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P28793

- FADB_PSEFR

UniProt

P28793 - FADB_PSEFR

Protein

Fatty acid oxidation complex subunit alpha

Gene

fadB

Organism
Pseudomonas fragi
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 1 (01 Dec 1992)
      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 – 2971Substrate
    Binding sitei325 – 3251NAD; via amide nitrogen
    Binding sitei344 – 3441NAD
    Binding sitei408 – 4081NAD
    Active sitei451 – 4511For 3-hydroxyacyl-CoA dehydrogenase activityUniRule annotation
    Binding sitei454 – 4541NAD
    Binding sitei501 – 5011Substrate
    Binding sitei660 – 6601Substrate

    Regions

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

    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
    6. protein binding Source: IntAct

    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

    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
    Synonyms:faoA
    OrganismiPseudomonas fragi
    Taxonomic identifieri296 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

    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_0000109276Add
    BLAST

    Expressioni

    Inductioni

    By palmitic acid.1 Publication

    Interactioni

    Subunit structurei

    Heterotetramer of two alpha chains (FadB) and two beta chains (FadA).1 PublicationUniRule annotation

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    fadAP287903EBI-1039318,EBI-1039311

    Protein-protein interaction databases

    DIPiDIP-29089N.
    IntActiP28793. 1 interaction.

    Structurei

    Secondary structure

    1
    715
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 127
    Helixi14 – 163
    Beta strandi17 – 226
    Beta strandi27 – 293
    Helixi34 – 4916
    Beta strandi55 – 6713
    Helixi71 – 777
    Helixi82 – 10019
    Beta strandi106 – 1105
    Helixi117 – 1237
    Beta strandi125 – 1317
    Beta strandi135 – 1373
    Helixi139 – 1435
    Turni148 – 1503
    Helixi151 – 1599
    Helixi161 – 17010
    Beta strandi173 – 1753
    Helixi176 – 1816
    Beta strandi184 – 1896
    Helixi191 – 1933
    Helixi194 – 20613
    Beta strandi207 – 2104
    Helixi212 – 2165
    Helixi217 – 2204
    Helixi227 – 24519
    Helixi250 – 26213
    Helixi267 – 28216
    Helixi285 – 30824
    Beta strandi315 – 3206
    Helixi323 – 33513
    Beta strandi340 – 3434
    Helixi347 – 36519
    Turni366 – 3683
    Helixi372 – 38110
    Beta strandi382 – 3887
    Helixi391 – 3933
    Beta strandi395 – 3995
    Helixi405 – 41612
    Beta strandi424 – 4274
    Beta strandi430 – 4323
    Helixi434 – 4374
    Helixi438 – 4403
    Helixi444 – 4463
    Beta strandi447 – 4515
    Turni456 – 4583
    Beta strandi461 – 4666
    Helixi472 – 48413
    Beta strandi488 – 4947
    Turni496 – 4994
    Helixi500 – 51617
    Helixi521 – 53111
    Helixi537 – 5448
    Helixi546 – 55914
    Helixi561 – 5644
    Helixi571 – 5777
    Turni583 – 5864
    Beta strandi587 – 5926
    Beta strandi599 – 6035
    Helixi607 – 6126
    Helixi613 – 6153
    Helixi624 – 64421
    Beta strandi647 – 6504
    Helixi651 – 66111
    Helixi666 – 6683
    Helixi671 – 6788
    Helixi680 – 68910
    Helixi690 – 6934
    Helixi695 – 6973
    Helixi701 – 7088

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1WDKX-ray2.50A/B1-715[»]
    1WDLX-ray3.50A/B1-715[»]
    1WDMX-ray3.80A/B1-715[»]
    2D3TX-ray3.40A/B1-715[»]
    ProteinModelPortaliP28793.
    SMRiP28793. Positions 1-715.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP28793.

    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

    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.

    P28793-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIYEGKAITV TALESGIVEL KFDLKGESVN KFNRLTLNEL RQAVDAIKAD    50
    ASVKGVIVSS GKDVFIVGAD ITEFVENFKL PDAELIAGNL EANKIFSDFE 100
    DLNVPTVAAI NGIALGGGLE MCLAADFRVM ADSAKIGLPE VKLGIYPGFG 150
    GTVRLPRLIG VDNAVEWIAS GKENRAEDAL KVSAVDAVVT ADKLGAAALD 200
    LIKRAISGEL DYKAKRQPKL EKLKLNAIEQ MMAFETAKGF VAGQAGPNYP 250
    APVEAIKTIQ KAANFGRDKA LEVEAAGFAK LAKTSASNCL IGLFLNDQEL 300
    KKKAKVYDKI AKDVKQAAVL GAGIMGGGIA YQSASKGTPI LMKDINEHGI 350
    EQGLAEAAKL LVGRVDKGRM TPAKMAEVLN GIRPTLSYGD FGNVDLVVEA 400
    VVENPKVKQA VLAEVENHVR EDAILASNTS TISISLLAKA LKRPENFVGM 450
    HFFNPVHMMP LVEVIRGEKS SDLAVATTVA YAKKMGKNPI VVNDCPGFLV 500
    NRVLFPYFGG FAKLVSAGVD FVRIDKVMEK FGWPMGPAYL MDVVGIDTGH 550
    HGRDVMAEGF PDRMKDDRRS AIDALYEAKR LGQKNGKGFY AYEADKKGKQ 600
    KKLVDSSVLE VLKPIVYEQR DVTDEDIINW MMIPLCLETV RCLEDGIVET 650
    AAEADMGLVY GIGFPLFRGG ALRYIDSIGV AEFVALADQY AELGALYHPT 700
    AKLREMAKNG QSFFG 715
    Length:715
    Mass (Da):77,137
    Last modified:December 1, 1992 - v1
    Checksum:iF22727CDEF7F3DB5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D10390 Genomic DNA. Translation: BAA01227.1.
    PIRiJX0199.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D10390 Genomic DNA. Translation: BAA01227.1 .
    PIRi JX0199.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1WDK X-ray 2.50 A/B 1-715 [» ]
    1WDL X-ray 3.50 A/B 1-715 [» ]
    1WDM X-ray 3.80 A/B 1-715 [» ]
    2D3T X-ray 3.40 A/B 1-715 [» ]
    ProteinModelPortali P28793.
    SMRi P28793. Positions 1-715.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-29089N.
    IntActi P28793. 1 interaction.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00659 .

    Miscellaneous databases

    EvolutionaryTracei P28793.

    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. "Primary structures of the genes, faoA and faoB, from Pseudomonas fragi B-0771 which encode the two subunits of the HDT multienzyme complex involved in fatty acid beta-oxidation."
      Sato S., Hayashi M., Imamura S., Ozeki Y., Kawaguchi A.
      J. Biochem. 111:8-15(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
      Strain: B-0771.
    2. "Transcription of the faoAB operon which encodes the HDT multienzyme complex involved in fatty acid beta-oxidation in Pseudomonas fragi B-0771."
      Sato S., Ozeki Y., Kawaguchi A.
      J. Biochem. 115:286-292(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    3. "Structural basis for channelling mechanism of a fatty acid beta-oxidation multienzyme complex."
      Ishikawa M., Tsuchiya D., Oyama T., Tsunaka Y., Morikawa K.
      EMBO J. 23:2745-2754(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEXES WITH NAD AND ACYL-COENZYME A, SUBUNIT.

    Entry informationi

    Entry nameiFADB_PSEFR
    AccessioniPrimary (citable) accession number: P28793
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: December 1, 1992
    Last modified: October 1, 2014
    This is version 105 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

    3D-structure, Direct protein sequencing, Multifunctional enzyme

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3