ID   ARGC_AZOPC              Reviewed;         318 AA.
AC   B6YQY8;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 1.
DT   25-MAY-2022, entry version 70.
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}; OrderedLocusNames=CFPG_347;
OS   Azobacteroides pseudotrichonymphae genomovar. CFP2.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales;
OC   Candidatus Azobacteroides.
OX   NCBI_TaxID=511995;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=19008447; DOI=10.1126/science.1165578;
RA   Hongoh Y., Sharma V.K., Prakash T., Noda S., Toh H., Taylor T.D., Kudo T.,
RA   Sakaki Y., Toyoda A., Hattori M., Ohkuma M.;
RT   "Genome of an endosymbiont coupling N2 fixation to cellulolysis within RT
RT   protist cells in termite gut.";
RL   Science 322:1108-1109(2008).
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; AP010656; BAG83610.1; -; Genomic_DNA.
DR   RefSeq; WP_012573371.1; NC_011565.1.
DR   AlphaFoldDB; B6YQY8; -.
DR   SMR; B6YQY8; -.
DR   STRING; 511995.CFPG_347; -.
DR   EnsemblBacteria; BAG83610; BAG83610; CFPG_347.
DR   KEGG; aps:CFPG_347; -.
DR   eggNOG; COG0002; Bacteria.
DR   HOGENOM; CLU_006384_0_1_10; -.
DR   OMA; FSWRNNN; -.
DR   OrthoDB; 951261at2; -.
DR   UniPathway; UPA00068; UER00108.
DR   Proteomes; UP000000723; 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; 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; Reference proteome.
FT   CHAIN           1..318
FT                   /note="N-acetyl-gamma-glutamyl-phosphate reductase"
FT                   /id="PRO_1000096713"
FT   ACT_SITE        132
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00150"
SQ   SEQUENCE   318 AA;  35474 MW;  1F8823AB9BCCFEFC CRC64;
     MVKVGIIGGG GYTAGELIRL LINHPNVNII FVHSYSNARN KIIDIHTGLI GEMDLIFSDS
     YDLNEIDVLF LCSAHGDSKK FIETHTIHTE LKIIDLSIDF RHKENAGGFV YGLPELNKEI
     IRKAQYIANP GCFATAVQLA LLPLAKKNLL RSEIHINAIT GSTGAGVRPT ASSHFSWRNN
     NISVYKAFTH QHLKEITESL NYEPSRFNFI PVRGNFSRGI FATVYTESNL DIKDAVQIYS
     NYYEDSAFTF ISDKNPDLKQ VINTNKCILH LEKHGNKLFI ISIIDNLLKG ASGQAVQNFN
     LICGLNEKTG LFLKANAF