ID S7TGD7_DESML Unreviewed; 429 AA.
AC S7TGD7;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:EPR35816.1};
GN ORFNames=dsmv_0521 {ECO:0000313|EMBL:EPR35816.1};
OS Desulfococcus multivorans DSM 2059.
OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC Desulfococcaceae; Desulfococcus.
OX NCBI_TaxID=1121405 {ECO:0000313|EMBL:EPR35816.1, ECO:0000313|Proteomes:UP000014977};
RN [1] {ECO:0000313|EMBL:EPR35816.1, ECO:0000313|Proteomes:UP000014977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2059 {ECO:0000313|EMBL:EPR35816.1,
RC ECO:0000313|Proteomes:UP000014977};
RX PubMed=23950126;
RA Brown S.D., Hurt R.A.Jr., Gilmour C.C., Elias D.A.;
RT "Draft genome sequences for three mercury-methylating, sulfate-reducing
RT bacteria.";
RL Genome Announc. 1:e00618-e00613(2013).
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:EPR35816.1}.
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DR EMBL; ATHJ01000105; EPR35816.1; -; Genomic_DNA.
DR RefSeq; WP_020877632.1; NZ_FUWN01000001.1.
DR AlphaFoldDB; S7TGD7; -.
DR STRING; 897.B2D07_15260; -.
DR PATRIC; fig|1121405.3.peg.3220; -.
DR eggNOG; COG0183; Bacteria.
DR OrthoDB; 4565318at2; -.
DR Proteomes; UP000014977; 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; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR18919; ACETYL-COA C-ACYLTRANSFERASE; 1.
DR PANTHER; PTHR18919:SF153; TRIFUNCTIONAL ENZYME SUBUNIT BETA, MITOCHONDRIAL; 1.
DR Pfam; PF02803; Thiolase_C; 1.
DR Pfam; PF00108; Thiolase_N; 2.
DR PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 2.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS00098; THIOLASE_1; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW Reference proteome {ECO:0000313|Proteomes:UP000014977};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:EPR35816.1}.
FT DOMAIN 4..51
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 78..297
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 307..428
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 123
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 385
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 415
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 429 AA; 45518 MW; DA38F88A6A0BAC5F CRC64;
MNEVVIVSGS RTAVGSFGGS LKTVSVVDMG ALVMKDVLKK ANLKPVLSDD MRAGVPEKLK
DQGPVDLEKQ AADWDDGATP IVIDEVIMGN VLQAGQGQNP ARQAMIRAGI CKETPAMSLN
KVCGSGLKAI AVGASAIMSG QAEVVLAGGQ ENMSMAPMAL PKARWGYRME LTGAGEVTDL
VVFDGLYEIF YGYHMGMTAE NIVKLYGISR EEQDELGVLS HNRARKAITD GLFKEEIVPV
VIKSRKGDVV FDTDERPMDT SLEKMARLKP AFKKDGSVTA GNASGINDAA AAVLMMTPEK
AKALGLQPIV RIKAFAGGGV DPAYMGLGPV PAIRKVLKTT GMTLNDIQMI ELNEAFAAQA
IGCMRELDIP VEKPNQLGSG ISIGHPIGCT GARQMVTCIH HMRRENLETG LISMCIGGGM
GMAMIVERV
//
