CHRY6_GIBZE
ID CHRY6_GIBZE Reviewed; 240 AA.
AC I1S3K6;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 25-MAY-2022, entry version 52.
DE RecName: Full=Glutamine amidotransferase-like protein chry6 {ECO:0000303|PubMed:28708398};
DE EC=3.-.-.- {ECO:0000305|PubMed:28708398};
DE AltName: Full=Chrysogine biosynthesis cluster protein 6 {ECO:0000303|PubMed:28708398};
GN Name=chry6 {ECO:0000303|PubMed:28708398};
GN ORFNames=FG11394, FGRAMPH1_01T21957;
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: Glutamine amidotransferase-like protein; part of the gene
CC cluster 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:0000305|PubMed:28708398}.
CC -!- SIMILARITY: Belongs to the peptidase C26 family. {ECO:0000305}.
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DR EMBL; HG970334; CEF87652.1; -; Genomic_DNA.
DR RefSeq; XP_011325839.1; XM_011327537.1.
DR AlphaFoldDB; I1S3K6; -.
DR SMR; I1S3K6; -.
DR STRING; 5518.FGSG_11394P0; -.
DR GeneID; 23558236; -.
DR KEGG; fgr:FGSG_11394; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G21957; -.
DR eggNOG; KOG3179; Eukaryota.
DR HOGENOM; CLU_054974_0_0_1; -.
DR InParanoid; I1S3K6; -.
DR Proteomes; UP000070720; Chromosome 3.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR CDD; cd01741; GATase1_1; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR044992; ChyE-like.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR017926; GATASE.
DR PANTHER; PTHR42695; PTHR42695; 1.
DR Pfam; PF00117; GATase; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 3: Inferred from homology;
KW Glutamine amidotransferase; Hydrolase; Reference proteome.
FT CHAIN 1..240
FT /note="Glutamine amidotransferase-like protein chry6"
FT /id="PRO_0000450176"
FT DOMAIN 13..205
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 102
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 185
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 187
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 240 AA; 25874 MW; CAC782F0ED892B1A CRC64;
MSSPSFRVAI LANFILDDTG GRPMIDKITQ LIRQSKPDAE INVYAAIEGD TLPDPETKDL
IILTGGPFNL LKDERPKWVV DTLEYLKTVT AGPSKPKILG ICWGQQAIAL ALGGALGKSD
KGQIVGIADI PLTPEGTKFF ESPSLTIHKN HEILVTDIGP HLLPLALNNE VLMSKDGQVL
TFQGHPEMDS VLSRLFVASD NPVLVGAGSD SGLKPIDSPH DGEIIFERIV RWASPETAHS
