ARGC_THENN
ID ARGC_THENN Reviewed; 339 AA.
AC Q9Z4S2; B9K8S5;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 25-MAY-2022, entry version 126.
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=CTN_1182;
OS Thermotoga neapolitana (strain ATCC 49049 / DSM 4359 / NBRC 107923 / NS-E).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=309803;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10931207; DOI=10.1046/j.1432-1327.2000.01593.x;
RA Marc F., Weigel P., Legrain C., Almeras Y., Santrot M., Glansdorff N.,
RA Sakanyan V.;
RT "Characterization and kinetic mechanism of mono- and bifunctional ornithine
RT acetyltransferases from thermophilic microorganisms.";
RL Eur. J. Biochem. 267:5217-5226(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49049 / DSM 4359 / NBRC 107923 / NS-E;
RA Lim S.K., Kim J.S., Cha S.H., Park B.C., Lee D.S., Tae H.S., Kim S.-J.,
RA Kim J.J., Park K.J., Lee S.Y.;
RT "The genome sequence of the hyperthermophilic bacterium Thermotoga
RT neapolitana.";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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; AJ009897; CAB38109.1; -; Genomic_DNA.
DR EMBL; CP000916; ACM23358.1; -; Genomic_DNA.
DR RefSeq; WP_015919673.1; NC_011978.1.
DR AlphaFoldDB; Q9Z4S2; -.
DR SMR; Q9Z4S2; -.
DR STRING; 309803.CTN_1182; -.
DR EnsemblBacteria; ACM23358; ACM23358; CTN_1182.
DR KEGG; tna:CTN_1182; -.
DR eggNOG; COG0002; Bacteria.
DR HOGENOM; CLU_006384_0_1_0; -.
DR OMA; PHLTPMI; -.
DR UniPathway; UPA00068; UER00108.
DR Proteomes; UP000000445; 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.
FT CHAIN 1..339
FT /note="N-acetyl-gamma-glutamyl-phosphate reductase"
FT /id="PRO_0000112467"
FT ACT_SITE 145
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00150"
FT CONFLICT 299
FT /note="L -> P (in Ref. 1; CAB38109)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 339 AA; 37928 MW; B15D69E17BF50DE0 CRC64;
MIRVGIVGAT GYTGIELFRL LKKHPSAKIV YMSSRTYAGK KMMEVYPSTL EEAVLEDFDS
RKISESCDVV FTALPAGVSY RLAMELQNVK IIDLGADFRF DDPNTYAEWY GNKLEDYNST
ERVYGLPELY RDSIKNARIV GNPGCYPTSV ILALTPALKS GIVEVDTIVV DSKSGVSGAG
RKETLDYTFS EVNENLRPYN VAKHRHVPEM EQELKKIAGK DVKVIFTPHL VPMTRGILST
IYVKTNASLE KIHRIYQEFY AGEPFVHVLP LGVFPSTKWC YGSNHVFIGM QLEERTGTLI
LMSAIDNLVK GASGQAIQNM NIMFDLKETE GLESLPIYP
