ARGC_RALSO
ID ARGC_RALSO Reviewed; 337 AA.
AC Q8Y339;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 118.
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=RSc0142;
GN ORFNames=RS01012;
OS Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=267608;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GMI1000;
RX PubMed=11823852; DOI=10.1038/415497a;
RA Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M.,
RA Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M.,
RA Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M.,
RA Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P.,
RA Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.;
RT "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL Nature 415:497-502(2002).
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; AL646052; CAD13670.1; -; Genomic_DNA.
DR RefSeq; WP_011000109.1; NC_003295.1.
DR AlphaFoldDB; Q8Y339; -.
DR SMR; Q8Y339; -.
DR STRING; 267608.RSc0142; -.
DR EnsemblBacteria; CAD13670; CAD13670; RSc0142.
DR GeneID; 60499650; -.
DR KEGG; rso:RSc0142; -.
DR PATRIC; fig|267608.8.peg.145; -.
DR eggNOG; COG0002; Bacteria.
DR HOGENOM; CLU_077118_0_0_4; -.
DR OMA; FSWRNNN; -.
DR UniPathway; UPA00068; UER00108.
DR Proteomes; UP000001436; 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; 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; Reference proteome.
FT CHAIN 1..337
FT /note="N-acetyl-gamma-glutamyl-phosphate reductase"
FT /id="PRO_0000112509"
FT ACT_SITE 116
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01110"
SQ SEQUENCE 337 AA; 36407 MW; 3B329FD3151A6102 CRC64;
MAFKVFVDGQ EGTTGLRLLD YLSQRDDIEL LRIAEDRRKD PAERAKFLNA ADVAFLCLPD
VASREAVSLV DNPNTCIIDA STAFRTSDDW AYGLPELAPG QRERLRNSKR IAVPGCHASA
FVLLMRPLVE AGIVPADYPI TAFSLTGYSG GGKKMIADYL AADNPKLQSP RPYALALTHK
HLPEMRVQSK LALPPIFTPV VGNFLKGLAV TIGLHPQHLA SKVSPADIAK VFADYYQGEQ
FIRVAPADNV ETLDNGFFDV QGANDTNRAD LFVFGSDERM VVTARLDNLG KGAAGAAVQC
MNVHLGVDEA TSLHVEAPVK AEGPAHPVRE AAPDFAT
