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Database: UniProt
Entry: A0A1I5TMS8_9SPHN
LinkDB: A0A1I5TMS8_9SPHN
Original site: A0A1I5TMS8_9SPHN 
ID   A0A1I5TMS8_9SPHN        Unreviewed;       395 AA.
AC   A0A1I5TMS8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Acetyl-CoA C-acetyltransferase {ECO:0000313|EMBL:SFP84350.1};
GN   ORFNames=SAMN04488241_108157 {ECO:0000313|EMBL:SFP84350.1};
OS   Sphingomonas rubra.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=634430 {ECO:0000313|EMBL:SFP84350.1, ECO:0000313|Proteomes:UP000199586};
RN   [1] {ECO:0000313|EMBL:SFP84350.1, ECO:0000313|Proteomes:UP000199586}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.9113 {ECO:0000313|EMBL:SFP84350.1,
RC   ECO:0000313|Proteomes:UP000199586};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FOXP01000008; SFP84350.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I5TMS8; -.
DR   STRING; 634430.SAMN04488241_108157; -.
DR   OrthoDB; 7181944at2; -.
DR   Proteomes; UP000199586; Unassembled WGS sequence.
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; -; 2.
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; 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; PS00099; THIOLASE_3; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199586};
KW   Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:SFP84350.1}.
FT   DOMAIN          4..261
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        89
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   395 AA;  40466 MW;  9BB4157784DAC862 CRC64;
     MEPIYIVAGV RTAIGDFGGS LKDHSPADLG AIVIAEAVRR AGLAPGDLEH VVMGQVIQTT
     PKDAYLARVA ALKAGVPERA PALTLNRLCG SGLQAIISAS QMIALGEVGI AVAGGAEVMS
     RAPHHVTAAR FGKKLGDMTM IDALTTVLSD PLDDYHMGVT AENVARDCAV TREDQDALAA
     ESHRRAARAQ AEGRFDAQIV PVPVRDGRST RDFAIDEHVR ADANEVAMAG LRPVFQKDGT
     VTAGNASGIN DGAAAVVLAS QAEVDARGLK PLGRILGWGH AGVAPTHMGL GPVEAVPIAL
     ARAGLSLDEI DVIESNEAFA AQACAVSRTL GFDPDKVNPN GSGISLGHPV GATGAILTVK
     ALYELARGGG RSALVTMCIG GGQGIAIVLS EARTT
//
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