ID   ARGC_TRIV2              Reviewed;         322 AA.
AC   Q3MG30;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   25-MAY-2022, entry version 99.
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=Ava_0430;
OS   Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Trichormus.
OX   NCBI_TaxID=240292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29413 / PCC 7937;
RX   PubMed=25197444; DOI=10.4056/sigs.3899418;
RA   Thiel T., Pratte B.S., Zhong J., Goodwin L., Copeland A., Lucas S., Han C.,
RA   Pitluck S., Land M.L., Kyrpides N.C., Woyke T.;
RT   "Complete genome sequence of Anabaena variabilis ATCC 29413.";
RL   Stand. Genomic Sci. 9:562-573(2014).
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; CP000117; ABA20056.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3MG30; -.
DR   SMR; Q3MG30; -.
DR   STRING; 240292.Ava_0430; -.
DR   EnsemblBacteria; ABA20056; ABA20056; Ava_0430.
DR   KEGG; ava:Ava_0430; -.
DR   eggNOG; COG0002; Bacteria.
DR   HOGENOM; CLU_077118_0_0_3; -.
DR   OMA; FSWRNNN; -.
DR   UniPathway; UPA00068; UER00108.
DR   Proteomes; UP000002533; 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.
FT   CHAIN           1..322
FT                   /note="N-acetyl-gamma-glutamyl-phosphate reductase"
FT                   /id="PRO_1000065137"
FT   ACT_SITE        117
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01110"
SQ   SEQUENCE   322 AA;  34832 MW;  A01B081ADD12A23C CRC64;
     MNKPKIFIDG EAGTTGLQIY SRLNERDDIE LVSIAASKRK DADERAKLLN SVDVAILCLP
     DDAAREAVSL VHSSQVKILD ASTAYRTAQG WVYGFPELNP GQREKIANAQ FVSNPGCYPT
     GFLACVRPLI AQGILPSSFP ITINAVSGYS GGGKSLIQKY DSFHEQQKGA TSDYPFGIYG
     LQFGHKHVKE MHQHSGLASP PLFIPAVGDF EQGMLVQIPL PLWTLDNPPS GEEIHQAIAQ
     YYQGEKFVQV ASFKDPSLLR DGTFLDATAV NGTNIVQVFV FANDNTKEAL LVARLDNLGK
     GASGAAVQNL NIMLGLPEEL GL