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Q6FF68

- FADB_ACIAD

UniProt

Q6FF68 - FADB_ACIAD

Protein

Fatty acid oxidation complex subunit alpha

Gene

fadB

Organism
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 80 (01 Oct 2014)
      Sequence version 1 (19 Jul 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
    Sitei120 – 1201Important for catalytic activityUniRule annotation
    Sitei140 – 1401Important for catalytic activityUniRule annotation
    Binding sitei298 – 2981SubstrateUniRule annotation
    Binding sitei326 – 3261NAD; via amide nitrogenUniRule annotation
    Binding sitei345 – 3451NADUniRule annotation
    Binding sitei409 – 4091NADUniRule annotation
    Active sitei452 – 4521For 3-hydroxyacyl-CoA dehydrogenase activityUniRule annotation
    Binding sitei455 – 4551NADUniRule annotation
    Binding sitei502 – 5021SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi402 – 4043NADUniRule annotation
    Nucleotide bindingi429 – 4313NADUniRule 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

    BioCyciASP62977:GJVV-321-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:ACIAD0335
    OrganismiAcinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
    Taxonomic identifieri62977 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacter
    ProteomesiUP000000430: 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 – 717717Fatty acid oxidation complex subunit alphaPRO_0000109264Add
    BLAST

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    STRINGi62977.ACIAD0335.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6FF68.
    SMRiQ6FF68. Positions 1-717.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 190190Enoyl-CoA hydratase/isomeraseUniRule annotationAdd
    BLAST
    Regioni313 – 7174053-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. 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.
    PS00166. ENOYL_COA_HYDRATASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q6FF68-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIHAGNAITV QMLSDGIAEF RFDLQGESVN KFNRATIEDF QAAIEAVKNH    50
    PEVKGLIVTS AKSTFIVGAD ITEFGQNFAQ GEKAIVEWAL PVHDIFNSFE 100
    DLDIPKVAAI NGMALGGGFE MCLVCDYRVM SDQAQVGLPE IKLGIFPGFG 150
    GTVRLSRLIG IDNAVEWIAM AAPKKPAAAL KDGAVDAVVS ADKLQEAAID 200
    LVKQALAGRV DWKAKRQEKL NPVKLNPLEQ MMAFNTAKGA VLAKANPAQY 250
    PAPKLMLDSL QAGASLGRDE ALKVETEGFA KAAITPQAEA LIGLFLNDQI 300
    IKKTSKKHEK GAHPVNQAAV LGAGIMGGGI AYQAASKGTP IIMKDIGNPQ 350
    LALGMQEANG LLTKQVERKK LTPAKMGETL ARIRPTLSYD EFKEVDIVIE 400
    AVTENPKIKE AVLADTEAKV RDNTIIASNT STISITRLAK ALKRPENFVG 450
    MHFFNPVHMM PLVEVIRGEQ TSEEAVATTV VLAQKMGKTP IVVNDCPGFL 500
    VNRVLFPYFG AFDLLLKDGA DFQQIDKVME KFGWPMGPAY LMDVVGIDTG 550
    VHGAEVMAEG FPDRMKPDYK GSIQTMYEAK RLGQKNDVGF YKYELDKKGK 600
    KAKTVDSTAY EVIAPVVTSE KREFDAQEII DRMMLALCNE TVRCLEDNIV 650
    ATPAEADMAM IMGIGFPPFR GGPCRYIDQT GVAEYVALCN KYAHLGKAYE 700
    APQLLRDMAE NNKKFYG 717
    Length:717
    Mass (Da):77,985
    Last modified:July 19, 2004 - v1
    Checksum:iC0981AB69CA14483
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR543861 Genomic DNA. Translation: CAG67289.1.
    RefSeqiYP_045111.1. NC_005966.1.

    Genome annotation databases

    EnsemblBacteriaiCAG67289; CAG67289; ACIAD0335.
    GeneIDi2881154.
    KEGGiaci:ACIAD0335.
    PATRICi20738624. VBIAciSp98416_0297.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR543861 Genomic DNA. Translation: CAG67289.1 .
    RefSeqi YP_045111.1. NC_005966.1.

    3D structure databases

    ProteinModelPortali Q6FF68.
    SMRi Q6FF68. Positions 1-717.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 62977.ACIAD0335.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAG67289 ; CAG67289 ; ACIAD0335 .
    GeneIDi 2881154.
    KEGGi aci:ACIAD0335.
    PATRICi 20738624. VBIAciSp98416_0297.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00659 .
    BioCyci ASP62977:GJVV-321-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. 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.
    PS00166. ENOYL_COA_HYDRATASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium."
      Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C.
      Nucleic Acids Res. 32:5766-5779(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 33305 / BD413 / ADP1.

    Entry informationi

    Entry nameiFADB_ACIAD
    AccessioniPrimary (citable) accession number: Q6FF68
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 6, 2005
    Last sequence update: July 19, 2004
    Last modified: October 1, 2014
    This is version 80 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