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A7MQP0

- FADB_CROS8

UniProt

A7MQP0 - FADB_CROS8

Protein

Fatty acid oxidation complex subunit alpha

Gene

fadB

Organism
Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 55 (01 Oct 2014)
      Sequence version 1 (02 Oct 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
    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

    BioCyciCSAK290339:GJ80-3703-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:ESA_03714
    OrganismiCronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii)
    Taxonomic identifieri290339 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeCronobacter
    ProteomesiUP000000260: 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 – 729729Fatty acid oxidation complex subunit alphaPRO_1000069563Add
    BLAST

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    STRINGi290339.ESA_03714.

    Structurei

    3D structure databases

    ProteinModelPortaliA7MQP0.
    SMRiA7MQP0. Positions 1-714.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 189189Enoyl-CoA hydratase/isomeraseUniRule annotationAdd
    BLAST
    Regioni311 – 7294193-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. 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.
    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.

    A7MQP0-1 [UniParc]FASTAAdd to Basket

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    MLYKGDTLYL NWLEDGIAEL VFDAPGSVNK LDTATVASLG HALDVLEKQH    50
    DLKALLLRSE KAAFIVGADI TEFLSLFQVP AEQLSQWLHF ANSVFNRLED 100
    LPVPTLCAIN GYALGGGCEC VLATDFRLAT PDARIGLPET KLGIMPGFGG 150
    SVRLPRLLGA DSALEIIAAG KDITADAALK VGLVDAVVKP EKLIEGALRM 200
    LRQAIDGELD WQARRQPKLE PLRLSKIEAT MSFTIAKGMV MQTAGKHYPA 250
    PMTAVKTIEA AAGLGRDEAL ALENKSFVPL ARSSEARALV GIFLNDQYVK 300
    GLAKKLTKET ETPKQAAVLG AGIMGGGIAY QSAWKGVPVI MKDINEKSLT 350
    LGISEASKLL NKQLERGKID GLKLAGVIAT IHPTLDYAGF ERADVVVEAV 400
    VENPKVKKAV LAETEEKVRP DTVIASNTST IPISELASVL KRPENFCGMH 450
    FFNPVHRMPL VEVIRGEKTS DATIAKVVSW ASKMGKTPIV VNDCPGFFVN 500
    RVLFPYFAGF SQLLRDGADF RQIDKVMEKQ FGWPMGPAYL LDVVGIDTAH 550
    HAQAVMAAGF PQRMQKDYRD AIDALFDAGR FGQKNGKGFY AYQEDSKGKP 600
    RKVPDDAVDS LLAEVSQPKR AFSDEEIVAR MMIPMVNEVV RCLEEGIIAS 650
    PAEADMALVY GLGFPPFHGG AFRWLDTQGS AKYLDMAQHY QHLGPLYEAP 700
    AGLRDKASHN APYYPQVEPA QPVGELQTA 729
    Length:729
    Mass (Da):79,184
    Last modified:October 2, 2007 - v1
    Checksum:i94EAC780BCF49DC1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000783 Genomic DNA. Translation: ABU78911.1.
    RefSeqiWP_012126024.1. NC_009778.1.
    YP_001439747.1. NC_009778.1.

    Genome annotation databases

    EnsemblBacteriaiABU78911; ABU78911; ESA_03714.
    GeneIDi5552271.
    KEGGiesa:ESA_03714.
    PATRICi20399113. VBICroSak107175_3301.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000783 Genomic DNA. Translation: ABU78911.1 .
    RefSeqi WP_012126024.1. NC_009778.1.
    YP_001439747.1. NC_009778.1.

    3D structure databases

    ProteinModelPortali A7MQP0.
    SMRi A7MQP0. Positions 1-714.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 290339.ESA_03714.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABU78911 ; ABU78911 ; ESA_03714 .
    GeneIDi 5552271.
    KEGGi esa:ESA_03714.
    PATRICi 20399113. VBICroSak107175_3301.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00659 .
    BioCyci CSAK290339:GJ80-3703-MONOMER.

    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.
    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. "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic hybridization analysis with other Cronobacter species."
      Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L., Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A., Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K., McClelland M., Forsythe S.J.
      PLoS ONE 5:E9556-E9556(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-894.

    Entry informationi

    Entry nameiFADB_CROS8
    AccessioniPrimary (citable) accession number: A7MQP0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 5, 2008
    Last sequence update: October 2, 2007
    Last modified: October 1, 2014
    This is version 55 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