ID   ARGC1_NOSS1             Reviewed;         352 AA.
AC   Q8YRB1;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=N-acetyl-gamma-glutamyl-phosphate reductase 1 {ECO:0000255|HAMAP-Rule:MF_00150};
DE            Short=AGPR 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_00150};
DE            Short=NAGSA dehydrogenase 1 {ECO:0000255|HAMAP-Rule:MF_00150};
GN   Name=argC1 {ECO:0000255|HAMAP-Rule:MF_00150}; OrderedLocusNames=alr3537;
OS   Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=103690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX   PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA   Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA   Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT   "Complete genomic sequence of the filamentous nitrogen-fixing
RT   cyanobacterium Anabaena sp. strain PCC 7120.";
RL   DNA Res. 8:205-213(2001).
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; BA000019; BAB75236.1; -; Genomic_DNA.
DR   PIR; AB2248; AB2248.
DR   RefSeq; WP_010997687.1; NZ_RSCN01000034.1.
DR   AlphaFoldDB; Q8YRB1; -.
DR   SMR; Q8YRB1; -.
DR   STRING; 103690.17132670; -.
DR   EnsemblBacteria; BAB75236; BAB75236; BAB75236.
DR   KEGG; ana:alr3537; -.
DR   eggNOG; COG0002; Bacteria.
DR   OMA; PHLTPMI; -.
DR   OrthoDB; 951261at2; -.
DR   UniPathway; UPA00068; UER00108.
DR   Proteomes; UP000002483; 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; 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; Reference proteome.
FT   CHAIN           1..352
FT                   /note="N-acetyl-gamma-glutamyl-phosphate reductase 1"
FT                   /id="PRO_0000112374"
SQ   SEQUENCE   352 AA;  38239 MW;  09C0AF871242635D 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 RVIVMSVIDN LIKGQAGQAI QCLNIMMGWD ETLGLPKMGF YP