ID A0A0G3GZM3_9CORY Unreviewed; 398 AA.
AC A0A0G3GZM3;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Probable acetyl-CoA acetyltransferase {ECO:0000256|ARBA:ARBA00040529};
DE EC=2.3.1.9 {ECO:0000256|ARBA:ARBA00012705};
GN Name=pcaF {ECO:0000313|EMBL:AKK04267.1};
GN ORFNames=CEPID_12220 {ECO:0000313|EMBL:AKK04267.1};
OS Corynebacterium epidermidicanis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1050174 {ECO:0000313|EMBL:AKK04267.1, ECO:0000313|Proteomes:UP000035368};
RN [1] {ECO:0000313|EMBL:AKK04267.1, ECO:0000313|Proteomes:UP000035368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45586 {ECO:0000313|EMBL:AKK04267.1,
RC ECO:0000313|Proteomes:UP000035368};
RA Ruckert C., Albersmeier A., Winkler A., Tauch A.;
RT "Complete genome sequence of Corynebacterium epidermidicanis DSM 45586,
RT isolated from the skin of a dog suffering from pruritus.";
RL Submitted (MAY-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}.
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DR EMBL; CP011541; AKK04267.1; -; Genomic_DNA.
DR RefSeq; WP_047241134.1; NZ_CP011541.1.
DR AlphaFoldDB; A0A0G3GZM3; -.
DR STRING; 1050174.CEPID_12220; -.
DR KEGG; cei:CEPID_12220; -.
DR PATRIC; fig|1050174.4.peg.2468; -.
DR OrthoDB; 4475716at2; -.
DR Proteomes; UP000035368; Chromosome.
DR GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; IEA:UniProtKB-EC.
DR CDD; cd00751; thiolase; 1.
DR Gene3D; 3.40.47.10; -; 1.
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:AKK04267.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000035368};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:AKK04267.1}.
FT DOMAIN 4..267
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 276..397
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 354
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 384
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 398 AA; 41235 MW; 2C47D9CDA61BCF69 CRC64;
MAAYLVSGTR TPVGRYGGAL SSVRPDDLAA LVVRQVVEDA GLPPEAVDEV ILGNANGAGE
ENRNVARMAW LLAGFPDSVP GITVNRLCAS GMSAIALATA MVESGQADVV VAGGVESMSR
APWVQAKPEK AFAKPGEIFD TSIGWRFVNP IFAAQEKTTF SMPETAEEVA RRCNISREDA
DAFAVESQAR AIAAIEAGLF EAEITPVPVK DRKGNVTYVS VDEGPRAGTT AEVLARLKPV
VKGGEVVTAG NSSSLNDGAS AIIVASSDAV ERYGLKARAR VVANANVGLE PAVMGLGPIP
ATRKVLERAG WSVDDVDAFE INEAFATQSV ATVRELGLDP ARVNAWGGAI ALGHPLGSSG
SRITLTLLSR LEQSGAERGV ATMCVGVGQG TAIAIERV
//
