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Database: UniProt
Entry: W0RNN8_9BACT
LinkDB: W0RNN8_9BACT
Original site: W0RNN8_9BACT 
ID   W0RNN8_9BACT            Unreviewed;       390 AA.
AC   W0RNN8;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=acetyl-CoA C-acyltransferase {ECO:0000256|ARBA:ARBA00024073};
DE            EC=2.3.1.16 {ECO:0000256|ARBA:ARBA00024073};
GN   ORFNames=J421_4418 {ECO:0000313|EMBL:AHG91955.1};
OS   Gemmatirosa kalamazoonensis.
OC   Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC   Gemmatimonadaceae; Gemmatirosa.
OX   NCBI_TaxID=861299 {ECO:0000313|EMBL:AHG91955.1, ECO:0000313|Proteomes:UP000019151};
RN   [1] {ECO:0000313|EMBL:AHG91955.1, ECO:0000313|Proteomes:UP000019151}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KBS708 {ECO:0000313|EMBL:AHG91955.1,
RC   ECO:0000313|Proteomes:UP000019151};
RX   PubMed=24699952;
RA   Debruyn J.M., Radosevich M., Wommack K.E., Polson S.W., Hauser L.J.,
RA   Fawaz M.N., Korlach J., Tsai Y.C.;
RT   "Genome Sequence and Methylome of Soil Bacterium Gemmatirosa
RT   kalamazoonensis KBS708T, a Member of the Rarely Cultivated Gemmatimonadetes
RT   Phylum.";
RL   Genome Announc. 2:e00226-14(2014).
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}.
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DR   EMBL; CP007128; AHG91955.1; -; Genomic_DNA.
DR   AlphaFoldDB; W0RNN8; -.
DR   STRING; 861299.J421_4418; -.
DR   KEGG; gba:J421_4418; -.
DR   PATRIC; fig|861299.3.peg.4471; -.
DR   eggNOG; COG0183; Bacteria.
DR   HOGENOM; CLU_031026_0_0_0; -.
DR   InParanoid; W0RNN8; -.
DR   OrthoDB; 23995at2; -.
DR   Proteomes; UP000019151; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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; 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   Reference proteome {ECO:0000313|Proteomes:UP000019151};
KW   Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:AHG91955.1}.
FT   DOMAIN          4..257
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          266..385
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        344
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        374
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ   SEQUENCE   390 AA;  40154 MW;  0000B1E2CF615828 CRC64;
     MDAVILSAVR TAVAKGKADG ALAKAGVLPI DISALVMREA VGRAGVDVAA VDDVIWGCAM
     PEASQGLNVA RNAALAAGLP VDASAATINR FCSSGLQSVA SAAQAVLSGM QDVVLAGGVE
     MMSQVPMSGY HTRLHPELTE SYIGMGYTAE RVAERYGVSR EDQDRFAYES QQKAARALAA
     NAFGDQIVPV PVKHVAWRGA EKTVTESTFD RDELPRTDTT LDGLAKLKPA FKNGGTVTAG
     NASPYSDGAA ALVVTSRAKA EQLGARPLAR LVTFAVAGID PDVMGVGPIN AIPKALKKAG
     MTLADIDLIE FNEAFAAQAV AVARHVGMDM DRVNVNGGAI ALGHPLGATG SKLSVQLIHE
     LRRRGGGVGM VTMCVGGGMG AAGIYEVYPA
//
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