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Database: UniProt
Entry: A0A0M0GI31_SPOGL
LinkDB: A0A0M0GI31_SPOGL
Original site: A0A0M0GI31_SPOGL 
ID   A0A0M0GI31_SPOGL        Unreviewed;       397 AA.
AC   A0A0M0GI31;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
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   ORFNames=AF332_23510 {ECO:0000313|EMBL:KON89494.1};
OS   Sporosarcina globispora (Bacillus globisporus).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Sporosarcina.
OX   NCBI_TaxID=1459 {ECO:0000313|EMBL:KON89494.1, ECO:0000313|Proteomes:UP000037109};
RN   [1] {ECO:0000313|Proteomes:UP000037109}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4 {ECO:0000313|Proteomes:UP000037109};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA   Shi H., Pan Z., Liu X.;
RT   "Fjat-10036 dsm4.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC       {ECO:0000256|ARBA:ARBA00010982, ECO:0000256|RuleBase:RU003557}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KON89494.1}.
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DR   EMBL; LGUF01000007; KON89494.1; -; Genomic_DNA.
DR   RefSeq; WP_053436860.1; NZ_LGUF01000007.1.
DR   AlphaFoldDB; A0A0M0GI31; -.
DR   STRING; 1459.AF332_23510; -.
DR   PATRIC; fig|1459.3.peg.5186; -.
DR   OrthoDB; 2774224at2; -.
DR   Proteomes; UP000037109; Unassembled WGS sequence.
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; IPR020617; Thiolase_C.
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.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW   ECO:0000313|EMBL:KON89494.1};
KW   Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:KON89494.1}.
FT   DOMAIN          9..266
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          273..394
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
FT   ACT_SITE        93
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        352
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        382
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ   SEQUENCE   397 AA;  42418 MW;  06631802AD555662 CRC64;
     MRWIRKRNVV ITSAVRTPIG TFGGAFKDLL PTDLIVPVLK EAAERSGLQS DEVDEVILGH
     CIQRTDEPNT ARTAALLAGF DDTTTGFTVQ RQCASGMQAI ISAALQIQSG MSDIVIAGGV
     EAMSSSPYVL KQHRWGARMQ HGQITDTVWE ILEDPIHHIM MGETAENLAE IHSITREEQD
     EAALLSHQRA LHAIENGYFD SQIVPITVKS RKGEVTVTKD ENPREDLTAE KLGSLKPVFR
     KGGSVTAGNA SSLNDGGAAL VLMPEELALE KGLKPMAKIV GCSVAGVDPK VMGRGPVPAV
     KKGLANVNWL LEDADLIEVN EAFAAQYLAV EKELGLSRDK VNVSGSGISL GHPIGCTGAR
     LVVSLVHELK RRGGRKGIAS LCVGGGMGAT VFVETYE
//
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