ID   ARGC2_NOSS1             Reviewed;         322 AA.
AC   P54894;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 126.
DE   RecName: Full=N-acetyl-gamma-glutamyl-phosphate reductase 2 {ECO:0000255|HAMAP-Rule:MF_01110};
DE            Short=AGPR 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_01110};
DE            Short=NAGSA dehydrogenase 2 {ECO:0000255|HAMAP-Rule:MF_01110};
GN   Name=argC2 {ECO:0000255|HAMAP-Rule:MF_01110}; Synonyms=argC;
GN   OrderedLocusNames=all2498;
OS   Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=103690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1406250; DOI=10.1111/j.1365-2958.1992.tb01381.x;
RA   Floriano B., Herrero A., Flores E.;
RT   "Isolation of arginine auxotrophs, cloning by mutant complementation, and
RT   sequence analysis of the argC gene from the cyanobacterium Anabaena species
RT   PCC 7120.";
RL   Mol. Microbiol. 6:2085-2094(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7929012; DOI=10.1128/jb.176.20.6397-6401.1994;
RA   Floriano B., Herrero A., Flores E.;
RT   "Analysis of expression of the argC and argD genes in the cyanobacterium
RT   Anabaena sp. strain PCC 7120.";
RL   J. Bacteriol. 176:6397-6401(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX   PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA   Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA   Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT   "Complete genomic sequence of the filamentous nitrogen-fixing
RT   cyanobacterium Anabaena sp. strain PCC 7120.";
RL   DNA Res. 8:205-213(2001).
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; X65511; CAA46483.1; -; Genomic_DNA.
DR   EMBL; BA000019; BAB74197.1; -; Genomic_DNA.
DR   PIR; AC2118; AC2118.
DR   PIR; S24753; S24753.
DR   RefSeq; WP_010996654.1; NZ_RSCN01000002.1.
DR   AlphaFoldDB; P54894; -.
DR   SMR; P54894; -.
DR   STRING; 103690.17131590; -.
DR   EnsemblBacteria; BAB74197; BAB74197; BAB74197.
DR   KEGG; ana:all2498; -.
DR   eggNOG; COG0002; Bacteria.
DR   OMA; FSWRNNN; -.
DR   OrthoDB; 951261at2; -.
DR   UniPathway; UPA00068; UER00108.
DR   Proteomes; UP000002483; 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..322
FT                   /note="N-acetyl-gamma-glutamyl-phosphate reductase 2"
FT                   /id="PRO_0000112503"
FT   ACT_SITE        117
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01110"
SQ   SEQUENCE   322 AA;  34823 MW;  1C41BA71630942F0 CRC64;
     MNKPKIFIDG EAGTTGLQIY SRLNERDDIE LVSIAASKRK DADERAKLLN SVDVAILCLP
     DDAAREAVSL VNSSQVKILD ASTAYRTAQG WVYGFPEMNP GQREKIANAQ FVSNPGCYPT
     GFLACVRPLI AQGILPSSFP ITINAVSGYS GGGKSLIQKY DSFHEQQKGA TSDYPFGIYG
     LQFGHKHVKE MHQHSGLASP PLFIPAVGDF EQGMLVQIPL PLWTLDNPPS GEEIHQAIAQ
     YYQGEKFVQV APFKDPSLLR DGTFLDATAV NGTNIVQVFV FGNDNTKEAL LVARLDNLGK
     GASGAAVQNL NIMLGLPEEL GL