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Q9HZJ2

- FADB_PSEAE

UniProt

Q9HZJ2 - FADB_PSEAE

Protein

Fatty acid oxidation complex subunit alpha

Gene

fadB

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      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 sitei297 – 2971SubstrateUniRule annotation
    Binding sitei325 – 3251NAD; via amide nitrogenUniRule annotation
    Binding sitei344 – 3441NADUniRule annotation
    Binding sitei408 – 4081NADUniRule annotation
    Active sitei451 – 4511For 3-hydroxyacyl-CoA dehydrogenase activityUniRule annotation
    Binding sitei454 – 4541NADUniRule annotation
    Binding sitei501 – 5011SubstrateUniRule annotation
    Binding sitei660 – 6601SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi401 – 4033NADUniRule annotation
    Nucleotide bindingi428 – 4303NADUniRule 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

    BioCyciMetaCyc:MONOMER-17591.
    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:PA3014
    OrganismiPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
    Taxonomic identifieri208964 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
    ProteomesiUP000002438: Chromosome

    Organism-specific databases

    PseudoCAPiPA3014.

    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 – 715715Fatty acid oxidation complex subunit alphaPRO_0000109274Add
    BLAST

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    STRINGi208964.PA3014.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9HZJ2.
    SMRiQ9HZJ2. Positions 1-715.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 190190Enoyl-CoA hydratase/isomeraseUniRule annotationAdd
    BLAST
    Regioni312 – 7154043-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.
    PhylomeDBiQ9HZJ2.

    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.

    Q9HZJ2-1 [UniParc]FASTAAdd to Basket

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    MIYQGKAITV KPLEGGIVEL NFDLKGESVN KFNRLTLSEL RAAVDAIKAD    50
    ASVKGVIVTS GKDVFIVGAD ITEFVDNFQL PDEELMAGNL EANKIFSDFE 100
    DLDVPTVAAI NGIALGGGLE MCLAADFRVM SATAKVGLPE VKLGIYPGFG 150
    GTVRLPRLIG CDNAVEWIAS GKENKAEDAL KVGAVDAVVA PEQLQAAALD 200
    LAKRAVAGEL DHKARRQPKL EKLKLNAIEQ MMAFETAKGF VAGQAGPNYP 250
    APVEAIKSIQ KAANFGRDKA LEVEAAGFVK LAKTSVAQSL IGLFLNDQEL 300
    KKKAKKYDEV AKDVKLAAVL GAGIMGGGIA YQSALKGTPI LMKDIREEGI 350
    QMGLNEAAKL LGKRVEKGRL TPAKMAEALN GIRPTMSYGD FGNVDIVVEA 400
    VVENPKVKQA VLAEVEGAVK EDAIIASNTS TISISLLAQA LKRPENFCGM 450
    HFFNPVHMMP LVEVIRGEKT GETAIATTVA YAKKMGKSPI VVNDCPGFLV 500
    NRVLFPYFGG FAKLLSFGVD FVRIDKVMEK FGWPMGPAYL SDVVGIDTGH 550
    HGRDVMAEGF PDRMAVEGKT AVDVMYEANR LGQKNGKGFY AYETDKRGKP 600
    KKVTDPQAYE VLKPIVVEQR EVTDEDIVNF MMIPLCLETV RCLEDGIVET 650
    AAEADMGLIY GIGFPPFRGG ALRYIDSIGV AEFVALADKY AELGALYHPT 700
    AKLREMAKNG QKFFG 715
    Length:715
    Mass (Da):76,954
    Last modified:March 1, 2001 - v1
    Checksum:i7ED8573BE8F31101
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE004091 Genomic DNA. Translation: AAG06402.1.
    PIRiG83269.
    RefSeqiNP_251704.1. NC_002516.2.

    Genome annotation databases

    EnsemblBacteriaiAAG06402; AAG06402; PA3014.
    GeneIDi878680.
    KEGGipae:PA3014.
    PATRICi19840585. VBIPseAer58763_3162.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE004091 Genomic DNA. Translation: AAG06402.1 .
    PIRi G83269.
    RefSeqi NP_251704.1. NC_002516.2.

    3D structure databases

    ProteinModelPortali Q9HZJ2.
    SMRi Q9HZJ2. Positions 1-715.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 208964.PA3014.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAG06402 ; AAG06402 ; PA3014 .
    GeneIDi 878680.
    KEGGi pae:PA3014.
    PATRICi 19840585. VBIPseAer58763_3162.

    Organism-specific databases

    PseudoCAPi PA3014.

    Phylogenomic databases

    eggNOGi COG1250.
    HOGENOMi HOG000261344.
    KOi K01825.
    OMAi NPIVVND.
    OrthoDBi EOG6M9F0M.
    PhylomeDBi Q9HZJ2.

    Enzyme and pathway databases

    UniPathwayi UPA00659 .
    BioCyci MetaCyc:MONOMER-17591.

    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: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.

    Entry informationi

    Entry nameiFADB_PSEAE
    AccessioniPrimary (citable) accession number: Q9HZJ2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 6, 2005
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 95 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