ID A0A0Q4LX12_9SPHN Unreviewed; 394 AA.
AC A0A0Q4LX12;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:KQN37618.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:KQN37618.1};
GN ORFNames=ASE97_08635 {ECO:0000313|EMBL:KQN37618.1};
OS Sphingomonas sp. Leaf42.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736219 {ECO:0000313|EMBL:KQN37618.1, ECO:0000313|Proteomes:UP000051880};
RN [1] {ECO:0000313|EMBL:KQN37618.1, ECO:0000313|Proteomes:UP000051880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf42 {ECO:0000313|EMBL:KQN37618.1,
RC ECO:0000313|Proteomes:UP000051880};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQN37618.1, ECO:0000313|Proteomes:UP000051880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf42 {ECO:0000313|EMBL:KQN37618.1,
RC ECO:0000313|Proteomes:UP000051880};
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|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:KQN37618.1}.
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DR EMBL; LMLF01000005; KQN37618.1; -; Genomic_DNA.
DR RefSeq; WP_055759874.1; NZ_LMLF01000005.1.
DR AlphaFoldDB; A0A0Q4LX12; -.
DR PATRIC; fig|1736219.3.peg.1862; -.
DR OrthoDB; 7181944at2; -.
DR Proteomes; UP000051880; 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; 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:KQN37618.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051880};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:KQN37618.1}.
FT DOMAIN 5..262
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 270..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; 40483 MW; 20399742F7023D90 CRC64;
MSDPIVILSY ARTPMGSFQG SLAGASATQL GATAVGAAVE RAGLSGEAIE RIYMGCVLPA
GLGQAPARQA ALGAGLPTHV EATTVNKMCG SGMQAAIMAA DALAAGSAEL IVAGGMESMT
NAPYLSTRHR SGARIGHDRL LDHMYLDGLE DAYDPGKLMG SFAEETAAEY QFTRAAQDDY
AIESLHRAQR AQKSGAFDRE IVAVEVAGRK GTTSVREDEQ PARGDVAKIP TLKPAFAKDG
TITAANASSI SDGAAALVLT RQSVADRLGL TPVARVVAHA GHAHAPAKFA TAPVFAMRKA
MARAGWSVGD IDLFEVNEAF ACVAMIAMRD LGLSHDTLNI HGGACALGHP IGASGVRVLA
TLLSALETTG QRRGLASLCI GGGEATAMAM ELLD
//
