ARGC_ECOLI
ID ARGC_ECOLI Reviewed; 334 AA.
AC P11446; Q2M8Q3;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=N-acetyl-gamma-glutamyl-phosphate reductase {ECO:0000255|HAMAP-Rule:MF_00150, ECO:0000305};
DE Short=AGPR {ECO:0000255|HAMAP-Rule:MF_00150, ECO:0000305};
DE EC=1.2.1.38 {ECO:0000255|HAMAP-Rule:MF_00150, ECO:0000269|PubMed:13863980};
DE AltName: Full=N-acetyl-glutamate semialdehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00150, ECO:0000303|PubMed:2851495};
DE Short=NAGSA dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00150, ECO:0000303|PubMed:2851495};
GN Name=argC {ECO:0000255|HAMAP-Rule:MF_00150};
GN OrderedLocusNames=b3958, JW3930;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2851495; DOI=10.1016/0378-1119(88)90030-3;
RA Parsot C., Boyen A., Cohen G.N., Glansdorff N.;
RT "Nucleotide sequence of Escherichia coli argB and argC genes: comparison of
RT N-acetylglutamate kinase and N-acetylglutamate-gamma-semialdehyde
RT dehydrogenase with homologous and analogous enzymes.";
RL Gene 68:275-283(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-48.
RC STRAIN=K12;
RX PubMed=6761650; DOI=10.1093/nar/10.24.8031;
RA Piette J., Cunin R., Boyen A., Charlier D.R.M., Crabeel M., van Vliet F.,
RA Glansdorff N., Squires C., Squires C.L.;
RT "The regulatory region of the divergent argECBH operon in Escherichia coli
RT K-12.";
RL Nucleic Acids Res. 10:8031-8048(1982).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-19.
RC STRAIN=K12;
RX PubMed=1551850; DOI=10.1128/jb.174.7.2323-2331.1992;
RA Meinnel T., Schmitt E., Mechulam Y., Blanquet S.;
RT "Structural and biochemical characterization of the Escherichia coli argE
RT gene product.";
RL J. Bacteriol. 174:2323-2331(1992).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=W / ATCC 11105 / DSM 1900;
RX PubMed=13863980; DOI=10.1016/0006-291x(62)90342-x;
RA Baich A., Vogel H.J.;
RT "N-Acetyl-gamma-Ilutamokinase and N-acetylglutamic gamma-semialdehyde
RT dehydrogenase: repressible enzymes of arginine synthesis in Escherichia
RT coli.";
RL Biochem. Biophys. Res. Commun. 7:491-496(1962).
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, ECO:0000269|PubMed:13863980}.
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 ECO:0000269|PubMed:13863980};
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, ECO:0000305|PubMed:13863980}.
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, ECO:0000305}.
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DR EMBL; M21446; AAA23477.1; -; Genomic_DNA.
DR EMBL; U00006; AAC43064.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76940.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77353.1; -; Genomic_DNA.
DR EMBL; J01587; AAB59146.1; -; Genomic_DNA.
DR EMBL; X55417; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; JT0332; RDECEP.
DR RefSeq; NP_418393.1; NC_000913.3.
DR RefSeq; WP_000935370.1; NZ_STEB01000037.1.
DR AlphaFoldDB; P11446; -.
DR SMR; P11446; -.
DR BioGRID; 4262190; 6.
DR BioGRID; 852751; 1.
DR IntAct; P11446; 1.
DR STRING; 511145.b3958; -.
DR PaxDb; P11446; -.
DR PRIDE; P11446; -.
DR EnsemblBacteria; AAC76940; AAC76940; b3958.
DR EnsemblBacteria; BAE77353; BAE77353; BAE77353.
DR GeneID; 66672132; -.
DR GeneID; 948455; -.
DR KEGG; ecj:JW3930; -.
DR KEGG; eco:b3958; -.
DR PATRIC; fig|1411691.4.peg.2747; -.
DR EchoBASE; EB0063; -.
DR eggNOG; COG0002; Bacteria.
DR HOGENOM; CLU_006384_0_1_6; -.
DR InParanoid; P11446; -.
DR OMA; PHLTPMI; -.
DR PhylomeDB; P11446; -.
DR BioCyc; EcoCyc:N-ACETYLGLUTPREDUCT-MON; -.
DR BioCyc; MetaCyc:N-ACETYLGLUTPREDUCT-MON; -.
DR BRENDA; 1.2.1.38; 2026.
DR UniPathway; UPA00068; UER00108.
DR PRO; PR:P11446; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase activity; IDA:EcoCyc.
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; IDA:EcoCyc.
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 1: Evidence at protein level;
KW Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm; NADP;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..334
FT /note="N-acetyl-gamma-glutamyl-phosphate reductase"
FT /id="PRO_0000112401"
FT ACT_SITE 154
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00150"
SQ SEQUENCE 334 AA; 35952 MW; 67AC195ECE1C4789 CRC64;
MLNTLIVGAS GYAGAELVTY VNRHPHMNIT ALTVSAQSND AGKLISDLHP QLKGIVDLPL
QPMSDISEFS PGVDVVFLAT AHEVSHDLAP QFLEAGCVVF DLSGAFRVND ATFYEKYYGF
THQYPELLEQ AAYGLAEWCG NKLKEANLIA VPGCYPTAAQ LALKPLIDAD LLDLNQWPVI
NATSGVSGAG RKAAISNSFC EVSLQPYGVF THRHQPEIAT HLGADVIFTP HLGNFPRGIL
ETITCRLKSG VTQAQVAQVL QQAYAHKPLV RLYDKGVPAL KNVVGLPFCD IGFAVQGEHL
IIVATEDNLL KGAAAQAVQC ANIRFGYAET QSLI
