CHRY4_GIBZE
ID CHRY4_GIBZE Reviewed; 259 AA.
AC I1S3L0;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Short-chain dehydrogenase chry4 {ECO:0000303|PubMed:28708398};
DE EC=1.1.1.- {ECO:0000305|PubMed:28708398};
DE AltName: Full=Chrysogine biosynthesis cluster protein 4 {ECO:0000303|PubMed:28708398};
GN Name=chry4 {ECO:0000303|PubMed:28708398};
GN ORFNames=FG11398, FGRAMPH1_01T21965;
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 FUNCTION, 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: Short-chain dehydrogenase; part of the gene cluster that
CC 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:0000305|PubMed:28708398}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; HG970334; CEF85999.1; -; Genomic_DNA.
DR RefSeq; XP_011325835.1; XM_011327533.1.
DR AlphaFoldDB; I1S3L0; -.
DR SMR; I1S3L0; -.
DR STRING; 5518.FGSG_11398P0; -.
DR GeneID; 23558240; -.
DR KEGG; fgr:FGSG_11398; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G21965; -.
DR eggNOG; KOG1208; Eukaryota.
DR HOGENOM; CLU_010194_44_5_1; -.
DR InParanoid; I1S3L0; -.
DR Proteomes; UP000070720; Chromosome 3.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 3: Inferred from homology;
KW NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..259
FT /note="Short-chain dehydrogenase chry4"
FT /id="PRO_0000450175"
FT ACT_SITE 154
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 5..13
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 31..32
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 77..79
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 154..158
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 185..187
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
SQ SEQUENCE 259 AA; 28450 MW; 2A1864F8D191AFB3 CRC64;
MARILITGST DGFGFEAARQ LIERKHQVYL HARNQERADE VKTKLPGAAG VLIADLTTVA
ETRKLADEAN AIGTFDAVIL NAGLLYGPFR KSDLGVPASV FVNLVSPYIF AALLNPPKRL
IFIASVLHHE ADTSLKDIFW LERGEKEWKD FPAYCDAKFH VVLLVNAIAR RFKDTSVIAV
HPGYVPTKLA GQDAPGKMED GIETYVMLAE GDYDTSLTGV YFDPKKERAQ PHALTADLDK
QEAVVKACEE LTGIKLPSP
