ARGC_CAMJE
ID ARGC_CAMJE Reviewed; 342 AA.
AC Q9PIS0; Q0PBT0; Q9RH00;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, 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=Cj0224;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43431 / TGH 9011 / Serotype O:3;
RX PubMed=10588044; DOI=10.1139/w99-095;
RA Hani E.K., Ng D., Chan V.-L.;
RT "Arginine biosynthesis in Campylobacter jejuni TGH9011: determination of
RT the argCOBD cluster.";
RL Can. J. Microbiol. 45:959-969(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(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; AF093219; AAF21802.1; -; Genomic_DNA.
DR EMBL; AL111168; CAL34379.1; -; Genomic_DNA.
DR PIR; H81439; H81439.
DR RefSeq; WP_002851634.1; NC_002163.1.
DR RefSeq; YP_002343667.1; NC_002163.1.
DR AlphaFoldDB; Q9PIS0; -.
DR SMR; Q9PIS0; -.
DR IntAct; Q9PIS0; 35.
DR STRING; 192222.Cj0224; -.
DR PaxDb; Q9PIS0; -.
DR PRIDE; Q9PIS0; -.
DR EnsemblBacteria; CAL34379; CAL34379; Cj0224.
DR GeneID; 906012; -.
DR KEGG; cje:Cj0224; -.
DR PATRIC; fig|192222.6.peg.218; -.
DR eggNOG; COG0002; Bacteria.
DR HOGENOM; CLU_006384_0_1_7; -.
DR OMA; PHLTPMI; -.
DR UniPathway; UPA00068; UER00108.
DR Proteomes; UP000000799; 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_0000112393"
FT ACT_SITE 147
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00150"
FT CONFLICT 76
FT /note="K -> E (in Ref. 1; AAF21802)"
FT /evidence="ECO:0000305"
FT CONFLICT 119
FT /note="E -> D (in Ref. 1; AAF21802)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="S -> N (in Ref. 1; AAF21802)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="V -> I (in Ref. 1; AAF21802)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="N -> G (in Ref. 1; AAF21802)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="L -> S (in Ref. 1; AAF21802)"
FT /evidence="ECO:0000305"
FT CONFLICT 296
FT /note="V -> I (in Ref. 1; AAF21802)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 342 AA; 38896 MW; D5CE90039C63179C CRC64;
MKIKVGILGA SGYAGNELVR ILLNHPKVEI SYLGSSSSVG QNYQDLYPNT PLNLCFENKN
LDELELDLLF LATPHKFSAK LLNENLLKKM KIIDLSADFR LKNPKDYELW YKFTHPNQEL
LQNAVYGLCE LYKEEIKKAS LVANPGCYTT CSILSLYPLF KEKIIDFSSV IIDAKSGVSG
AGRSAKVENL FCEVNENIKA YNLALHRHTP EIEEHLSYAA KEKITLQFTP HLVPMQRGIL
ISAYANLKED LQEQDIRDIY TKYYQNNKFI RLLPPQSLPQ TRWVKSSNFA DINFSVDQRT
KRVIVLGAID NLIKGAAGQA VQNMNLMFDF DEDEGLKFFA NL
