ARGC2_PSEPK
ID ARGC2_PSEPK Reviewed; 313 AA.
AC P59308;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 12-FEB-2003, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=N-acetyl-gamma-glutamyl-phosphate reductase 2 {ECO:0000255|HAMAP-Rule:MF_01110};
DE Short=AGPR 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_01110};
DE Short=NAGSA dehydrogenase 2 {ECO:0000255|HAMAP-Rule:MF_01110};
GN Name=argC2 {ECO:0000255|HAMAP-Rule:MF_01110}; OrderedLocusNames=PP_3633;
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(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; AE015451; AAN69233.1; -; Genomic_DNA.
DR RefSeq; NP_745769.1; NC_002947.4.
DR RefSeq; WP_010954475.1; NC_002947.4.
DR AlphaFoldDB; P59308; -.
DR SMR; P59308; -.
DR STRING; 160488.PP_3633; -.
DR EnsemblBacteria; AAN69233; AAN69233; PP_3633.
DR KEGG; ppu:PP_3633; -.
DR PATRIC; fig|160488.4.peg.3866; -.
DR eggNOG; COG0002; Bacteria.
DR HOGENOM; CLU_077118_0_0_6; -.
DR OMA; FSWRNNN; -.
DR PhylomeDB; P59308; -.
DR BioCyc; PPUT160488:G1G01-3871-MON; -.
DR UniPathway; UPA00068; UER00108.
DR Proteomes; UP000000556; 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; 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..313
FT /note="N-acetyl-gamma-glutamyl-phosphate reductase 2"
FT /id="PRO_0000112508"
FT ACT_SITE 117
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01110"
SQ SEQUENCE 313 AA; 33396 MW; CC4602FB3DF1E335 CRC64;
MHTPVVFIDG DQGTTGLQIH ARLQGRSDLR LLTLPEAERK DPQRRCEAIN SADIALLCLP
DDAAREAVAA IHNPQVRVID ASSAHRTTPG WVYGLPELDE QQAERIAQST RVSNPGCYPT
GAIALLHPLV KAGLLPADYP LNIHAVSGYS GGGRAAVERH EQPGAAKAPA LQLYGLELAH
KHVPEIQQHA GLSARPMFMP GYGAYRQGIA LSIPLQLRLL PGQVSAEHLQ ACLEQHYQGA
RHVQVMPLHQ CGAAANLDPE ALNGSNDLRL ALYANPEHGQ VLLTAVFDNL GKGASGAAVQ
NLDLMLGALQ AHG
