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Database: UniProt
Entry: F1ZAH2_9SPHN
LinkDB: F1ZAH2_9SPHN
Original site: F1ZAH2_9SPHN 
ID   F1ZAH2_9SPHN            Unreviewed;       385 AA.
AC   F1ZAH2;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:EGD58420.1};
GN   ORFNames=Y88_0475 {ECO:0000313|EMBL:EGD58420.1};
OS   Novosphingobium nitrogenifigens DSM 19370.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=983920 {ECO:0000313|EMBL:EGD58420.1, ECO:0000313|Proteomes:UP000004728};
RN   [1] {ECO:0000313|EMBL:EGD58420.1, ECO:0000313|Proteomes:UP000004728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19370 {ECO:0000313|EMBL:EGD58420.1,
RC   ECO:0000313|Proteomes:UP000004728};
RX   PubMed=22156397; DOI=10.1128/JB.06381-11;
RA   Strabala T.J., Macdonald L., Liu V., Smit A.M.;
RT   "Draft Genome Sequence of Novosphingobium nitrogenifigens Y88T.";
RL   J. Bacteriol. 194:201-201(2012).
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:EGD58420.1}.
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DR   EMBL; AEWJ01000041; EGD58420.1; -; Genomic_DNA.
DR   AlphaFoldDB; F1ZAH2; -.
DR   STRING; 983920.Y88_0475; -.
DR   eggNOG; COG0183; Bacteria.
DR   HOGENOM; CLU_031026_1_1_5; -.
DR   InParanoid; F1ZAH2; -.
DR   Proteomes; UP000004728; Unassembled WGS sequence.
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; 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.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004728};
KW   Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:EGD58420.1}.
FT   DOMAIN          12..254
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          263..383
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
FT   ACT_SITE        98
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        341
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        371
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ   SEQUENCE   385 AA;  38660 MW;  294C494702DD3F9F CRC64;
     MRKLEGCSMP DVVVAGFARS PFHLAGKGAL ARTRPDDLAG AVVRGLVERT GVDVSAIEDL
     VVGCAFPEGE QGFNVARLIG MLAGLPQSVG GMTVNRFCGS SMSAVHYAAG QIALGAGEVF
     VAAGIESMSR VPMMGFNPLP NPELAKTSAA YIGMGDTAEN LATRYGIDRA QQEAFAVASQ
     QKAGAAMAAG RFADEIVPIV TKGGTVDVDG CPRPATTAET LAGLKPAFSA TGTVTAGTSS
     PLTDGASAVL VASEAYARAN GLPILARIRA TAISGCSPDI MGIGPVESSR KALARAGIGV
     GDLDVIELNE AFASQALACI ADLGLDPTKI NLDGGAIALG HPLGATGARI VGKAAALLKR
     EGGRFALATQ CIGGGQGIAT VLEAI
//
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