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P21177 (FADB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fatty acid oxidation complex subunit alpha

Including the following 2 domains:

  1. Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase
    EC=4.2.1.17
    EC=5.1.2.3
    EC=5.3.3.8
  2. 3-hydroxyacyl-CoA dehydrogenase
    EC=1.1.1.35
Gene names
Name:fadB
Synonyms:oldB
Ordered Locus Names:b3846, JW3822
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length729 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8 Ref.9 Ref.10 Ref.11 Ref.13

Catalytic activity

(S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH. Ref.9 Ref.10 Ref.11

(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O. Ref.9 Ref.10 Ref.11

(S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA. Ref.9 Ref.10 Ref.11

(3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-CoA. Ref.9 Ref.10 Ref.11

Pathway

Lipid metabolism; fatty acid beta-oxidation. HAMAP-Rule MF_01621

Subunit structure

Heterotetramer of two alpha chains (FadB) and two beta chains (FadA). Ref.8

Induction

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. HAMAP-Rule MF_01621

Sequence similarities

In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.

In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.

Biophysicochemical properties

Kinetic parameters:

KM=53 µM for crotonyl-CoA (for enoyl-CoA hydratase activity) Ref.9 Ref.10 Ref.11

KM=8.7 mM for L-3-hydroxy-4-trans-decenoyl-CoA (for enoyl-CoA hydratase activity)

KM=38 mM for D-3-hydroxy-4-trans-decenoyl-CoA (for enoyl-CoA hydratase activity)

KM=5.8 µM for 3-cis-tetradecenoyl-CoA (for Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase activity)

KM=69 µM for acetoacetyl-CoA (for 3-hydroxyacyl-CoA dehydrogenase activity)

KM=2.0 µM for NADH (for 3-hydroxyacyl-CoA dehydrogenase activity)

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 729729Fatty acid oxidation complex subunit alpha HAMAP-Rule MF_01621
PRO_0000109268

Regions

Nucleotide binding400 – 4023NAD By similarity
Nucleotide binding427 – 4293NAD By similarity
Region1 – 189189Enoyl-CoA hydratase/isomerase HAMAP-Rule MF_01621
Region311 – 7294193-hydroxyacyl-CoA dehydrogenase HAMAP-Rule MF_01621

Sites

Active site4501For 3-hydroxyacyl-CoA dehydrogenase activity Ref.10 Ref.11
Binding site2961Substrate By similarity
Binding site3241NAD; via amide nitrogen Probable
Binding site3431NAD By similarity
Binding site4071NAD By similarity
Binding site4531NAD By similarity
Binding site5001Substrate By similarity
Binding site6601Substrate By similarity
Site1191Important for catalytic activity By similarity
Site1391Important for catalytic activity By similarity

Experimental info

Mutagenesis1161G → 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. Ref.10
Mutagenesis3221G → A: 10-fold increase in KM for NADH. Ref.11
Mutagenesis4501H → A or Q: Almost complete loss of 3-hydroxyacyl-CoA dehydrogenase activity. Ref.11
Sequence conflict5181A → R in AAA23750. Ref.1
Sequence conflict6641F → L in CAB40809. Ref.3
Sequence conflict6661P → A in CAB40809. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P21177 [UniParc].

Last modified August 1, 1992. Version 2.
Checksum: 6F1055E402F6B129

FASTA72979,594
        10         20         30         40         50         60 
MLYKGDTLYL DWLEDGIAEL VFDAPGSVNK LDTATVASLG EAIGVLEQQS DLKGLLLRSN 

        70         80         90        100        110        120 
KAAFIVGADI TEFLSLFLVP EEQLSQWLHF ANSVFNRLED LPVPTIAAVN GYALGGGCEC 

       130        140        150        160        170        180 
VLATDYRLAT PDLRIGLPET KLGIMPGFGG SVRMPRMLGA DSALEIIAAG KDVGADQALK 

       190        200        210        220        230        240 
IGLVDGVVKA EKLVEGAKAV LRQAINGDLD WKAKRQPKLE PLKLSKIEAT MSFTIAKGMV 

       250        260        270        280        290        300 
AQTAGKHYPA PITAVKTIEA AARFGREEAL NLENKSFVPL AHTNEARALV GIFLNDQYVK 

       310        320        330        340        350        360 
GKAKKLTKDV ETPKQAAVLG AGIMGGGIAY QSAWKGVPVV MKDINDKSLT LGMTEAAKLL 

       370        380        390        400        410        420 
NKQLERGKID GLKLAGVIST IHPTLDYAGF DRVDIVVEAV VENPKVKKAV LAETEQKVRQ 

       430        440        450        460        470        480 
DTVLASNTST IPISELANAL ERPENFCGMH FFNPVHRMPL VEIIRGEKSS DETIAKVVAW 

       490        500        510        520        530        540 
ASKMGKTPIV VNDCPGFFVN RVLFPYFAGF SQLLRDGADF RKIDKVMEKQ FGWPMGPAYL 

       550        560        570        580        590        600 
LDVVGIDTAH HAQAVMAAGF PQRMQKDYRD AIDALFDANR FGQKNGLGFW RYKEDSKGKP 

       610        620        630        640        650        660 
KKEEDAAVED LLAEVSQPKR DFSEEEIIAR MMIPMVNEVV RCLEEGIIAT PAEADMALVY 

       670        680        690        700        710        720 
GLGFPPFHGG AFRWLDTLGS AKYLDMAQQY QHLGPLYEVP EGLRNKARHN EPYYPPVEPA 


RPVGDLKTA 

« Hide

References

« Hide 'large scale' references
[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]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA39592.
RefSeqNP_418288.1. NC_000913.3.
YP_491598.1. NC_007779.1.

3D structure databases

ProteinModelPortalP21177.
SMRP21177. Positions 1-714.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-9560N.
IntActP21177. 7 interactions.
STRING511145.b3846.

Proteomic databases

PaxDbP21177.
PRIDEP21177.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76849; AAC76849; b3846.
BAE77457; BAE77457; BAE77457.
GeneID12934454.
948336.
KEGGecj:Y75_p3334.
eco:b3846.
PATRIC32123189. VBIEscCol129921_3960.

Organism-specific databases

EchoBASEEB0275.
EcoGeneEG10279. fadB.

Phylogenomic databases

eggNOGCOG1250.
HOGENOMHOG000261344.
KOK01825.
OMANPIVVND.
OrthoDBEOG6M9F0M.
PhylomeDBP21177.
ProtClustDBPRK11730.

Enzyme and pathway databases

BioCycEcoCyc:FADB-MONOMER.
ECOL316407:JW3822-MONOMER.
MetaCyc:FADB-MONOMER.
UniPathwayUPA00659.

Gene expression databases

GenevestigatorP21177.

Family and domain databases

Gene3D1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
HAMAPMF_01621. FadB.
InterProIPR006180. 3-OHacyl-CoA_DH_CS.
IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
IPR006108. 3HC_DH_C.
IPR008927. 6-PGluconate_DH_C-like.
IPR001753. Crotonase_core_superfam.
IPR013328. DH_multihelical.
IPR018376. Enoyl-CoA_hyd/isom_CS.
IPR012799. FadB.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF00725. 3HCDH. 2 hits.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH. 1 hit.
[Graphical view]
SUPFAMSSF48179. SSF48179. 2 hits.
TIGRFAMsTIGR02437. FadB. 1 hit.
PROSITEPS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROP21177.

Entry information

Entry nameFADB_ECOLI
AccessionPrimary (citable) accession number: P21177
Secondary accession number(s): Q2M8E9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: August 1, 1992
Last modified: April 16, 2014
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene