ID I2JPI0_9GAMM Unreviewed; 382 AA.
AC I2JPI0;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:EIF44882.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:EIF44882.1};
GN ORFNames=DOK_01594 {ECO:0000313|EMBL:EIF44882.1};
OS gamma proteobacterium BDW918.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Spongiibacteraceae.
OX NCBI_TaxID=1168065 {ECO:0000313|EMBL:EIF44882.1, ECO:0000313|Proteomes:UP000003473};
RN [1] {ECO:0000313|EMBL:EIF44882.1, ECO:0000313|Proteomes:UP000003473}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BDW918 {ECO:0000313|EMBL:EIF44882.1,
RC ECO:0000313|Proteomes:UP000003473};
RX PubMed=22740675; DOI=10.1128/JB.00678-12;
RA Kim S.M., Cho S.J., Lee S.B.;
RT "Genome Sequence of the Unclassified Marine Gammaproteobacterium BDW918.";
RL J. Bacteriol. 194:3753-3754(2012).
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000256|ARBA:ARBA00010982, ECO:0000256|RuleBase:RU003557}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EIF44882.1}.
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DR EMBL; AJMK01000006; EIF44882.1; -; Genomic_DNA.
DR AlphaFoldDB; I2JPI0; -.
DR PATRIC; fig|1168065.3.peg.335; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_2_3_6; -.
DR OrthoDB; 9764638at2; -.
DR Proteomes; UP000003473; Unassembled WGS sequence.
DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IEA:UniProtKB-EC.
DR CDD; cd00751; thiolase; 1.
DR Gene3D; 3.40.47.10; -; 2.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020613; Thiolase_CS.
DR InterPro; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR43365; BLR7806 PROTEIN; 1.
DR PANTHER; PTHR43365:SF1; STEROID 3-KETOACYL-COA THIOLASE FADA6; 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; PS00737; THIOLASE_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU003557};
KW Reference proteome {ECO:0000313|Proteomes:UP000003473};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:EIF44882.1}.
FT DOMAIN 5..252
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 260..381
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 338
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 368
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 382 AA; 40956 MW; FD304AA7432A1436 CRC64;
MAEAYIVDAV RSPTGRRKGG LAHVHGADLG AHVLKAIVER NGIPDNEYDD VIFGCVDAIG
PLAGDIARSA WLAAGLSDEV PGTTIDRQCG SSQQSVHFAA QAIMSGTMDV VVAGGVQTMT
QIPISSAMTA AIPMGFSDPF SGSTGWVARY GAEPPTQFKS AQMIAEKWGF SRRDLEEYSF
ESHQRALRAI AEGRFDREII PFGDVKMDET PRNSSLEKMA ELDFLFGCDK VTAAVSSQTC
DASSAMLLVS EDALKRYNLT PRARIHHISV RADDPIWMLT APIAATAYAL KKAGMSMQDI
DLVEINEAFA SVSMAWLKET GYDHAKTNVN GGAIALGHPL GATGTKLMTT LLHELERTGG
RYGLQTMCEG GGQANVTIIE RL
//
