ARGC_RUEST
ID ARGC_RUEST Reviewed; 342 AA.
AC Q1GHL0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 1.
DT 25-MAY-2022, entry version 111.
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=TM1040_1123;
OS Ruegeria sp. (strain TM1040) (Silicibacter sp.).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ruegeria; unclassified Ruegeria.
OX NCBI_TaxID=292414;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TM1040;
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 Brettin T., Bruce D., Han C., Tapia R., Goodwin L., Thompson L.S.,
RA Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Belas R., Moran M.A., Buchan A., Gonzalez J.M., Schell M.A., Sun F.,
RA Richardson P.;
RT "Complete sequence of chromosome of Silicibacter sp. TM1040.";
RL Submitted (MAY-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_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; CP000377; ABF63856.1; -; Genomic_DNA.
DR RefSeq; WP_011538463.1; NC_008044.1.
DR AlphaFoldDB; Q1GHL0; -.
DR SMR; Q1GHL0; -.
DR STRING; 292414.TM1040_1123; -.
DR PRIDE; Q1GHL0; -.
DR EnsemblBacteria; ABF63856; ABF63856; TM1040_1123.
DR KEGG; sit:TM1040_1123; -.
DR eggNOG; COG0002; Bacteria.
DR HOGENOM; CLU_006384_0_1_5; -.
DR OMA; PHLTPMI; -.
DR OrthoDB; 951261at2; -.
DR UniPathway; UPA00068; UER00108.
DR Proteomes; UP000000636; 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; 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.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm; NADP;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..342
FT /note="N-acetyl-gamma-glutamyl-phosphate reductase"
FT /id="PRO_1000011064"
FT ACT_SITE 149
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00150"
SQ SEQUENCE 342 AA; 36986 MW; F0DC12B18B5EC421 CRC64;
MTHNVAILGA SGYTGAELIR LISQHPSITI KALAAERKAG MEMADVFPHL RHLSLPTLCK
IDEIDFAQID LCFCALPHKT SQEVIAKLPG DLKIVDLSAD FRLRDPEAYE KWYGNPHAAL
EQQQEAVYGL TEFYRDEIKG ARLVAGTGCN AATGQFALRP LIAAGVIDLD EIILDMKCAV
SGAGRALKEN LLHAELSEGY NAYAIGGTHR HIGEFDQEFS AIAGRPVKVQ FTPHLLPVNR
GILATTYVKG DAQAIYETFA KAYADEPFVE LLPFGEAPST HHVRGSNFVH IGVTADRIAG
RAIVIVALDN LTKGSSGQAL QNANLMLGED ETAGLMMAPL FP
