ID   ARGC_CAUVN              Reviewed;         317 AA.
AC   B8H555;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=N-acetyl-gamma-glutamyl-phosphate reductase {ECO:0000255|HAMAP-Rule:MF_01110};
DE            Short=AGPR {ECO:0000255|HAMAP-Rule:MF_01110};
DE            EC=1.2.1.38 {ECO:0000255|HAMAP-Rule:MF_01110};
DE   AltName: Full=N-acetyl-glutamate semialdehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01110};
DE            Short=NAGSA dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01110};
GN   Name=argC {ECO:0000255|HAMAP-Rule:MF_01110}; OrderedLocusNames=CCNA_01442;
OS   Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=565050;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NA1000 / CB15N;
RX   PubMed=20472802; DOI=10.1128/jb.00255-10;
RA   Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA   Walunas T.L., Crosson S.;
RT   "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL   J. Bacteriol. 192:3678-3688(2010).
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_01110}.
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_01110};
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_01110}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01110}.
CC   -!- SIMILARITY: Belongs to the NAGSA dehydrogenase family. Type 2
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01110}.
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DR   EMBL; CP001340; ACL94907.1; -; Genomic_DNA.
DR   RefSeq; WP_010919254.1; NC_011916.1.
DR   RefSeq; YP_002516815.1; NC_011916.1.
DR   AlphaFoldDB; B8H555; -.
DR   SMR; B8H555; -.
DR   PRIDE; B8H555; -.
DR   EnsemblBacteria; ACL94907; ACL94907; CCNA_01442.
DR   GeneID; 7330172; -.
DR   KEGG; ccs:CCNA_01442; -.
DR   PATRIC; fig|565050.3.peg.1426; -.
DR   HOGENOM; CLU_077118_0_0_5; -.
DR   OMA; FSWRNNN; -.
DR   OrthoDB; 951261at2; -.
DR   PhylomeDB; B8H555; -.
DR   UniPathway; UPA00068; UER00108.
DR   Proteomes; UP000001364; 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:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01110; ArgC_type2; 1.
DR   InterPro; IPR010136; AGPR_type-2.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR   Pfam; PF01118; Semialdhyde_dh; 1.
DR   SMART; SM00859; Semialdhyde_dh; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR01851; argC_other; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm; NADP;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..317
FT                   /note="N-acetyl-gamma-glutamyl-phosphate reductase"
FT                   /id="PRO_1000163994"
FT   ACT_SITE        118
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01110"
SQ   SEQUENCE   317 AA;  33278 MW;  FC798C7D3EE74561 CRC64;
     MANAPKVFID GEAGTTGLQI RERLVGRTDL QLISIDPDKR KDADARAEML NSADAVILCL
     PDDAAKEAVS LVSNPNTVII DASTAYRTAE GWAYGFAELD SEQRGKIAAS KRISNPGCYP
     TGAIALTRPL VSAGILPAEL PVSYNAVSGY TGGGKAMIAQ FEDESAADHT RAPYFIYGLS
     LSHKHVPEMQ KHGGLLTRPI FTPAVGRYAQ GMIVEMPLHL STLNGAPSLA DIHAALVKHY
     KGEAFVEVAS LDEAKALTTL DPEGLNGTNR LKLFVFGSDA GGQARLVALL DNLGKGASGA
     AVQNLNIALG LDEAAGL