455.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    FM954972 Genomic DNA. Translation: CAV17097.1 .
    RefSeqi WP_012602959.1. NC_011753.2.
    YP_002415749.1. NC_011753.2.

    3D structure databases

    ProteinModelPortali B7VGL4.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 575788.VS_0041.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAV17097 ; CAV17097 ; VS_0041 .
    GeneIDi 7159737.
    KEGGi vsp:VS_0041.
    PATRICi 20150830. VBIVibSpl48387_1455.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00659 .
    BioCyci VSPL575788:GH64-41-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.
    IPR018376. Enoyl-CoA_hyd/isom_CS.
    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.
    PS00166. ENOYL_COA_HYDRATASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Vibrio splendidus str. LGP32 complete genome."
      Mazel D., Le Roux F.
      Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: LGP32.

    Entry informationi

    Entry nameiFADB_VIBSL
    AccessioniPrimary (citable) accession number: B7VGL4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 28, 2009
    Last sequence update: February 10, 2009
    Last modified: October 1, 2014
    This is version 46 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