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Database: UniProt
Entry: A0A285X406_9FLAO
LinkDB: A0A285X406_9FLAO
Original site: A0A285X406_9FLAO 
ID   A0A285X406_9FLAO        Unreviewed;       392 AA.
AC   A0A285X406;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=acetyl-CoA C-acetyltransferase {ECO:0000256|ARBA:ARBA00012705};
DE            EC=2.3.1.9 {ECO:0000256|ARBA:ARBA00012705};
GN   ORFNames=SAMN06296241_1636 {ECO:0000313|EMBL:SOC80091.1};
OS   Salinimicrobium sediminis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Salinimicrobium.
OX   NCBI_TaxID=1343891 {ECO:0000313|EMBL:SOC80091.1, ECO:0000313|Proteomes:UP000219193};
RN   [1] {ECO:0000313|Proteomes:UP000219193}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.12641 {ECO:0000313|Proteomes:UP000219193};
RA   Varghese N., Submissions S.;
RL   Submitted (SEP-2017) 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; OCMF01000002; SOC80091.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A285X406; -.
DR   OrthoDB; 9764892at2; -.
DR   Proteomes; UP000219193; Unassembled WGS sequence.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:SF171; ACETYL-COA ACETYLTRANSFERASE, CYTOSOLIC; 1.
DR   PANTHER; PTHR18919; ACETYL-COA C-ACYLTRANSFERASE; 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   Reference proteome {ECO:0000313|Proteomes:UP000219193};
KW   Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:SOC80091.1}.
FT   DOMAIN          5..262
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          270..391
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
FT   ACT_SITE        89
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        348
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        378
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ   SEQUENCE   392 AA;  41210 MW;  AFD5B509395666A1 CRC64;
     MNKEVVIVSA ARTPIGSFLG SLSTVPATKL GSIAIKGALA KINLKPEMVE EVLMGNVVQA
     GNGQAPARQA ALGAGIPTSV PCTTVNKVCA SGMKAVMQAA QAISLGDASI VVAGGMENMS
     LIPHYLHLRN GHKFGPAQME DGMQKDGLVD AYDHNAMGVA ADHCAKEHNY TREEQDKFAI
     QSYERSRKAW EDGKFNEEVV PVEVPQRKGD PVIVKEDEEY KNVKMDKIAS LRPAFGKEGT
     VTAANASTIN DGAAALVLMS REKAEELGLE ILASIKGFAD AATDPIWFTT APAKALPKAL
     DKAGISIDKV DYFEFNEAFS VVGLVNMKIL GLEDKNVNVN GGAVSLGHPL GCSGARILVT
     LLNVLKQNDG KIGAAAVCNG GGGASAMILE RQ
//
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