ID   ARGC_NOSEL              Reviewed;         352 AA.
AC   O87890;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 97.
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}; Synonyms=argL;
OS   Nostoc ellipsosporum.
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=45916;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=B1453-7 / CPB311;
RX   PubMed=9695912; DOI=10.1099/00221287-144-7-1799;
RA   Leganes F., Fernandez-Pinas F., Wolk C.P.;
RT   "A transposition-induced mutant of Nostoc ellipsosporum implicates an
RT   arginine-biosynthetic gene in the formation of cyanophycin granules and of
RT   functional heterocysts and akinetes.";
RL   Microbiology 144:1799-1805(1998).
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   -!- CAUTION: Ser-155 is present instead of the conserved Cys which is
CC       expected to be an active site residue. {ECO:0000305}.
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DR   EMBL; U48355; AAC36190.1; -; Genomic_DNA.
DR   AlphaFoldDB; O87890; -.
DR   SMR; O87890; -.
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; 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.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm; NADP;
KW   Oxidoreductase.
FT   CHAIN           1..352
FT                   /note="N-acetyl-gamma-glutamyl-phosphate reductase"
FT                   /id="PRO_0000112430"
SQ   SEQUENCE   352 AA;  38197 MW;  FD85AF8712427847 CRC64;
     MGNFGRVPVG IVGASGYGGV QLVRLLMDHP EIELVYLGGE SSVGKSFASL YPHLAHAVKL
     SIEEVDPEVI ARRCEVVFLS MPNGLACQIV PTLLEKGCKV LDLSADYRFR NLTTYTTWYG
     VERSDRTTAD TAIYGLPELY RDRISEAQLV GCPGSYPTAS LLALSPLLKQ GLIVPETAIV
     DAKSGTSGGG REAKTYLLLA EADNSLAPYS VVRHRHTPEI EQICSDLAGH EVTVQFTPHL
     VPIVRGILAT VYATLRDPGL VGDDLTTIYT AFYRNSPWVK VCESGIYPQT KWAAGSNLCY
     IGVEVDPRTG RVIGMSVIDN LIKGQAGQAI QCLNIMMGWD ETLGLPKMGF YP