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Database: UniProt
Entry: A0A1V2QWP7_9PSEU
LinkDB: A0A1V2QWP7_9PSEU
Original site: A0A1V2QWP7_9PSEU 
ID   A0A1V2QWP7_9PSEU        Unreviewed;       344 AA.
AC   A0A1V2QWP7;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=3-oxoacyl-ACP synthase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ALI22I_02670 {ECO:0000313|EMBL:ONI92663.1};
OS   Saccharothrix sp. ALI-22-I.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharothrix.
OX   NCBI_TaxID=1933778 {ECO:0000313|EMBL:ONI92663.1, ECO:0000313|Proteomes:UP000188617};
RN   [1] {ECO:0000313|EMBL:ONI92663.1, ECO:0000313|Proteomes:UP000188617}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ALI-22-I {ECO:0000313|EMBL:ONI92663.1,
RC   ECO:0000313|Proteomes:UP000188617};
RX   PubMed=28087533;
RA   Yeager C.M., Gallegos-Graves V., Dunbar J., Hesse C.N., Daligault H.,
RA   Kuske C.R.;
RT   "Polysaccharide degradation capability of Actinomycetales soil isolates
RT   from a semi-arid grassland of the Colorado Plateau.";
RL   Appl. Environ. Microbiol. 0:0-0(2017).
CC   -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000256|ARBA:ARBA00004792}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. FabH family.
CC       {ECO:0000256|ARBA:ARBA00008642}.
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:ONI92663.1}.
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DR   EMBL; MTQP01000031; ONI92663.1; -; Genomic_DNA.
DR   RefSeq; WP_077003966.1; NZ_MTQP01000031.1.
DR   AlphaFoldDB; A0A1V2QWP7; -.
DR   STRING; 1933778.ALI22I_02670; -.
DR   OrthoDB; 7055207at2; -.
DR   Proteomes; UP000188617; Unassembled WGS sequence.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   CDD; cd00827; init_cond_enzymes; 1.
DR   Gene3D; 3.40.47.10; -; 2.
DR   InterPro; IPR013747; ACP_syn_III_C.
DR   InterPro; IPR013751; ACP_syn_III_N.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR34069; 3-OXOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE 3; 1.
DR   PANTHER; PTHR34069:SF2; BETA-KETOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE III; 1.
DR   Pfam; PF08545; ACP_syn_III; 1.
DR   Pfam; PF08541; ACP_syn_III_C; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
PE   3: Inferred from homology;
KW   Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW   Reference proteome {ECO:0000313|Proteomes:UP000188617}.
FT   DOMAIN          109..186
FT                   /note="Beta-ketoacyl-[acyl-carrier-protein] synthase III N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08545"
FT   DOMAIN          244..335
FT                   /note="Beta-ketoacyl-[acyl-carrier-protein] synthase III C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08541"
SQ   SEQUENCE   344 AA;  37186 MW;  D16DE34A3BC405D4 CRC64;
     MRYDDLHIAG LGWFHPKTVS VEEAVADGRC EPAAAQRTQT RHVAIAGPED TQPDMAVRAG
     KQALVRSGHR PEDVDLLLHA VANYNGLDGW NAASFVQHRV LGRSGVSYEI RQLSNGGVAS
     IQLAAAYLEG RPGRAAMITA SDKFTEPAWN RWRSSAGLLF ADGASAVVLS RRGGFARVLS
     AVTVSDPELE GLQRGNQPFH DYADPAQYPV ELEARTLEFS DLMPLDESGP RRAAGMRRAA
     NQALAEADTA IEDIRRFVAP NFGFELMRLS CLVPLGIELE RTTWEWGSQV GHTGAADQFA
     GLSHLVETGA VEAGDRVMVV GVGGGFNWTA AVVEITEVPD WSER
//
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