ARGC_PSEAE
ID ARGC_PSEAE Reviewed; 344 AA.
AC Q9I5Q9;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 124.
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=PA0662;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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; AE004091; AAG04051.1; -; Genomic_DNA.
DR PIR; E83562; E83562.
DR RefSeq; NP_249353.1; NC_002516.2.
DR RefSeq; WP_003113169.1; NZ_QZGE01000010.1.
DR AlphaFoldDB; Q9I5Q9; -.
DR SMR; Q9I5Q9; -.
DR STRING; 287.DR97_3615; -.
DR PaxDb; Q9I5Q9; -.
DR PRIDE; Q9I5Q9; -.
DR DNASU; 882004; -.
DR EnsemblBacteria; AAG04051; AAG04051; PA0662.
DR GeneID; 882004; -.
DR KEGG; pae:PA0662; -.
DR PATRIC; fig|208964.12.peg.693; -.
DR PseudoCAP; PA0662; -.
DR HOGENOM; CLU_006384_0_1_6; -.
DR InParanoid; Q9I5Q9; -.
DR OMA; PHLTPMI; -.
DR PhylomeDB; Q9I5Q9; -.
DR BioCyc; PAER208964:G1FZ6-667-MON; -.
DR UniPathway; UPA00068; UER00108.
DR Proteomes; UP000002438; 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; IPR023013; AGPR_AS.
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.
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..344
FT /note="N-acetyl-gamma-glutamyl-phosphate reductase"
FT /id="PRO_0000112437"
FT ACT_SITE 150
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00150"
SQ SEQUENCE 344 AA; 36684 MW; 308E65418D4C6C5A CRC64;
MIKVGIVGGT GYTGVELLRL LAQHPQARVE VITSRSEAGV KVADMYPNLR GHYDDLQFSV
PDAQRLGACD VVFFATPHGV AHALAGELLD AGTRVIDLSA DFRLADAEEW ARWYGQPHGA
PALLDEAVYG LPEVNREKIR QARLIAVPGC YPTATQLGLI PLLEAGLADA SRLIADCKSG
VSGAGRGAKV GSLFCEAGES MMAYAVKGHR HLPEISQGLR RASGGDVGLT FVPHLTPMIR
GIHATLYAHV ADRSVDLQAL FEKRYADEPF VDVMPAGSHP ETRSVRGANV CRIAVHRPQG
GDLVVVLSVI DNLVKGASGQ ALQNMNILFG LDERLGLSHA ALLP
