Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

A1ADI8

- FADJ_ECOK1

UniProt

A1ADI8 - FADJ_ECOK1

Protein

Fatty acid oxidation complex subunit alpha

Gene

fadJ

Organism
Escherichia coli O1:K1 / APEC
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 63 (01 Oct 2014)
      Sequence version 1 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalyzes the formation of a hydroxyacyl-CoA by addition of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase and 3-hydroxyacyl-CoA dehydrogenase activities.UniRule annotation

    Catalytic activityi

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei118 – 1181Important for catalytic activityUniRule annotation
    Sitei140 – 1401Important for catalytic activityUniRule annotation

    GO - Molecular functioni

    1. 3-hydroxyacyl-CoA dehydrogenase activity Source: UniProtKB-HAMAP
    2. 3-hydroxybutyryl-CoA epimerase activity Source: UniProtKB-HAMAP
    3. enoyl-CoA hydratase activity Source: UniProtKB-HAMAP
    4. NAD binding Source: InterPro

    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

    UniPathwayiUPA00659.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fatty acid oxidation complex subunit alphaUniRule annotation
    Including the following 2 domains:
    Enoyl-CoA hydratase/3-hydroxybutyryl-CoA epimeraseUniRule annotation (EC:4.2.1.17UniRule annotation, EC:5.1.2.3UniRule annotation)
    3-hydroxyacyl-CoA dehydrogenaseUniRule annotation (EC:1.1.1.35UniRule annotation)
    Gene namesi
    Name:fadJUniRule annotation
    Ordered Locus Names:Ecok1_22340
    ORF Names:APECO1_4225
    OrganismiEscherichia coli O1:K1 / APEC
    Taxonomic identifieri405955 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000008216: Chromosome

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 714714Fatty acid oxidation complex subunit alphaPRO_1000069485Add
    BLAST

    Interactioni

    Subunit structurei

    Heterotetramer of two alpha chains (FadJ) and two beta chains (FadI).UniRule annotation

    Protein-protein interaction databases

    STRINGi405955.APECO1_4225.

    Structurei

    3D structure databases

    ProteinModelPortaliA1ADI8.
    SMRiA1ADI8. Positions 1-707.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 190190Enoyl-CoA hydrataseUniRule annotationAdd
    BLAST
    Regioni306 – 7144093-hydroxyacyl-CoA dehydrogenaseUniRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG1250.
    HOGENOMiHOG000261346.
    KOiK01782.
    OMAiPFRYMDT.
    OrthoDBiEOG6M9F0M.

    Family and domain databases

    Gene3Di1.10.1040.10. 2 hits.
    3.40.50.720. 1 hit.
    3.90.226.10. 1 hit.
    HAMAPiMF_01617. FadJ.
    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.
    IPR012802. FadJ.
    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.
    TIGRFAMsiTIGR02440. FadJ. 1 hit.
    PROSITEiPS00067. 3HCDH. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    A1ADI8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEMASAFTLN VRLDNIAIIT IDVPGEKMNT LKAEFASQVR AIIKQIRENK    50
    ELRGVVFVSA KPDNFIAGAD INMIGNCKTA QEAEVLARQG QQLMAEIHAL 100
    PIPVIAAIHG ACLGGGLELA LACHGRVCTD DPKTVLGLPE VQLGLLPGSG 150
    GTQRLPRLIG VSTALEMILT GKQLRAKQAV KLGLVDDVVP HSILLEAAVE 200
    LAKQDRPSSR PLPVRERILA GPLGRALLFK MVGKKTEHKT QGNYPATERI 250
    LEVVETGLAQ GTSSGYDAEA RAFGELAMTP QSQALRNIFF ASTDVKKDPG 300
    SDAPPAPLNS VGILGGGLMG GGIAYVTACK AGLPVRIKDI NPRGINHALK 350
    YSWDQLEGKV RRRHLKASER DKQLALISGT TDYCGFAHRD LIIEAVFENL 400
    ELKQQMVAEV EQNCATHTIF ASNTSSLPIG DIAAHAARPE QVIGLHFFSP 450
    VEKMPLVEII PHASTSAQTI ATTVKLAKKQ GKTPIVVRDK AGFYVNRILA 500
    PYINEAIRML TEGERIEHID AALVKFGFPV GPIQLLDEVG IDTGTKIMPV 550
    LEAAYGERFS APANVVSSIL NDDRKGRKNG RGFYLYGQKG RKSKKQVDPA 600
    IYPLIGAQGQ GRLSAPQVAE RCVMLMLNEA VRCLDEQVIR SVRDGDIGAV 650
    FGIGFPPFLG GPFRYIDSLG AGEVVAIMQR LATQYGSRFT PCDRLVEMSE 700
    RGESFWKTTA TDLQ 714
    Length:714
    Mass (Da):77,148
    Last modified:January 23, 2007 - v1
    Checksum:iD05212AF62C80111
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000468 Genomic DNA. Translation: ABJ01728.1.
    RefSeqiYP_853442.1. NC_008563.1.

    Genome annotation databases

    EnsemblBacteriaiABJ01728; ABJ01728; APECO1_4225.
    GeneIDi4495596.
    KEGGiecv:APECO1_4225.
    PATRICi18216607. VBIEscCol127180_2565.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000468 Genomic DNA. Translation: ABJ01728.1 .
    RefSeqi YP_853442.1. NC_008563.1.

    3D structure databases

    ProteinModelPortali A1ADI8.
    SMRi A1ADI8. Positions 1-707.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 405955.APECO1_4225.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABJ01728 ; ABJ01728 ; APECO1_4225 .
    GeneIDi 4495596.
    KEGGi ecv:APECO1_4225.
    PATRICi 18216607. VBIEscCol127180_2565.

    Phylogenomic databases

    eggNOGi COG1250.
    HOGENOMi HOG000261346.
    KOi K01782.
    OMAi PFRYMDT.
    OrthoDBi EOG6M9F0M.

    Enzyme and pathway databases

    UniPathwayi UPA00659 .

    Family and domain databases

    Gene3Di 1.10.1040.10. 2 hits.
    3.40.50.720. 1 hit.
    3.90.226.10. 1 hit.
    HAMAPi MF_01617. FadJ.
    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.
    IPR012802. FadJ.
    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 TIGR02440. FadJ. 1 hit.
    PROSITEi PS00067. 3HCDH. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The genome sequence of avian pathogenic Escherichia coli strain O1:K1:H7 shares strong similarities with human extraintestinal pathogenic E. coli genomes."
      Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., Johnson S.J., Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., Nolan L.K.
      J. Bacteriol. 189:3228-3236(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

    Entry informationi

    Entry nameiFADJ_ECOK1
    AccessioniPrimary (citable) accession number: A1ADI8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 5, 2008
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 63 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

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3