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Protein

Acyl-CoA thioester hydrolase YbgC

Gene

ybgC

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

Functioni

Thioesterase that appears to be involved in phospholipid metabolism. Some specific acyl-ACPs could be physiological substrates. Displays acyl-CoA thioesterase activity on malonyl-CoA in vitro, catalyzing the hydrolysis of the thioester bond.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei18 – 181PROSITE-ProRule annotation

GO - Molecular functioni

  • thiolester hydrolase activity Source: EcoCyc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid metabolism

Enzyme and pathway databases

BioCyciEcoCyc:EG11110-MONOMER.
ECOL316407:JW0726-MONOMER.
BRENDAi3.1.2.2. 2026.

Names & Taxonomyi

Protein namesi
Recommended name:
Acyl-CoA thioester hydrolase YbgC (EC:3.1.2.-)
Short name:
Acyl-CoA thioesterase
Gene namesi
Name:ybgC
Ordered Locus Names:b0736, JW0726
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11110. ybgC.

Subcellular locationi

  • Cell inner membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 134134Acyl-CoA thioester hydrolase YbgCPRO_0000087762Add
BLAST

Proteomic databases

PaxDbiP0A8Z3.

Interactioni

Subunit structurei

Interacts with ACP, PlsB and PssA, forming altogether a complex at the inner membrane.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
acpPP0A6A86EBI-543276,EBI-542566
espPO325912EBI-543276,EBI-852989From a different organism.
secAP104082EBI-543276,EBI-543213

Protein-protein interaction databases

BioGridi4259452. 197 interactions.
DIPiDIP-29375N.
IntActiP0A8Z3. 11 interactions.
MINTiMINT-1222012.
STRINGi511145.b0736.

Structurei

Secondary structure

1
134
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 116Combined sources
Helixi14 – 163Combined sources
Beta strandi21 – 233Combined sources
Helixi25 – 4218Combined sources
Helixi47 – 526Combined sources
Beta strandi56 – 6611Combined sources
Beta strandi75 – 8511Combined sources
Beta strandi87 – 9711Combined sources
Beta strandi103 – 11513Combined sources
Turni116 – 1194Combined sources
Helixi126 – 1316Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1S5UX-ray1.70A/B/C/D/E/F/G/H1-134[»]
ProteinModelPortaliP0A8Z3.
SMRiP0A8Z3. Positions 1-134.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A8Z3.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4107YD3. Bacteria.
COG0824. LUCA.
HOGENOMiHOG000004132.
InParanoidiP0A8Z3.
KOiK07107.
OMAiELGFAQS.
OrthoDBiEOG6JQH7N.
PhylomeDBiP0A8Z3.

Family and domain databases

Gene3Di3.10.129.10. 1 hit.
InterProiIPR008272. HB-CoA_thioesterase_AS.
IPR029069. HotDog_dom.
IPR006683. Thioestr_dom.
IPR014166. Tol-Pal_acyl-CoA_thioesterase.
IPR006684. YbgC/YbaW.
[Graphical view]
PfamiPF03061. 4HBT. 1 hit.
[Graphical view]
PIRSFiPIRSF003230. YbgC. 1 hit.
SUPFAMiSSF54637. SSF54637. 1 hit.
TIGRFAMsiTIGR02799. thio_ybgC. 1 hit.
TIGR00051. TIGR00051. 1 hit.
PROSITEiPS01328. 4HBCOA_THIOESTERASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0A8Z3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNTTLFRWPV RVYYEDTDAG GVVYHASYVA FYERARTEML RHHHFSQQAL
60 70 80 90 100
MAERVAFVVR KMTVEYYAPA RLDDMLEIQT EITSMRGTSL VFTQRIVNAE
110 120 130
NTLLNEAEVL VVCVDPLKMK PRALPKSIVA EFKQ
Length:134
Mass (Da):15,562
Last modified:June 21, 2005 - v1
Checksum:iC44582B6EC3BE989
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M16489 Genomic DNA. Translation: AAA83918.1.
U00096 Genomic DNA. Translation: AAC73830.1.
AP009048 Genomic DNA. Translation: BAA35402.1.
U30934 Genomic DNA. Translation: AAA74398.1.
PIRiA25980. WMEC15.
RefSeqiNP_415264.1. NC_000913.3.
WP_001098384.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73830; AAC73830; b0736.
BAA35402; BAA35402; BAA35402.
GeneIDi948907.
KEGGiecj:JW0726.
eco:b0736.
PATRICi32116671. VBIEscCol129921_0768.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M16489 Genomic DNA. Translation: AAA83918.1.
U00096 Genomic DNA. Translation: AAC73830.1.
AP009048 Genomic DNA. Translation: BAA35402.1.
U30934 Genomic DNA. Translation: AAA74398.1.
PIRiA25980. WMEC15.
RefSeqiNP_415264.1. NC_000913.3.
WP_001098384.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1S5UX-ray1.70A/B/C/D/E/F/G/H1-134[»]
ProteinModelPortaliP0A8Z3.
SMRiP0A8Z3. Positions 1-134.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259452. 197 interactions.
DIPiDIP-29375N.
IntActiP0A8Z3. 11 interactions.
MINTiMINT-1222012.
STRINGi511145.b0736.

Proteomic databases

PaxDbiP0A8Z3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73830; AAC73830; b0736.
BAA35402; BAA35402; BAA35402.
GeneIDi948907.
KEGGiecj:JW0726.
eco:b0736.
PATRICi32116671. VBIEscCol129921_0768.

Organism-specific databases

EchoBASEiEB1101.
EcoGeneiEG11110. ybgC.

Phylogenomic databases

eggNOGiENOG4107YD3. Bacteria.
COG0824. LUCA.
HOGENOMiHOG000004132.
InParanoidiP0A8Z3.
KOiK07107.
OMAiELGFAQS.
OrthoDBiEOG6JQH7N.
PhylomeDBiP0A8Z3.

Enzyme and pathway databases

BioCyciEcoCyc:EG11110-MONOMER.
ECOL316407:JW0726-MONOMER.
BRENDAi3.1.2.2. 2026.

Miscellaneous databases

EvolutionaryTraceiP0A8Z3.
PROiP0A8Z3.

Family and domain databases

Gene3Di3.10.129.10. 1 hit.
InterProiIPR008272. HB-CoA_thioesterase_AS.
IPR029069. HotDog_dom.
IPR006683. Thioestr_dom.
IPR014166. Tol-Pal_acyl-CoA_thioesterase.
IPR006684. YbgC/YbaW.
[Graphical view]
PfamiPF03061. 4HBT. 1 hit.
[Graphical view]
PIRSFiPIRSF003230. YbgC. 1 hit.
SUPFAMiSSF54637. SSF54637. 1 hit.
TIGRFAMsiTIGR02799. thio_ybgC. 1 hit.
TIGR00051. TIGR00051. 1 hit.
PROSITEiPS01328. 4HBCOA_THIOESTERASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of a gene cluster involved in entry of E colicins and single-stranded DNA of infecting filamentous bacteriophages into Escherichia coli."
    Sun T.-P., Webster R.E.
    J. Bacteriol. 169:2667-2674(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-20.
    Strain: K12 / MG1655 / ATCC 47076.
  6. "Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite chromatography."
    Fountoulakis M., Takacs M.-F., Berndt P., Langen H., Takacs B.
    Electrophoresis 20:2181-2195(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: B / BL21.
  7. "Enzyme genomics: application of general enzymatic screens to discover new enzymes."
    Kuznetsova E., Proudfoot M., Sanders S.A., Reinking J., Savchenko A., Arrowsmith C.H., Edwards A.M., Yakunin A.F.
    FEMS Microbiol. Rev. 29:263-279(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACYL-COA THIOESTERASE ACTIVITY.
  8. "A protein network for phospholipid synthesis uncovered by a variant of the tandem affinity purification method in Escherichia coli."
    Gully D., Bouveret E.
    Proteomics 6:282-293(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHOLIPID METABOLISM, SUBCELLULAR LOCATION, INTERACTION WITH ACP; PLSB AND PSSA.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  9. "Crystal structure of hypothetical protein Ec709 from Escherichia coli."
    Kim Y., Joachimiak A., Skarina T., Savchenko A., Edwards A.M.
    Submitted (MAY-2004) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).

Entry informationi

Entry nameiYBGC_ECOLI
AccessioniPrimary (citable) accession number: P0A8Z3
Secondary accession number(s): P08999
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: June 21, 2005
Last modified: March 16, 2016
This is version 91 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.