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Database: UniProt
Entry: S4N228_9ACTN
LinkDB: S4N228_9ACTN
Original site: S4N228_9ACTN 
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
//
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