ID Q8DV73_STRMU Unreviewed; 409 AA.
AC Q8DV73;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE SubName: Full=Thioesterase {ECO:0000313|EMBL:AAN58367.1};
GN OrderedLocusNames=SMU_633 {ECO:0000313|EMBL:AAN58367.1};
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007 {ECO:0000313|EMBL:AAN58367.1, ECO:0000313|Proteomes:UP000002512};
RN [1] {ECO:0000313|EMBL:AAN58367.1, ECO:0000313|Proteomes:UP000002512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159 {ECO:0000313|Proteomes:UP000002512};
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H., Lin S., Qian Y., Li S., Zhu H.,
RA Najar F., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
CC -!- SIMILARITY: Belongs to the C/M/P thioester hydrolase family.
CC {ECO:0000256|ARBA:ARBA00006538}.
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DR EMBL; AE014133; AAN58367.1; -; Genomic_DNA.
DR RefSeq; NP_721061.1; NC_004350.2.
DR RefSeq; WP_002261908.1; NC_004350.2.
DR AlphaFoldDB; Q8DV73; -.
DR STRING; 210007.SMU_633; -.
DR ESTHER; strmu-SMU.633; Acyl-CoA_Thioesterase.
DR DNASU; 1028069; -.
DR KEGG; smu:SMU_633; -.
DR PATRIC; fig|210007.7.peg.559; -.
DR eggNOG; COG1073; Bacteria.
DR HOGENOM; CLU_029849_3_0_9; -.
DR OrthoDB; 8922993at2; -.
DR PhylomeDB; Q8DV73; -.
DR Proteomes; UP000002512; Chromosome.
DR GO; GO:0016790; F:thiolester hydrolase activity; IEA:InterPro.
DR GO; GO:0006637; P:acyl-CoA metabolic process; IEA:InterPro.
DR Gene3D; 2.60.40.2240; Acyl-CoA thioester hydrolase/BAAT N-terminal domain; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR016662; Acyl-CoA_thioEstase_long-chain.
DR InterPro; IPR014940; BAAT_C.
DR InterPro; IPR006862; Thio_Ohase/aa_AcTrfase.
DR InterPro; IPR042490; Thio_Ohase/BAAT_N.
DR PANTHER; PTHR10824; ACYL-COENZYME A THIOESTERASE-RELATED; 1.
DR PANTHER; PTHR10824:SF4; PROTEIN CBG14567; 1.
DR Pfam; PF08840; BAAT_C; 1.
DR Pfam; PF04775; Bile_Hydr_Trans; 1.
DR PIRSF; PIRSF016521; Acyl-CoA_hydro; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000002512}.
FT DOMAIN 15..144
FT /note="Acyl-CoA thioester hydrolase/bile acid-CoA amino
FT acid N-acetyltransferase"
FT /evidence="ECO:0000259|Pfam:PF04775"
FT DOMAIN 210..406
FT /note="BAAT/Acyl-CoA thioester hydrolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08840"
FT ACT_SITE 239
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR016521-1"
FT ACT_SITE 335
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR016521-1"
FT ACT_SITE 370
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR016521-1"
SQ SEQUENCE 409 AA; 47021 MW; E6EF2A55151F4D10 CRC64;
MLTFKLKSQN NHLADSPFEL IIERLPPCCQ VKVRLDLDHY YNINAPMNLS SQAPWQAEAL
FYSDDKGILD LSESNPYHNL SIMELFFKSQ PIVCKKAKLS QQLESIPLNP FYDLKISIFK
GHSLLGETSV RRYYQLPSIS CLDLNFSRAK GRFFYDKTSS QQPAIIVLSG SDGRIEKAQN
IAQLLASHGF TTLALAYFGL EGLASHLEKI PLEIIQEAID YLKKSPYADS IRLGLYGRSK
GAEFALLAAS HYADFKCLVL NSPSYLCLEG LKQWRNSKTS SWTYQGQELP YHPFLWKDFF
QRLILKKDLK NINHQAVIPV EKINGSLLLL VSKKDEVWDA YGSAITIVNR LQQKRFKYPY
QVESYENCGH MMTVAYQPNH RYKKVALEKI MADTNDSWQK TLVFFRNRL
//
