ID A0A0N0SH33_9ACTN Unreviewed; 1491 AA.
AC A0A0N0SH33;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Beta-ketoacyl synthase {ECO:0000313|EMBL:KOU49176.1};
GN ORFNames=ADK54_11040 {ECO:0000313|EMBL:KOU49176.1};
OS Streptomyces sp. WM6378.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1415557 {ECO:0000313|EMBL:KOU49176.1, ECO:0000313|Proteomes:UP000037774};
RN [1] {ECO:0000313|Proteomes:UP000037774}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WM6378 {ECO:0000313|Proteomes:UP000037774};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (JUL-2015) 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:KOU49176.1}.
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DR EMBL; LGDD01000094; KOU49176.1; -; Genomic_DNA.
DR PATRIC; fig|1415557.3.peg.2475; -.
DR Proteomes; UP000037774; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion 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 CDD; cd00833; PKS; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.90.470.20; 4'-phosphopantetheinyl transferase domain; 2.
DR Gene3D; 3.30.70.250; Malonyl-CoA ACP transacylase, ACP-binding; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR InterPro; IPR008278; 4-PPantetheinyl_Trfase_dom.
DR InterPro; IPR037143; 4-PPantetheinyl_Trfase_dom_sf.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR029069; HotDog_dom_sf.
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; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR049551; PKS_DH_C.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43074; OMEGA-3 POLYUNSATURATED FATTY ACID SYNTHASE PFAB-RELATED; 1.
DR PANTHER; PTHR43074:SF1; PKS_AT DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01648; ACPS; 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; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF56214; 4'-phosphopantetheinyl transferase; 2.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF54637; Thioesterase/thiol ester dehydrase-isomerase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..452
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT REGION 864..885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 962..984
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1491 AA; 158577 MW; 5B64CE68CEC895B2 CRC64;
MAVLLPGAKD LDAYWRNLVD GVDAVREVPE GRWDPVYYRP GDQGGAADRI YCRRGGFVDG
LAEVDAARFG IMPSSVAGTE PDQLIALSVA ARAIADAGGE ERLPERGRVG VVLGRGGYLN
PGLVRLDQRV RTAHQLTRTL GELMPHLAPD QLDRVRAAFT EALGPEHPES AIGLVPNLAA
SRIANRLDLR GPAYTVDAAC ASSLIAVDQA VGELAAGRCD LMLAGGVHHC HDITLWSVFA
QLRALSPSQR SRPFHAAADG ILVGEGTGVV VLKRLADAER DGDRVYAVIR GTGVAGDGRA
AGLMNPDPGG QTRAVRQAWR AAGLDPRAPG SLGLLEAHGT GTPAGDAAEL ATLAEVFGPG
ADGADAAVIG SVKSMIGHCM PAAGVAGLVK AALAVHHATL LPTLHCDEPH PALARTRFRP
AALARPWEGP LRRAAVNAFG FGGINAHVVL EQAPGAVPAR PRAAVREPER VLRLSADTAE
DLARLLDADD TTVRARGDAS SAQAASAAYG PSASVPYAQG TSETPAARLG IVDPTAKRLA
LARRAVAQGC PWRGRSDVWF APRPLLGKAG GGKVAFVFPG LEAEFTPRVD EVAEHYGLRL
PGRAYTEATD VARHGLGVLR VGRILDEALR ALGVRPDGVA GHSVGEWTAM IAGGMFAADE
ADDFFASFDP DSLRVPGLAF AAIGAPAARV SEALTDWPDL VLSHDNSPGQ SMVCGPEQPV
EEFAAKLRAE RVICQVLPFR SGFHTPMLAP YLGPMKRGVD AAEILPQRVP VWSGTTAAPF
PAGPDEVRAL FVRHLLEPVR FRPLVDAMYA AGFRAFVQVG TGRLTSLIDD TLKDRDHLTL
SANSPRRGGL AQLLRVETGL WAEGYEPKPA RPGRPRASEA TSTSAAPIPL DLTAALVPLD
PHRLDELRAE LRPRPEREAE LPIPTRLLSD SLTRRHPVAA ELDALMRETV DSVTAVLEGA
GAPAASVTPA APDSATPPPE HRTRLRVSTT AMPYLLDHCF FPQRPGWPDP ADRHPVVPAT
TVLHHLMAAA ERAAPGQRAV AVHDVRLEKW VNAIPAVDVT ITARPQGPGR WAVAFGPYAR
ATVQLAPAYP APPPAPPLDA ADEHPPDIAA AQLYEDRWMF HGPAFRGVTA LHGVGPGHVR
GTITTPAAPG ALLDNVGQLL GYWLMSTHHT RTVIFPVALE RARFHGPPPP TGTRVDCHAV
ITSLTEDTLL ADVRLTLPDG TVWAELSGWR DRRFSGLDAR RSGGYPEHRA LAEAQPGGWC
LLRDAWPDLA SRDLLTRMQL GRAERAAYEA RPPRGRRQWL LGRIAAKDAV RRWLWERGEG
AVFPAEIEIV NEKSGRPRAV GVHGRRLPAL DLSLAHRGDL AVALVRPPGH GPYANGVGID
VEEIADRTPE THRVALGPRE LALLGRLVAA GSGESEALWF TRFWAAKEAA AKAEGTGFGG
RPHAFEVTGA APDSLTVTVD GRHHHVHCTL VDPTHVVAWT TSATTLKEST Q
//
