ARGC2_LACPL
ID ARGC2_LACPL Reviewed; 341 AA.
AC O08318; F9UL03;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 25-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=N-acetyl-gamma-glutamyl-phosphate reductase 2 {ECO:0000255|HAMAP-Rule:MF_00150};
DE Short=AGPR 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_00150};
DE Short=NAGSA dehydrogenase 2 {ECO:0000255|HAMAP-Rule:MF_00150};
GN Name=argC2 {ECO:0000255|HAMAP-Rule:MF_00150}; Synonyms=argC;
GN OrderedLocusNames=lp_0528;
OS Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
OS (Lactobacillus plantarum).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactiplantibacillus.
OX NCBI_TaxID=220668;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 8014 / CCM 1904 / DSM 20205 / NCDO 82 / NCIB 6376;
RX PubMed=9098069; DOI=10.1128/jb.179.8.2697-2706.1997;
RA Bringel F., Frey L., Boivin S., Hubert J.-C.;
RT "Arginine biosynthesis and regulation in Lactobacillus plantarum: the carA
RT gene and the argCJBDF cluster are divergently transcribed.";
RL J. Bacteriol. 179:2697-2706(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX PubMed=12566566; DOI=10.1073/pnas.0337704100;
RA Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P.,
RA Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W.E.J.,
RA Stiekema W., Klein Lankhorst R.M., Bron P.A., Hoffer S.M.,
RA Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., De Vos W.M.,
RA Siezen R.J.;
RT "Complete genome sequence of Lactobacillus plantarum WCFS1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX PubMed=22156394; DOI=10.1128/jb.06275-11;
RA Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M.,
RA Kleerebezem M., van Hijum S.A.;
RT "Complete resequencing and reannotation of the Lactobacillus plantarum
RT WCFS1 genome.";
RL J. Bacteriol. 194:195-196(2012).
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; X99978; CAA68239.1; -; Genomic_DNA.
DR EMBL; AL935263; CCC78018.1; -; Genomic_DNA.
DR RefSeq; WP_003646527.1; NC_004567.2.
DR RefSeq; YP_004888532.1; NC_004567.2.
DR AlphaFoldDB; O08318; -.
DR SMR; O08318; -.
DR STRING; 220668.lp_0528; -.
DR EnsemblBacteria; CCC78018; CCC78018; lp_0528.
DR KEGG; lpl:lp_0528; -.
DR PATRIC; fig|220668.9.peg.436; -.
DR eggNOG; COG0002; Bacteria.
DR HOGENOM; CLU_006384_0_1_9; -.
DR OMA; PHLTPMI; -.
DR PhylomeDB; O08318; -.
DR BioCyc; LPLA220668:G1GW0-439-MON; -.
DR UniPathway; UPA00068; UER00108.
DR Proteomes; UP000000432; 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..341
FT /note="N-acetyl-gamma-glutamyl-phosphate reductase 2"
FT /id="PRO_0000112413"
FT ACT_SITE 146
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00150"
FT CONFLICT 119
FT /note="S -> P (in Ref. 1; CAA68239)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="V -> A (in Ref. 1; CAA68239)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 341 AA; 36940 MW; CD35D297041CC42A CRC64;
MQVALVGVTG YSGMVLYRLL KQHPEIDRIQ LYGHVGATTV ALKTVAAMYQ KETAVIRPFD
ATAIMRDNAI VFFATSAGIT RQLALPFIAA HFPVIDLSGD FRLHDPEQYQ RWYQRDPASA
TALAQASYGL ADMPAPLSTY IANPGCYATA TLLGLAPLAQ QQLVEPTSIV VDAKSGLSGA
GKRATAASHY VAVNDNLSLY KLNQHQHIPE MMQQLQQWWS AISAIEFTTT LIPVTRGIMT
TIYAKAKSAL TTTQVRAAFT ATYHEQPFVQ VLPTGMPTLK DVVGSNNCAL GVDYNPVTNT
IVVVSVIDNL MKGAAGQAVQ NFNRYFDFAV TAGLPTLPVF P
