ID A0A0H3GUX4_KLEPH Unreviewed; 392 AA.
AC A0A0H3GUX4;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:AEW63033.1};
GN OrderedLocusNames=KPHS_43350 {ECO:0000313|EMBL:AEW63033.1};
OS Klebsiella pneumoniae subsp. pneumoniae (strain HS11286).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=1125630 {ECO:0000313|EMBL:AEW63033.1, ECO:0000313|Proteomes:UP000007841};
RN [1] {ECO:0000313|EMBL:AEW63033.1, ECO:0000313|Proteomes:UP000007841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HS11286 {ECO:0000313|EMBL:AEW63033.1,
RC ECO:0000313|Proteomes:UP000007841};
RX PubMed=22408243; DOI=10.1128/JB.00043-12;
RA Liu P., Li P., Jiang X., Bi D., Xie Y., Tai C., Deng Z., Rajakumar K.,
RA Ou H.Y.;
RT "Complete genome sequence of Klebsiella pneumoniae subsp. pneumoniae
RT HS11286, a multidrug-resistant strain isolated from human sputum.";
RL J. Bacteriol. 194:1841-1842(2012).
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; CP003200; AEW63033.1; -; Genomic_DNA.
DR RefSeq; WP_002916052.1; NC_016845.1.
DR RefSeq; YP_005228635.1; NC_016845.1.
DR AlphaFoldDB; A0A0H3GUX4; -.
DR SMR; A0A0H3GUX4; -.
DR STRING; 1125630.KPHS_43350; -.
DR GeneID; 11849386; -.
DR KEGG; kpm:KPHS_43350; -.
DR PATRIC; fig|1125630.4.peg.4234; -.
DR HOGENOM; CLU_031026_0_0_6; -.
DR Proteomes; UP000007841; Chromosome.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
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|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU003557};
KW Reference proteome {ECO:0000313|Proteomes:UP000007841};
KW Transferase {ECO:0000256|RuleBase:RU003557}.
FT DOMAIN 4..261
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 270..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 348
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 378
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 392 AA; 41079 MW; 055142E74ABACAE6 CRC64;
MKDVVIVGAL RTPIGCFQGA LSRHSAVELG SVVVKALVEK TGIDPHSVDE VILGQVLTAG
TGQNPARQSA IRGGLPNTVS AITINDVCGS GLKALHLATQ AIQCGEADVV IAGGQENMSR
APHVLTDSRT GAQLGNSQLI DSLVHDGLWD AFNDYHMGVT AENLAREFGI SRELQDAWAL
SSQHKARKAI DSGRFRDEIV PVVTEHNGAA RTVDTDEQPR VDASAEGLAS LQPTFDRLGS
VTAGNASSIN DGAAAVMMMS EAKALELGLP ILARIRAFAS VGVDPALMGI APVHATRRCL
ERAGWRLDDV DLIEANEAFA AQAISVGRVL EWDERRVNVN GGAIALGHPI GASGCRILVS
LVHEMIKRDA RKGLATLCIG GGQGVALAVE RA
//
