ID   NPS6_COCMI              Reviewed;        1761 AA.
AC   Q09MP5;
DT   20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Nonribosomal peptide synthetase 6 {ECO:0000303|PubMed:17056706};
DE            Short=NPRS 6 {ECO:0000303|PubMed:17056706};
DE            EC=6.3.2.- {ECO:0000305|PubMed:17056706};
DE   AltName: Full=Extracellular siderophore synthetase {ECO:0000303|PubMed:17056706};
GN   Name=NPS6 {ECO:0000303|PubMed:17056706};
OS   Cochliobolus miyabeanus (Brown spot disease fungus) (Bipolaris oryzae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX   NCBI_TaxID=101162;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, DOMAIN,
RP   AND PATHWAY.
RC   STRAIN=WK-1C;
RX   PubMed=17056706; DOI=10.1105/tpc.106.045633;
RA   Oide S., Moeder W., Krasnoff S., Gibson D., Haas H., Yoshioka K.,
RA   Turgeon B.G.;
RT   "NPS6, encoding a nonribosomal peptide synthetase involved in siderophore-
RT   mediated iron metabolism, is a conserved virulence determinant of plant
RT   pathogenic ascomycetes.";
RL   Plant Cell 18:2836-2853(2006).
CC   -!- FUNCTION: NRPS involved in extracellular coprogen-type siderophores
CC       biosynthesis including coprogen, neocoprogen I and neocoprogen II
CC       (PubMed:17056706). The role of extracellular siderophores in fungal
CC       virulence to plants is to supply iron to the fungus during plant
CC       infection, but not to act as phytotoxins, depriving their hosts of iron
CC       (PubMed:17056706). {ECO:0000269|PubMed:17056706}.
CC   -!- PATHWAY: Siderophore biosynthesis. {ECO:0000269|PubMed:17056706}.
CC   -!- DOMAIN: NRP synthetases are composed of discrete domains (adenylation
CC       (A), thiolation (T) or peptidyl carrier protein (PCP) and condensation
CC       (C) domains) which when grouped together are referred to as a single
CC       module (By similarity). Each module is responsible for the recognition
CC       (via the A domain) and incorporation of a single amino acid into the
CC       growing peptide product (By similarity). Thus, an NRP synthetase is
CC       generally composed of one or more modules and can terminate in a
CC       thioesterase domain (TE) that releases the newly synthesized peptide
CC       from the enzyme (By similarity). Occasionally, methyltransferase
CC       domains (responsible for amino acid methylation) are present within the
CC       NRP synthetase (By similarity). NPS6 contains a degenerate A domain
CC       (dA) in the second module and has the following architecture: A-T-C-dA-
CC       T-T-C (PubMed:17056706). {ECO:0000250|UniProtKB:A0A144KPJ6,
CC       ECO:0000305|PubMed:17056706}.
CC   -!- DISRUPTION PHENOTYPE: Leads to increased sensitivity to oxidative
CC       stress and reduces the virulence toward rice plants (PubMed:17056706).
CC       {ECO:0000269|PubMed:17056706}.
CC   -!- SIMILARITY: Belongs to the NRP synthetase family. {ECO:0000305}.
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DR   EMBL; DQ860090; ABI51982.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q09MP5; -.
DR   SMR; Q09MP5; -.
DR   PHI-base; PHI:1008; -.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1200.10; -; 3.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.30.559.10; -; 2.
DR   Gene3D; 3.40.50.12780; -; 1.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR001242; Condensatn.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF00668; Condensation; 2.
DR   Pfam; PF00550; PP-binding; 3.
DR   SMART; SM00823; PKS_PP; 3.
DR   SUPFAM; SSF47336; SSF47336; 3.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 3.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 3.
PE   3: Inferred from homology;
KW   Ligase; Multifunctional enzyme; Phosphopantetheine; Phosphoprotein.
FT   CHAIN           1..1761
FT                   /note="Nonribosomal peptide synthetase 6"
FT                   /id="PRO_0000444387"
FT   DOMAIN          600..675
FT                   /note="Carrier 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          1169..1242
FT                   /note="Carrier 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          1237..1313
FT                   /note="Carrier 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          63..468
FT                   /note="Adenylation"
FT                   /evidence="ECO:0000250|UniProtKB:Q5D6D3, ECO:0000255"
FT   REGION          712..1135
FT                   /note="Condensation 1"
FT                   /evidence="ECO:0000250|UniProtKB:Q5D6D3, ECO:0000255"
FT   REGION          1354..1677
FT                   /note="Condensation 2"
FT                   /evidence="ECO:0000250|UniProtKB:Q5D6D3, ECO:0000255"
FT   MOD_RES         636
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         1203
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         1274
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   1761 AA;  194707 MW;  2ABFFB7C8307FC70 CRC64;
     MSRHQAVLQL HFFASILETL LKDVNHPLSH FDKVSEDELD ELWSWNTPLQ PELRFCMHEK
     VSERAALHPE KIAIDAWDGT LTYGQIEDYS DKLAKLLRLL DDSSNRIIPV LFEKSRWTSV
     AVLAIMKSGA CFALLDPAQP EGRLRAVVQQ VNAKIFLSSK AQSTLAARVA PAATIIPISK
     SKFNKIFSPY TAEQPNTTLP PVSPDQPLYI QFTSGSTGVP KGCILTHSQY TSGAIPRAAA
     VGYYPHSRVL DFASYAFDVC IDSMLCTLAH GATLCTPSDE RRMNDMSGAM RDMRVTFAGM
     TPSVARTLDV DILNNLESIA LGGEGVSISD AMSWGQRTRV VNAYGPSEAT VGATINDNVA
     AKPYITMGQR KGCALWLTEP EDHNKLVPVG AVGELLIEGP IVGNGYLNNP SKTKEVFIED
     PEFLIKGSKS YPGRHGRIYK TGDLVRFDPD GDGEPIFVGR QDQQVKLRGQ RIELAEIEFN
     MQKHLPPDTQ LAAEVIKPSG GGEQTLVAFL VEQKKNGMRH LDGNVFGSFT NKFQSALRDM
     TKQLFVDLPS YMVPSAYIPL WKMPLLVSCK TDRKRLREIG ASVTRQDLRR FNSAVSEKKE
     ATTEMELKLQ SLWAKVLGGD ADFSANDNFF SMGGDSLRAM RLVAAARDEA IVLSVPDIML
     NPTLSAMAEK AKPVSAEETN EVPPFSMIGK DWDADAARRE SARLCGVDAA NVEDVYPCTP
     LQEGLIALSA KFQDAYVAQR VATLPAKTAL RLKEAFDTAV EGSPVLRTRI VNVTGRGLFQ
     VVLKDGQLVR EHGTDTSEYL RRDRNEPMDL GTALFRYGLV KEPESDQMNF VITMHHAVYD
     GWSMPLVFDH VNSAFNGLHT ERPTSFKHFI KHLTSLDPAD AQQYWKKRLE GTSPHQFPPL
     PQKGYTTQAD SLLEHYVTVP TSAHSKLTLA TIIRGAWALV SSLYIGHPDI VFGETLTGRS
     APVPGIEQIE GPMITTVPIR VRLSLDRPIT EYLQMIHAVT VKQIPHEHLG LQNIRRLSKD
     ARVACDLRTG LVLHPKEDED WGKVSLETPA NTFLPASDEE GAREALKFNT YALMLVCTLE
     ENGFLVMASF DSNCISKEAM ERVLVVLDRI VHAFLGNPES KLGDVAVLDP AEARDAEAMR
     PRDVMSDSAL GMSPVDGLES MDASLKELSP NEEKLRNILG RILGMKETDI RPSDSFFDLG
     GDSIGAMRLV SDARAQGLNL TVAQVFQSRS LSDLAASASN EREDKLAEIL SRILGIAKSD
     IKSSDSFFEL GGDSIGAMRL VSDARAQGLS ITVAQVFQSK SLAELASSAE EEMPSQPKTN
     VDAPFIALGK DANLHSPDRV GVYLENQEWE ITNIYPTRPL QQLAVEGTVD LPRYSLRYEL
     IKFATPIDRQ KLEQACQELV ARNEVLRTVF VKDNELTLGV VLSALRVPYT ETAVPEGEDA
     DAFIQAGIKQ DIEAPKPYGS SFVAFNLFTH PNGASTLVFR ISHAQYDEIC LPILFEQLSA
     LYSGTTVPET VPFSKHVNHV VLDNIPKAIP YWENLLSGSE MTVLKPTIPL THRGPADIYR
     EFDISSRPAN ITIGSLPTAA WALVLSRRLN LTDVVFGEVV SGRNVGAPNA DRIFGPTWQY
     IPFRVPFSKS WSYLDLLRYV QDQHMTSAAY ESMGFSEIVK NCTNWDEDKV QWFDTVVHQA
     PAWVEELPFG NGVEAKFQTL YPHGEPLREW KCQAFVKEGG RKLGIEIVTF EEWIGEAEGV
     LEEVGKALEC LMEGRVGESI F