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Database: UniProt
Entry: A0A1C5IF35_9ACTN
LinkDB: A0A1C5IF35_9ACTN
Original site: A0A1C5IF35_9ACTN 
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
//
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