ID Q3ABQ2_CARHZ Unreviewed; 393 AA.
AC Q3ABQ2;
DT 22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2005, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE RecName: Full=Acetyl-CoA acetyltransferase {ECO:0000256|ARBA:ARBA00044137};
DE EC=2.3.1.9 {ECO:0000256|ARBA:ARBA00012705};
DE AltName: Full=Acetoacetyl-CoA thiolase {ECO:0000256|ARBA:ARBA00030755};
GN OrderedLocusNames=CHY_1604 {ECO:0000313|EMBL:ABB16200.1};
OS Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 /
OS Z-2901).
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Carboxydothermus.
OX NCBI_TaxID=246194 {ECO:0000313|EMBL:ABB16200.1, ECO:0000313|Proteomes:UP000002706};
RN [1] {ECO:0000313|EMBL:ABB16200.1, ECO:0000313|Proteomes:UP000002706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-161 / DSM 6008 / Z-2901
RC {ECO:0000313|Proteomes:UP000002706};
RX PubMed=16311624; DOI=10.1371/journal.pgen.0010065;
RA Wu M., Ren Q., Durkin A.S., Daugherty S.C., Brinkac L.M., Dodson R.J.,
RA Madupu R., Sullivan S.A., Kolonay J.F., Haft D.H., Nelson W.C.,
RA Tallon L.J., Jones K.M., Ulrich L.E., Gonzalez J.M., Zhulin I.B.,
RA Robb F.T., Eisen J.A.;
RT "Life in hot carbon monoxide: the complete genome sequence of
RT Carboxydothermus hydrogenoformans Z-2901.";
RL PLoS Genet. 1:563-574(2005).
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000256|ARBA:ARBA00010982, ECO:0000256|RuleBase:RU003557}.
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DR EMBL; CP000141; ABB16200.1; -; Genomic_DNA.
DR RefSeq; WP_011344507.1; NC_007503.1.
DR AlphaFoldDB; Q3ABQ2; -.
DR STRING; 246194.CHY_1604; -.
DR KEGG; chy:CHY_1604; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_0_0_9; -.
DR InParanoid; Q3ABQ2; -.
DR OrthoDB; 56116at2; -.
DR Proteomes; UP000002706; Chromosome.
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; IPR020610; Thiolase_AS.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020613; Thiolase_CS.
DR InterPro; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR18919; ACETYL-COA C-ACYLTRANSFERASE; 1.
DR PANTHER; PTHR18919:SF153; TRIFUNCTIONAL ENZYME SUBUNIT BETA, MITOCHONDRIAL; 1.
DR Pfam; PF02803; Thiolase_C; 1.
DR Pfam; PF00108; Thiolase_N; 1.
DR PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS00098; THIOLASE_1; 1.
DR PROSITE; PS00737; THIOLASE_2; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW ECO:0000313|EMBL:ABB16200.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002706};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:ABB16200.1}.
FT DOMAIN 4..263
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 271..391
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 88
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 349
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 379
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 393 AA; 41602 MW; DE8FEB1E7A91D858 CRC64;
MREVVIVSAA RTPFGKFGGG LSALKAVDLG AIAIKAAVER SGVSPEEFDY VYMGQVLQGG
AGQIPSRQAA RKAGLPWEVP SVTVNKVCAS GLIAVAMAAK MIALGEIDVA VAGGMESMSN
APYILPSARW GQRMFNFEAI DLMVHDGLWC AFYDRHMAVH GSEVAKEYGI SRQAQDEWAY
ISQMRAKEAM EKGRLNDEIV KVEVPGKKGE VVVIEKDEQP RPNTTIEALS KLPPVFDANG
TVTAGNAPGV NDGAGALVLM SREKARELGI KPLATYLNHA EVALDAKYIA TAPGQAINKL
LAKKGMKIEQ IDLLEVNEAF AAVVLVSQKI AGYNLEKVNV NGGAVAFGHP IGASGARILM
TLIYELRRRG GGTGIAAICS GAAQGDAMLI KVE
//