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A5WH99

- FADB_PSYWF

UniProt

A5WH99 - FADB_PSYWF

Protein

Fatty acid oxidation complex subunit alpha

Gene

fadB

Organism
Psychrobacter sp. (strain PRwf-1)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 58 (01 Oct 2014)
      Sequence version 1 (10 Jul 2007)
      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

    BioCyciPPRW349106:GHZF-2148-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:PsycPRwf_2100
    OrganismiPsychrobacter sp. (strain PRwf-1)
    Taxonomic identifieri349106 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaePsychrobacter
    ProteomesiUP000001993: 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 – 719719Fatty acid oxidation complex subunit alphaPRO_1000073634Add
    BLAST

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    STRINGi349106.PsycPRwf_2100.

    Structurei

    3D structure databases

    ProteinModelPortaliA5WH99.
    SMRiA5WH99. Positions 1-716.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 190190Enoyl-CoA hydratase/isomeraseUniRule annotationAdd
    BLAST
    Regioni313 – 7194073-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.
    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.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    A5WH99-1 [UniParc]FASTAAdd to Basket

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    MIYQGNRITV SLLDDGIANM QFNAEGESVN KFDAETNKQF DEAVSALEKA    50
    DNVKGLIVTS SKGVFIAGAD ITEFVSHFNK EAAEIEKWIV DINGVFNRFE 100
    DLPFPKVAAI NGAALGGGCE MTLVCEYRVM GDKAQIGLPE TQLGIFPGFG 150
    GSVRTPRVIG IDNAVELIAT GKAQKPAEAL KLGLVDAVVA QDDLQEAAVD 200
    LVKKCIAGDL DWQAKREEKL QPVKLNQLEQ TMAFSTAKAA IFAKANPKQY 250
    PAPAIAIETI EKHVNLGRDE AIKVEAAGFA KAAKTPQAES LVGLFLNDQT 300
    VKKLAKQHTK NAHDINEAAV LGAGIMGGGI AYQAASKGLP IIMKDIKSEQ 350
    LDLGMGEASK LLGKMVERKK MTPAQMGETL SRIRPTLNYG DFGETDIVIE 400
    AVVENPKVKH AVLKEVEGLV KDNAILASNT STISITYLAT VLERPENFVG 450
    MHFFNPVHRM PLVEVIRGEK SSEEAIATTV ALAQRMGKVP VVVNDCPGFL 500
    VNRVLFPYFG AFDLLLKQGA DFVHVDKVME KFGWPMGPAY LIDVVGLDTG 550
    VHGAEVMAEG FPDRMKPDYK GAIKHLFENN RLGQKNGVGF YKYEKDSRGK 600
    PKKTADDATY ALLKDTTDTD NQQFDDQTII DRMMLAFCNE TVRCLEDNIV 650
    ATPSEADMAM IMGVGFPAFR GGPCRYIDQV GLDNYLALCE KYAHLGKAYE 700
    APQKIRDMAA AGETFYPKA 719
    Length:719
    Mass (Da):78,228
    Last modified:July 10, 2007 - v1
    Checksum:iA736BBCF01D446D7
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000713 Genomic DNA. Translation: ABQ95040.1.
    RefSeqiWP_011961313.1. NC_009524.1.
    YP_001280990.1. NC_009524.1.

    Genome annotation databases

    EnsemblBacteriaiABQ95040; ABQ95040; PsycPRwf_2100.
    GeneIDi5206032.
    KEGGiprw:PsycPRwf_2100.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000713 Genomic DNA. Translation: ABQ95040.1 .
    RefSeqi WP_011961313.1. NC_009524.1.
    YP_001280990.1. NC_009524.1.

    3D structure databases

    ProteinModelPortali A5WH99.
    SMRi A5WH99. Positions 1-716.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 349106.PsycPRwf_2100.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABQ95040 ; ABQ95040 ; PsycPRwf_2100 .
    GeneIDi 5206032.
    KEGGi prw:PsycPRwf_2100.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00659 .
    BioCyci PPRW349106:GHZF-2148-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.
    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.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: PRwf-1.

    Entry informationi

    Entry nameiFADB_PSYWF
    AccessioniPrimary (citable) accession number: A5WH99
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 26, 2008
    Last sequence update: July 10, 2007
    Last modified: October 1, 2014
    This is version 58 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