ID   ARGC1_LACPL             Reviewed;         339 AA.
AC   P59391; F9UKW9;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 2.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=N-acetyl-gamma-glutamyl-phosphate reductase 1 {ECO:0000255|HAMAP-Rule:MF_00150};
DE            Short=AGPR 1 {ECO:0000255|HAMAP-Rule:MF_00150};
DE            EC=1.2.1.38 {ECO:0000255|HAMAP-Rule:MF_00150};
DE   AltName: Full=N-acetyl-glutamate semialdehyde dehydrogenase 1 {ECO:0000255|HAMAP-Rule:MF_00150};
DE            Short=NAGSA dehydrogenase 1 {ECO:0000255|HAMAP-Rule:MF_00150};
GN   Name=argC1 {ECO:0000255|HAMAP-Rule:MF_00150}; OrderedLocusNames=lp_0487;
OS   Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
OS   (Lactobacillus plantarum).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactiplantibacillus.
OX   NCBI_TaxID=220668;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX   PubMed=12566566; DOI=10.1073/pnas.0337704100;
RA   Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P.,
RA   Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W.E.J.,
RA   Stiekema W., Klein Lankhorst R.M., Bron P.A., Hoffer S.M.,
RA   Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., De Vos W.M.,
RA   Siezen R.J.;
RT   "Complete genome sequence of Lactobacillus plantarum WCFS1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX   PubMed=22156394; DOI=10.1128/jb.06275-11;
RA   Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M.,
RA   Kleerebezem M., van Hijum S.A.;
RT   "Complete resequencing and reannotation of the Lactobacillus plantarum
RT   WCFS1 genome.";
RL   J. Bacteriol. 194:195-196(2012).
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_00150}.
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_00150};
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_00150}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00150}.
CC   -!- SIMILARITY: Belongs to the NAGSA dehydrogenase family. Type 1
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00150}.
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DR   EMBL; AL935263; CCC77984.1; -; Genomic_DNA.
DR   RefSeq; WP_011101026.1; NC_004567.2.
DR   RefSeq; YP_004888498.1; NC_004567.2.
DR   AlphaFoldDB; P59391; -.
DR   SMR; P59391; -.
DR   STRING; 220668.lp_0487; -.
DR   EnsemblBacteria; CCC77984; CCC77984; lp_0487.
DR   KEGG; lpl:lp_0487; -.
DR   PATRIC; fig|220668.9.peg.401; -.
DR   eggNOG; COG0002; Bacteria.
DR   HOGENOM; CLU_006384_0_1_9; -.
DR   PhylomeDB; P59391; -.
DR   BioCyc; LPLA220668:G1GW0-405-MON; -.
DR   UniPathway; UPA00068; UER00108.
DR   Proteomes; UP000000432; 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_00150; ArgC_type1; 1.
DR   InterPro; IPR000706; AGPR_type-1.
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; TIGR01850; argC; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm; NADP;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..339
FT                   /note="N-acetyl-gamma-glutamyl-phosphate reductase 1"
FT                   /id="PRO_0000112412"
FT   ACT_SITE        149
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00150"
SQ   SEQUENCE   339 AA;  37212 MW;  0130254DFB3A6095 CRC64;
     MKVGILGGSG YAGAELYRLL LNHPNFNVTF ISSEKYAGKP VEKMLKGFAH NGHSHNLRFN
     HLDDLPFDLD FVFSALPTGV LPKYVEKILE KTSLIFNVSG DFRFKDATTL QQYYPETLAI
     ESDQILSSYY IPEFSDFDKN ANIINLPGCM ALASIYAAYP LVKNKLINPN IFVDVKTGSS
     GAGKSTKETA ADRFGNFRLY RAFNHRHLPE IAMALGSSVG KVGFAAYSLD ISRGIYASVY
     SQIKKGVTEV DVKKAYFKTY KSCKFVANLT GKQSVPMLKS TNGTNFAEVK ATVHEGQCIA
     VVSLDNLLKG AAGQAVQAAN KYYQLVEDTG LDTLAGMWP