ID   ARGC_METMJ              Reviewed;         328 AA.
AC   A3CRT6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   28-JAN-2026, entry version 102.
DE   RecName: Full=N-acetyl-gamma-glutamyl-phosphate reductase {ECO:0000255|HAMAP-Rule:MF_00150};
DE            Short=AGPR {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 {ECO:0000255|HAMAP-Rule:MF_00150};
DE            Short=NAGSA dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00150};
GN   Name=argC {ECO:0000255|HAMAP-Rule:MF_00150};
GN   OrderedLocusNames=Memar_0151;
OS   Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1).
OC   Archaea; Methanobacteriati; Methanobacteriota; Stenosarchaea group;
OC   Methanomicrobia; Methanomicrobiales; Methanomicrobiaceae; Methanoculleus.
OX   NCBI_TaxID=368407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35101 / DSM 1498 / JR1;
RX   PubMed=21304656; DOI=10.4056/sigs.32535;
RA   Anderson I.J., Sieprawska-Lupa M., Lapidus A., Nolan M., Copeland A.,
RA   Glavina Del Rio T., Tice H., Dalin E., Barry K., Saunders E., Han C.,
RA   Brettin T., Detter J.C., Bruce D., Mikhailova N., Pitluck S., Hauser L.,
RA   Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.;
RT   "Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981
RT   type strain JR1.";
RL   Stand. Genomic Sci. 1:189-196(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_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: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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000562; ABN56086.1; -; Genomic_DNA.
DR   RefSeq; WP_011843007.1; NC_009051.1.
DR   AlphaFoldDB; A3CRT6; -.
DR   SMR; A3CRT6; -.
DR   STRING; 368407.Memar_0151; -.
DR   GeneID; 4846168; -.
DR   GeneID; 76730733; -.
DR   KEGG; mem:Memar_0151; -.
DR   eggNOG; arCOG00495; Archaea.
DR   HOGENOM; CLU_006384_0_1_2; -.
DR   OrthoDB; 372053at2157; -.
DR   UniPathway; UPA00068; UER00108.
DR   Proteomes; UP000002146; 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   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; Arginine biosynthesis; Cytoplasm; NADP;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..328
FT                   /note="N-acetyl-gamma-glutamyl-phosphate reductase"
FT                   /id="PRO_1000011014"
FT   ACT_SITE        143
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00150"
SQ   SEQUENCE   328 AA;  35305 MW;  1718F288CE46E85E CRC64;
     MEIAIIGASG YTGGELMRLL LHHPSADVVA ATSRKLDGTP VASVHPHLRG LTDLVFRNAG
     AGDIDADFAF LAVPHTAAMK VAGTLAERGI RTVDLSADYR LPKDVYEKIY GVTHEAYFEA
     PYGLPELHRD EIRGASFVAN PGCFPTGATL AAAPLAKFAH TIIYDSKTGV SGAGTSPSAT
     THYPNVGDNF SAYKWTSHRH LAEMKQEAAR LGSTARCYFT PHLLPVNRGI LTTAHILLRE
     PMGQDEVEAL YKKFYADEFF VRYQKPTLAA VRGTNFCDVA VESEGDRVVA VSAIDNLVKG
     ASGQAIQNMN LMCGFAEDTG LRTAGMFP
//