ID W9H9S1_9PROT Unreviewed; 400 AA.
AC W9H9S1;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:EWY41457.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:EWY41457.1};
GN ORFNames=N825_28555 {ECO:0000313|EMBL:EWY41457.1};
OS Skermanella stibiiresistens SB22.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Skermanella.
OX NCBI_TaxID=1385369 {ECO:0000313|EMBL:EWY41457.1, ECO:0000313|Proteomes:UP000019486};
RN [1] {ECO:0000313|EMBL:EWY41457.1, ECO:0000313|Proteomes:UP000019486}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB22 {ECO:0000313|EMBL:EWY41457.1,
RC ECO:0000313|Proteomes:UP000019486};
RA Zhu W., Wang G.;
RT "The genome sequence of Skermanella stibiiresistens.";
RL Submitted (AUG-2013) 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:EWY41457.1}.
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DR EMBL; AVFL01000004; EWY41457.1; -; Genomic_DNA.
DR RefSeq; WP_037449368.1; NZ_AVFL01000004.1.
DR AlphaFoldDB; W9H9S1; -.
DR STRING; 1385369.N825_28555; -.
DR PATRIC; fig|1385369.3.peg.1653; -.
DR OrthoDB; 9764638at2; -.
DR Proteomes; UP000019486; 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; IPR020610; Thiolase_AS.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR18919:SF138; ACETYL-COA C-ACETYLTRANSFERASE; 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; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW ECO:0000313|EMBL:EWY41457.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000019486};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:EWY41457.1}.
FT DOMAIN 11..268
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 277..398
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 95
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 355
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 385
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 400 AA; 41318 MW; 9A2BF1405EA85FF9 CRC64;
MSNTSPTVDP IVIVAAARTP LGRFQGDLAA VSAPQLGAHV IRAALARAGL APDRIDEALM
GCVLPAGQGQ APARQAVRGA GLPDQVGATT VNKVCGSGMK ATMLAHDLIR AGSADIVVAG
GMESMSGAPY LLAKARARYR VGHDRILDHM MLDGLEDAYE AGRSMGDFGE AAAHEYRFSR
ADQDAYAVET LTRARSAIAE GAFKAEIAPV TVAAKGGERV VDTDEHPLKV SPEKIPALKP
AFRPDGTITA ASASANADGA AALILTRRSI ARADGLPILA EIKAHATHSQ EPAWYTTAPI
PAIRKLLDKT GWTAADVDLF EINEAFAVVA MAAARDLGIP RDQLNVHGGA CALGHPIGAT
GARLIVTLLH ALERRGLSRG VAALCIGGGE ATAIAVERVG
//
