ID   Q9X992_9ACTO            Unreviewed;      1847 AA.
AC   Q9X992;
DT   01-NOV-1999, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1999, sequence version 1.
DT   19-JAN-2010, entry version 50.
DE   SubName: Full=PimS0 protein;
DE   SubName: Full=Polyketide synthase;
GN   Name=pimS0;
OS   Streptomyces natalensis.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Streptomycineae; Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=68242;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=99214571; PubMed=10187796; DOI=10.1074/jbc.274.15.10133;
RA   Aparicio J.F., Colina A.J., Ceballos E., Martin J.F.;
RT   "The biosynthetic gene cluster for the 26-membered ring polyene
RT   macrolide pimaricin. A new polyketide synthase organization encoded by
RT   two subclusters separated by functionalization genes.";
RL   J. Biol. Chem. 274:10133-10139(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=20547809; PubMed=11094342; DOI=10.1016/S1074-5521(00)00038-7;
RA   Aparicio J.F., Fouces R., Mendes M.V., Olivera N., Martin J.F.;
RT   "A complex multienzyme system encoded by five polyketide synthase
RT   genes is involved in the biosynthesis of the 26-membered polyene
RT   macrolide pimaricin in Streptomyces natalensis.";
RL   Chem. Biol. 7:895-905(2000).
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AJ132221; CAB41040.1; -; Genomic_DNA.
DR   EMBL; AJ278573; CAC20930.1; -; Genomic_DNA.
DR   HSSP; P08659; 1LCI.
DR   SMR; Q9X992; 551-644, 558-673, 660-1543, 1577-1657, 1677-1769.
DR   GO; GO:0000036; F:acyl carrier activity; IEA:InterPro.
DR   GO; GO:0048037; F:cofactor binding; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   InterPro; IPR001227; Ac_transferase_dom.
DR   InterPro; IPR009081; Acyl_carrier_prot-like.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPlipase.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR000794; Beta-ketoacyl_synthase.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   InterPro; IPR006163; Phsphopanteth_bd.
DR   InterPro; IPR020801; PKS_acyl_transferase.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_reg.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR006162; PPantetheine_attach_site.
DR   InterPro; IPR016039; Thiolase-like.
DR   InterPro; IPR016038; Thiolase-like_subgr.
DR   Gene3D; G3DSA:3.40.366.10; Ac_transferase_reg; 1.
DR   Gene3D; G3DSA:3.40.47.10; Thiolase-like_subgr; 2.
DR   PANTHER; PTHR11712; Ketoacyl_synth; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF00550; PP-binding; 2.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 2.
DR   PROSITE; PS50075; ACP_DOMAIN; 2.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
PE   4: Predicted;
KW   Phosphopantetheine; Transferase.
SQ   SEQUENCE   1847 AA;  193383 MW;  F61AE9AADD6FC1F9 CRC64;
     MVPVHTDDYA IQPPADTAHG GGGFTLPAVF EAAVESAPDA VALVDGTVPG PGRMWRADVD
     ALARGLQESG IAPGDVVAVR LPNCGRFPTL HLAVAAVGAV LLPIHQGTPL PEVDALLTRA
     EPALLVLSAA GSDGLATARS LLESVPSLRG VLLAGASGDG ESGSVGGGES GSGRRSLDGL
     LAGWAGSGPR PVDVTPDMPL VLVPSSGTVS ARPKLCVHSH DGLLSNTAAV TAEAADAFDG
     PVLTACPMTH LFGLQSLHAA LFAACTQVLL TGWDVDRFLE QAREHGPRVV FAVPAQLRDV
     VTRLARTGEP AGFTPYQVRT AGAAVAPALA VRVRAVLDCE LVVVWGMSEI GTGTRTRAHH
     PDGCVGEPVS GVDVRVVDEH GQECAADERG ELQYRGPGLF RGYFREPELT RSALTDDGWL
     RTGDLATVDA DGVVVLHGRA AELINTGGRK FSAGEVEGLL SGFTDLGPLA VVGAPDDRLG
     EYPCLVVTDH ADGTIGLSEV TAFLRRLGLA DHKIPLELVT VRELPFSPAG KLDRGALKRL
     LANLAEVSVP ARLGAVPPYT AEEALDLVRD CVGRVLRYGG AAVPFPPDKD FFSPDKDFRQ
     LGLDSIGAVR LRNLLREETG LPLPATLAFD SPTPRAVARV LAEQEEPSQD EPRENPADGA
     DPVAIVGMAC RLPGGADSPD ALWELLADGT DAMSPFPTDR GWDLDRLFDE DADRPGTSYA
     REGGFLHDAG DFDAGFFGLS DQEATATDPQ QRLLLEAAWE TFERAGIDPQ SLRGSRTGVF
     TGAMDRGYGT SASAAPSAWE SMLITGTAGS AVSGRIAYTY GLEGPALTVD TASSSSLVAL
     HLACRSLRSG ETDLALAGGV TVMATPAPFA HFSRLRALSP DSRSMAYADA ANGSAWSEGA
     GLLLLERLSD ARRNGHRVLA LVRGSAVNQD GASNGLTAPS GPAQQRVIRQ ALADAGLTPQ
     DVDAVEGHGT GTPLGDPIEA QALLATYGQQ RPVERPLWLG SVKSNFGHTQ AAAGVVGVIK
     TVLALRHGVL PQTLHVDAPS AKVDWSAGSV RLLTEARPWP RESGRTRRAG VSSFGLTGTN
     AHVILEEAPG EAAAGARAEV PEEARCASSP ARLPEPPGDA AAPWVLSARS RAALRAQALR
     LADQVAADPG LRAQDVAHAL ATSRTLHRHR AVVSGSDRAQ MLAAAKRFGL GERTAGVTPD
     DSAPGLLAFV FSGQGSQRSG MGRAAAEAFP VFGRALGEVC AALDPLLTRP LTSVMWAAPG
     SEEAARLDDT TYTQPALFAV QVALYRLFES WGVVPDQLVG HSVGEISAAH VAGVLGLRDA
     CTLVAARSRL MGALPPGGAM VAVRITEPEV TPWLAELTDE VSIAAVNGPH SLVLAGAEAP
     LVALTDRLAA AGHKTRRLMV STAPHSPLMD PMLEEFRAVV RTLSYAAPAV PLVSTVTGRP
     LTGEEARDPD HWVRHVRQSV RFKDAIGRLR DERVTGFLEL GAEPALTPMI DECLESADGQ
     PGTALVPSLR AGVPERDALL TAVARVHAQG VPVDWDAVLP GAEASVTVRG LPAADRQWFR
     FVPDQGAPLT LADRSLHLEG AAHLRDVGGC RTADGRWVKM GVLYRTNNLH ALTDADLAKL
     QRLGIRTDFD LRMPGERAKA PNRVPTGARY IVADAFDAHL RDGLSLSERD LERLREARLS
     GLDEAEQHAL VLALVLAETS AVLGGQETPG EEPHGEEGHR TFKEMGINSL NAVELRNRLI
     AATDLRLPAT LVYDYPTPKA VVRLVRERLA RPASPARDVA SVVAELESLL TAGAEVSEET
     AARLKAVTAV STGTTGSGSG TGAGSGGALD LVSASDEELF RLMDAES
//