ID S7TP16_DESML Unreviewed; 396 AA.
AC S7TP16;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Thiolase domain-containing protein {ECO:0000313|EMBL:EPR38646.1};
GN ORFNames=dsmv_2854 {ECO:0000313|EMBL:EPR38646.1};
OS Desulfococcus multivorans DSM 2059.
OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC Desulfococcaceae; Desulfococcus.
OX NCBI_TaxID=1121405 {ECO:0000313|EMBL:EPR38646.1, ECO:0000313|Proteomes:UP000014977};
RN [1] {ECO:0000313|EMBL:EPR38646.1, ECO:0000313|Proteomes:UP000014977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2059 {ECO:0000313|EMBL:EPR38646.1,
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:EPR38646.1}.
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DR EMBL; ATHJ01000095; EPR38646.1; -; Genomic_DNA.
DR RefSeq; WP_020877922.1; NZ_FUWN01000029.1.
DR AlphaFoldDB; S7TP16; -.
DR STRING; 897.B2D07_12360; -.
DR PATRIC; fig|1121405.3.peg.2908; -.
DR eggNOG; COG0183; Bacteria.
DR OrthoDB; 9764638at2; -.
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; IPR020617; Thiolase_C.
DR InterPro; IPR020616; Thiolase_N.
DR PANTHER; PTHR18919:SF140; ACETYL-COA C-ACETYLTRANSFERASE (ACETOACETYL-COA THIOLASE) (ACAB-5); 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.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW Reference proteome {ECO:0000313|Proteomes:UP000014977};
KW Transferase {ECO:0000256|RuleBase:RU003557}.
FT DOMAIN 14..263
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 278..394
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 90
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 352
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 382
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 396 AA; 42535 MW; CDB42FF361177C0B CRC64;
MLAKAFIPYG GYYSTPFARW QGSLAGENAI VLASDTSKRW IAGKEWDPKM FDYVILGVTV
GQPKLFYGGP WSAALIGSVD TPGLLISQAC STSTTGIFQA AMAIETGFCE NAYTLFTDRC
SNGPHTIWPN PAGPGGQVIS EDWVMDHFGK DPWGGTSMIQ TAENVAAMAG VTREECDQVA
LRRYEQYADA IKDDRAFQKR YMVPVEVKLS KKKTLHIEAD EGITKTTAEG LAGLRPVLPN
GVHTFGAQTH PADGHCAVVV TTREKAKTLS TQPDIEIQVV SYGFSRVKKA HMAIAPVPAA
QMALLKAGLK VEDMTVIKTH NPFSANDIYM AKEMKLDVNS FNNYGCSLVF GHPQAPTAGR
SIIEGIEEAV IRGGGYVLFT GCAAGDTGGA LILKVG
//
