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P21177

- FADB_ECOLI

UniProt

P21177 - FADB_ECOLI

Protein

Fatty acid oxidation complex subunit alpha

Gene

fadB

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 2 (01 Aug 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.5 PublicationsUniRule 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

    Kineticsi

    1. KM=53 µM for crotonyl-CoA (for enoyl-CoA hydratase activity)3 Publications
    2. KM=8.7 mM for L-3-hydroxy-4-trans-decenoyl-CoA (for enoyl-CoA hydratase activity)3 Publications
    3. KM=38 mM for D-3-hydroxy-4-trans-decenoyl-CoA (for enoyl-CoA hydratase activity)3 Publications
    4. KM=5.8 µM for 3-cis-tetradecenoyl-CoA (for Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase activity)3 Publications
    5. KM=69 µM for acetoacetyl-CoA (for 3-hydroxyacyl-CoA dehydrogenase activity)3 Publications
    6. KM=2.0 µM for NADH (for 3-hydroxyacyl-CoA dehydrogenase activity)3 Publications

    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 nitrogenCurated
    Binding sitei343 – 3431NADUniRule annotation
    Binding sitei407 – 4071NADUniRule annotation
    Active sitei450 – 4501For 3-hydroxyacyl-CoA dehydrogenase activity2 PublicationsUniRule 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
    2. 3-hydroxybutyryl-CoA epimerase activity Source: UniProtKB
    3. coenzyme binding Source: InterPro
    4. dodecenoyl-CoA delta-isomerase activity Source: UniProtKB
    5. enoyl-CoA hydratase activity Source: UniProtKB

    GO - Biological processi

    1. fatty acid beta-oxidation Source: EcoCyc

    Keywords - Molecular functioni

    Isomerase, Lyase, Oxidoreductase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid degradation, Lipid metabolism

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BioCyciEcoCyc:FADB-MONOMER.
    ECOL316407:JW3822-MONOMER.
    MetaCyc:FADB-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
    Synonyms:oldB
    Ordered Locus Names:b3846, JW3822
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10279. fadB.

    Subcellular locationi

    GO - Cellular componenti

    1. fatty acid beta-oxidation multienzyme complex Source: InterPro

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi116 – 1161G → F: Absence of both enoyl-CoA hydratase and 3-hydroxyacyl-CoA epimerase activities. Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase is only slightly affected. 1 Publication
    Mutagenesisi322 – 3221G → A: 10-fold increase in KM for NADH. 1 Publication
    Mutagenesisi450 – 4501H → A or Q: Almost complete loss of 3-hydroxyacyl-CoA dehydrogenase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 729729Fatty acid oxidation complex subunit alphaPRO_0000109268Add
    BLAST

    Proteomic databases

    PaxDbiP21177.
    PRIDEiP21177.

    Expressioni

    Inductioni

    Repressed by FadR in the absence of LCFAs (fatty acids of, at least, 12 carbon atoms). When LCFAs are present in the medium, they are converted to long-chain acyl-CoAs which bind to FadR resulting in its release from the DNA and thus derepression of the transcription.

    Gene expression databases

    GenevestigatoriP21177.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    DIPiDIP-9560N.
    IntActiP21177. 7 interactions.
    STRINGi511145.b3846.

    Structurei

    3D structure databases

    ProteinModelPortaliP21177.
    SMRiP21177. Positions 1-714.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 189189Enoyl-CoA hydratase/isomeraseAdd
    BLAST
    Regioni311 – 7294193-hydroxyacyl-CoA dehydrogenaseAdd
    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.
    PhylomeDBiP21177.

    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.
    IPR018376. Enoyl-CoA_hyd/isom_CS.
    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.
    PS00166. ENOYL_COA_HYDRATASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P21177-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLYKGDTLYL DWLEDGIAEL VFDAPGSVNK LDTATVASLG EAIGVLEQQS    50
    DLKGLLLRSN KAAFIVGADI TEFLSLFLVP EEQLSQWLHF ANSVFNRLED 100
    LPVPTIAAVN GYALGGGCEC VLATDYRLAT PDLRIGLPET KLGIMPGFGG 150
    SVRMPRMLGA DSALEIIAAG KDVGADQALK IGLVDGVVKA EKLVEGAKAV 200
    LRQAINGDLD WKAKRQPKLE PLKLSKIEAT MSFTIAKGMV AQTAGKHYPA 250
    PITAVKTIEA AARFGREEAL NLENKSFVPL AHTNEARALV GIFLNDQYVK 300
    GKAKKLTKDV ETPKQAAVLG AGIMGGGIAY QSAWKGVPVV MKDINDKSLT 350
    LGMTEAAKLL NKQLERGKID GLKLAGVIST IHPTLDYAGF DRVDIVVEAV 400
    VENPKVKKAV LAETEQKVRQ DTVLASNTST IPISELANAL ERPENFCGMH 450
    FFNPVHRMPL VEIIRGEKSS DETIAKVVAW ASKMGKTPIV VNDCPGFFVN 500
    RVLFPYFAGF SQLLRDGADF RKIDKVMEKQ FGWPMGPAYL LDVVGIDTAH 550
    HAQAVMAAGF PQRMQKDYRD AIDALFDANR FGQKNGLGFW RYKEDSKGKP 600
    KKEEDAAVED LLAEVSQPKR DFSEEEIIAR MMIPMVNEVV RCLEEGIIAT 650
    PAEADMALVY GLGFPPFHGG AFRWLDTLGS AKYLDMAQQY QHLGPLYEVP 700
    EGLRNKARHN EPYYPPVEPA RPVGDLKTA 729
    Length:729
    Mass (Da):79,594
    Last modified:August 1, 1992 - v2
    Checksum:i6F1055E402F6B129
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti518 – 5181A → R in AAA23750. (PubMed:1699931)Curated
    Sequence conflicti664 – 6641F → L in CAB40809. (PubMed:2204034)Curated
    Sequence conflicti666 – 6661P → A in CAB40809. (PubMed:2204034)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M59368 Genomic DNA. Translation: AAA23750.1.
    X52837 Genomic DNA. Translation: CAB40809.1.
    M74164 Genomic DNA. Translation: AAA62777.1.
    M87049 Genomic DNA. Translation: AAA67643.1.
    U00096 Genomic DNA. Translation: AAC76849.1.
    AP009048 Genomic DNA. Translation: BAE77457.1.
    PIRiA39592.
    RefSeqiNP_418288.1. NC_000913.3.
    YP_491598.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76849; AAC76849; b3846.
    BAE77457; BAE77457; BAE77457.
    GeneIDi12934454.
    948336.
    KEGGiecj:Y75_p3334.
    eco:b3846.
    PATRICi32123189. VBIEscCol129921_3960.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M59368 Genomic DNA. Translation: AAA23750.1 .
    X52837 Genomic DNA. Translation: CAB40809.1 .
    M74164 Genomic DNA. Translation: AAA62777.1 .
    M87049 Genomic DNA. Translation: AAA67643.1 .
    U00096 Genomic DNA. Translation: AAC76849.1 .
    AP009048 Genomic DNA. Translation: BAE77457.1 .
    PIRi A39592.
    RefSeqi NP_418288.1. NC_000913.3.
    YP_491598.1. NC_007779.1.

    3D structure databases

    ProteinModelPortali P21177.
    SMRi P21177. Positions 1-714.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-9560N.
    IntActi P21177. 7 interactions.
    STRINGi 511145.b3846.

    Proteomic databases

    PaxDbi P21177.
    PRIDEi P21177.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76849 ; AAC76849 ; b3846 .
    BAE77457 ; BAE77457 ; BAE77457 .
    GeneIDi 12934454.
    948336.
    KEGGi ecj:Y75_p3334.
    eco:b3846.
    PATRICi 32123189. VBIEscCol129921_3960.

    Organism-specific databases

    EchoBASEi EB0275.
    EcoGenei EG10279. fadB.

    Phylogenomic databases

    eggNOGi COG1250.
    HOGENOMi HOG000261344.
    KOi K01825.
    OMAi NPIVVND.
    OrthoDBi EOG6M9F0M.
    PhylomeDBi P21177.

    Enzyme and pathway databases

    UniPathwayi UPA00659 .
    BioCyci EcoCyc:FADB-MONOMER.
    ECOL316407:JW3822-MONOMER.
    MetaCyc:FADB-MONOMER.

    Miscellaneous databases

    PROi P21177.

    Gene expression databases

    Genevestigatori P21177.

    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.
    IPR018376. Enoyl-CoA_hyd/isom_CS.
    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.
    PS00166. ENOYL_COA_HYDRATASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Primary sequence of the Escherichia coli fadBA operon, encoding the fatty acid-oxidizing multienzyme complex, indicates a high degree of homology to eucaryotic enzymes."
      Dirusso C.C.
      J. Bacteriol. 172:6459-6468(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Nucleotide sequence of the fadA gene. Primary structure of 3-ketoacyl-coenzyme A thiolase from Escherichia coli and the structural organization of the fadAB operon."
      Yang S.-Y., Yang X.-Y.H., Healy-Louie G., Schulz H., Elzinga M.
      J. Biol. Chem. 265:10424-10429(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10.
      Strain: K12.
    3. "Nucleotide sequence of the fadA and fadB genes from Escherichia coli."
      Nakahigashi K., Inokuchi H.
      Nucleic Acids Res. 18:4937-4937(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    4. "Nucleotide sequence of the promoter and fadB gene of the fadBA operon and primary structure of the multifunctional fatty acid oxidation protein from Escherichia coli."
      Yang X.Y.H., Schulz H., Elzinga M., Yang S.Y.
      Biochemistry 30:6788-6795(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes."
      Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.
      Science 257:771-778(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    7. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    8. "Five different enzymatic activities are associated with the multienzyme complex of fatty acid oxidation from Escherichia coli."
      Pramanik A., Pawar S., Antonian E., Schulz H.
      J. Bacteriol. 137:469-473(1979) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT.
    9. "Epimerization of 3-hydroxy-4-trans-decenoyl coenzyme A by a dehydration/hydration mechanism catalyzed by the multienzyme complex of fatty acid oxidation from Escherichia coli."
      Smeland T.E., Cuebas D., Schulz H.
      J. Biol. Chem. 266:23904-23908(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS AN EPIMERASE AND HYDRATASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    10. "Association of both enoyl coenzyme A hydratase and 3-hydroxyacyl coenzyme A epimerase with an active site in the amino-terminal domain of the multifunctional fatty acid oxidation protein from Escherichia coli."
      Yang S.Y., Elzinga M.
      J. Biol. Chem. 268:6588-6592(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS AN EPIMERASE AND HYDRATASE, CATALYTIC ACTIVITY, ACTIVE SITE, MUTAGENESIS OF GLY-116, BIOPHYSICOCHEMICAL PROPERTIES.
    11. "Histidine-450 is the catalytic residue of L-3-hydroxyacyl coenzyme A dehydrogenase associated with the large alpha-subunit of the multienzyme complex of fatty acid oxidation from Escherichia coli."
      He X.Y., Yang S.Y.
      Biochemistry 35:9625-9630(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A DEHYDROGENASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE, NAD-BINDING, MUTAGENESIS OF GLY-322 AND HIS-450.
    12. "Escherichia coli proteome analysis using the gene-protein database."
      VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
      Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY 2D-GEL.
    13. "A new Escherichia coli metabolic competency: growth on fatty acids by a novel anaerobic beta-oxidation pathway."
      Campbell J.W., Morgan-Kiss R.M., Cronan J.E. Jr.
      Mol. Microbiol. 47:793-805(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN ANAEROBIC BETA-OXIDATION PATHWAY.
      Strain: K12 / MG1655 / ATCC 47076.

    Entry informationi

    Entry nameiFADB_ECOLI
    AccessioniPrimary (citable) accession number: P21177
    Secondary accession number(s): Q2M8E9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1991
    Last sequence update: August 1, 1992
    Last modified: October 1, 2014
    This is version 137 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3