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)

B4TQC2

- FADJ_SALSV

UniProt

B4TQC2 - FADJ_SALSV

Protein

Fatty acid oxidation complex subunit alpha

Gene

fadJ

Organism
Salmonella schwarzengrund (strain CVM19633)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 46 (01 Oct 2014)
      Sequence version 1 (23 Sep 2008)
      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

    BioCyciSENT439843:GHHR-1618-MONOMER.
    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:SeSA_A2617
    OrganismiSalmonella schwarzengrund (strain CVM19633)
    Taxonomic identifieri439843 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
    ProteomesiUP000001865: 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 – 715715Fatty acid oxidation complex subunit alphaPRO_1000185954Add
    BLAST

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    STRINGi439843.SeSA_A2617.

    Structurei

    3D structure databases

    ProteinModelPortaliB4TQC2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 190190Enoyl-CoA hydrataseUniRule annotationAdd
    BLAST
    Regioni306 – 7154103-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.
    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. 1 hit.
    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.

    B4TQC2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTTTSAFMLN VRLDNVAVVA IDVPGEKVNT LKAEFAAQVR AILKQIRENK    50
    ALQGVVFISA KADNFIAGAD INMIGHCQNA QEAETLARQG QQLMAEIQAL 100
    PVPVIAAIHG ACLGGGLEMA LACHRRICTD DVKTVLGLPE VQLGLLPGSG 150
    GTQRLPRLVG VSTALDMILT GKQLRARQAL RAGLVDDVVP QTILLEAAVE 200
    LAKKERLAQR TLPVRERILA GPLGRALLFR LVRKKTAQKT QGNYPATERI 250
    IDVIETGLAQ GSSSGYDAEA RAFGELAMTP QSQALRAIFF ASTEVKKDPG 300
    SDAPPGPLNS VGILGGGLMG GGIAWVTACK GGLPVRIKDI NTQGINHALK 350
    YSWDLLETKV RRRHIKASER DKQLALISGS TDYRGFSHRD LVIEAVFEDL 400
    PLKQQMVAEV EQNCAAHTIF ASNTSSLPIG DIAANAARPE QVIGLHFFSP 450
    VEKMPLVEVI PHASTSAQTI ATTVKLAKKQ GKTPIVVSDK AGFYVNRILA 500
    PYINEAIRML TEGERVEHID AALVKFGFPV GPIQLLDEVG IDTGTKIIPV 550
    LEAAYGERFS APANVVASIL NDDRKGRKNG RGFYLYGEKG RKSKKQVDPA 600
    IYKLIGVQGQ SRLSAQQVAD RCVMLMLNEA ARCFDEKVIR SARDGDIGAV 650
    FGIGFPPFLG GPFRYMDALG PGEMVATLQR LAALYGPRYA PCEQLVRMAE 700
    RREHFWTNGE TDQGN 715
    Length:715
    Mass (Da):77,239
    Last modified:September 23, 2008 - v1
    Checksum:i202B08B03511538B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001127 Genomic DNA. Translation: ACF90192.1.
    RefSeqiYP_002115457.1. NC_011094.1.

    Genome annotation databases

    EnsemblBacteriaiACF90192; ACF90192; SeSA_A2617.
    PATRICi32373875. VBISalEnt87589_2675.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001127 Genomic DNA. Translation: ACF90192.1 .
    RefSeqi YP_002115457.1. NC_011094.1.

    3D structure databases

    ProteinModelPortali B4TQC2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 439843.SeSA_A2617.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACF90192 ; ACF90192 ; SeSA_A2617 .
    PATRICi 32373875. VBISalEnt87589_2675.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00659 .
    BioCyci SENT439843:GHHR-1618-MONOMER.

    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. 1 hit.
    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. "Comparative genomics of 28 Salmonella enterica isolates: evidence for CRISPR-mediated adaptive sublineage evolution."
      Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G., Leclerc J.E., Ravel J., Cebula T.A.
      J. Bacteriol. 193:3556-3568(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: CVM19633.

    Entry informationi

    Entry nameiFADJ_SALSV
    AccessioniPrimary (citable) accession number: B4TQC2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 28, 2009
    Last sequence update: September 23, 2008
    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

    Documents

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

    External Data

    Dasty 3