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 27-MAR-2024, entry version 154.
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; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; 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; 69621907; -.
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 OrthoDB; 9801289at2; -.
DR BioCyc; CORYNE:G18NG-10973-MONOMER; -.
DR UniPathway; UPA00068; UER00108.
DR Proteomes; UP000000582; Chromosome.
DR Proteomes; UP000001009; 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:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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 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; PF02774; Semialdhyde_dhC; 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..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
//
