ID   ARGC_PSELT              Reviewed;         341 AA.
AC   A8F448;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   25-MAY-2022, entry version 89.
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=Tlet_0365;
OS   Pseudothermotoga lettingae (strain ATCC BAA-301 / DSM 14385 / NBRC 107922 /
OS   TMO) (Thermotoga lettingae).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Pseudothermotoga.
OX   NCBI_TaxID=416591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-301 / DSM 14385 / NBRC 107922 / TMO;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Foster B., Bruce D., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Nelson K., Gogarten J.P., Noll K.,
RA   Richardson P.;
RT   "Complete sequence of Thermotoga lettingae TMO.";
RL   Submitted (AUG-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; CP000812; ABV32932.1; -; Genomic_DNA.
DR   RefSeq; WP_012002413.1; NC_009828.1.
DR   AlphaFoldDB; A8F448; -.
DR   SMR; A8F448; -.
DR   STRING; 416591.Tlet_0365; -.
DR   EnsemblBacteria; ABV32932; ABV32932; Tlet_0365.
DR   KEGG; tle:Tlet_0365; -.
DR   eggNOG; COG0002; Bacteria.
DR   HOGENOM; CLU_006384_0_1_0; -.
DR   OMA; PHLTPMI; -.
DR   OrthoDB; 951261at2; -.
DR   UniPathway; UPA00068; UER00108.
DR   Proteomes; UP000002016; 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; 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.
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"
FT                   /id="PRO_1000123252"
FT   ACT_SITE        148
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00150"
SQ   SEQUENCE   341 AA;  38504 MW;  92C7E3036D6EBC9C CRC64;
     MKIRVGILGA TGYTGLELLR MLKNHPQVKI TYLSSNNFSG QSMKDIYPFA EIDILLSKID
     VKEIKANCDV VFTALPAGIS YDIVKSLRDE NLKIIDLGAD LRFDDPSLYE KWYGRTLQDY
     GLIKRVYGLP ELYRSEIKES RFIGNPGCYP TSILLATAPI LKRKLLVNGE IIVDSKSGVS
     GAGKKEELAY SFCEIDGSLK PYSVINHKHV PEIQEQMKKI YHSEVTVIFA PHLVPMVRGI
     LSTIYLKTRL SADELYGLYS EFYRDEYFVH VLKPAIYPST KWSYGSNHVF ISMKKDERTD
     TAVLISVLDN LVKGASGQAI QNMNILFSLR EDTGLTFTVY P