ARGC_DEIRA
ID ARGC_DEIRA Reviewed; 306 AA.
AC Q9RY72;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 125.
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=DR_0078;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
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; AE000513; AAF09671.1; -; Genomic_DNA.
DR PIR; D75562; D75562.
DR RefSeq; NP_293804.1; NC_001263.1.
DR RefSeq; WP_010886726.1; NZ_CP015081.1.
DR AlphaFoldDB; Q9RY72; -.
DR SMR; Q9RY72; -.
DR STRING; 243230.DR_0078; -.
DR EnsemblBacteria; AAF09671; AAF09671; DR_0078.
DR KEGG; dra:DR_0078; -.
DR PATRIC; fig|243230.17.peg.241; -.
DR eggNOG; COG0002; Bacteria.
DR HOGENOM; CLU_077118_0_0_0; -.
DR InParanoid; Q9RY72; -.
DR OMA; WGAYGFN; -.
DR OrthoDB; 951261at2; -.
DR UniPathway; UPA00068; UER00108.
DR Proteomes; UP000002524; Chromosome I.
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; Reference proteome.
FT CHAIN 1..306
FT /note="N-acetyl-gamma-glutamyl-phosphate reductase"
FT /id="PRO_0000112507"
FT ACT_SITE 117
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01110"
SQ SEQUENCE 306 AA; 32656 MW; 43D11A780EDC9883 CRC64;
MNKPKIFIDG EAGTTGLQIR ERLAGRSDLE LLSIDPVRRK DSAARAELLN AADVSILCLH
DDAAREAVSL TTNPASRLLD ASTAHRIHPD WVFGFPELSA EQPEKIRQAR YVANPGCYST
GAIALLAPLT GRGLLPADFP VHIQGYSGYT GGGRALVDAH EQGSAHPSKG AFISYGLTLE
HKHLPETMVY GGLTRKPVFT PNVGGWAQGM TVTVPLHLAE LGVSAEALHA ALKEHYAGQQ
YVKVFELADN PEILDPQTLN GTNNLELFVY PAADGERALL AARLDNLGKG ASGAAVQNLE
LMLGLS
