ID A0A2P7TL88_9SPHI Unreviewed; 392 AA.
AC A0A2P7TL88;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=acetyl-CoA C-acyltransferase {ECO:0000256|ARBA:ARBA00024073};
DE EC=2.3.1.16 {ECO:0000256|ARBA:ARBA00024073};
GN ORFNames=C7N43_18735 {ECO:0000313|EMBL:PSJ75486.1};
OS Sphingobacteriales bacterium UPWRP_1.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales.
OX NCBI_TaxID=2116516 {ECO:0000313|EMBL:PSJ75486.1, ECO:0000313|Proteomes:UP000240367};
RN [1] {ECO:0000313|EMBL:PSJ75486.1, ECO:0000313|Proteomes:UP000240367}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UPWRP_1 {ECO:0000313|EMBL:PSJ75486.1,
RC ECO:0000313|Proteomes:UP000240367};
RA Tan S.M.;
RT "Obtaining draft genomes of rare unknown microbial groups and defining 1
RT their spatial structures from highly complex communities.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
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:PSJ75486.1}.
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DR EMBL; PXYE01000077; PSJ75486.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P7TL88; -.
DR Proteomes; UP000240367; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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; IPR020615; Thiolase_acyl_enz_int_AS.
DR InterPro; IPR020610; Thiolase_AS.
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:SF8; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 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; PS00737; THIOLASE_2; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW ECO:0000313|EMBL:PSJ75486.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000240367};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:PSJ75486.1}.
FT DOMAIN 5..260
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 269..389
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 347
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 377
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 392 AA; 41416 MW; F794F8955AE95AFD CRC64;
MQEAYIVAGY RTAVTKAKRG GFRFVRPDDL AVDVIAHLLK AVPQLDPVRV EDLIVGNAVP
EAEQGLQVGR MIAVRVLPKT TAGVTVNRYC GSGVETIAMA TAKIRAGMAD CIIAGGTESM
SLVPTVGWKT ALNYEVANTT PDYYLGMGLT AEAVAKEYSI SREAQDEFSY HSHRKAANAI
QQGYFKGGIC PITVNEVYVN EKGKRAQRQF VIDTDEGVRT DTTIEGLATL KPVFANRGTV
TAGNSSQTSD GAAFVLVMSE RMVKELGLTP IGRMVTCTAV GVEPRIMGIG PVAAIPKALK
MAGMNLADMN LIELNEAFAA QSVAVIQQAG LNPDVVNING GAIALGHPLG CTGAKLTVQL
LHDLKRTGGK YGMVTACIGG GQGIAAVYER LN
//
