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Database: UniProt
Entry: G2GEF7_9ACTN
LinkDB: G2GEF7_9ACTN
Original site: G2GEF7_9ACTN 
ID   G2GEF7_9ACTN            Unreviewed;      1286 AA.
AC   G2GEF7;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 60.
DE   SubName: Full=Beta-ketoacyl synthase {ECO:0000313|EMBL:EGX58132.1};
GN   ORFNames=SZN_19450 {ECO:0000313|EMBL:EGX58132.1};
OS   Streptomyces zinciresistens K42.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=700597 {ECO:0000313|EMBL:EGX58132.1, ECO:0000313|Proteomes:UP000004217};
RN   [1] {ECO:0000313|EMBL:EGX58132.1, ECO:0000313|Proteomes:UP000004217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K42 {ECO:0000313|EMBL:EGX58132.1,
RC   ECO:0000313|Proteomes:UP000004217};
RA   Lin Y., Hao X., Johnstone L., Miller S.J., Wei G., Rensing C.;
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
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:EGX58132.1}.
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DR   EMBL; AGBF01000066; EGX58132.1; -; Genomic_DNA.
DR   RefSeq; WP_007497521.1; NZ_AGBF01000066.1.
DR   PATRIC; fig|700597.3.peg.3813; -.
DR   OrthoDB; 9778690at2; -.
DR   Proteomes; UP000004217; Unassembled WGS sequence.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; 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   GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.30.70.3290; -; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.10.129.10; Hotdog Thioesterase; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   InterPro; IPR001227; Ac_transferase_dom_sf.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR018201; Ketoacyl_synth_AS.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   InterPro; IPR032821; PKS_assoc.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF16197; KAsynt_C_assoc; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SMART; SM01294; PKS_PP_betabranch; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   4: Predicted;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004217};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          7..431
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1160..1242
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          1128..1152
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1134..1148
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1286 AA;  132697 MW;  AB19323C1D468CFE CRC64;
     MAEVGGDGAV AVVGLGCRVP GADTVEALWR LLDERRDEIT PVPAGRESLH RAVTAAGAGA
     TGAGWGGFVA GLESWDPGFF GISPSEAARI DPQQALALEV AWRALESAGV VHDDLLGSRT
     GVFLGQATHD HAMLLGGRSA HEAQGPYTNP GLSHAITANR LSYLWDLRGP SLTVDTACSS
     SLVAVHLAVR SLLSGECDRA VAGGVNALLS PVPQLGAAGL TALAADGRCR TFDASGQGYV
     RSEGAGAVVL RRLADALAAG EHVHAVITGS GVNQDGRTNG LTAPSGRAQT ELMARTLRQA
     GVTSATALGY AELHGTGTPL GDPIEGRALG AALDQAVGAD RPPLPVGSVK ANIGHLEAAA
     GVLGLIKAAL VLRHGVVPGN PHLREVNPRI DLDGFGLSMS AAHTPLPARA GAVTVSSFGF
     GGTNACVVLA RAPRRPCPGQ DGAREDSGPV VLALSARSAR SLAVTAGDWA QWLESLEDWA
     DVRRAARAAS AHRTAFEWRA AVAAADRGEL RERLAEFADG TRGARETRTA GPPSVGFVYS
     GHGSQWEGMG RELLRRCPPF ARRVREADAV LAPMLGWSPL AALEGTAPAD LDDICVAQPL
     IFTVQLALTA QLADLGIRPA AVAGHSMGEL SAAVVAGRLG LATACRVLRA RNDAVAAARG
     TGGMAVVEAG AREAAEILAG LGSPVTVAAD NSPRSCVLSG PGEALDAALD AFGRQGRDTR
     RVKVDYPSHG PLMEGPAEQL GRVLGTVEAP GRGCGPAFYS SVLGRLHDAP LDAGYWLDNL
     THPVRAREAV TAMADDGVTH VLEISPHPVL LVALRESLMA LGEGAVALPT GHREQRGDLG
     LRDVEAALFE HGLHLRADAD AATRAWADRL PVHPFHRTPV YRAPEAVPGG RAGGSGPGVL
     TEASFQPGTF LGEFTLPEPR EEHLVAGEPA VSVTELVAAA LRAAREAGVE DAEFVQDLEM
     HRPLPADPDA ARQVVVHLGG GGARPARSAA VRFLHRRSGG WTTAASCTVG VRPPAPLAEI
     DSAVRCEVSV PALPPTASPA SSAGVLDRAL PEVARALLAG RPGLDPDRTA VTRVGAVRVT
     AEAWTADKAV ARGRLRECDG EVVMDLAFVS TAGSLLAQVQ HMALAQLSGR GGDDPQDRVA
     DPDERAGSGG GLRRTLFALP TEAERRQALG GWLRGVLGGI LPNGLREDAA DDLPFAEMGL
     ESLMGVELRN RLEKELDIRL SATLVWAHPT IGQLTDALLG RVVQGAEQVR QAAPAAPEAT
     GAAGASGSDA LSQLLAELDG RPRGKA
//
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