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
//