ID A0A2S0HZ10_9FLAO Unreviewed; 392 AA.
AC A0A2S0HZ10;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=acetyl-CoA C-acetyltransferase {ECO:0000256|ARBA:ARBA00012705};
DE EC=2.3.1.9 {ECO:0000256|ARBA:ARBA00012705};
GN ORFNames=C5O00_12300 {ECO:0000313|EMBL:AVI51892.1};
OS Pukyongia salina.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Pukyongia.
OX NCBI_TaxID=2094025 {ECO:0000313|EMBL:AVI51892.1, ECO:0000313|Proteomes:UP000238442};
RN [1] {ECO:0000313|EMBL:AVI51892.1, ECO:0000313|Proteomes:UP000238442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RR4-38 {ECO:0000313|EMBL:AVI51892.1,
RC ECO:0000313|Proteomes:UP000238442};
RA Kim Y.-S., Jang Y.H., Kim K.-H.;
RT "Genomic analysis of the strain RR4-38 isolated from a seawater
RT recirculating aquaculture system.";
RL Submitted (FEB-2018) 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; CP027062; AVI51892.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S0HZ10; -.
DR KEGG; aue:C5O00_12300; -.
DR OrthoDB; 9764892at2; -.
DR Proteomes; UP000238442; Chromosome.
DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IEA:UniProtKB-EC.
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 ECO:0000313|EMBL:AVI51892.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000238442};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:AVI51892.1}.
FT DOMAIN 5..262
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 269..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; 40895 MW; B9A89D51FA6BF45C CRC64;
MSKKVVIVSA ARTPIGSFMG SLSSLSASAL GSTAIKGAMS KINLDPALVD EVYMGNVVQA
GVGQAPARQA ALGAGIPDSV PCTTVNKVCA SGMKAVMLAA QAITLGDADI IVAGGMESMS
NIPHYLHLRN GHKFGPKTMI DGMQKDGLVD AYDEQAMGVC ADLCATEHQF SREEQDAFAI
QSYERSAKAW AEGKFANEVV SVEVPQRRGE PIIISEDEEF KNVRMDKIPT LRPAFSKDGT
VTAANASTIN DGAGAVILMS EEKASAMGLT PLAIIKSYAD AAQEPKWFTT APAKALPKAL
AKAGLDISEI DYFEFNEAFA VVGLANMKIL GLNDENVNVN GGAVSLGHPL GCSGVRILIT
LMNILDQNNA RYGAAAICNG GGGASAVVIE RV
//
