ID   NPHT7_STRC1             Reviewed;         329 AA.
AC   D7URV0;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 1.
DT   25-MAY-2022, entry version 36.
DE   RecName: Full=Acetoacetyl CoA synthase NphT7;
DE            EC=2.3.1.194;
GN   Name=nphT7; Synonyms=fhsA;
OS   Streptomyces sp. (strain CL190).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=93372;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, SUBUNIT, GENE NAME, AND MUTAGENESIS
RP   OF CYS-115 AND HIS-256.
RC   STRAIN=CL190;
RX   PubMed=20534558; DOI=10.1073/pnas.1000532107;
RA   Okamura E., Tomita T., Sawa R., Nishiyama M., Kuzuyama T.;
RT   "Unprecedented acetoacetyl-coenzyme A synthesizing enzyme of the thiolase
RT   superfamily involved in the mevalonate pathway.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:11265-11270(2010).
CC   -!- FUNCTION: Catalyzes the condensation of acetyl-CoA and malonyl-CoA to
CC       form acetoacetyl-CoA and CoA. Does not accept malonyl-[acyl-carrier-
CC       protein] as a substrate. Can also convert malonyl-CoA into acetyl-CoA
CC       via decarboxylation of malonyl-CoA. {ECO:0000269|PubMed:20534558}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + H(+) + malonyl-CoA = acetoacetyl-CoA + CO2 + CoA;
CC         Xref=Rhea:RHEA:28250, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57286, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:57384; EC=2.3.1.194;
CC         Evidence={ECO:0000269|PubMed:20534558};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=68 uM for acetyl-CoA {ECO:0000269|PubMed:20534558};
CC         KM=28 uM for malonyl-CoA {ECO:0000269|PubMed:20534558};
CC         Vmax=8.9 umol/min/mg enzyme {ECO:0000269|PubMed:20534558};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate
CC       biosynthesis. {ECO:0000269|PubMed:20534558}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:20534558}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. FabH family.
CC       {ECO:0000305}.
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DR   EMBL; AB540131; BAJ10048.1; -; Genomic_DNA.
DR   EMBL; AB272317; BAJ83474.1; -; Genomic_DNA.
DR   AlphaFoldDB; D7URV0; -.
DR   SMR; D7URV0; -.
DR   DIP; DIP-59345N; -.
DR   KEGG; ag:BAJ10048; -.
DR   BRENDA; 2.3.1.194; 15673.
DR   SABIO-RK; D7URV0; -.
DR   UniPathway; UPA00058; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IDA:UniProtKB.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   GO; GO:0019287; P:isopentenyl diphosphate biosynthetic process, mevalonate pathway; IDA:UniProtKB.
DR   Gene3D; 3.40.47.10; -; 1.
DR   InterPro; IPR013751; ACP_syn_III.
DR   InterPro; IPR013747; ACP_syn_III_C.
DR   InterPro; IPR016039; Thiolase-like.
DR   Pfam; PF08545; ACP_syn_III; 1.
DR   Pfam; PF08541; ACP_syn_III_C; 1.
DR   SUPFAM; SSF53901; SSF53901; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Cytoplasm; Transferase.
FT   CHAIN           1..329
FT                   /note="Acetoacetyl CoA synthase NphT7"
FT                   /id="PRO_0000418421"
FT   ACT_SITE        115
FT                   /evidence="ECO:0000305"
FT   ACT_SITE        256
FT                   /evidence="ECO:0000305"
FT   ACT_SITE        286
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         115
FT                   /note="C->A: Loss of condensation activity, but retains
FT                   decarboxylation activity."
FT                   /evidence="ECO:0000269|PubMed:20534558"
FT   MUTAGEN         256
FT                   /note="H->A: 40-fold decrease in activity."
FT                   /evidence="ECO:0000269|PubMed:20534558"
SQ   SEQUENCE   329 AA;  34518 MW;  308F3B9115AE04F1 CRC64;
     MTDVRFRIIG TGAYVPERIV SNDEVGAPAG VDDDWITRKT GIRQRRWAAD DQATSDLATA
     AGRAALKAAG ITPEQLTVIA VATSTPDRPQ PPTAAYVQHH LGATGTAAFD VNAVCSGTVF
     ALSSVAGTLV YRGGYALVIG ADLYSRILNP ADRKTVVLFG DGAGAMVLGP TSTGTGPIVR
     RVALHTFGGL TDLIRVPAGG SRQPLDTDGL DAGLQYFAMD GREVRRFVTE HLPQLIKGFL
     HEAGVDAADI SHFVPHQANG VMLDEVFGEL HLPRATMHRT VETYGNTGAA SIPITMDAAV
     RAGSFRPGEL VLLAGFGGGM AASFALIEW