ID S4N228_9ACTN Unreviewed; 1284 AA.
AC S4N228;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE SubName: Full=Putative Erythronolide synthase, modules 3 and 4 {ECO:0000313|EMBL:EPJ40912.1};
GN ORFNames=STAFG_2043 {ECO:0000313|EMBL:EPJ40912.1};
OS Streptomyces afghaniensis 772.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1283301 {ECO:0000313|EMBL:EPJ40912.1, ECO:0000313|Proteomes:UP000015001};
RN [1] {ECO:0000313|EMBL:EPJ40912.1, ECO:0000313|Proteomes:UP000015001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=772 {ECO:0000313|EMBL:EPJ40912.1,
RC ECO:0000313|Proteomes:UP000015001};
RA Gruening B.A., Praeg A., Erxleben A., Guenther S., Fiedler H.-P.,
RA Goodfellow M., Mueller M.;
RT "Draft Genome Sequence of Streptomyces afghaniensis, Which Produces
RT Compounds of the Julimycin B-Complex.";
RL Submitted (FEB-2013) 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:EPJ40912.1}.
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DR EMBL; AOPY01001352; EPJ40912.1; -; Genomic_DNA.
DR PATRIC; fig|1283301.3.peg.2016; -.
DR HOGENOM; CLU_000022_16_6_11; -.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000015001; 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; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 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; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020807; PKS_DH.
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 Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 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:UP000015001};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..427
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1210..1284
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1284 AA; 135429 MW; 8892880C81AFACE9 CRC64;
MPDIAIVGMG CRFPGAPGVR EFWHLLERNT DAVTPVPEDR FDVRRYHSAR PGEPGTTVSR
HGGFIDDLYG FDAAFFGIAP REALAMDPQQ RVLLQVVWEA LEDAHIRPSS LAGSRTGVFV
GQATAEYADL AESDGHQDVH GMAGSRLRTM TAGRLSFALD LRGPSLMVDT ACSSSLVAVH
LARQSLLTGE SDLAVAAGVN AVLSPSDAIT YSQGGMLAPD GRCKFADASG DGFVRSEGVG
TVLLKRLPDA LRDGDQVLAV LRGSAVTNDG QGSGTLLQPA VSGQTEMIRS ACRSAGITPD
RLDYVEAHGT GTPVGDDVEL RALAEAVGDE GRSRSRPLPI GSVKTNIGHA EAAAGIAGLI
KTVLIARHRT IPASLHLRTP HPVLAGDAAA LAVVTRNTPL VPGDRPALMG VSSFGLSGTN
AHVIVGEYVP EPRTGRLPHR TSDAPEEAQL MLLSARTPAA LSRLAARYAD FLDGDEGRAF
PLRDICHTAA TRRDAHPHRL WAVGRTHDEL AAALRALAAG EETPDGGTAD AGFTGDRRTA
FVFPGQGSQW LGMGRRLLAS EEVFRRTLTE CDGAVREELG WSVIGLLTGD GEDAPAQELP
DDVAVVQPLL WAVQVSLAAL LRAKGVEPDL CVGHSMGEVA AAQVCGALSL RDAASVICRR
SSLMQGQAGR GAMLAVELDA PAAADAAAPH GDAVCVAAEN APASTVLAGD ARALHLIAER
LQAQGVSCRY VKVNVASHSP YMAELRDDLA DALAHLTPLP ARTAMFSTTR CEPVDGPELD
AAYWVDNLRE RVRFVEAVRA AAKEETVFLE VSPHPLLAQS VTAVLDEQGA APAAVATLKR
HQDDGENLTR ALGQLFSHGG RIDWNSYFQG AAPRVPLPTY AWDQEQFRKE PAPAPAPAAP
AEHVREVELR ELGLDDLGQS VRTGDGAAVV PPVLYVKAVL RAADGIGPRG EGVLEDVEFG
DRPWELAHAR DAAVRVCLTP AAQQGCFVFT VTALRTADGT RDGELCMTGR FRTAAPAAEE
GEGAAGRSGT AEPYGRELLD AGLTRCTAYV PAAEFYRRAQ ARGYTIDAAL CTVAQLWGSE
GESVARMRRS PGAGTAGLEA GLLTMLAAWP HATGAGGRPD GYVPVSFGRV LVRDEAGVGQ
DHWCVARFTP SDGTDDARCD VWLTAEDGHV IAEFRDIRLR RRAAGPAREA LDAEGPVPVP
VPATTAPGRA PTPDDVLKQA ATVLGLSATR LDPRRPLRTL GLDSLLATEL RVRLHRTAGV
DISARRLLGR EPIGVIAASV ASQP
//