ID   ARGC_CHESB              Reviewed;         310 AA.
AC   Q11J68;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   25-MAY-2022, entry version 96.
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=Meso_1161;
OS   Chelativorans sp. (strain BNC1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Chelativorans; unclassified Chelativorans.
OX   NCBI_TaxID=266779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BNC1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT   "Complete sequence of chromosome of Mesorhizobium sp. BNC1.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000390; ABG62557.1; -; Genomic_DNA.
DR   RefSeq; WP_011580500.1; NC_008254.1.
DR   AlphaFoldDB; Q11J68; -.
DR   SMR; Q11J68; -.
DR   STRING; 266779.Meso_1161; -.
DR   EnsemblBacteria; ABG62557; ABG62557; Meso_1161.
DR   KEGG; mes:Meso_1161; -.
DR   eggNOG; COG0002; Bacteria.
DR   HOGENOM; CLU_077118_0_0_5; -.
DR   OMA; FSWRNNN; -.
DR   OrthoDB; 951261at2; -.
DR   UniPathway; UPA00068; UER00108.
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.
FT   CHAIN           1..310
FT                   /note="N-acetyl-gamma-glutamyl-phosphate reductase"
FT                   /id="PRO_1000065142"
FT   ACT_SITE        116
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01110"
SQ   SEQUENCE   310 AA;  33593 MW;  3DB0518A69AF63CE CRC64;
     MTAKIFIDGE HGTTGLQIRA RLGERRDIEL LSIPVERRKD PAARAEFLNA ADIAILCLPD
     DAARESVSLI ANDTTRVIDA STAYRVSEGW AYGFPEMDKS QSKAIAQAKR VANPGCWPQG
     PIALLRPLVS AGLLPADFPV TINGITGYSG GGRSMIEDYE GKGEDAPEFF PYGLTLSHKH
     LPELRTYAKL ARDPLMQPVV GNFAQGMITM VPLQLGHLPR VPKGEELHAA IADHYAGIEG
     SAVEVAPFQA IERSPEIEPE RYNDTNTMRL YVFANDARAQ ALLLAVYDNL GKGASGAAVQ
     NLDLMLSGLR