CHRY2_GIBZE
ID CHRY2_GIBZE Reviewed; 671 AA.
AC I1S3K8; A0A098E1Z9;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 25-MAY-2022, entry version 59.
DE RecName: Full=Amidase chry2 {ECO:0000303|PubMed:28708398};
DE EC=3.-.-.- {ECO:0000305|PubMed:28708398};
DE AltName: Full=Chrysogine biosynthesis cluster protein 2 {ECO:0000303|PubMed:28708398};
GN Name=chry2 {ECO:0000303|PubMed:28708398};
GN ORFNames=FG11396, FGRAMPH1_01T21961;
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: Amidase; part of the gene cluster that mediates the
CC biosynthesis of the yellow pigment chrysogine (PubMed:28708398).
CC Pyruvic acid and anthranilic acid are likely substrates for the
CC nonribosomal peptide synthetase chry1/NRPS14, with pyruvic acid
CC adenylated by the first A domain and anthranilic acid by the second
CC (Probable). If pyruvic acid and anthranilic acid are merged and
CC released from chry1/NRPS14 by hydrolysis, a subsequent amidation would
CC lead to 2-pyruvoylaminobenzamide (Probable). This process is probably
CC catalyzed by the amidotransferase chry2 using glutamine as amino donor
CC (Probable). The dehydrogenase chry5 that has a terminal berberine
CC bridge domain for C-N cyclization could catalyze the cyclization of 2-
CC pyruvoylaminobenzamide to yield acetyl-4(3H)-quinazolidinone
CC (Probable). A final reduction of acetyl-4(3H)-quinazolidinone catalyzed
CC by the oxidoreductase chry4 would result in chrysogine (Probable).
CC {ECO:0000269|PubMed:28708398, ECO:0000305|PubMed:28708398}.
CC -!- PATHWAY: Pigment biosynthesis. {ECO:0000305|PubMed:28708398}.
CC -!- SIMILARITY: Belongs to the asparagine synthetase family. {ECO:0000305}.
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DR EMBL; HG970334; CEF87644.1; -; Genomic_DNA.
DR RefSeq; XP_011325837.1; XM_011327535.1.
DR AlphaFoldDB; I1S3K8; -.
DR SMR; I1S3K8; -.
DR STRING; 5518.FGSG_11396P0; -.
DR GeneID; 23558238; -.
DR KEGG; fgr:FGSG_11396; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G21961; -.
DR eggNOG; KOG0571; Eukaryota.
DR HOGENOM; CLU_014658_1_0_1; -.
DR InParanoid; I1S3K8; -.
DR Proteomes; UP000070720; Chromosome 3.
DR GO; GO:0004066; F:asparagine synthase (glutamine-hydrolyzing) activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006529; P:asparagine biosynthetic process; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR CDD; cd01991; Asn_Synthase_B_C; 1.
DR CDD; cd00712; AsnB; 1.
DR Gene3D; 3.40.50.620; -; 2.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR006426; Asn_synth_AEB.
DR InterPro; IPR001962; Asn_synthase.
DR InterPro; IPR033738; AsnB_N.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF00733; Asn_synthase; 1.
DR Pfam; PF13537; GATase_7; 1.
DR PIRSF; PIRSF001589; Asn_synthetase_glu-h; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR TIGRFAMs; TIGR01536; asn_synth_AEB; 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Glutamine amidotransferase; Hydrolase; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..671
FT /note="Amidase chry2"
FT /id="PRO_0000450173"
FT DOMAIN 2..220
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT DOMAIN 251..639
FT /note="Asparagine synthetase"
FT /evidence="ECO:0000255"
FT ACT_SITE 2
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
SQ SEQUENCE 671 AA; 76115 MW; B277CA9F7F0B0F74 CRC64;
MCGISAFITH PGHSRSPVLN GDAKQVVEEL ETSLDLIAHR GPDARGRWFS DNHHVGLGHV
RLSIIDLSPS GNQPFHDEQG GIHAVVNGEL YDYERYKAQL ADEFKFVGNS DCEIVIALYK
HYGLSFISHL RGEFAFVLWD ENRQQLIAAR DRYGIKSLYY TVHQNKLLVA TEIKSFLAFG
LEPEWCVRSL RDQSWRVDST TFFEGVYKVR PGHYLICRPN EREEQHPYWD LEYPDKFAKD
LRSEDEITEG VRERLLEAVR IRLKADVPVA VYLSGGIDSS SVAGMVSHLI KQGTKLGNET
SLLPSSMKCY TVQFDEGSGA DESAIARRTA DFLGVDIHLV KMDEEALVSR FEDTTWYSEV
PLPDLNGMGR LALAEAVHAQ GIKAVITGEG SDEHFGGYDA FRADSLSEPD HSWPAMMTDT
ERQEAHALAS KEAQYGIFGD FTPKVPISTK RMFYSNHVAS SIARVGSLPF SDWTKVYGNS
IPETTMIEGF DGRVRDNILK RWHPVHTAQY MFVKTFMPHF ILRYNGDNID MVHQVESRCP
FLDHHLTEYV NNVPPSLKMR YNAKDKSWRE KHILREAVKP FVTDEVYNMS KKAYMGPRKF
WPGGPLHKKI SELVTKANVE NLGFVDWQAT QDAMDGAFNK QEGLALRRII TVAQFVVLGQ
RFGVKRASGR R
