ID A0A0C1UGJ1_9ACTN Unreviewed; 392 AA.
AC A0A0C1UGJ1;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Probable acetyl-CoA acetyltransferase {ECO:0000256|ARBA:ARBA00040529};
DE EC=2.3.1.9 {ECO:0000256|ARBA:ARBA00012705};
GN ORFNames=MB52_04265 {ECO:0000313|EMBL:KIE50918.1};
OS marine actinobacterium MedAcidi-G1.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1550399 {ECO:0000313|EMBL:KIE50918.1, ECO:0000313|Proteomes:UP000031399};
RN [1] {ECO:0000313|EMBL:KIE50918.1, ECO:0000313|Proteomes:UP000031399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mizuno C.M., Rodriguez-Valera F., Ghai R.;
RT "Novel reconstructed genomes of marine planktonic Acidimicrobiales.";
RL Submitted (SEP-2014) 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:KIE50918.1}.
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DR EMBL; JUEM01000010; KIE50918.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C1UGJ1; -.
DR Proteomes; UP000031399; 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; 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:KIE50918.1};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:KIE50918.1}.
FT DOMAIN 4..261
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 392 AA; 40546 MW; 060EC6BE1E79D5E7 CRC64;
MSPIVILAGA RTPIGRLQGG LKSVSATDLG ANAIKAACNR AGVEPTQIDF SYLGNVISAG
IGQVPARRAA VDAGIPMTSP STLLNRACLS GMHAIHLASQ MVRLQEADIV LAGGMESMTN
SPYMISGARS GLRFGDSELI DSMLFDGLTC TIENCSMGEA TDRFAEELGI SRQDQDTFAA
QSHQRAAKAQ KDGLLNEEIC TVEIPLRNGD NLTVKDDEGI RQDADFESMS RLSPAFTKNG
TITAGNASQI SDGAAAVIVT TMDKAEEIGI EPVAEIVAHG QVAGPDTSLL HQPSSAINVA
LDLAGMKVSD LDLFEINEAF AAVALASMSH LGLSDEIVNV NGGAIALGHP IGMSGTRVVL
TLIHELQRRG GGLGAASLCG GGGQGEALIL KV
//
