ID A0A0Q6KRN9_9SPHN Unreviewed; 392 AA.
AC A0A0Q6KRN9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:KQU55990.1};
GN ORFNames=ASG67_07885 {ECO:0000313|EMBL:KQU55990.1};
OS Sphingomonas sp. Leaf339.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736343 {ECO:0000313|EMBL:KQU55990.1, ECO:0000313|Proteomes:UP000051371};
RN [1] {ECO:0000313|EMBL:KQU55990.1, ECO:0000313|Proteomes:UP000051371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf339 {ECO:0000313|EMBL:KQU55990.1,
RC ECO:0000313|Proteomes:UP000051371};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQU55990.1, ECO:0000313|Proteomes:UP000051371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf339 {ECO:0000313|EMBL:KQU55990.1,
RC ECO:0000313|Proteomes:UP000051371};
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:KQU55990.1}.
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DR EMBL; LMRS01000012; KQU55990.1; -; Genomic_DNA.
DR RefSeq; WP_056528786.1; NZ_LMRS01000012.1.
DR AlphaFoldDB; A0A0Q6KRN9; -.
DR STRING; 1736343.ASG67_07885; -.
DR OrthoDB; 7181944at2; -.
DR Proteomes; UP000051371; Unassembled WGS sequence.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
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; IPR020617; Thiolase_C.
DR InterPro; IPR020613; Thiolase_CS.
DR InterPro; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR43853; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 1.
DR PANTHER; PTHR43853:SF22; ACETYL-COA ACETYLTRANSFERASE; 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; PS00737; THIOLASE_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW Reference proteome {ECO:0000313|Proteomes:UP000051371};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:KQU55990.1}.
FT DOMAIN 5..262
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 269..390
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 90
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 348
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 378
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 392 AA; 41054 MW; E225107AAE60ED4F CRC64;
MRSAVIVSTA RTPIGRAYRG AFNNLPSPSL AAHAIKAAVE RAKLDGGEVD DVVWGAALQQ
GHQAGNIART SLLRAGLPTT VSGMSVDRQC ASGLMAIATA AKQVIVDGMD IAIGGGVDSI
SLVQTPKMNI APDPKLLAMH KDIYMPMLQT AEIVAKRYGI TRDQMDEYSL QSQQRTAAAQ
AAGRFDDEIV PVTATMAIVN KETKEVTHQE VTLTKDEGNR ADTTLAGLSS LKPVLGEDAT
ITAGNASQLS DGASASVLMT EEEAAHRGLT PLGRYVGMAV AGTEPDEMGI GPVFAIPKLL
ARNGLTMDDI GLWELNEAFA VQVLYCRDKL GIPNDLLNVD GGAISIGHPY GMSGARMTGH
ALIEGKRRGA KYVVVTMCVG GGMGAAGLFE VL
//
