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B1J5A5

- FADB_PSEPW

UniProt

B1J5A5 - FADB_PSEPW

Protein

Fatty acid oxidation complex subunit alpha

Gene

fadB

Organism
Pseudomonas putida (strain W619)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 56 (01 Oct 2014)
      Sequence version 1 (29 Apr 2008)
      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

    BioCyciPPUT390235:GHHJ-1691-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:PputW619_1652
    OrganismiPseudomonas putida (strain W619)
    Taxonomic identifieri390235 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
    ProteomesiUP000000720: 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 – 715715Fatty acid oxidation complex subunit alphaPRO_1000186046Add
    BLAST

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    STRINGi390235.PputW619_1652.

    Structurei

    3D structure databases

    ProteinModelPortaliB1J5A5.
    SMRiB1J5A5. Positions 1-714.
    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.

    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.

    B1J5A5-1 [UniParc]FASTAAdd to Basket

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    MIYEGKAITV KALESGIVEL KFDLKGESVN KFNRLTLDEL RQAVEAIKAD    50
    ASVKGVIVSS GKDVFIVGAD ITEFVDNFKL PEAELVAGNL EANRIFNAFE 100
    DLEVPTVAAI NGIALGGGLE MCLAADYRVM STSAKIGLPE VKLGIYPGFG 150
    GTVRLPRLIG SDNAIEWIAA GKENRAEDAL KVGAVDAVVA PELLQAGALD 200
    LVKRAISGEL DYKAKRQPKL EKLKLNAIEQ MMAFETAKGF VAGQAGPNYP 250
    APVEAIKSIQ KAANFGRDKA LEVEAAGFAK LAKTSVAQSL IGLFLNDQEL 300
    KRKAKAHDEI AHDVKQAAVL GAGIMGGGIA YQSAVKGTPI LMKDIREEAI 350
    QLGLNEASKL LGNRVEKGRL TPAKMAEALN AIRPTLSYGD FANVDIVVEA 400
    VVENPKVKQA VLAEVEGQVK EDAILASNTS TISINLLAKA LKRPENFVGM 450
    HFFNPVHMMP LVEVIRGEKS SEVAVATTVA YAKKMGKNPI VVNDCPGFLV 500
    NRVLFPYFGG FAKLVSAGVD FVRIDKVMEK FGWPMGPAYL MDVVGIDTGH 550
    HGRDVMAEGF PDRMKDERRS AVDALYEANR LGQKNGKGFY AYETDKRGKP 600
    KKVFDATVLD VLKPIVFEQR EVTDEDIINW MMVPLCLETV RCLEDGIVET 650
    AAEADMGLVY GIGFPPFRGG ALRYIDSIGV AEFVALADQY ADLGPLYHPT 700
    AKLREMAKNG QRFFS 715
    Length:715
    Mass (Da):77,341
    Last modified:April 29, 2008 - v1
    Checksum:i11C060EBD7EAC5DE
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000949 Genomic DNA. Translation: ACA72157.1.
    RefSeqiWP_012313559.1. NC_010501.1.
    YP_001748526.1. NC_010501.1.

    Genome annotation databases

    EnsemblBacteriaiACA72157; ACA72157; PputW619_1652.
    GeneIDi6110598.
    KEGGippw:PputW619_1652.
    PATRICi19953109. VBIPsePut93764_1660.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000949 Genomic DNA. Translation: ACA72157.1 .
    RefSeqi WP_012313559.1. NC_010501.1.
    YP_001748526.1. NC_010501.1.

    3D structure databases

    ProteinModelPortali B1J5A5.
    SMRi B1J5A5. Positions 1-714.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 390235.PputW619_1652.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACA72157 ; ACA72157 ; PputW619_1652 .
    GeneIDi 6110598.
    KEGGi ppw:PputW619_1652.
    PATRICi 19953109. VBIPsePut93764_1660.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00659 .
    BioCyci PPUT390235:GHHJ-1691-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: W619.

    Entry informationi

    Entry nameiFADB_PSEPW
    AccessioniPrimary (citable) accession number: B1J5A5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 28, 2009
    Last sequence update: April 29, 2008
    Last modified: October 1, 2014
    This is version 56 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