ID A0A1C5IF35_9ACTN Unreviewed; 430 AA.
AC A0A1C5IF35;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Acetyl-CoA C-acetyltransferase {ECO:0000313|EMBL:SCG56874.1};
GN ORFNames=GA0070213_105389 {ECO:0000313|EMBL:SCG56874.1};
OS Micromonospora humi.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=745366 {ECO:0000313|EMBL:SCG56874.1, ECO:0000313|Proteomes:UP000199360};
RN [1] {ECO:0000313|EMBL:SCG56874.1, ECO:0000313|Proteomes:UP000199360}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45647 {ECO:0000313|EMBL:SCG56874.1,
RC ECO:0000313|Proteomes:UP000199360};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000256|RuleBase:RU003557}.
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DR EMBL; FMDM01000005; SCG56874.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C5IF35; -.
DR STRING; 745366.GA0070213_105389; -.
DR OrthoDB; 5167532at2; -.
DR Proteomes; UP000199360; Unassembled WGS sequence.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR CDD; cd00751; thiolase; 1.
DR Gene3D; 3.40.47.10; -; 1.
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; PTHR42689; ACETYL-COA ACYLTRANSFERASE FADA2 (3-KETOACYL-COA THIOLASE) (BETA-KETOTHIOLASE)-RELATED; 1.
DR PANTHER; PTHR42689:SF1; ACETYL-COA ACYLTRANSFERASE FADA2 (3-KETOACYL-COA THIOLASE) (BETA-KETOTHIOLASE)-RELATED; 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 Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:SCG56874.1}.
FT DOMAIN 7..280
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 307..430
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT REGION 229..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 91
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 387
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 417
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 430 AA; 45645 MW; 88070622BB0E797A CRC64;
MQSVRRVAVI GGNRIPFARS NSRYAHASNA DMLGAALDGL VARFGLAGER VGEVVAGAVL
KHSRDFNLTR EVVLGSRLDP HTPAYDVQQA CGTGLEAAIL VANKIALGQI EVGIAGGVDT
TSDAPLAVNE DMRRTLIQLN SARTLGARLK VAAKLRPLQP FKPEIPRNAE PRTGLSMGDH
AAVTALRWNV DRAAQDDLAL RSHQRLAAAY EKGFFDDLMT PYLGLTRDQN LRPDTSPEKL
GSLKPVFGTR GPDAERATMT AGNSSPLTDG ASTVLLASEE WARAHSLPVL AWFSWSETAA
VDFVHGDEGL LMAPAYAVPR MLARAGLTLQ DFDFYEIHEA FASQVLATLA AWESPEFCKE
RLGLDAPLGS IDREKLNVNG SSLAAGHPFA ATGGRIVATL AKLLDAKGGG RGLISICAAG
GQGVTAILER
//