ID   ARGC_BACTN              Reviewed;         322 AA.
AC   Q8A1A7;
DT   02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 118.
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=BT_3759;
OS   Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS   CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=226186;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC   VPI-5482 / E50;
RX   PubMed=12663928; DOI=10.1126/science.1080029;
RA   Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA   Hooper L.V., Gordon J.I.;
RT   "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL   Science 299:2074-2076(2003).
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; AE015928; AAO78864.1; -; Genomic_DNA.
DR   RefSeq; NP_812670.1; NC_004663.1.
DR   RefSeq; WP_008762696.1; NZ_UYXG01000036.1.
DR   AlphaFoldDB; Q8A1A7; -.
DR   SMR; Q8A1A7; -.
DR   STRING; 226186.BT_3759; -.
DR   PaxDb; Q8A1A7; -.
DR   PRIDE; Q8A1A7; -.
DR   EnsemblBacteria; AAO78864; AAO78864; BT_3759.
DR   GeneID; 60924929; -.
DR   KEGG; bth:BT_3759; -.
DR   PATRIC; fig|226186.12.peg.3821; -.
DR   eggNOG; COG0002; Bacteria.
DR   HOGENOM; CLU_006384_0_1_10; -.
DR   InParanoid; Q8A1A7; -.
DR   OMA; FSWRNNN; -.
DR   UniPathway; UPA00068; UER00108.
DR   Proteomes; UP000001414; 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..322
FT                   /note="N-acetyl-gamma-glutamyl-phosphate reductase"
FT                   /id="PRO_0000112386"
FT   ACT_SITE        132
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00150"
SQ   SEQUENCE   322 AA;  35838 MW;  074D784C4F7AB7F7 CRC64;
     MIKAGIIGGA GYTAGELIRL LLNHPETEIV FINSSSNAGN RITDVHEGLY GETDLRFTDQ
     LPLDAIDVLF FCTAHGDTKK FMESHNVPED LKIIDLSMDY RIKSDDHDFI YGLPELNRRA
     TCTAKHVANP GCFATCIQLG LLPLAKNLML TGDVSVNAIT GSTGAGVKPG ATSHFSWRNN
     NISIYKAFDH QHVPEIKQSL KQLQNSFDSE IDFIPYRGDF PRGIFATLVV KTKVALEEIV
     RMYEEYYAKD SFVHIVDKNI DLKQVVNTNK CLIHLEKHGD KLLIISCIDN LLKGASGQAV
     HNMNLMFNLE ETVGLRLKPS AF