ID   ARGC_METLZ              Reviewed;         330 AA.
AC   A2STZ4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-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=Mlab_1639;
OS   Methanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanocorpusculaceae; Methanocorpusculum.
OX   NCBI_TaxID=410358;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43576 / DSM 4855 / Z;
RX   PubMed=21304657; DOI=10.4056/sigs.35575;
RA   Anderson I.J., Sieprawska-Lupa M., Goltsman E., Lapidus A., Copeland A.,
RA   Glavina Del Rio T., Tice H., Dalin E., Barry K., Pitluck S., Hauser L.,
RA   Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.;
RT   "Complete genome sequence of Methanocorpusculum labreanum type strain Z.";
RL   Stand. Genomic Sci. 1:197-203(2009).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000559; ABN07800.1; -; Genomic_DNA.
DR   RefSeq; WP_011834003.1; NC_008942.1.
DR   AlphaFoldDB; A2STZ4; -.
DR   SMR; A2STZ4; -.
DR   STRING; 410358.Mlab_1639; -.
DR   EnsemblBacteria; ABN07800; ABN07800; Mlab_1639.
DR   GeneID; 4795329; -.
DR   KEGG; mla:Mlab_1639; -.
DR   eggNOG; arCOG00495; Archaea.
DR   HOGENOM; CLU_006384_0_1_2; -.
DR   OMA; PHLTPMI; -.
DR   OrthoDB; 51061at2157; -.
DR   UniPathway; UPA00068; UER00108.
DR   Proteomes; UP000000365; 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..330
FT                   /note="N-acetyl-gamma-glutamyl-phosphate reductase"
FT                   /id="PRO_1000011011"
FT   ACT_SITE        143
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00150"
SQ   SEQUENCE   330 AA;  36211 MW;  C79538DABF062264 CRC64;
     MDIAIIGASG YAGGDLIRLL LTHKEADIVC ATSRKLAGTP VTKDHIHLKN LIDLEYTNPD
     VENIDADFAF LAVPHTAAMQ YAGKLKERGI KTVDFSADYR LPREIYEKTY GVKHSDYFKA
     PYGIPELHRN EVKNASFVAN PGCFPTGATL AAAPVAKLAH TIIYDSKSGV SGAGDSISET
     THFPNVAENI LPYKITAHRH LPEMRQEAAF LGSKANVYFT PHLLPAIRGI ITTAHILFNE
     PMELEMIQKL YQDFYKNEPF VRLQPAKLGG VRGSNFCDIN FELENDGTRL VAVSAIDNLV
     KGAAGQAVQN MNIMCGFDEA EGIRMPGMFP