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Q489W3

- FADB_COLP3

UniProt

Q489W3 - FADB_COLP3

Protein

Fatty acid oxidation complex subunit alpha

Gene

fadB

Organism
Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio psychroerythus)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 68 (01 Oct 2014)
      Sequence version 1 (13 Sep 2005)
      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: TIGR
    2. 3-hydroxybutyryl-CoA epimerase activity Source: TIGR
    3. coenzyme binding Source: InterPro
    4. dodecenoyl-CoA delta-isomerase activity Source: TIGR
    5. enoyl-CoA hydratase activity Source: TIGR

    GO - Biological processi

    1. fatty acid beta-oxidation Source: UniProtKB-UniPathway
    2. fatty acid catabolic process Source: TIGR

    Keywords - Molecular functioni

    Isomerase, Lyase, Oxidoreductase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid degradation, Lipid metabolism

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BioCyciCPSY167879:GI48-393-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:CPS_0393
    OrganismiColwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio psychroerythus)
    Taxonomic identifieri167879 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesColwelliaceaeColwellia
    ProteomesiUP000000547: 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 – 722722Fatty acid oxidation complex subunit alphaPRO_0000109265Add
    BLAST

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    STRINGi167879.CPS_0393.

    Structurei

    3D structure databases

    ProteinModelPortaliQ489W3.
    SMRiQ489W3. Positions 1-715.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 189189Enoyl-CoA hydratase/isomeraseUniRule annotationAdd
    BLAST
    Regioni311 – 7224123-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. 1 hit.
    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. 1 hit.
    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.

    Q489W3-1 [UniParc]FASTAAdd to Basket

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    MIYQGKSLSA QLLEDGIVEF KFDAQGSVNK FDQATFEEYI AVVAAINNCS    50
    EAKGVIVTSG KSTFIVGADI TEFLVSFSQP EDALASWAKK ASDVFDSFED 100
    IQLPTIAAIN GIALGGGCEM TLACDYRVAA TTASIGLPEV KLGLMPGFGG 150
    TVRLPRLIGF DNAATWMSTG KAFKPAAALA QGAIDAVVEP ENLQAAAISM 200
    LKLAIDGKLD WRAKRQPKLE ALKLSPTELI MSSTTCKGMI AAKAGKHYPA 250
    PMVMINTLIA SANLDRTGAM AAENTGFAKL AKTDAATAQI GLFMADQVIK 300
    GKAKKASKLA TKAVNKAAVL GAGIMGGGIA YQSAYKGTPI IMKDINDQAL 350
    DLGLTTATGI LTKQVERGRM NAKKMAGVLN NITPSLSYDS VKDVDIVVEA 400
    VVENPKVKGM VLAEVEGVIG EDAILTSNTS TISIDLLAQS VKRPQNFCGM 450
    HFFNPVNKMP LVEVIRGKDT SDETVAAVVA YAAKMGKSPI VVNDCPGFYV 500
    NRVLFPYFAG FSQLVLEGAD FTAIDKVMEK QFGWPMGPAY LLDVVGVDTA 550
    DHCTGVMSSG FPTRMKKIDN DPVSTLYANE RLGQKNGKGF YDHIKDKRGR 600
    PMKVPAPVAY ELLGQHCADK KDFSSEEIIA RMMIPMVNEV VRCLEEGVVD 650
    TAAEADMGLI YGVGFPPFRG GAIRYLETLG LDNFIAMADK YTDLGEIYHV 700
    TDGLREMAKS GKSYFTTDVK LA 722
    Length:722
    Mass (Da):77,146
    Last modified:September 13, 2005 - v1
    Checksum:iA174E51D6CB6A318
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000083 Genomic DNA. Translation: AAZ26244.1.
    RefSeqiYP_267151.1. NC_003910.7.

    Genome annotation databases

    EnsemblBacteriaiAAZ26244; AAZ26244; CPS_0393.
    GeneIDi3520494.
    KEGGicps:CPS_0393.
    PATRICi21464151. VBIColPsy94388_0340.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000083 Genomic DNA. Translation: AAZ26244.1 .
    RefSeqi YP_267151.1. NC_003910.7.

    3D structure databases

    ProteinModelPortali Q489W3.
    SMRi Q489W3. Positions 1-715.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 167879.CPS_0393.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAZ26244 ; AAZ26244 ; CPS_0393 .
    GeneIDi 3520494.
    KEGGi cps:CPS_0393.
    PATRICi 21464151. VBIColPsy94388_0340.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00659 .
    BioCyci CPSY167879:GI48-393-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_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. 1 hit.
    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 34H / ATCC BAA-681.

    Entry informationi

    Entry nameiFADB_COLP3
    AccessioniPrimary (citable) accession number: Q489W3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 6, 2005
    Last sequence update: September 13, 2005
    Last modified: October 1, 2014
    This is version 68 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