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Database: UniProt
Entry: A0A1T5NGW8_9BACT
LinkDB: A0A1T5NGW8_9BACT
Original site: A0A1T5NGW8_9BACT 
ID   A0A1T5NGW8_9BACT        Unreviewed;       390 AA.
AC   A0A1T5NGW8;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-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=SAMN05660461_1549 {ECO:0000313|EMBL:SKC99652.1};
OS   Chitinophaga ginsengisegetis.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Chitinophaga.
OX   NCBI_TaxID=393003 {ECO:0000313|EMBL:SKC99652.1, ECO:0000313|Proteomes:UP000190166};
RN   [1] {ECO:0000313|EMBL:SKC99652.1, ECO:0000313|Proteomes:UP000190166}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18108 {ECO:0000313|EMBL:SKC99652.1,
RC   ECO:0000313|Proteomes:UP000190166};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
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; FUZZ01000001; SKC99652.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T5NGW8; -.
DR   STRING; 393003.SAMN05660461_1549; -.
DR   Proteomes; UP000190166; 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; 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:SF156; ACETYL-COA ACETYLTRANSFERASE, MITOCHONDRIAL; 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   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Potassium {ECO:0000256|ARBA:ARBA00022958};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190166};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003557}.
FT   DOMAIN          4..259
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          267..389
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        346
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        376
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ   SEQUENCE   390 AA;  40778 MW;  36DFF070E1BD242A CRC64;
     MKEVFIVAVA RTPIGSFNGA LASIPATQLG AHVIKAALER AGIAPAQVNE VYMGNVLSAN
     LGQAPANQAS LAAGVPNNVP CTTVNKVCAS GMKAIMLGAQ SIMLGDNDVV VAGGMENMSA
     TPYYLDKART GYKLGHGAIT DGIIRDGLWD PYKDFHMGNA AELCATEYKI TREDQDAYAI
     ESYKRAAAAW EKGYFKDEVV PVQVPGKQVV TVSEDEDYKK VIFEKVPSLK PSFQKDGTIT
     AANASNINDG AAAVVLVSGE KLKALGLKPL AKIISFADAS QAPEWFTTTP VKAINNALTK
     AGLKISDMDV AEVNEAFSCV PIANAKDLGL SLDKVNVWGG AVAMGHPIGC SGARIVVTLN
     AILHQQQARY GVAGICNGGG GASAIIIERV
//
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