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Protein

Fatty acid oxidation complex subunit alpha

Gene

fadB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 annotation5 Publications

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

    Pathway: fatty acid beta-oxidation

    This protein is involved in the pathway fatty acid beta-oxidation, which is part of Lipid metabolism.UniRule annotation
    View all proteins of this organism that are known to be involved in the pathway fatty acid beta-oxidation and in Lipid metabolism.

    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 activityUniRule annotation2 Publications
    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

    • 3-hydroxyacyl-CoA dehydrogenase activity Source: UniProtKB
    • 3-hydroxybutyryl-CoA epimerase activity Source: UniProtKB
    • dodecenoyl-CoA delta-isomerase activity Source: UniProtKB
    • enoyl-CoA hydratase activity Source: UniProtKB

    GO - Biological processi

    • fatty acid beta-oxidation Source: EcoCyc
    Complete GO annotation...

    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 Componenti: Chromosome UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10279. fadB.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    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.

    Interactioni

    Subunit structurei

    Heterotetramer of two alpha chains (FadB) and two beta chains (FadA).UniRule annotation1 Publication

    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.
    InParanoidiP21177.
    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.
    IPR013328. 6PGD_dom_2.
    IPR029045. ClpP/crotonase-like_dom.
    IPR001753. Crotonase_core_superfam.
    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

            10         20         30         40         50
    MLYKGDTLYL DWLEDGIAEL VFDAPGSVNK LDTATVASLG EAIGVLEQQS
    60 70 80 90 100
    DLKGLLLRSN KAAFIVGADI TEFLSLFLVP EEQLSQWLHF ANSVFNRLED
    110 120 130 140 150
    LPVPTIAAVN GYALGGGCEC VLATDYRLAT PDLRIGLPET KLGIMPGFGG
    160 170 180 190 200
    SVRMPRMLGA DSALEIIAAG KDVGADQALK IGLVDGVVKA EKLVEGAKAV
    210 220 230 240 250
    LRQAINGDLD WKAKRQPKLE PLKLSKIEAT MSFTIAKGMV AQTAGKHYPA
    260 270 280 290 300
    PITAVKTIEA AARFGREEAL NLENKSFVPL AHTNEARALV GIFLNDQYVK
    310 320 330 340 350
    GKAKKLTKDV ETPKQAAVLG AGIMGGGIAY QSAWKGVPVV MKDINDKSLT
    360 370 380 390 400
    LGMTEAAKLL NKQLERGKID GLKLAGVIST IHPTLDYAGF DRVDIVVEAV
    410 420 430 440 450
    VENPKVKKAV LAETEQKVRQ DTVLASNTST IPISELANAL ERPENFCGMH
    460 470 480 490 500
    FFNPVHRMPL VEIIRGEKSS DETIAKVVAW ASKMGKTPIV VNDCPGFFVN
    510 520 530 540 550
    RVLFPYFAGF SQLLRDGADF RKIDKVMEKQ FGWPMGPAYL LDVVGIDTAH
    560 570 580 590 600
    HAQAVMAAGF PQRMQKDYRD AIDALFDANR FGQKNGLGFW RYKEDSKGKP
    610 620 630 640 650
    KKEEDAAVED LLAEVSQPKR DFSEEEIIAR MMIPMVNEVV RCLEEGIIAT
    660 670 680 690 700
    PAEADMALVY GLGFPPFHGG AFRWLDTLGS AKYLDMAQQY QHLGPLYEVP
    710 720
    EGLRNKARHN EPYYPPVEPA RPVGDLKTA
    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:
    EMBLi
    GenBanki
    DDBJi
    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.

    Genome annotation databases

    EnsemblBacteriaiAAC76849; AAC76849; b3846.
    BAE77457; BAE77457; BAE77457.
    GeneIDi948336.
    KEGGiecj:Y75_p3334.
    eco:b3846.
    PATRICi32123189. VBIEscCol129921_3960.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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.

    3D structure databases

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

    Protein-protein interaction databases

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

    Proteomic databases

    PaxDbiP21177.
    PRIDEiP21177.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC76849; AAC76849; b3846.
    BAE77457; BAE77457; BAE77457.
    GeneIDi948336.
    KEGGiecj:Y75_p3334.
    eco:b3846.
    PATRICi32123189. VBIEscCol129921_3960.

    Organism-specific databases

    EchoBASEiEB0275.
    EcoGeneiEG10279. fadB.

    Phylogenomic databases

    eggNOGiCOG1250.
    HOGENOMiHOG000261344.
    InParanoidiP21177.
    KOiK01825.
    OMAiNPIVVND.
    OrthoDBiEOG6M9F0M.
    PhylomeDBiP21177.

    Enzyme and pathway databases

    UniPathwayiUPA00659.
    BioCyciEcoCyc:FADB-MONOMER.
    ECOL316407:JW3822-MONOMER.
    MetaCyc:FADB-MONOMER.

    Miscellaneous databases

    PROiP21177.

    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.
    IPR013328. 6PGD_dom_2.
    IPR029045. ClpP/crotonase-like_dom.
    IPR001753. Crotonase_core_superfam.
    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]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    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: June 24, 2015
    This is version 143 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.