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
//