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Q6LW06

- FADB_PHOPR

UniProt

Q6LW06 - FADB_PHOPR

Protein

Fatty acid oxidation complex subunit alpha

Gene

fadB

Organism
Photobacterium profundum (Photobacterium sp. (strain SS9))
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 (05 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
    Sitei119 – 1191Important for catalytic activityUniRule annotation
    Sitei139 – 1391Important for catalytic activityUniRule annotation
    Binding sitei296 – 2961SubstrateUniRule annotation
    Binding sitei324 – 3241NAD; via amide nitrogenUniRule annotation
    Binding sitei343 – 3431NADUniRule annotation
    Binding sitei407 – 4071NADUniRule annotation
    Active sitei450 – 4501For 3-hydroxyacyl-CoA dehydrogenase activityUniRule annotation
    Binding sitei453 – 4531NADUniRule annotation
    Binding sitei500 – 5001SubstrateUniRule annotation
    Binding sitei660 – 6601SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi400 – 4023NADUniRule annotation
    Nucleotide bindingi427 – 4293NADUniRule 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

    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:PBPRA0064
    OrganismiPhotobacterium profundum (Photobacterium sp. (strain SS9))
    Taxonomic identifieri74109 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaePhotobacterium
    ProteomesiUP000000593: Chromosome 1

    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 – 720720Fatty acid oxidation complex subunit alphaPRO_0000109272Add
    BLAST

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    STRINGi298386.PBPRA0064.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6LW06.
    SMRiQ6LW06. Positions 1-715.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 189189Enoyl-CoA hydratase/isomeraseUniRule annotationAdd
    BLAST
    Regioni311 – 7204103-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.
    OMAiNPIVVND.
    OrthoDBiEOG6M9F0M.

    Family and domain databases

    Gene3Di1.10.1040.10. 2 hits.
    3.40.50.720. 1 hit.
    3.90.226.10. 2 hits.
    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.

    Q6LW06-1 [UniParc]FASTAAdd to Basket

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    MIYQGETLSV RYLDDGIAEL NLNAPGAVNK FDLKTLECLN EALNALYQQS    50
    DLKGLLITSD KDAFIVGADI TEFLGLFAKP AEELSQWLTR ANDIFNKLED 100
    LPVPTLSAIN GHALGGGCEC VLATDFRLAD ITARIGLPET RLGIMPGFGG 150
    TVRLPRLLGA DSAMEIITAG KDKKAQDALK LGLVDAVVAP TALKDAALSM 200
    IKDAIAGKLD WQKRRAQKKA PLTLNKIEAT MSFTMAKAMV AQVAGKHYPA 250
    PMTAVIAIEA AARMSRDEAL VVENKHFITL AKTDVAQSLV GIFLNDQYIK 300
    GKAKKAAKEG QPTKKGVVLG AGIMGGGIAY QSALKGVPVL MKDIAVPSLD 350
    LGMAEAAKLL NKQLERGRID GVKMAKVLSG ITPSLHYAGA EDADIVVEAV 400
    VENPKIKAAV LAEVESNVSD TTVIASNTST IPINLLAQSL KRPENFCGMH 450
    FFNPVHRMPL VEIIRGEHTS EETISRVVAY AAKMGKSPIV VNDCPGFFVN 500
    RVLFPYFAGF SLLLRDGADF TQVDKVMEKQ FGWPMGPAYL LDVVGIDTAH 550
    HAQAVMAEGF PDRMGKNYKD AVDVMFEQQR FGQKNGNGFF AYSVDRRGKP 600
    KKNVDPAVAE LLAPVLGAAT DFTSDEIIAR MMIPMINEVV RCLEECIIAT 650
    PAEADMALVY GLGFPPFRGG VFRYIDTLGL AEYVAMADKF AHLGAVYEVP 700
    TGLREKAAKG ESYYTQQVNA 720
    Length:720
    Mass (Da):77,647
    Last modified:July 5, 2004 - v1
    Checksum:i859AC731FF016A06
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR378663 Genomic DNA. Translation: CAG18519.1.
    RefSeqiYP_128321.1. NC_006370.1.

    Genome annotation databases

    EnsemblBacteriaiCAG18519; CAG18519; PBPRA0064.
    GeneIDi3123934.
    KEGGippr:PBPRA0064.
    PATRICi22930758. VBIPhoPro109272_0142.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR378663 Genomic DNA. Translation: CAG18519.1 .
    RefSeqi YP_128321.1. NC_006370.1.

    3D structure databases

    ProteinModelPortali Q6LW06.
    SMRi Q6LW06. Positions 1-715.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 298386.PBPRA0064.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAG18519 ; CAG18519 ; PBPRA0064 .
    GeneIDi 3123934.
    KEGGi ppr:PBPRA0064.
    PATRICi 22930758. VBIPhoPro109272_0142.

    Phylogenomic databases

    eggNOGi COG1250.
    HOGENOMi HOG000261344.
    KOi K01825.
    OMAi NPIVVND.
    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. 2 hits.
    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: SS9.

    Entry informationi

    Entry nameiFADB_PHOPR
    AccessioniPrimary (citable) accession number: Q6LW06
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 6, 2005
    Last sequence update: July 5, 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