ID   ARGC_METJA              Reviewed;         341 AA.
AC   Q58496;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   25-MAY-2022, entry version 125.
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}; OrderedLocusNames=MJ1096;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB99099.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; L77117; AAB99099.1; ALT_INIT; Genomic_DNA.
DR   PIR; G64436; G64436.
DR   RefSeq; WP_010870608.1; NC_000909.1.
DR   AlphaFoldDB; Q58496; -.
DR   SMR; Q58496; -.
DR   STRING; 243232.MJ_1096; -.
DR   EnsemblBacteria; AAB99099; AAB99099; MJ_1096.
DR   GeneID; 1451992; -.
DR   KEGG; mja:MJ_1096; -.
DR   eggNOG; arCOG00495; Archaea.
DR   HOGENOM; CLU_006384_0_1_2; -.
DR   InParanoid; Q58496; -.
DR   OMA; PHLTPMI; -.
DR   OrthoDB; 51061at2157; -.
DR   PhylomeDB; Q58496; -.
DR   UniPathway; UPA00068; UER00108.
DR   Proteomes; UP000000805; 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:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00150; ArgC_type1; 1.
DR   InterPro; IPR023013; AGPR_AS.
DR   InterPro; IPR000706; AGPR_type-1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR   InterPro; IPR012280; Semialdhyde_DH_dimer_dom.
DR   Pfam; PF01118; Semialdhyde_dh; 1.
DR   Pfam; PF02774; Semialdhyde_dhC; 1.
DR   SMART; SM00859; Semialdhyde_dh; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR01850; argC; 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..341
FT                   /note="N-acetyl-gamma-glutamyl-phosphate reductase"
FT                   /id="PRO_0000112486"
FT   ACT_SITE        149
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00150"
SQ   SEQUENCE   341 AA;  38172 MW;  72AE13AD35061D88 CRC64;
     MKEVAIIGAT GYTGAELLRL LANHEKVNVT YITSRKEAGK HVFKVHPHLK GIEKYKNLCF
     TGDIDKVDAY LVFTATPHGA SMDIVPDFIE RGMKVIDLSG DYRFEDLSLY EKYYKIKHKG
     LPDVKIAYGL PELHREEIKE AQLVANPGCF PTGAILAVAP LVKENIIEER IIFDSKTGVS
     GAGIKPTETT HFPNVNENIN PYKITTHRHT PEIEKELKKL GKAKVSFTPH LAPITRGILT
     TAHTFLAKDV DREEIIKIYE KFYGSEVFVR IFSEEIPKLT WVRGTNFCDI GGFEIDEHGR
     LVVISAIDNL VKGASGQAIQ NMNIMFGFDE KEGLFDVGLN P