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Q6DAP5

- FADB_PECAS

UniProt

Q6DAP5 - FADB_PECAS

Protein

Fatty acid oxidation complex subunit alpha

Gene

fadB

Organism
Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia carotovora subsp. atroseptica)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 79 (01 Oct 2014)
      Sequence version 1 (16 Aug 2004)
      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 sitei324 – 3241NAD; via amide nitrogenUniRule annotation
    Binding sitei343 – 3431NADUniRule annotation
    Binding sitei407 – 4071NADUniRule annotation
    Active sitei450 – 4501For 3-hydroxyacyl-CoA dehydrogenase activityUniRule annotation
    Binding sitei453 – 4531NADUniRule annotation
    Binding sitei500 – 5001SubstrateUniRule annotation
    Binding sitei660 – 6601SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi400 – 4023NADUniRule annotation
    Nucleotide bindingi427 – 4293NADUniRule 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

    BioCyciPATR218491:GJNB-209-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:ECA0208
    OrganismiPectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia carotovora subsp. atroseptica)
    Taxonomic identifieri218491 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaePectobacterium
    ProteomesiUP000007966: Chromosome

    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 – 729729Fatty acid oxidation complex subunit alphaPRO_0000109267Add
    BLAST

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    STRINGi218491.ECA0208.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6DAP5.
    SMRiQ6DAP5. Positions 1-714.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 189189Enoyl-CoA hydratase/isomeraseUniRule annotationAdd
    BLAST
    Regioni311 – 7294193-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.
    OMAiAKGMVMQ.
    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.

    Q6DAP5-1 [UniParc]FASTAAdd to Basket

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    MLYQGESLYL NWLEDGIAEL VFSAPGSVNT LDTRTVASLG KALDVLAEQP    50
    NLKGLLLRSD KPAFIVGADI TEFLSLFAAP AEKLHEWLVF ANSIFNRLED 100
    LPVPTLSAIN SYALGGGCEC VLATDFRLAT PDARIGLPET KLGIMPGFGG 150
    TVRLPRLLGA DSALEIIAAG KDVSAADALK VGLVQAVVAN EKLIPAAIKM 200
    LKQAINGELD WLGYRRPKLE ALKLNKIEAM MSFTTAKAMV LQTAGKHYPA 250
    PMLAVKTIEA AATMTRDEAL QLETQHFVQL ARSNEARALV GIFLNDQYVK 300
    GKAKKLVGET PVPQQAAVLG AGIMGGGIAY QSAFKGVPIR MKDINEKPLA 350
    LGMNEAAKLL NKQMERGKLD GMKMATILAN IHPTLDYAGF ERTDIVVEAV 400
    VENPKIKASV LAETESHISE STILASNTST IPIAVLAAAL KRPQNFCGMH 450
    FFNPVHRMPL VEIIRGPKTS DSTIASVVAY ASKMGKTPIV VNDCPGFFVN 500
    RVLFPYFAAF SLLLRDGADF REIDNAMEKK FGWPMGPAYL LDVVGIDTAH 550
    HAQAVMAEGF PQRMAKDYRD AIDVLFEHQR FGQKNGQGFY RYQTDSKGKQ 600
    RKEQDDAVDA LLKNISQPKK AFSAEEIIAR MMIPMINEVA RCLEEGIVAS 650
    PAEADMALVY GLGFPPFHGG ACRYLDTLGS ERYVEMAQQL AHLGAIYQVP 700
    DGLQQKARSN EGYYPSVAPH ADVSHGQPA 729
    Length:729
    Mass (Da):79,145
    Last modified:August 16, 2004 - v1
    Checksum:i997B1F78B0BD52FB
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX950851 Genomic DNA. Translation: CAG73127.1.
    RefSeqiYP_048335.1. NC_004547.2.

    Genome annotation databases

    EnsemblBacteriaiCAG73127; CAG73127; ECA0208.
    GeneIDi2883864.
    KEGGieca:ECA0208.
    PATRICi20475559. VBIPecAtr54885_0207.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX950851 Genomic DNA. Translation: CAG73127.1 .
    RefSeqi YP_048335.1. NC_004547.2.

    3D structure databases

    ProteinModelPortali Q6DAP5.
    SMRi Q6DAP5. Positions 1-714.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 218491.ECA0208.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAG73127 ; CAG73127 ; ECA0208 .
    GeneIDi 2883864.
    KEGGi eca:ECA0208.
    PATRICi 20475559. VBIPecAtr54885_0207.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00659 .
    BioCyci PATR218491:GJNB-209-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: SCRI 1043 / ATCC BAA-672.

    Entry informationi

    Entry nameiFADB_PECAS
    AccessioniPrimary (citable) accession number: Q6DAP5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 6, 2005
    Last sequence update: August 16, 2004
    Last modified: October 1, 2014
    This is version 79 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