ID   TESB_HAEIN              Reviewed;         286 AA.
AC   P44498;
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 2;
DE            EC=3.1.2.20 {ECO:0000250|UniProtKB:P0AGG2};
DE   AltName: Full=Thioesterase II;
DE            Short=TEII;
GN   Name=tesB; OrderedLocusNames=HI_0076;
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).
CC   -!- FUNCTION: Thioesterase that has relatively broad substrate specificity,
CC       hydrolyzing primarily medium- and long-chain acyl-CoA substrates to
CC       free fatty acids and CoA. {ECO:0000250|UniProtKB:P0AGG2}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a fatty acyl-CoA + H2O = a fatty acid + CoA + H(+);
CC         Xref=Rhea:RHEA:16781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:28868, ChEBI:CHEBI:57287, ChEBI:CHEBI:77636; EC=3.1.2.20;
CC         Evidence={ECO:0000250|UniProtKB:P0AGG2};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16782;
CC         Evidence={ECO:0000250|UniProtKB:P0AGG2};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P0AGG2}.
CC   -!- SIMILARITY: Belongs to the C/M/P thioester hydrolase family.
CC       {ECO:0000305}.
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DR   EMBL; L42023; AAC21752.1; -; Genomic_DNA.
DR   PIR; B64047; B64047.
DR   RefSeq; NP_438249.1; NC_000907.1.
DR   RefSeq; WP_005693846.1; NC_000907.1.
DR   AlphaFoldDB; P44498; -.
DR   SMR; P44498; -.
DR   STRING; 71421.HI_0076; -.
DR   EnsemblBacteria; AAC21752; AAC21752; HI_0076.
DR   KEGG; hin:HI_0076; -.
DR   PATRIC; fig|71421.8.peg.77; -.
DR   eggNOG; COG1946; Bacteria.
DR   HOGENOM; CLU_032690_0_0_6; -.
DR   OMA; SQVWFRT; -.
DR   PhylomeDB; P44498; -.
DR   BioCyc; HINF71421:G1GJ1-77-MON; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0047617; F:acyl-CoA hydrolase activity; IBA:GO_Central.
DR   GO; GO:0006637; P:acyl-CoA metabolic process; IBA:GO_Central.
DR   GO; GO:0009062; P:fatty acid catabolic process; IBA:GO_Central.
DR   Gene3D; 2.40.160.210; -; 1.
DR   InterPro; IPR042171; Acyl-CoA_hotdog.
DR   InterPro; IPR003703; Acyl_CoA_thio.
DR   InterPro; IPR025652; Acyl_CoA_thio_II_dom.
DR   InterPro; IPR029069; HotDog_dom_sf.
DR   PANTHER; PTHR11066; PTHR11066; 1.
DR   Pfam; PF02551; Acyl_CoA_thio; 2.
DR   SUPFAM; SSF54637; SSF54637; 2.
DR   TIGRFAMs; TIGR00189; tesB; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Lipid metabolism; Reference proteome.
FT   CHAIN           1..286
FT                   /note="Acyl-CoA thioesterase 2"
FT                   /id="PRO_0000202146"
FT   ACT_SITE        204
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P0AGG2"
FT   ACT_SITE        228
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P0AGG2"
FT   ACT_SITE        278
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P0AGG2"
SQ   SEQUENCE   286 AA;  32406 MW;  529390BF7189CDD7 CRC64;
     MSDILNNLIH LLKLEKIDDL IFRGESQDLG FRQVFGGQVV AQALSAAMQV APEDRILHSC
     HAYFLAPGDS QYPIIYDVET LREGRNFSAL CVKAIQHKNT ICHVTASFQV PEKGFEHQNT
     MPNVGAPEDF TDENVMLQKV AQTLPEPLNE KFAAERPFEV RTKYLNNPFN GTKLPAEQYS
     WFKTNGETPL DIKIQQCLLA YFSDFHCILT ALHPHEKGFL QKGMKVATID HSIWFHRPFD
     LNHWHLHAIE SNNAFGGRGL AQGQIFSQDG QLIATTQQEG LIRFSE