ID   ARGC_DEIDV              Reviewed;         308 AA.
AC   C1D141;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=N-acetyl-gamma-glutamyl-phosphate reductase {ECO:0000255|HAMAP-Rule:MF_01110};
DE            Short=AGPR {ECO:0000255|HAMAP-Rule:MF_01110};
DE            EC=1.2.1.38 {ECO:0000255|HAMAP-Rule:MF_01110};
DE   AltName: Full=N-acetyl-glutamate semialdehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01110};
DE            Short=NAGSA dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01110};
GN   Name=argC {ECO:0000255|HAMAP-Rule:MF_01110}; OrderedLocusNames=Deide_07080;
OS   Deinococcus deserti (strain DSM 17065 / CIP 109153 / LMG 22923 / VCD115).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=546414;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17065 / CIP 109153 / LMG 22923 / VCD115;
RX   PubMed=19370165; DOI=10.1371/journal.pgen.1000434;
RA   de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B.,
RA   Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M.,
RA   Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J.;
RT   "Alliance of proteomics and genomics to unravel the specificities of Sahara
RT   bacterium Deinococcus deserti.";
RL   PLoS Genet. 5:E1000434-E1000434(2009).
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of N-acetyl-5-
CC       glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
CC       {ECO:0000255|HAMAP-Rule:MF_01110}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate =
CC         H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH; Xref=Rhea:RHEA:21588,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29123, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:57936, ChEBI:CHEBI:58349; EC=1.2.1.38;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01110};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC       L-ornithine from L-glutamate: step 3/4. {ECO:0000255|HAMAP-
CC       Rule:MF_01110}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01110}.
CC   -!- SIMILARITY: Belongs to the NAGSA dehydrogenase family. Type 2
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01110}.
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DR   EMBL; CP001114; ACO45565.1; -; Genomic_DNA.
DR   RefSeq; WP_012692688.1; NC_012526.1.
DR   AlphaFoldDB; C1D141; -.
DR   SMR; C1D141; -.
DR   STRING; 546414.Deide_07080; -.
DR   PaxDb; C1D141; -.
DR   EnsemblBacteria; ACO45565; ACO45565; Deide_07080.
DR   KEGG; ddr:Deide_07080; -.
DR   eggNOG; COG0002; Bacteria.
DR   HOGENOM; CLU_077118_0_0_0; -.
DR   OMA; WGAYGFN; -.
DR   OrthoDB; 951261at2; -.
DR   UniPathway; UPA00068; UER00108.
DR   Proteomes; UP000002208; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01110; ArgC_type2; 1.
DR   InterPro; IPR023013; AGPR_AS.
DR   InterPro; IPR010136; AGPR_type-2.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR   Pfam; PF01118; Semialdhyde_dh; 1.
DR   SMART; SM00859; Semialdhyde_dh; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR01851; argC_other; 1.
DR   PROSITE; PS01224; ARGC; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm; NADP;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..308
FT                   /note="N-acetyl-gamma-glutamyl-phosphate reductase"
FT                   /id="PRO_1000213574"
FT   ACT_SITE        117
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01110"
SQ   SEQUENCE   308 AA;  32657 MW;  456BBE5AF3270608 CRC64;
     MTRPRVFIDG EAGTTGLQIR ARLSGRTDLE LLSIDPARRK DPQARAELLN AANVSILCLH
     DDAAREAVAL TTNPEARLLD ASTAHRVHPE WVFGFPELSA QQPDRIRAAR YVANPGCYST
     GAIALLAPLT AAGLLSADFP VSIQGYSGYT GGGRALVDAH EKGEAHPMRG PFLSYALGLG
     HKHIPETMRY GGLSRTPIFT PNVGAWAQGM TVTIPLHLSD LGVSAQALHG ALTAHYAGQK
     YVRVAAMESN PEILDPQTLN GTNDLDLFVY ASQDGERAVL AARLDNLGKG AGGAAVQNLN
     LMLGLPDA