ARGC_SINMW
ID ARGC_SINMW Reviewed; 310 AA.
AC A6U7T4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 80.
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=Smed_0859;
OS Sinorhizobium medicae (strain WSM419) (Ensifer medicae).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=366394;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM419;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Reeve W.G.,
RA Richardson P.;
RT "Complete sequence of Sinorhizobium medicae WSM419 chromosome.";
RL Submitted (JUN-2007) 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; CP000738; ABR59714.1; -; Genomic_DNA.
DR RefSeq; WP_011975053.1; NC_009636.1.
DR RefSeq; YP_001326549.1; NC_009636.1.
DR AlphaFoldDB; A6U7T4; -.
DR SMR; A6U7T4; -.
DR STRING; 366394.Smed_0859; -.
DR EnsemblBacteria; ABR59714; ABR59714; Smed_0859.
DR GeneID; 61612307; -.
DR KEGG; smd:Smed_0859; -.
DR PATRIC; fig|366394.8.peg.3973; -.
DR eggNOG; COG0002; Bacteria.
DR HOGENOM; CLU_077118_0_0_5; -.
DR OMA; FSWRNNN; -.
DR OrthoDB; 951261at2; -.
DR UniPathway; UPA00068; UER00108.
DR Proteomes; UP000001108; 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; IPR023013; AGPR_AS.
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.
DR PROSITE; PS01224; ARGC; 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_1000065146"
FT ACT_SITE 117
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01110"
SQ SEQUENCE 310 AA; 33402 MW; 21CD974F2213966A CRC64;
MKPKIFIDGE HGTTGLQIRT RMAGRTDLEL LSIPEAERRN AAMREDLLNS ADIAILCLPD
DASREAVAMV AGNNRVRIID TSTAHRVAPD WAYGFAEMDK AQPRKIRDAR HVANPGCYPT
GAIALIRPLR QAGILPDGYP VTVNAVSGYT GGGKQMIAQI EDDKSPDHIR APHFLYGLTL
KHKHVPEMKM HGLLERAPVF SPSVGKFAQG MIVQVPLYVD DLAAGATIES IHRALVDHYA
GQSIVEVVPL EESAKLARID ATELAGKDTM KLFVFGTDGG AHVNMVALLD NLGKGASGAA
VQNMDLMLSA