ID   ARGC_CORGL              Reviewed;         347 AA.
AC   Q59279; O32353;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2002, sequence version 3.
DT   03-AUG-2022, entry version 146.
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=Cgl1394, cg1580;
OS   Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS   JCM 1318 / LMG 3730 / NCIMB 10025).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196627;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613;
RA   Chun J.Y., Lee E.J., Cheon C.I., Min K.H., Lee M.-S.;
RL   Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613;
RA   Park M.Y., Chun J.Y., Ko S.-Y., Lee M.-S.;
RT   "Molecular cloning of the arginine biosynthetic genes from Corynebacterium
RT   glutamicum.";
RL   Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA   Ikeda M., Nakagawa S.;
RT   "The Corynebacterium glutamicum genome: features and impacts on
RT   biotechnological processes.";
RL   Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA   Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA   Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA   Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA   Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA   Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT   "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT   impact on the production of L-aspartate-derived amino acids and vitamins.";
RL   J. Biotechnol. 104:5-25(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 243-347.
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=8581175; DOI=10.1099/13500872-142-1-99;
RA   Sakanyan V., Petrosyan P., Lecocq M., Boyen A., Legrain C., Demarez M.N.,
RA   Hallet J.-N., Glansdorff N.;
RT   "Genes and enzymes of the acetyl cycle of arginine biosynthesis in
RT   Corynebacterium glutamicum: enzyme evolution in the early steps of the
RT   arginine pathway.";
RL   Microbiology 142:99-108(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=CAF21405.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF005242; AAB62245.1; -; Genomic_DNA.
DR   EMBL; AF049897; AAC24812.1; -; Genomic_DNA.
DR   EMBL; BA000036; BAB98787.1; -; Genomic_DNA.
DR   EMBL; BX927152; CAF21405.1; ALT_INIT; Genomic_DNA.
DR   EMBL; X86157; CAA60096.1; -; Genomic_DNA.
DR   RefSeq; NP_600613.1; NC_003450.3.
DR   RefSeq; WP_003858698.1; NC_006958.1.
DR   AlphaFoldDB; Q59279; -.
DR   SMR; Q59279; -.
DR   STRING; 196627.cg1580; -.
DR   GeneID; 58310594; -.
DR   KEGG; cgb:cg1580; -.
DR   KEGG; cgl:Cgl1394; -.
DR   PATRIC; fig|196627.13.peg.1363; -.
DR   eggNOG; COG0002; Bacteria.
DR   HOGENOM; CLU_006384_0_0_11; -.
DR   OMA; PHLTPMI; -.
DR   UniPathway; UPA00068; UER00108.
DR   Proteomes; UP000000582; 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..347
FT                   /note="N-acetyl-gamma-glutamyl-phosphate reductase"
FT                   /id="PRO_0000112400"
FT   ACT_SITE        151
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00150"
FT   CONFLICT        14
FT                   /note="A -> T (in Ref. 1; AAB62245 and 2; AAC24812)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        21
FT                   /note="L -> I (in Ref. 1; AAB62245 and 2; AAC24812)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        25
FT                   /note="H -> Q (in Ref. 1; AAB62245 and 2; AAC24812)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        102
FT                   /note="C -> R (in Ref. 1; AAB62245 and 2; AAC24812)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        277
FT                   /note="L -> S (in Ref. 1; AAB62245 and 2; AAC24812)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        341
FT                   /note="P -> A (in Ref. 1; AAB62245 and 2; AAC24812)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   347 AA;  35888 MW;  44A73448E7BF4864 CRC64;
     MTIKVAIAGA SGYAGGEILR LLLGHPAYAS GELEIGALTA ASTAGSTLGE LMPHIPQLAD
     RVIQDTTAET LAGHDVVFLG LPHGFSAEIA LQLGPDVTVI DCAADFRLQN AADWEKFYGS
     EHQGTWPYGI PEMPGHREAL RGAKRVAVPG CFPTGATLAL LPAVQAGLIE PDVSVVSITG
     VSGAGKKASV ALLGSETMGS LKAYNTSGKH RHTPEIAQNL GEVSDKPVKV SFTPVLAPLP
     RGILTTATAP LKEGVTAEQA RAVYEEFYAQ ETFVHVLPEG AQPQTQAVLG SNMCHVQVEI
     DEEAGKVLVT SAIDNLTKGT AGAAVQCMNL SVGFDEAAGL PQVGVAP