ID A0A072NAN5_9DEIO Unreviewed; 394 AA.
AC A0A072NAN5;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:KEF34759.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:KEF34759.1};
GN ORFNames=RDMS_05365 {ECO:0000313|EMBL:KEF34759.1};
OS Deinococcus sp. RL.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=1489678 {ECO:0000313|EMBL:KEF34759.1, ECO:0000313|Proteomes:UP000027898};
RN [1] {ECO:0000313|EMBL:KEF34759.1, ECO:0000313|Proteomes:UP000027898}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RL {ECO:0000313|EMBL:KEF34759.1,
RC ECO:0000313|Proteomes:UP000027898};
RA Lal R., Mahato N.K., Tripathi C., Verma H., Kumari R., Singh N.;
RT "Draft genome sequence of Deinococcus sp. strain RL isolated from sediments
RT of hot springs located at Manikaran, India.";
RL Submitted (MAY-2014) 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}.
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:KEF34759.1}.
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DR EMBL; JMQF01000024; KEF34759.1; -; Genomic_DNA.
DR RefSeq; WP_034403734.1; NZ_JMQF01000024.1.
DR AlphaFoldDB; A0A072NAN5; -.
DR eggNOG; COG0183; Bacteria.
DR OrthoDB; 9764892at2; -.
DR Proteomes; UP000027898; 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; 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:SF107; 3-KETOACYL-COA THIOLASE, 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 ECO:0000313|EMBL:KEF34759.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000027898};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:KEF34759.1}.
FT DOMAIN 8..262
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 271..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 349
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 379
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 394 AA; 40380 MW; E6AC2B980040B778 CRC64;
MKSADTLVIT AARRTPIGSF LGTLADVSAV DLGVTATRAV LEGVDPDEVA DVIVGNVLQA
GQGMNVARQI ALRSGLPQHV PGQTVNRVCG SGLQAVVSAV QGLKSGDGRL YLAGGTESMS
GAPYLLPRAR QGYRLGHTQA LDSILKDGLT DVFHDVHMGI TAENIAEEWK LSREEQDAFA
VESQRRAAAA IESGAFADEL VPVEVPSKKG PVLFDRDEYV RPGTTAEALA KLKPAFKPGG
TVTAGNASGL NDGAAMLAVT TEGYAQANGL PILAEIASYA AIGVDPRIMG IGPAKAVPVA
LERAGMGVGD VDLFELNEAF AAQSLAVVRD LGVDPARVNV TGGAIALGHP IGASGARVLV
TLIHALRRSG KETGVASLCI GGGMGIAMVV RARA
//
