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P77399

- FADJ_ECOLI

UniProt

P77399 - FADJ_ECOLI

Protein

Fatty acid oxidation complex subunit alpha

Gene

fadJ

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 1 (01 Feb 1997)
      Previous versions | rss
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    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. Strongly involved in the anaerobic degradation of long and medium-chain fatty acids in the presence of nitrate and weakly involved in the aerobic degradation of long-chain fatty acids.2 Publications

    Catalytic activityi

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

    Pathwayi

    Sites

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

    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

    BioCyciEcoCyc:G7212-MONOMER.
    ECOL316407:JW2338-MONOMER.
    MetaCyc:G7212-MONOMER.
    UniPathwayiUPA00659.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fatty acid oxidation complex subunit alpha
    Including the following 2 domains:
    Enoyl-CoA hydratase/3-hydroxybutyryl-CoA epimerase (EC:4.2.1.17, EC:5.1.2.3)
    3-hydroxyacyl-CoA dehydrogenase (EC:1.1.1.35)
    Gene namesi
    Name:fadJ
    Synonyms:yfcX
    Ordered Locus Names:b2341, JW2338
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG14127. fadJ.

    Subcellular locationi

    Cytoplasm By similarity

    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_0000109298Add
    BLAST

    Expressioni

    Inductioni

    Unlike the aerobic pathway, the anaerobic pathway is not strongly repressed by FadR regulatory protein.

    Gene expression databases

    GenevestigatoriP77399.

    Interactioni

    Subunit structurei

    Heterotetramer of two alpha chains (FadJ) and two beta chains (FadI).By similarity

    Protein-protein interaction databases

    DIPiDIP-11990N.
    IntActiP77399. 8 interactions.
    STRINGi511145.b2341.

    Structurei

    3D structure databases

    ProteinModelPortaliP77399.
    SMRiP77399. Positions 6-706.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 190190Enoyl-CoA hydrataseAdd
    BLAST
    Regioni306 – 7144093-hydroxyacyl-CoA dehydrogenaseAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG1250.
    HOGENOMiHOG000261346.
    KOiK01782.
    OMAiPFRYMDT.
    OrthoDBiEOG6M9F0M.
    PhylomeDBiP77399.

    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.

    P77399-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEMTSAFTLN VRLDNIAVIT IDVPGEKMNT LKAEFASQVR AIIKQLRENK    50
    ELRGVVFVSA KPDNFIAGAD INMIGNCKTA QEAEALARQG QQLMAEIHAL 100
    PIQVIAAIHG ACLGGGLELA LACHGRVCTD DPKTVLGLPE VQLGLLPGSG 150
    GTQRLPRLIG VSTALEMILT GKQLRAKQAL KLGLVDDVVP HSILLEAAVE 200
    LAKKERPSSR PLPVRERILA GPLGRALLFK MVGKKTEHKT QGNYPATERI 250
    LEVVETGLAQ GTSSGYDAEA RAFGELAMTP QSQALRSIFF ASTDVKKDPG 300
    SDAPPAPLNS VGILGGGLMG GGIAYVTACK AGIPVRIKDI NPQGINHALK 350
    YSWDQLEGKV RRRHLKASER DKQLALISGT TDYRGFAHRD LIIEAVFENL 400
    ELKQQMVAEV EQNCAAHTIF ASNTSSLPIG DIAAHATRPE QVIGLHFFSP 450
    VEKMPLVEII PHAGTSAQTI ATTVKLAKKQ GKTPIVVRDK AGFYVNRILA 500
    PYINEAIRML TQGERVEHID AALVKFGFPV GPIQLLDEVG IDTGTKIIPV 550
    LEAAYGERFS APANVVSSIL NDDRKGRKNG RGFYLYGQKG RKSKKQVDPA 600
    IYPLIGTQGQ GRISAPQVAE RCVMLMLNEA VRCVDEQVIR SVRDGDIGAV 650
    FGIGFPPFLG GPFRYIDSLG AGEVVAIMQR LATQYGSRFT PCERLVEMGA 700
    RGESFWKTTA TDLQ 714
    Length:714
    Mass (Da):77,072
    Last modified:February 1, 1997 - v1
    Checksum:iF4E0A75680039A0D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U00096 Genomic DNA. Translation: AAC75401.1.
    AP009048 Genomic DNA. Translation: BAA16195.1.
    PIRiC65007.
    RefSeqiNP_416843.1. NC_000913.3.
    YP_490583.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75401; AAC75401; b2341.
    BAA16195; BAA16195; BAA16195.
    GeneIDi12931539.
    949097.
    KEGGiecj:Y75_p2307.
    eco:b2341.
    PATRICi32120055. VBIEscCol129921_2437.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U00096 Genomic DNA. Translation: AAC75401.1 .
    AP009048 Genomic DNA. Translation: BAA16195.1 .
    PIRi C65007.
    RefSeqi NP_416843.1. NC_000913.3.
    YP_490583.1. NC_007779.1.

    3D structure databases

    ProteinModelPortali P77399.
    SMRi P77399. Positions 6-706.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-11990N.
    IntActi P77399. 8 interactions.
    STRINGi 511145.b2341.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC75401 ; AAC75401 ; b2341 .
    BAA16195 ; BAA16195 ; BAA16195 .
    GeneIDi 12931539.
    949097.
    KEGGi ecj:Y75_p2307.
    eco:b2341.
    PATRICi 32120055. VBIEscCol129921_2437.

    Organism-specific databases

    EchoBASEi EB3879.
    EcoGenei EG14127. fadJ.

    Phylogenomic databases

    eggNOGi COG1250.
    HOGENOMi HOG000261346.
    KOi K01782.
    OMAi PFRYMDT.
    OrthoDBi EOG6M9F0M.
    PhylomeDBi P77399.

    Enzyme and pathway databases

    UniPathwayi UPA00659 .
    BioCyci EcoCyc:G7212-MONOMER.
    ECOL316407:JW2338-MONOMER.
    MetaCyc:G7212-MONOMER.

    Miscellaneous databases

    PROi P77399.

    Gene expression databases

    Genevestigatori P77399.

    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. "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
      Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T.
      , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
      DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    4. "YfcX enables medium-chain-length poly(3-hydroxyalkanoate) formation from fatty acids in recombinant Escherichia coli fadB strains."
      Snell K.D., Feng F., Zhong L., Martin D., Madison L.L.
      J. Bacteriol. 184:5696-5705(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
      Strain: K12 / MG1655 / ATCC 47076.
    5. "A new Escherichia coli metabolic competency: growth on fatty acids by a novel anaerobic beta-oxidation pathway."
      Campbell J.W., Morgan-Kiss R.M., Cronan J.E. Jr.
      Mol. Microbiol. 47:793-805(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN ANAEROBIC BETA-OXIDATION PATHWAY.
      Strain: K12 / MG1655 / ATCC 47076.

    Entry informationi

    Entry nameiFADJ_ECOLI
    AccessioniPrimary (citable) accession number: P77399
    Secondary accession number(s): Q6KCX2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: February 1, 1997
    Last modified: October 1, 2014
    This is version 131 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. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3