ID A0A411YD81_9ACTN Unreviewed; 403 AA.
AC A0A411YD81;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Probable acetyl-CoA acetyltransferase {ECO:0000256|ARBA:ARBA00040529};
DE EC=2.3.1.9 {ECO:0000256|ARBA:ARBA00012705};
GN ORFNames=ER308_05830 {ECO:0000313|EMBL:QBI19107.1};
OS Egibacter rhizosphaerae.
OC Bacteria; Actinomycetota; Nitriliruptoria; Egibacterales; Egibacteraceae;
OC Egibacter.
OX NCBI_TaxID=1670831 {ECO:0000313|EMBL:QBI19107.1, ECO:0000313|Proteomes:UP000291469};
RN [1] {ECO:0000313|EMBL:QBI19107.1, ECO:0000313|Proteomes:UP000291469}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EGI 80759 {ECO:0000313|EMBL:QBI19107.1,
RC ECO:0000313|Proteomes:UP000291469};
RA Chen D.-D., Tian Y., Jiao J.-Y., Zhang X.-T., Zhang Y.-G., Zhang Y.,
RA Xiao M., Shu W.-S., Li W.-J.;
RT "Egibacter rhizosphaerae EGI 80759T.";
RL Submitted (JAN-2019) 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; CP036402; QBI19107.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A411YD81; -.
DR KEGG; erz:ER308_05830; -.
DR OrthoDB; 1402717at2; -.
DR Proteomes; UP000291469; Chromosome.
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; IPR020613; Thiolase_CS.
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; 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 Reference proteome {ECO:0000313|Proteomes:UP000291469};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:QBI19107.1}.
FT DOMAIN 18..272
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 281..401
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 98
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 359
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 389
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 403 AA; 41024 MW; F11940299A0EE101 CRC64;
MTADHPAVDP RREPVLLGYA RTPIGRLGGA FAGLAAVDLG GRAIASALER AGVPADRVDQ
VLMGHVLQAG QGQITARQAA QQGGIGMNVP ATTINKVCLS GMSAVALADQ QIRLGEASVV
VAGGMESMSQ APYLLPDARF GYRMGDGKLV DAMVHDGLWC AFDDAHMGAT SDAMNARYGI
DRAVQDEWAA RSHERAATAT KEGRFEGEVV PVEIPQRRGE PEIVTEDEGV RPGTTTESLG
KLKPAFAADG TITAGNASQI SDGAAALVVA SRAVAEELGA TPVGRIRGYG TVAGPDPSLH
HQPAEAIRLA AEKAGVAPDG LEVYEINEAF AAVAKHSTDL LGVDEARVNP HGGAVAVGHP
IGASGARITA AVLHQLAARG GGFGAAALCG GGGQGDALLL EVG
//
