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
//