ID   YBGC_HAEIN              Reviewed;         136 AA.
AC   P44679;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Acyl-CoA thioesterase YbgC;
DE            EC=3.1.2.-;
GN   Name=ybgC; OrderedLocusNames=HI_0386;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
RN   [2]
RP   FUNCTION, MUTAGENESIS OF ASP-18, ACTIVE SITE, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RX   PubMed=11959124; DOI=10.1016/s0014-5793(02)02533-4;
RA   Zhuang Z., Song F., Martin B.M., Dunaway-Mariano D.;
RT   "The YbgC protein encoded by the ybgC gene of the tol-pal gene cluster of
RT   Haemophilus influenzae catalyzes acyl-coenzyme A thioester hydrolysis.";
RL   FEBS Lett. 516:161-163(2002).
CC   -!- FUNCTION: Displays acyl-CoA thioesterase activity with short chain
CC       aliphatic acyl-CoA thioesters, such as propionyl-CoA and butyryl-CoA.
CC       Enzyme activity is relatively low, suggesting that the acyl-CoA
CC       thioesters used in the assays are not the physiological substrates. Has
CC       no detectable activity with 4-hydroxybenzoyl-CoA, lauroyl-CoA (C12:0),
CC       arachidoyl-CoA (C20:0) and arachidonoyl-CoA (C20:4).
CC       {ECO:0000269|PubMed:11959124}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=11 mM for propionyl-CoA {ECO:0000269|PubMed:11959124};
CC         KM=16 mM for iso-butyryl-CoA {ECO:0000269|PubMed:11959124};
CC         KM=24 mM for n-butyryl-CoA {ECO:0000269|PubMed:11959124};
CC         KM=20 mM for D,L-beta-hydroxybutyryl-CoA
CC         {ECO:0000269|PubMed:11959124};
CC         Note=kcat is 0.44 sec(-1) with propionyl-CoA, 0.54 sec(-1) with iso-
CC         butyryl-CoA and 0.17 sec(-1) with n-butyryl-CoA.;
CC   -!- SIMILARITY: Belongs to the 4-hydroxybenzoyl-CoA thioesterase family.
CC       {ECO:0000305}.
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DR   EMBL; L42023; AAC22044.1; -; Genomic_DNA.
DR   PIR; H64150; H64150.
DR   RefSeq; NP_438547.1; NC_000907.1.
DR   RefSeq; WP_005693784.1; NC_000907.1.
DR   AlphaFoldDB; P44679; -.
DR   SMR; P44679; -.
DR   STRING; 71421.HI_0386; -.
DR   EnsemblBacteria; AAC22044; AAC22044; HI_0386.
DR   KEGG; hin:HI_0386; -.
DR   PATRIC; fig|71421.8.peg.404; -.
DR   eggNOG; COG0824; Bacteria.
DR   HOGENOM; CLU_101141_7_1_6; -.
DR   OMA; YHASYLR; -.
DR   PhylomeDB; P44679; -.
DR   BioCyc; HINF71421:G1GJ1-401-MON; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0047617; F:acyl-CoA hydrolase activity; IBA:GO_Central.
DR   InterPro; IPR008272; HB-CoA_thioesterase_AS.
DR   InterPro; IPR029069; HotDog_dom_sf.
DR   InterPro; IPR006683; Thioestr_dom.
DR   InterPro; IPR014166; Tol-Pal_acyl-CoA_thioesterase.
DR   InterPro; IPR006684; YbgC/YbaW.
DR   Pfam; PF03061; 4HBT; 1.
DR   PIRSF; PIRSF003230; YbgC; 1.
DR   SUPFAM; SSF54637; SSF54637; 1.
DR   TIGRFAMs; TIGR02799; thio_ybgC; 1.
DR   TIGRFAMs; TIGR00051; TIGR00051; 1.
DR   PROSITE; PS01328; 4HBCOA_THIOESTERASE; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..136
FT                   /note="Acyl-CoA thioesterase YbgC"
FT                   /id="PRO_0000087766"
FT   ACT_SITE        18
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10041,
FT                   ECO:0000269|PubMed:11959124"
FT   MUTAGEN         18
FT                   /note="D->N: Abolishes enzyme activity."
FT                   /evidence="ECO:0000269|PubMed:11959124"
SQ   SEQUENCE   136 AA;  15597 MW;  E1D5D2E3F800B261 CRC64;
     MLDNGFSFPV RVYYEDTDAG GVVYHARYLH FFERARTEYL RTLNFTQQTL LEEQQLAFVV
     KTLAIDYCVA AKLDDLLMVE TEVSEVKGAT ILFEQRLMRN TLMLSKATVK VACVDLGKMK
     PVAFPKEVKA AFHHLK