ARGC_BURL3
ID ARGC_BURL3 Reviewed; 315 AA.
AC Q38ZT5;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 97.
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};
GN OrderedLocusNames=Bcep18194_B3171;
OS Burkholderia lata (strain ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 /
OS R18194 / 383).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=482957;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 / R18194 / 383;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A.,
RA Richardson P.;
RT "Complete sequence of chromosome 2 of Burkholderia sp. 383.";
RL Submitted (OCT-2005) 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; CP000152; ABB13281.1; -; Genomic_DNA.
DR RefSeq; WP_011356758.1; NC_007511.1.
DR AlphaFoldDB; Q38ZT5; -.
DR SMR; Q38ZT5; -.
DR EnsemblBacteria; ABB13281; ABB13281; Bcep18194_B3171.
DR GeneID; 45099467; -.
DR KEGG; bur:Bcep18194_B3171; -.
DR PATRIC; fig|482957.22.peg.7006; -.
DR HOGENOM; CLU_077118_0_0_4; -.
DR OMA; FSWRNNN; -.
DR OrthoDB; 951261at2; -.
DR UniPathway; UPA00068; UER00108.
DR Proteomes; UP000002705; Chromosome 2.
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..315
FT /note="N-acetyl-gamma-glutamyl-phosphate reductase"
FT /id="PRO_1000137115"
FT ACT_SITE 117
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01110"
SQ SEQUENCE 315 AA; 33423 MW; 62E92B22AEC4E58E CRC64;
MSQPTVYIDG DQGTTGLLIH ERLRGRIDLQ LVTLPDAERK DPVRRAEAIN AADIAILCLP
DAAAREAVGF IRNPAVRVID ASSAHRTQPD WVYGFPEMAN GHAQTIAHAR RVTNPGCYPT
GAIALLRPLQ QAGLLPRDYP VSIHAVSGYS GGGRAAVDAF ESGDASQAKP LQVYGLALAH
KHVPEIQLHA GLTNRPMFVP AYGAYRQGIV LTVPIELRLL PAGVTGEQLH ACLAHHYADA
RHVDVTPLAD TQAITHLDPQ ALNGTNDMRL GVFVNAEHGQ VLLSAVFDNL GKGASGAAVQ
NLDLMLGAAD VAKAA