ID W2PXI7_PHYPN Unreviewed; 717 AA.
AC W2PXI7;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=N-acetyl-gamma-glutamyl-phosphate reductase {ECO:0000313|EMBL:ETN04735.1};
GN ORFNames=PPTG_14524 {ECO:0000313|EMBL:ETN04735.1};
OS Phytophthora parasitica (strain INRA-310).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=761204 {ECO:0000313|EMBL:ETN04735.1, ECO:0000313|Proteomes:UP000018817};
RN [1] {ECO:0000313|Proteomes:UP000018817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=INRA-310 {ECO:0000313|Proteomes:UP000018817};
RG The Broad Institute Genome Sequencing Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D.,
RA Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ETN04735.1, ECO:0000313|Proteomes:UP000018817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=INRA-310 {ECO:0000313|EMBL:ETN04735.1,
RC ECO:0000313|Proteomes:UP000018817};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Phytophthora parasitica INRA-310.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the NAGSA
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007239}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the acetylglutamate
CC kinase family. {ECO:0000256|ARBA:ARBA00006830}.
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DR EMBL; KI669603; ETN04735.1; -; Genomic_DNA.
DR RefSeq; XP_008910129.1; XM_008911881.1.
DR AlphaFoldDB; W2PXI7; -.
DR STRING; 761204.W2PXI7; -.
DR EnsemblProtists; ETN04735; ETN04735; PPTG_14524.
DR GeneID; 20183807; -.
DR VEuPathDB; FungiDB:PPTG_14524; -.
DR OMA; IAFIPHV; -.
DR OrthoDB; 987250at2759; -.
DR UniPathway; UPA00068; UER00108.
DR Proteomes; UP000018817; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR HAMAP; MF_00150; ArgC_type1; 1.
DR InterPro; IPR036393; AceGlu_kinase-like_sf.
DR InterPro; IPR004662; AcgluKinase_fam.
DR InterPro; IPR023013; AGPR_AS.
DR InterPro; IPR000706; AGPR_type-1.
DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR NCBIfam; TIGR00761; argB; 1.
DR NCBIfam; TIGR01850; argC; 1.
DR PANTHER; PTHR23342; N-ACETYLGLUTAMATE SYNTHASE; 1.
DR PANTHER; PTHR23342:SF0; N-ACETYLGLUTAMATE SYNTHASE, MITOCHONDRIAL; 1.
DR Pfam; PF00696; AA_kinase; 1.
DR Pfam; PF01118; Semialdhyde_dh; 1.
DR SMART; SM00859; Semialdhyde_dh; 1.
DR SUPFAM; SSF53633; Carbamate kinase-like; 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 Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000018817};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 366..512
FT /note="Semialdehyde dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00859"
FT ACT_SITE 522
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10010"
SQ SEQUENCE 717 AA; 76785 MW; B66A90D50903FE69 CRC64;
MWRSVAKQMP VLNRAAARSS QALAMTVTSR ACATPFASVA QPALSASLQT RTLSSKASDD
YALNLAKVLA PEATLEEFKK LYRTPGAKHT TVIKIGGDVI IHELETLIES LRFMKDTGLF
PILVHGAGPQ MNAELDKQGV EPQYVGGNRV TDQKTLDIAQ KIFVDTNATL VAALNKAGVP
ARGITSGVIQ ADFKDKDVYG FVGEVNKIHG DPVQAVIDAG EIPVLSCLGE SANGQTLNIN
ADVAARQLAL NLQPLKTIFV NAKGGWIEDD GTKLKTINMA KDYERMAARD YTGRQGTLLK
LNEINTLLQG LPSTSSVVLT SASELMREIV SKKSAGTTCI KGEKPAASAK NTAKVSVPRG
PNGKYRVGLL GARGYVGREL IRVIGRHPEL ELVCASSRAL EGEKVLDVAS VPPLNPHTKL
PAKPVEDLKL NIDPELKFCE LGLDGIPSSP FGESVDVWVL ALPNGYCEDY ATALDALRRK
DKIIIDLSAD QRFNAEWTYG LPEAPGGRTR LQGATHIANP GCYATGAQVG LMPLLGGKPQ
VSGKLIDESV PPHVFGISGY SGAGTNPSAA NDLNKLQNNI IAYKSVNHIH ENEVSHQLGT
PVRFMPHVAP YFQGIHLTLS AQLADNGLIT SAKQAEELYH EFFANEALVK VKSDIPFVKD
NAYHPHVAVG GFQLDQDTGR LVVIATIDNL LKGAATQAVQ NINVALGIDE YSGIDLE
//
