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B7I3P1

- FADB_ACIB5

UniProt

B7I3P1 - FADB_ACIB5

Protein

Fatty acid oxidation complex subunit alpha

Gene

fadB

Organism
Acinetobacter baumannii (strain AB0057)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 44 (01 Oct 2014)
      Sequence version 1 (10 Feb 2009)
      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

    BioCyciABAU480119:GHQY-399-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:AB57_0387
    OrganismiAcinetobacter baumannii (strain AB0057)
    Taxonomic identifieri480119 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacterAcinetobacter calcoaceticus/baumannii complex
    ProteomesiUP000007094: 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_1000186027Add
    BLAST

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    STRINGi480119.AB57_0387.

    Structurei

    3D structure databases

    ProteinModelPortaliB7I3P1.
    SMRiB7I3P1. 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. 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.

    B7I3P1-1 [UniParc]FASTAAdd to Basket

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    MIHAGNAITV QMLADGIAEF RFDLQGESVN KFNRATIEDF KAAIAAVKAN    50
    NDIKGLVVTS GKSTFIVGAD ITEFGQNFAQ GEKAIVDWLM PVHEIFNSFE 100
    DLDLPKVAAI NGMALGGGFE MCLVCDYRVM SEAAQVGLPE IKLGIYPGFG 150
    GSVRLSRLIG IDNAVEWMAM ATPKKPAAAL KDGAVDAVVA ADKLLDAATD 200
    LVKQAISGRL NWKAKRQEKL EAVKLNPLEQ MMAFNTAKGA VLAKANPAQY 250
    PAPKLLLDSL QAGASLARDE ALKAEAEGFA KAAVTPQAEA LIGLFINDQV 300
    VKKASKQHEK GAHPVNQAAV LGAGIMGGGI AYQAASKGTP IIMKDIGNPQ 350
    LALGMKEANN LLTKQVERKK MKPVQMGETL ARIRPTLSYE EFKEVDIVIE 400
    AVTENPKVKE IVLAETEKNV RENTIIASNT STISITRLAK ALQRPENFVG 450
    MHFFNPVHMM PLVEVIRGEK TSEEAIATTV VLAQKMGKTP IVVNDCPGFL 500
    VNRVLFPYFG AFDLLVKDGA DFQQIDNVMS KFGWPMGPAY LIDVVGIDTG 550
    VHGAEVMAEG FPDRMKPDYK GAIEAMYEAK RLGQKNDVGF YKYELDKKGK 600
    KAKTVDPTAY EVIAPFVTGE KREFDNQEII DRMMLALCNE TVRCLEDNIV 650
    ATASEADMAM IMGIGFPPFR GGPCRYIDQT GVAEYVALCD KYAHLGKAYE 700
    APQMLRDMAA NNKKFYG 717
    Length:717
    Mass (Da):77,874
    Last modified:February 10, 2009 - v1
    Checksum:iC8F7CAC439DE6C1B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001182 Genomic DNA. Translation: ACJ39813.1.
    RefSeqiYP_002317796.1. NC_011586.1.

    Genome annotation databases

    EnsemblBacteriaiACJ39813; ACJ39813; AB57_0387.
    GeneIDi7046045.
    KEGGiabn:AB57_0387.
    PATRICi20694593. VBIAciBau111166_0385.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001182 Genomic DNA. Translation: ACJ39813.1 .
    RefSeqi YP_002317796.1. NC_011586.1.

    3D structure databases

    ProteinModelPortali B7I3P1.
    SMRi B7I3P1. Positions 1-717.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 480119.AB57_0387.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACJ39813 ; ACJ39813 ; AB57_0387 .
    GeneIDi 7046045.
    KEGGi abn:AB57_0387.
    PATRICi 20694593. VBIAciBau111166_0385.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00659 .
    BioCyci ABAU480119:GHQY-399-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: AB0057.

    Entry informationi

    Entry nameiFADB_ACIB5
    AccessioniPrimary (citable) accession number: B7I3P1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 28, 2009
    Last sequence update: February 10, 2009
    Last modified: October 1, 2014
    This is version 44 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

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3