ID   Q1MS70_LAWIP            Unreviewed;       353 AA.
AC   Q1MS70;
DT   30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   30-MAY-2006, sequence version 1.
DT   28-JAN-2026, entry version 124.
DE   RecName: Full=N-acetyl-gamma-glutamyl-phosphate reductase {ECO:0000256|HAMAP-Rule:MF_00150};
DE            Short=AGPR {ECO:0000256|HAMAP-Rule:MF_00150};
DE            EC=1.2.1.38 {ECO:0000256|HAMAP-Rule:MF_00150};
DE   AltName: Full=N-acetyl-glutamate semialdehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00150};
DE            Short=NAGSA dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00150};
GN   Name=argC {ECO:0000256|HAMAP-Rule:MF_00150,
GN   ECO:0000313|EMBL:CAJ54155.1};
GN   OrderedLocusNames=LI0099 {ECO:0000313|EMBL:CAJ54155.1};
OS   Lawsonia intracellularis (strain PHE/MN1-00).
OC   Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfovibrionia;
OC   Desulfovibrionales; Desulfovibrionaceae; Lawsonia.
OX   NCBI_TaxID=363253 {ECO:0000313|EMBL:CAJ54155.1, ECO:0000313|Proteomes:UP000002430};
RN   [1] {ECO:0000313|EMBL:CAJ54155.1, ECO:0000313|Proteomes:UP000002430}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHE/MN1-00 {ECO:0000313|EMBL:CAJ54155.1,
RC   ECO:0000313|Proteomes:UP000002430};
RA   Kaur K., Zhang Q., Beckler D., Munir S., Li L., Kinsley K., Herron L.,
RA   Peterson A., May B., Singh S., Gebhart C., Kapur V.;
RT   "The complete genome sequence of Lawsonia intracellularis: the causative
RT   agent of proliferative enteropathy.";
RL   Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of N-acetyl-5-
CC       glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
CC       {ECO:0000256|HAMAP-Rule:MF_00150}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-acetyl-L-glutamate 5-semialdehyde + phosphate + NADP(+) = N-
CC         acetyl-L-glutamyl 5-phosphate + NADPH + H(+); 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:0000256|ARBA:ARBA00050557, ECO:0000256|HAMAP-
CC         Rule:MF_00150};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC       L-ornithine from L-glutamate: step 3/4. {ECO:0000256|ARBA:ARBA00004862,
CC       ECO:0000256|HAMAP-Rule:MF_00150}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00150}.
CC   -!- SIMILARITY: Belongs to the NAGSA dehydrogenase family. Type 1
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00150}.
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DR   EMBL; AM180252; CAJ54155.1; -; Genomic_DNA.
DR   RefSeq; WP_011526182.1; NC_008011.1.
DR   AlphaFoldDB; Q1MS70; -.
DR   STRING; 363253.LI0099; -.
DR   KEGG; lip:LI0099; -.
DR   eggNOG; COG0002; Bacteria.
DR   HOGENOM; CLU_006384_0_1_7; -.
DR   OrthoDB; 9801289at2; -.
DR   UniPathway; UPA00068; UER00108.
DR   Proteomes; UP000002430; 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:0070401; F:NADP+ binding; IEA:InterPro.
DR   GO; GO:0006526; P:L-arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd23934; AGPR_1_C; 1.
DR   CDD; cd17895; AGPR_1_N; 1.
DR   FunFam; 3.30.360.10:FF:000014; N-acetyl-gamma-glutamyl-phosphate reductase; 1.
DR   Gene3D; 3.30.360.10; Dihydrodipicolinate Reductase, domain 2; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   HAMAP; MF_00150; ArgC_type1; 1.
DR   InterPro; IPR050085; AGPR.
DR   InterPro; IPR023013; AGPR_AS.
DR   InterPro; IPR058924; AGPR_dimerisation_dom.
DR   InterPro; IPR000706; AGPR_type-1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR   NCBIfam; TIGR01850; argC; 1.
DR   PANTHER; PTHR32338:SF10; N-ACETYL-GAMMA-GLUTAMYL-PHOSPHATE REDUCTASE, CHLOROPLASTIC-RELATED; 1.
DR   PANTHER; PTHR32338; N-ACETYL-GAMMA-GLUTAMYL-PHOSPHATE REDUCTASE, CHLOROPLASTIC-RELATED-RELATED; 1.
DR   Pfam; PF01118; Semialdhyde_dh; 1.
DR   Pfam; PF22698; Semialdhyde_dhC_1; 1.
DR   SMART; SM00859; Semialdhyde_dh; 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, ECO:0000256|HAMAP-
KW   Rule:MF_00150};
KW   Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571, ECO:0000256|HAMAP-
KW   Rule:MF_00150}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00150};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_00150};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_00150}; Reference proteome {ECO:0000313|Proteomes:UP000002430}.
FT   DOMAIN          7..148
FT                   /note="Semialdehyde dehydrogenase NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00859"
FT   ACT_SITE        156
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00150,
FT                   ECO:0000256|PROSITE-ProRule:PRU10010"
SQ   SEQUENCE   353 AA;  39108 MW;  6F8B20D308E3C517 CRC64;
     MGIQKIQAAI IGGTGYTGIE LIRLLSLHPN IQPIFIISRE QCGKKLYEVH PFLSGMPYAE
     TIFSPLDHKA IGKTCDVAFL AVPHGTGMEI APQLLEQGTK VIDLSADFRL NNPMTYSQWY
     HLEHNASHLL SEAVYGIPEL NEEFIKRANI VANPGCYPTS IILGLYPAIK HGLIKFENII
     IDSKSGTSGA GRNTSTSSLL FCEIQNSFKA YNIGIHRHTP EIEQELSYIA KQPITVTFSP
     HLLPTTRGIL STIYTQLALP ISQDEVYRLY TNTWKDQPWI RIVPSSKLPE TRNVCGTMFC
     DIGLVVDIRT QRLIIISAID NLCRGASGQA IANANLMFNL PMTTGLIFCP LLP
//