THLA_CLOD6
ID THLA_CLOD6 Reviewed; 391 AA.
AC Q18AR0;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Acetyl-CoA acetyltransferase {ECO:0000250|UniProtKB:P45359};
DE EC=2.3.1.9 {ECO:0000250|UniProtKB:P45359};
DE AltName: Full=Acetoacetyl-CoA thiolase {ECO:0000250|UniProtKB:P45359};
GN Name=thlA; OrderedLocusNames=CD630_10590;
OS Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Clostridioides.
OX NCBI_TaxID=272563;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=630;
RX PubMed=16804543; DOI=10.1038/ng1830;
RA Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K., Unwin L.,
RA Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.;
RT "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT mobile, mosaic genome.";
RL Nat. Genet. 38:779-786(2006).
RN [2] {ECO:0007744|PDB:4DD5}
RP X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS).
RA Filippova E.V., Wawrzak Z., Kudritska M., Edwards A., Savchenko A.,
RA Anderson W.F.;
RT "Biosynthetic Thiolase (ThlA1) from Clostridium difficile.";
RL Submitted (JAN-2012) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the condensation of two molecules of acetyl-CoA to
CC produce acetoacetyl-CoA. {ECO:0000250|UniProtKB:P45359}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 acetyl-CoA = acetoacetyl-CoA + CoA; Xref=Rhea:RHEA:21036,
CC ChEBI:CHEBI:57286, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.9;
CC Evidence={ECO:0000250|UniProtKB:P45359};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P45359}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P45359}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000305}.
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DR EMBL; AM180355; CAJ67900.1; -; Genomic_DNA.
DR RefSeq; WP_009888868.1; NZ_CP010905.2.
DR RefSeq; YP_001087540.1; NC_009089.1.
DR PDB; 4DD5; X-ray; 1.25 A; A=1-391.
DR PDBsum; 4DD5; -.
DR AlphaFoldDB; Q18AR0; -.
DR SMR; Q18AR0; -.
DR STRING; 272563.CD630_10590; -.
DR PRIDE; Q18AR0; -.
DR EnsemblBacteria; CAJ67900; CAJ67900; CD630_10590.
DR GeneID; 66353490; -.
DR KEGG; cdf:CD630_10590; -.
DR KEGG; pdc:CDIF630_01199; -.
DR PATRIC; fig|272563.120.peg.1099; -.
DR eggNOG; COG0183; Bacteria.
DR OMA; VNQFHGA; -.
DR PhylomeDB; Q18AR0; -.
DR BioCyc; PDIF272563:G12WB-1179-MON; -.
DR Proteomes; UP000001978; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IEA:UniProtKB-EC.
DR CDD; cd00751; thiolase; 1.
DR Gene3D; 3.40.47.10; -; 2.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020615; Thiolase_acyl_enz_int_AS.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020613; Thiolase_CS.
DR InterPro; IPR020616; Thiolase_N.
DR Pfam; PF02803; Thiolase_C; 1.
DR Pfam; PF00108; Thiolase_N; 1.
DR PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1.
DR SUPFAM; SSF53901; SSF53901; 2.
DR TIGRFAMs; TIGR01930; AcCoA-C-Actrans; 1.
DR PROSITE; PS00098; THIOLASE_1; 1.
DR PROSITE; PS00737; THIOLASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..391
FT /note="Acetyl-CoA acetyltransferase"
FT /id="PRO_5000077784"
FT ACT_SITE 88
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000250|UniProtKB:P45359"
FT ACT_SITE 348
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P45359"
FT ACT_SITE 378
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P45359"
FT STRAND 4..11
FT /evidence="ECO:0007829|PDB:4DD5"
FT TURN 20..23
FT /evidence="ECO:0007829|PDB:4DD5"
FT HELIX 26..40
FT /evidence="ECO:0007829|PDB:4DD5"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:4DD5"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:4DD5"
FT HELIX 65..72
FT /evidence="ECO:0007829|PDB:4DD5"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:4DD5"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:4DD5"
FT HELIX 90..103
FT /evidence="ECO:0007829|PDB:4DD5"
FT STRAND 108..118
FT /evidence="ECO:0007829|PDB:4DD5"
FT TURN 126..130
FT /evidence="ECO:0007829|PDB:4DD5"
FT HELIX 142..146
FT /evidence="ECO:0007829|PDB:4DD5"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:4DD5"
FT TURN 151..154
FT /evidence="ECO:0007829|PDB:4DD5"
FT HELIX 157..168
FT /evidence="ECO:0007829|PDB:4DD5"
FT HELIX 172..191
FT /evidence="ECO:0007829|PDB:4DD5"
FT TURN 192..198
FT /evidence="ECO:0007829|PDB:4DD5"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:4DD5"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:4DD5"
FT HELIX 225..230
FT /evidence="ECO:0007829|PDB:4DD5"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:4DD5"
FT TURN 243..245
FT /evidence="ECO:0007829|PDB:4DD5"
FT STRAND 250..260
FT /evidence="ECO:0007829|PDB:4DD5"
FT HELIX 261..267
FT /evidence="ECO:0007829|PDB:4DD5"
FT STRAND 272..282
FT /evidence="ECO:0007829|PDB:4DD5"
FT HELIX 285..290
FT /evidence="ECO:0007829|PDB:4DD5"
FT HELIX 292..303
FT /evidence="ECO:0007829|PDB:4DD5"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:4DD5"
FT STRAND 311..315
FT /evidence="ECO:0007829|PDB:4DD5"
FT HELIX 320..330
FT /evidence="ECO:0007829|PDB:4DD5"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:4DD5"
FT HELIX 343..346
FT /evidence="ECO:0007829|PDB:4DD5"
FT TURN 350..352
FT /evidence="ECO:0007829|PDB:4DD5"
FT HELIX 353..368
FT /evidence="ECO:0007829|PDB:4DD5"
FT STRAND 371..379
FT /evidence="ECO:0007829|PDB:4DD5"
FT TURN 380..382
FT /evidence="ECO:0007829|PDB:4DD5"
FT STRAND 383..390
FT /evidence="ECO:0007829|PDB:4DD5"
SQ SEQUENCE 391 AA; 40860 MW; 7B6713CCC8F70899 CRC64;
MREVVIASAA RTAVGSFGGA FKSVSAVELG VTAAKEAIKR ANITPDMIDE SLLGGVLTAG
LGQNIARQIA LGAGIPVEKP AMTINIVCGS GLRSVSMASQ LIALGDADIM LVGGAENMSM
SPYLVPSARY GARMGDAAFV DSMIKDGLSD IFNNYHMGIT AENIAEQWNI TREEQDELAL
ASQNKAEKAQ AEGKFDEEIV PVVIKGRKGD TVVDKDEYIK PGTTMEKLAK LRPAFKKDGT
VTAGNASGIN DGAAMLVVMA KEKAEELGIE PLATIVSYGT AGVDPKIMGY GPVPATKKAL
EAANMTIEDI DLVEANEAFA AQSVAVIRDL NIDMNKVNVN GGAIAIGHPI GCSGARILTT
LLYEMKRRDA KTGLATLCIG GGMGTTLIVK R
