CHRY1_GIBZE
ID CHRY1_GIBZE Reviewed; 2381 AA.
AC I1S3K7; A0A098E4T5;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=Nonribosomal peptide synthetase chry1 {ECO:0000303|PubMed:28708398};
DE Short=NRPS chry1 {ECO:0000303|PubMed:28708398};
DE EC=2.3.2.- {ECO:0000305|PubMed:28708398};
DE AltName: Full=Chrysogine biosynthesis cluster protein 1 {ECO:0000303|PubMed:28708398};
GN Name=chry1 {ECO:0000303|PubMed:28708398};
GN Synonyms=NRPS14 {ECO:0000303|PubMed:22377171};
GN ORFNames=FG11395, FGRAMPH1_01T21959;
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
RN [4]
RP INDUCTION.
RX PubMed=21585270; DOI=10.1094/mpmi-02-11-0038;
RA Lysoee E., Seong K.Y., Kistler H.C.;
RT "The transcriptome of Fusarium graminearum during the infection of wheat.";
RL Mol. Plant Microbe Interact. 24:995-1000(2011).
RN [5]
RP IDENTIFICATION, AND DOMAIN.
RX PubMed=22377171; DOI=10.1016/j.ijfoodmicro.2012.01.018;
RA Hansen F.T., Soerensen J.L., Giese H., Sondergaard T.E., Frandsen R.J.;
RT "Quick guide to polyketide synthase and nonribosomal synthetase genes in
RT Fusarium.";
RL Int. J. Food Microbiol. 155:128-136(2012).
RN [6]
RP IDENTIFICATION, AND DOMAIN.
RX PubMed=25543026; DOI=10.1016/j.fgb.2014.12.004;
RA Hansen F.T., Gardiner D.M., Lysoee E., Fuertes P.R., Tudzynski B.,
RA Wiemann P., Sondergaard T.E., Giese H., Brodersen D.E., Soerensen J.L.;
RT "An update to polyketide synthase and non-ribosomal synthetase genes and
RT nomenclature in Fusarium.";
RL Fungal Genet. Biol. 75:20-29(2015).
RN [7]
RP FUNCTION, DOMAIN, DISRUPTION PHENOTYPE, AND PATHWAY.
RX PubMed=28708398; DOI=10.1021/acs.jnatprod.6b00822;
RA Wollenberg R.D., Saei W., Westphal K.R., Klitgaard C.S., Nielsen K.L.,
RA Lysoee E., Gardiner D.M., Wimmer R., Sondergaard T.E., Soerensen J.L.;
RT "Chrysogine biosynthesis is mediated by a two-module nonribosomal peptide
RT synthetase.";
RL J. Nat. Prod. 80:2131-2135(2017).
CC -!- FUNCTION: Nonribosomal peptide synthetase; part of the gene cluster
CC that mediates the biosynthesis of the yellow pigment chrysogine
CC (PubMed:28708398). Pyruvic acid and anthranilic acid are likely
CC substrates for the nonribosomal peptide synthetase chry1/NRPS14, with
CC pyruvic acid adenylated by the first A domain and anthranilic acid by
CC the second (Probable). If pyruvic acid and anthranilic acid are merged
CC and released from chry1/NRPS14 by hydrolysis, a subsequent amidation
CC would lead to 2-pyruvoylaminobenzamide (Probable). This process is
CC probably catalyzed by the amidotransferase chry2 using glutamine as
CC amino donor (Probable). The dehydrogenase chry5 that has a terminal
CC berberine bridge domain for C-N cyclization could catalyze the
CC cyclization of 2-pyruvoylaminobenzamide to yield acetyl-4(3H)-
CC quinazolidinone (Probable). A final reduction of acetyl-4(3H)-
CC quinazolidinone catalyzed by the oxidoreductase chry4 would result in
CC chrysogine (Probable). {ECO:0000269|PubMed:28708398,
CC ECO:0000305|PubMed:28708398}.
CC -!- PATHWAY: Pigment biosynthesis. {ECO:0000269|PubMed:28708398}.
CC -!- INDUCTION: Expression is induced during the infection of wheat and
CC barley. {ECO:0000269|PubMed:21585270}.
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. Each module is responsible for the recognition (via the A
CC domain) and incorporation of a single amino acid into the growing
CC peptide product. Thus, an NRP synthetase is generally composed of one
CC or more modules and can terminate in a thioesterase domain (TE) that
CC releases the newly synthesized peptide from the enzyme. Occasionally,
CC epimerase (E) domains (responsible for L- to D-amino acid conversion)
CC are present within the NRP synthetase. VerP has the following
CC architecture: A-T-C-A-T-C. {ECO:0000305|PubMed:22377171,
CC ECO:0000305|PubMed:25543026}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of chrysogine.
CC {ECO:0000269|PubMed:28708398}.
CC -!- SIMILARITY: Belongs to the NRP synthetase family. {ECO:0000305}.
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DR EMBL; HG970334; CEF88223.1; -; Genomic_DNA.
DR RefSeq; XP_011325838.1; XM_011327536.1.
DR AlphaFoldDB; I1S3K7; -.
DR SMR; I1S3K7; -.
DR STRING; 5518.FGSG_11395P0; -.
DR GeneID; 23558237; -.
DR KEGG; fgr:FGSG_11395; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G21959; -.
DR eggNOG; KOG1176; Eukaryota.
DR eggNOG; KOG1178; Eukaryota.
DR HOGENOM; CLU_000022_60_2_1; -.
DR InParanoid; I1S3K7; -.
DR Proteomes; UP000070720; Chromosome 3.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1200.10; -; 2.
DR Gene3D; 3.30.300.30; -; 2.
DR Gene3D; 3.30.559.10; -; 2.
DR Gene3D; 3.40.50.12780; -; 2.
DR InterPro; IPR010071; AA_adenyl_domain.
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; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR Pfam; PF00501; AMP-binding; 2.
DR Pfam; PF00668; Condensation; 2.
DR Pfam; PF00550; PP-binding; 2.
DR SUPFAM; SSF47336; SSF47336; 2.
DR TIGRFAMs; TIGR01733; AA-adenyl-dom; 2.
DR PROSITE; PS00455; AMP_BINDING; 2.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 2: Evidence at transcript level;
KW Ligase; Phosphopantetheine; Phosphoprotein; Reference proteome; Repeat;
KW Transferase.
FT CHAIN 1..2381
FT /note="Nonribosomal peptide synthetase chry1"
FT /id="PRO_0000450172"
FT DOMAIN 770..846
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 1845..1921
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 232..632
FT /note="Adenylation 1"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:22377171,
FT ECO:0000305|PubMed:25543026"
FT REGION 882..1286
FT /note="Condensation 1"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:22377171,
FT ECO:0000305|PubMed:25543026"
FT REGION 1309..1701
FT /note="Adenylation 2"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:22377171,
FT ECO:0000305|PubMed:25543026"
FT REGION 1977..2372
FT /note="Condensation 2"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:22377171,
FT ECO:0000305|PubMed:25543026"
FT MOD_RES 807
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1882
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2381 AA; 260936 MW; 50F0E1FEDD45D175 CRC64;
MAPPAAVSPL FVPQVGAPTD FHGLEPQWDT VGVECSGLTN KALANWLHKE RHSHLSLIQA
AWALCLRGYT GSEDVSFTCL GPERNYCCHV SPTQPVRSLF DLQHVESIGQ NRTTFWDAIS
VVLTHEDLIE VTNPSAMFDL AVCFSQRVEA HLPSIKVYYR SSKVMSAMAE MIAATVAKSI
EEIVAKIDSQ INDLELCSDL DINRLARWNI LSNAQDPIPQ PIHRVISQNS TLHPTSIAVS
AWDGDFTYRE LDRLATGLAI WLQHLGIVGP EVFVPLVFDK SKWAVVAQLA VLKAGGAYFF
INPSHPVQYS RELCSSLNPL VAVCSANHSG IAKELVCEAI ALGDSVRELL ESIPVDDTPG
SPTVNISTSN AMYITFTSGT TGKPKGIITE HSAFYCMAVA NAKSLQINNT TRMLQFASYS
FDVSNRDTLV TLMFGGRVCI PSESDRLNNL AGFMRDHEVN LASLTPSMAS TLSPSSCPSL
RGLVLGGEPM TESHISTWSK HVQLFNAYGV SESTGIAALA SNIKSGVSPS NIGYGCGSRL
WVVAIDQPDK LAPIGALGEL VIEGPSISRG YLDDKARTDQ HFTSDPTWKK RIYQEYGSRQ
SGKRTFRTGD LVRYNLDGSL QLAGRRDHQV KVNGQRLELT AVEHHISACP QVLEAGFGHV
AVVAVKAGNS GSTKLVAFLG RDTSRETCTP AQMVPEQLKD MDGLRSDLEG FLLLDLPSYM
VPSEFVFLQH MPLTTSNKLN RLLLQNTAAQ ALAVDHDEQL NGHDLSDGEA PSTDDERILA
ETWAKILGIK ESTISRNDSF FRRGGDSMAA IRMVASLREA GFVISVSDIF KTSILSELAL
LMVQADDKST STLPAPFSML EDSQKTIQSI ATESGLLVDD IEDAYPCTHM QQGLLALTAQ
NSRAYIGTYF WQLASGVDMD RFKQAWQDVW QHNPILRTRA VQTPEGLLQV VVRADMPWEL
VSSVTGFSTK IDINEGPLAR FYLSADTFRL DIHHALFDEW SLDLLLAQVQ QAYAGEALQM
KPFSPFVRHI LQQDHLSSEK FWRQQFSSLE VEHFPPTASK VGDTTKTNVL ERDLPLDAGM
STKYTISSVV RLAWAILLWH QTGSEDVVFG ATVSGRNASI DGIDQISGPT LASLPVRIKL
PTGSSVQDGL AEVQDQFVNM IPHEQTGLSR IRQYSNEAAE ACNFQNLLVV QPHEQKVDSA
VFRSSTGGAA SSDNTTAFAS YPLVLTCRPD EGRVNFKAAF DSDLITSETI EGLLRQLSHV
VRQIMTSESV AIRDISTVPP QDMEKLQMWN ETVPKAVDIC VHDRIRDLSK SQPDALAVHS
MDLDLTYQQV EDYSNHFASH LISQGVTQGD FVPVLIERSP WAPVIMLAVL KTGAAFVLLD
LSHPIQRLRT MCSMIDAKIL VAFEQTRHIG EGLSLPITTF EPVEYLERQH QVCGTLPPIV
SPHLDSPACV VFSSGSTGVP KGIVLPHGAI ATSAAVMREQ GNLTATSRVF HFASFAFDIS
IGEILFTLAA GACICVPHEQ ERRDNPGKAA GDLKATWALL TPSVINLFDP SDVPTLKTLG
SCGEPLTSQI VDIWAHRLNL FAMYAPAECT VISHIGRVLP ETHPSHIGRS FGAASWVVDP
TDHNRLVPIG TIGELLVEGP VVSTGYLKDK ARSDLVFVEN PSWLSQFRSS CGRMYKTGDL
VRQTPDGSLQ FLGRKDDQVK LHGQRLEVGE VEHCLMSVCE DIKAVAVECV KVANQNNRAV
LVAFIAPHTE GAWGQVASEA EGGDVQWVAS PNEEFYSTIE TMDTSARDQL PSYMVPAYFI
PVAHIPLSLS GKINRRLLRE TFSASISKNL DQYQLRTNTV EVDGTPETAH DREIQEIFAK
VLSLDAQSVP MNGNFFSMGG DSISAMAAST LARRRGIDLA VATIFTHQVL SKISLACAPV
DGETTKAGEH TEGQAGNASN GGHITLDKLP HHIPRDVLEN VIEASPATEF QAMTLYNFYS
RYLWIALPDG VDEERLKAAY NSLVQKHSIL RTVFYTNADG SIVQLTLRDM PVALTHYTDV
DDMEKHCADD SLSMGVPIDG NPGIQAQLLK LKDSRKILAL RLPHALFDGM SLSTICDDLN
SAYKGQEMSP CGQFSDHVRQ VWEKRRPETY QVWKDVLQDT PITVMDSESL PVAKKTASAQ
VSDEPQLVTA TLETGPISTP RNSTTATLVK LAWAITLSKL FTLGQNDNSL GDVVFGQVVH
GRVLGIPHED RIIGPCLNII PVRVHFPSSP EKHDLLSQVQ QQHVQTMAVQ NLGLGEITRN
CTTWESGTRF GSFIRFQNFT NSQESTCDFD GHACETGLYS LPNRPSKTAD VLVAPKGSRL
SIAMTVSSEV MDEEAADYVV RYFGDVMESL SRDEEACSYL C
