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Protein

Long-chain acyl-CoA thioesterase FadM

Gene

fadM

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Long-chain acyl-CoA thioesterase with a preference for 3,5-tetradecadienoyl-CoA. Could be involved in beta-oxidation of fatty acids.1 Publication

Kineticsi

  1. KM=3.0 µM for 3,5-cis-tetradecadienoyl-CoA1 Publication
  2. KM=10.8 µM for 3,5-cis-dodecadienoyl-CoA1 Publication
  3. KM=5.8 µM for 3-hydroxytetradecanoyl-CoA1 Publication
  4. KM=6.0 µM for palmitoyl-CoA1 Publication
  5. KM=6.3 µM for myristoyl-CoA1 Publication
  6. KM=13.0 µM for lauroyl-CoA1 Publication
  1. Vmax=101.3 µmol/min/mg enzyme with 3,5-cis-tetradecadienoyl-CoA as substrate1 Publication
  2. Vmax=92.3 µmol/min/mg enzyme with 3,5-cis-dodecadienoyl-CoA as substrate1 Publication
  3. Vmax=45.5 µmol/min/mg enzyme with 3-hydroxytetradecanoyl-CoA as substrate1 Publication
  4. Vmax=43.5 µmol/min/mg enzyme with palmitoyl-CoA as substrate1 Publication
  5. Vmax=26.4 µmol/min/mg enzyme with myristoyl-CoA as substrate1 Publication
  6. Vmax=6.9 µmol/min/mg enzyme with lauroyl-CoA as substrate1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei13 – 131Sequence analysis

GO - Molecular functioni

  • acyl-CoA hydrolase activity Source: EcoCyc

GO - Biological processi

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

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BioCyciEcoCyc:G6244-MONOMER.
ECOL316407:JW0433-MONOMER.
MetaCyc:G6244-MONOMER.
BRENDAi3.1.2.20. 2026.

Names & Taxonomyi

Protein namesi
Recommended name:
Long-chain acyl-CoA thioesterase FadM (EC:3.1.2.-)
Alternative name(s):
Acyl-CoA thioester hydrolase
Thioesterase 3
Gene namesi
Name:fadM
Synonyms:tesC, ybaW
Ordered Locus Names:b0443, JW0433
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13251. fadM.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 132132Long-chain acyl-CoA thioesterase FadMPRO_0000168630Add
BLAST

Proteomic databases

PaxDbiP77712.

Expressioni

Inductioni

Up-regulated by growth on oleic acid. Repressed by FadR and by the cyclic AMP receptor protein-cAMP (CRP-cAMP) complex.2 Publications

Interactioni

Subunit structurei

Homotetramer.Curated

Protein-protein interaction databases

BioGridi4259836. 162 interactions.
IntActiP77712. 4 interactions.
STRINGi511145.b0443.

Structurei

Secondary structure

132
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1 – 66Combined sources
Helixi9 – 113Combined sources
Beta strandi16 – 183Combined sources
Helixi20 – 3617Combined sources
Helixi39 – 468Combined sources
Beta strandi49 – 6012Combined sources
Beta strandi69 – 8012Combined sources
Beta strandi83 – 9210Combined sources
Turni93 – 964Combined sources
Beta strandi97 – 11014Combined sources
Turni111 – 1133Combined sources
Beta strandi115 – 1173Combined sources
Turni121 – 1244Combined sources
Helixi125 – 1317Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NJKX-ray1.90A/B/C/D1-132[»]
ProteinModelPortaliP77712.
SMRiP77712. Positions 1-132.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP77712.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4108TGP. Bacteria.
COG0824. LUCA.
HOGENOMiHOG000004132.
InParanoidiP77712.
KOiK12500.
OMAiANININY.
OrthoDBiEOG6JQH7N.

Family and domain databases

Gene3Di3.10.129.10. 1 hit.
InterProiIPR029069. HotDog_dom.
IPR006684. YbgC/YbaW.
[Graphical view]
PIRSFiPIRSF003230. YbgC. 1 hit.
SUPFAMiSSF54637. SSF54637. 1 hit.
TIGRFAMsiTIGR00051. TIGR00051. 1 hit.

Sequencei

Sequence statusi: Complete.

P77712-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQTQIKVRGY HLDVYQHVNN ARYLEFLEEA RWDGLENSDS FQWMTAHNIA
60 70 80 90 100
FVVVNININY RRPAVLSDLL TITSQLQQLN GKSGILSQVI TLEPEGQVVA
110 120 130
DALITFVCID LKTQKALALE GELREKLEQM VK
Length:132
Mass (Da):15,088
Last modified:February 1, 1997 - v1
Checksum:iEBB3539149A37383
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D82943 Genomic DNA. Translation: BAA11647.1.
U82664 Genomic DNA. Translation: AAB40199.1.
U00096 Genomic DNA. Translation: AAC73546.1.
AP009048 Genomic DNA. Translation: BAE76223.1.
PIRiC64774.
RefSeqiNP_414977.1. NC_000913.3.
WP_001194534.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73546; AAC73546; b0443.
BAE76223; BAE76223; BAE76223.
GeneIDi945812.
KEGGiecj:JW0433.
eco:b0443.
PATRICi32116039. VBIEscCol129921_0461.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D82943 Genomic DNA. Translation: BAA11647.1.
U82664 Genomic DNA. Translation: AAB40199.1.
U00096 Genomic DNA. Translation: AAC73546.1.
AP009048 Genomic DNA. Translation: BAE76223.1.
PIRiC64774.
RefSeqiNP_414977.1. NC_000913.3.
WP_001194534.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NJKX-ray1.90A/B/C/D1-132[»]
ProteinModelPortaliP77712.
SMRiP77712. Positions 1-132.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259836. 162 interactions.
IntActiP77712. 4 interactions.
STRINGi511145.b0443.

Proteomic databases

PaxDbiP77712.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73546; AAC73546; b0443.
BAE76223; BAE76223; BAE76223.
GeneIDi945812.
KEGGiecj:JW0433.
eco:b0443.
PATRICi32116039. VBIEscCol129921_0461.

Organism-specific databases

EchoBASEiEB3040.
EcoGeneiEG13251. fadM.

Phylogenomic databases

eggNOGiENOG4108TGP. Bacteria.
COG0824. LUCA.
HOGENOMiHOG000004132.
InParanoidiP77712.
KOiK12500.
OMAiANININY.
OrthoDBiEOG6JQH7N.

Enzyme and pathway databases

BioCyciEcoCyc:G6244-MONOMER.
ECOL316407:JW0433-MONOMER.
MetaCyc:G6244-MONOMER.
BRENDAi3.1.2.20. 2026.

Miscellaneous databases

EvolutionaryTraceiP77712.
PROiP77712.

Family and domain databases

Gene3Di3.10.129.10. 1 hit.
InterProiIPR029069. HotDog_dom.
IPR006684. YbgC/YbaW.
[Graphical view]
PIRSFiPIRSF003230. YbgC. 1 hit.
SUPFAMiSSF54637. SSF54637. 1 hit.
TIGRFAMsiTIGR00051. TIGR00051. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Hatada E., Ohmori H., Qiao Y., Tsuji M., Fukuda R.
    Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  2. "Sequence of minutes 4-25 of Escherichia coli."
    Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "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.
  5. "Identification and characterization of Escherichia coli thioesterase III that functions in fatty acid beta-oxidation."
    Nie L., Ren Y., Schulz H.
    Biochemistry 47:7744-7751(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, IDENTIFICATION BY MASS SPECTROMETRY, INDUCTION.
  6. "A new member of the Escherichia coli fad regulon: transcriptional regulation of fadM (ybaW)."
    Feng Y., Cronan J.E.
    J. Bacteriol. 191:6320-6328(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION, GENE NAME.
    Strain: K12.
  7. "Crystal structure of Escherichia coli hypothetical protein Ybaw."
    Midwest center for structural genomics (MCSG)
    Submitted (JAN-2005) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), SUBUNIT.

Entry informationi

Entry nameiFADM_ECOLI
AccessioniPrimary (citable) accession number: P77712
Secondary accession number(s): Q2MBY3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: January 20, 2016
This is version 118 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, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.