ID   ARGC_RHOCB              Reviewed;         342 AA.
AC   Q9LA02; D5ANG4;
DT   12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   12-FEB-2003, sequence version 2.
DT   25-MAY-2022, entry version 114.
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=RCAP_rcc00553;
OS   Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=272942;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MT1131;
RX   PubMed=10632883; DOI=10.1046/j.1365-2958.2000.01683.x;
RA   Deshmukh M., Brasseur G., Daldal F.;
RT   "Novel Rhodobacter capsulatus genes required for the biogenesis of various
RT   c-type cytochromes.";
RL   Mol. Microbiol. 35:123-138(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX   PubMed=20418398; DOI=10.1128/jb.00366-10;
RA   Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA   Haselkorn R.;
RT   "Complete genome sequence of the photosynthetic purple nonsulfur bacterium
RT   Rhodobacter capsulatus SB 1003.";
RL   J. Bacteriol. 192:3545-3546(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_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=AAF26220.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF156104; AAF26220.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP001312; ADE84318.1; -; Genomic_DNA.
DR   RefSeq; WP_013066297.1; NC_014034.1.
DR   AlphaFoldDB; Q9LA02; -.
DR   SMR; Q9LA02; -.
DR   STRING; 272942.RCAP_rcc00553; -.
DR   EnsemblBacteria; ADE84318; ADE84318; RCAP_rcc00553.
DR   GeneID; 31489504; -.
DR   KEGG; rcp:RCAP_rcc00553; -.
DR   eggNOG; COG0002; Bacteria.
DR   HOGENOM; CLU_006384_0_1_5; -.
DR   OMA; PHLTPMI; -.
DR   OrthoDB; 951261at2; -.
DR   UniPathway; UPA00068; UER00108.
DR   Proteomes; UP000002361; 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..342
FT                   /note="N-acetyl-gamma-glutamyl-phosphate reductase"
FT                   /id="PRO_0000112441"
FT   ACT_SITE        149
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00150"
SQ   SEQUENCE   342 AA;  36780 MW;  4DEE9490FBEE5CE0 CRC64;
     MTQKIAILGA SGYTGAELAR IIATHPEMEI TALSGDRKAG MRMGEVFPHL RHIGLPDLVK
     IEEIDFSGID LAFCALPHAT SQAVIAELPR DLKVVDLSAD FRLRDAAEYE KWYGKPHAAM
     DLQAEAVYGL TEFYREELKT ARLCAGTGCN AAAGQYAIRP LIEAGVIDLD EIVIDLKAGV
     SGAGRSLKEN LLHAELAGGT MPYSAGGKHR HLGEFDQEFS KVAGRPVRVQ FTPHLMPFNR
     GILATVYVRG TPEDIHAALA SRYENEVFLE VLPFGQLAST RSVAGSNFVH LGVIGDRLPG
     RAVVTVALDN LTKGSSGQAI QNANLMLGLP ETLGLMLAPV FP