ARGC_STRCO
ID ARGC_STRCO Reviewed; 342 AA.
AC P54895;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 25-MAY-2022, entry version 136.
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=SCO1580;
GN ORFNames=SCI35.02c;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-249.
RC STRAIN=A3(2) / NRRL B-16638;
RX PubMed=8180696; DOI=10.1099/13500872-140-2-311;
RA Hindle Z., Callis R., Dowden S., Rudd B.A.M., Baumberg S.;
RT "Cloning and expression in Escherichia coli of a Streptomyces coelicolor
RT A3(2) argCJB gene cluster.";
RL Microbiology 140:311-320(1994).
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; AL939109; CAA20791.1; -; Genomic_DNA.
DR EMBL; X66783; CAA47283.1; -; Genomic_DNA.
DR PIR; S22861; S22861.
DR PIR; T36815; T36815.
DR RefSeq; NP_625856.1; NC_003888.3.
DR RefSeq; WP_003977244.1; NZ_VNID01000021.1.
DR AlphaFoldDB; P54895; -.
DR SMR; P54895; -.
DR STRING; 100226.SCO1580; -.
DR GeneID; 1097011; -.
DR KEGG; sco:SCO1580; -.
DR PATRIC; fig|100226.15.peg.1592; -.
DR eggNOG; COG0002; Bacteria.
DR HOGENOM; CLU_006384_0_0_11; -.
DR InParanoid; P54895; -.
DR OMA; PHLTPMI; -.
DR PhylomeDB; P54895; -.
DR UniPathway; UPA00068; UER00108.
DR Proteomes; UP000001973; 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..342
FT /note="N-acetyl-gamma-glutamyl-phosphate reductase"
FT /id="PRO_0000112458"
FT ACT_SITE 146
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00150"
SQ SEQUENCE 342 AA; 34615 MW; D2EFF6E047D7621A CRC64;
MAVRAAVAGA SGYAGGELLR LLLTHPEVEI GALTGNSNAG QRLGALQPHL LPLADRVLEA
TTPEVLGGHD VVFLALPHGQ SAAVAEQLGP DVLVVDMGAD FRLKDAGDWE RFYGSPHAGT
WPYGLPELPG ARAALEGSKR IAVPGCYPTA VSLALFPAYA ASLAEPEAVI VAASGTSGAG
KAAKPHLLGS EVMGSMSPYG VGGGHRHTPE MIQNLGAVAG EPVTVSFTPT LAPMPRGILA
TCTAKAKPGV TAESVRAAYE KALADEPFVH LLPEGQWPAT ASVYGSNAVQ VQVAHDAAAG
RIIAISAIDN LAKGTAGGAV QSMNLALGLD ETTGLTTIGV AP
