ID   ARGC_STRCL              Reviewed;         341 AA.
AC   P54896; Q9LCS8;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   12-FEB-2003, sequence version 2.
DT   25-MAY-2022, entry version 104.
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};
OS   Streptomyces clavuligerus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1901;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / NRRL
RC   3585 / VKM Ac-602;
RX   PubMed=1339424; DOI=10.1128/jb.174.14.4606-4613.1992;
RA   Ludovice M., Martin J.F., Carrachas P., Liras P.;
RT   "Characterization of the Streptomyces clavuligerus argC gene encoding N-
RT   acetylglutamyl-phosphate reductase: expression in Streptomyces lividans and
RT   effect on clavulanic acid production.";
RL   J. Bacteriol. 174:4606-4613(1992).
RN   [2]
RP   SEQUENCE REVISION.
RC   STRAIN=ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / NRRL
RC   3585 / VKM Ac-602;
RX   PubMed=11075930;
RA   Rodriguez-Garcia A., de la Fuente A., Perez-Redondo R., Martin J.F.,
RA   Liras P.;
RT   "Characterization and expression of the arginine biosynthesis gene cluster
RT   of Streptomyces clavuligerus.";
RL   J. Mol. Microbiol. Biotechnol. 2:543-550(2000).
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}.
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DR   EMBL; Z49111; CAB82479.1; -; Genomic_DNA.
DR   AlphaFoldDB; P54896; -.
DR   SMR; P54896; -.
DR   STRING; 443255.SCLAV_0801; -.
DR   eggNOG; COG0002; Bacteria.
DR   UniPathway; UPA00068; UER00108.
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.
FT   CHAIN           1..341
FT                   /note="N-acetyl-gamma-glutamyl-phosphate reductase"
FT                   /id="PRO_0000112457"
FT   ACT_SITE        145
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00150"
SQ   SEQUENCE   341 AA;  34939 MW;  08E68547332A5D79 CRC64;
     MTVRVAVAGA SGYAGGEVVR LLLGHPAESW VALTAFSQAG QAVGHPHLGP VAGRVFEPIS
     AQAPLAGHDV VFLALPPAQS AALAEEAGAR VVDRNMGADF RLRDAGVWER FYGSPWRGCW
     PYGLPESPGA REALAGARRI AVPGCYPTAV TLALFPAVGA GLVDREVVTA VSGTSGAGRA
     LKPHLLGAEV MGSVSPYAVG GTHRHTPEIA QNSTAVTDGE PVSVSFTPLL APMPRGILAT
     CSARLTPGTD ARQVRAVYEK TYADEPFVSL LPEGVWPSTG AVLGSNQVQV QVAVDPAADR
     LVVVSAIDNL TKGTAGGALQ SMNLALGLPE TTGLPRTGLA P