ID A0A172XZK8_9FLAO Unreviewed; 392 AA.
AC A0A172XZK8;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=acetyl-CoA C-acetyltransferase {ECO:0000256|ARBA:ARBA00012705};
DE EC=2.3.1.9 {ECO:0000256|ARBA:ARBA00012705};
GN ORFNames=A0O34_18735 {ECO:0000313|EMBL:ANF52429.1};
OS Chryseobacterium glaciei.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=1685010 {ECO:0000313|EMBL:ANF52429.1, ECO:0000313|Proteomes:UP000077824};
RN [1] {ECO:0000313|EMBL:ANF52429.1, ECO:0000313|Proteomes:UP000077824}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IHBB 10212 {ECO:0000313|EMBL:ANF52429.1,
RC ECO:0000313|Proteomes:UP000077824};
RA Pal M., Swarnkar M.K., Kaushal K., Chhibber S., Singh A.K., Gulati A.;
RT "Complete Genome Sequence of Chryseobacterium sp. IHBB 10212.";
RL Submitted (APR-2016) 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; CP015199; ANF52429.1; -; Genomic_DNA.
DR RefSeq; WP_066758159.1; NZ_CP015199.1.
DR AlphaFoldDB; A0A172XZK8; -.
DR STRING; 1685010.A0O34_18735; -.
DR KEGG; chh:A0O34_18735; -.
DR OrthoDB; 9764892at2; -.
DR Proteomes; UP000077824; Chromosome.
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: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 Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:ANF52429.1}.
FT DOMAIN 4..261
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 269..390
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 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; 41127 MW; 082F1C4173C56758 CRC64;
MKEVFIVSAV RTPMGSFLGS LSTVPATKLG SAAVKGALDK INLDPKNVQE IYMGNVLQAG
EGQSPARQVA LGAGLSNETI ATTINKVCAS GMKAVSMAAQ AIKAGDADVI VAGGMENMSS
VPHYYNARNA TKLGDVKMLD GMVLDGLTDV YNKVHMGVCA EKCATDYNIT REEQDNFAIE
SYKRSAKAWS EGKFAEEVVP VSIPQRKGDP IIFAEDEEYK AVNFDRLPTL PTVFKKEEGT
VTAANASTLN DGASALILVS KEKMEELGLK PLARIVSYAD AAHEPENFTT APSKALPIAL
KKAGLTLADI DFFEFNEAFS VVGLANNKIL GLDAAKVNVN GGAVALGHPL GSSGSRIIVT
LINVLKQNNA KYGAAAICNG GGGASAIVIE NL
//
