YCIA_SHIFL
ID YCIA_SHIFL Reviewed; 132 AA.
AC P0A8Z2; P04379;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-1987, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Acyl-CoA thioester hydrolase YciA;
DE EC=3.1.2.-;
GN Name=yciA; OrderedLocusNames=SF1256, S1342;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
CC -!- FUNCTION: Catalyzes the hydrolysis of the thioester bond in palmitoyl-
CC CoA and malonyl-CoA. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the acyl coenzyme A hydrolase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE005674; AAN42869.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP16754.1; -; Genomic_DNA.
DR RefSeq; NP_707162.1; NC_004337.2.
DR RefSeq; WP_000108160.1; NZ_WPGW01000009.1.
DR AlphaFoldDB; P0A8Z2; -.
DR SMR; P0A8Z2; -.
DR STRING; 198214.SF1256; -.
DR EnsemblBacteria; AAN42869; AAN42869; SF1256.
DR EnsemblBacteria; AAP16754; AAP16754; S1342.
DR GeneID; 1024202; -.
DR GeneID; 66674925; -.
DR KEGG; sfl:SF1256; -.
DR KEGG; sfx:S1342; -.
DR PATRIC; fig|198214.7.peg.1476; -.
DR HOGENOM; CLU_050164_2_0_6; -.
DR OMA; MDEMAFL; -.
DR OrthoDB; 1712258at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; Chromosome.
DR GO; GO:0016790; F:thiolester hydrolase activity; IEA:InterPro.
DR InterPro; IPR040170; Cytosol_ACT.
DR InterPro; IPR033120; HOTDOG_ACOT.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR006683; Thioestr_dom.
DR PANTHER; PTHR11049; PTHR11049; 1.
DR Pfam; PF03061; 4HBT; 1.
DR SUPFAM; SSF54637; SSF54637; 1.
DR PROSITE; PS51770; HOTDOG_ACOT; 1.
PE 3: Inferred from homology;
KW Hydrolase; Reference proteome.
FT CHAIN 1..132
FT /note="Acyl-CoA thioester hydrolase YciA"
FT /id="PRO_0000053821"
FT DOMAIN 8..123
FT /note="HotDog ACOT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01106"
SQ SEQUENCE 132 AA; 14231 MW; EF29C49DBB6B50DA CRC64;
MSTTHNVPQG DLVLRTLAMP ADTNANGDIF GGWLMSQMDI GGAILAKEIA HGRVVTVRVE
GMTFLRPVAV GDVVCCYARC VQKGTTSVSI NIEVWVKKVA SEPIGQRYKA TEALFKYVAV
DPEGKPRALP VE