ID A0A0Q9T935_9ACTN Unreviewed; 431 AA.
AC A0A0Q9T935;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:KRF35995.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:KRF35995.1};
GN ORFNames=ASG94_00395 {ECO:0000313|EMBL:KRF35995.1};
OS Nocardioides sp. Soil805.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736416 {ECO:0000313|EMBL:KRF35995.1, ECO:0000313|Proteomes:UP000051356};
RN [1] {ECO:0000313|EMBL:KRF35995.1, ECO:0000313|Proteomes:UP000051356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil805 {ECO:0000313|EMBL:KRF35995.1,
RC ECO:0000313|Proteomes:UP000051356};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRF35995.1, ECO:0000313|Proteomes:UP000051356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil805 {ECO:0000313|EMBL:KRF35995.1,
RC ECO:0000313|Proteomes:UP000051356};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {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:KRF35995.1}.
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DR EMBL; LMSU01000001; KRF35995.1; -; Genomic_DNA.
DR RefSeq; WP_056924486.1; NZ_LMSU01000001.1.
DR AlphaFoldDB; A0A0Q9T935; -.
DR STRING; 1736416.ASG94_00395; -.
DR OrthoDB; 4440515at2; -.
DR Proteomes; UP000051356; 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; -; 1.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR42689; ACETYL-COA ACYLTRANSFERASE FADA2 (3-KETOACYL-COA THIOLASE) (BETA-KETOTHIOLASE)-RELATED; 1.
DR PANTHER; PTHR42689:SF1; ACETYL-COA ACYLTRANSFERASE FADA2 (3-KETOACYL-COA THIOLASE) (BETA-KETOTHIOLASE)-RELATED; 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 ECO:0000313|EMBL:KRF35995.1};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:KRF35995.1}.
FT DOMAIN 8..276
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 285..431
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 92
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 383
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 418
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 431 AA; 45752 MW; FC27CF88A6DC474F CRC64;
MNSSTRRVAV LGGNRIPFAR SNTVYVDVSN QEMLTAAIDG LVSRYGLEGE RLGEVVAGAV
LKHARDFNLA RESVLGSKLS AETPATDIQQ ACGTGLQAAI QVADKIALGQ IDVGIAGGTD
TTSDAPVAIS DRLRKKLMRV NAARDTKGKL TALGRIRPGD IGLEIPQNGE PRTRLSMGEH
AALTALEWRI SREAQDELAA SSHQKMAAAY DRGFFDDQVT PFRGVERDNN LRPDSTAEKL
ATLKPVFGKG EAATMTAGNS TPLSDGASAV LLASEDWAEE HDLPVLAWFV DHETAAVDYV
NGHEGLLMAP AYAVPRMLAR NGLSLQDFDF YEIHEAFASQ VLSTLAAWED PVFCKERLGL
DEPLGAIDRD KLNVTGSSLA AAHPFAATGG RIISTLAHLL DERAASTGEG GRGLISICAA
GGQGVVAILE R
//
