ID W7MX42_GIBM7 Unreviewed; 387 AA.
AC W7MX42;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=N-acetyl-gamma-glutamyl-phosphate reductase {ECO:0000313|EMBL:EWG52330.1};
GN ORFNames=FVEG_11104 {ECO:0000313|EMBL:EWG52330.1};
OS Gibberella moniliformis (strain M3125 / FGSC 7600) (Maize ear and stalk rot
OS fungus) (Fusarium verticillioides).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=334819 {ECO:0000313|EMBL:EWG52330.1, ECO:0000313|Proteomes:UP000009096};
RN [1] {ECO:0000313|EMBL:EWG52330.1, ECO:0000313|Proteomes:UP000009096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M3125 / FGSC 7600 {ECO:0000313|Proteomes:UP000009096};
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., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.,
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., Mukherjee M.,
RA Park G., Park J., Park S.Y., Proctor R.H., Regev A., Ruiz-Roldan M.C.,
RA Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G.,
RA Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A.,
RA Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC L-ornithine from L-glutamate: step 3/4.
CC {ECO:0000256|ARBA:ARBA00004862}.
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DR EMBL; DS022257; EWG52330.1; -; Genomic_DNA.
DR RefSeq; XP_018758521.1; XM_018900270.1.
DR AlphaFoldDB; W7MX42; -.
DR STRING; 334819.W7MX42; -.
DR EnsemblFungi; FVEG_11104T0; FVEG_11104T0; FVEG_11104.
DR GeneID; 30068639; -.
DR KEGG; fvr:FVEG_11104; -.
DR VEuPathDB; FungiDB:FVEG_11104; -.
DR eggNOG; KOG4354; Eukaryota.
DR HOGENOM; CLU_006384_3_0_1; -.
DR OMA; PHLTPMI; -.
DR OrthoDB; 987250at2759; -.
DR UniPathway; UPA00068; UER00108.
DR Proteomes; UP000009096; Chromosome 9.
DR GO; GO:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0070401; F:NADP+ binding; IEA:InterPro.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR HAMAP; MF_00150; ArgC_type1; 1.
DR InterPro; IPR023013; AGPR_AS.
DR InterPro; IPR000706; AGPR_type-1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR NCBIfam; TIGR01850; argC; 1.
DR PANTHER; PTHR32338:SF10; N-ACETYL-GAMMA-GLUTAMYL-PHOSPHATE REDUCTASE, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR32338; N-ACETYL-GAMMA-GLUTAMYL-PHOSPHATE REDUCTASE, CHLOROPLASTIC-RELATED-RELATED; 1.
DR Pfam; PF01118; Semialdhyde_dh; 1.
DR SMART; SM00859; Semialdhyde_dh; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS01224; ARGC; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000009096}.
FT DOMAIN 74..197
FT /note="Semialdehyde dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00859"
FT ACT_SITE 206
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10010"
SQ SEQUENCE 387 AA; 41960 MW; 9675DBE297EE3AFE CRC64;
MLSATSFALR TSARRVAPRA AALVAPMPKI SLGRSFTVAQ ARCLSSTGRL SYAAQTNPNP
PLGMKNASND APSRIGLIGA RGYTGQALID LLNQHPMMDL RHVSSRELQG QELKGYSKRK
IIYESLSPEE VAQLDKDGKV DAWILALPNA VCQPFVEALG SSKSLIVDLS ADYRFDEDQK
TWKYGLCELQ PRSKLATATR ISNPGCYATG SQLALAPIVE HLGGIPSIFG VSGYSGAGTK
PSPKNDTNNL KDNLLPYSLT GHIHEREISH HLGTSAAFMP HVASWFRGIH LTVNIPLNKE
MTSRDIRQIY QDRYAGEKLV KVVGEAPVVK AIQDKHHVEI GGFAVDSTGK RVVVCATIDN
LNKGAATQCL QNMNLALGYD EYQGIPI
//
