ID ARGC_SULNB Reviewed; 335 AA. AC A6Q9U8; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 21-AUG-2007, sequence version 1. DT 24-JAN-2024, entry version 115. 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=SUN_1304; OS Sulfurovum sp. (strain NBC37-1). OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales; OC Sulfurovaceae; Sulfurovum. OX NCBI_TaxID=387093; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBC37-1; RX PubMed=17615243; DOI=10.1073/pnas.0700687104; RA Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K., RA Horikoshi K.; RT "Deep-sea vent epsilon-proteobacterial genomes provide insights into RT emergence of pathogens."; RL Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007). 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; AP009179; BAF72257.1; -; Genomic_DNA. DR AlphaFoldDB; A6Q9U8; -. DR SMR; A6Q9U8; -. DR STRING; 387093.SUN_1304; -. DR KEGG; sun:SUN_1304; -. DR eggNOG; COG0002; Bacteria. DR HOGENOM; CLU_006384_0_1_7; -. DR OMA; PHLTPMI; -. DR UniPathway; UPA00068; UER00108. DR Proteomes; UP000006378; 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:0070401; F:NADP+ 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 Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. 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 NCBIfam; TIGR01850; argC; 1. DR PANTHER; PTHR32338:SF10; N-ACETYL-GAMMA-GLUTAMYL-PHOSPHATE REDUCTASE, CHLOROPLASTIC-RELATED; 1. DR PANTHER; PTHR32338; N-ACETYL-GAMMA-GLUTAMYL-PHOSPHATE REDUCTASE, CHLOROPLASTIC-RELATED-RELATED; 1. DR Pfam; PF01118; Semialdhyde_dh; 1. DR Pfam; PF02774; Semialdhyde_dhC; 1. DR SMART; SM00859; Semialdhyde_dh; 1. DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR PROSITE; PS01224; ARGC; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm; NADP; KW Oxidoreductase. FT CHAIN 1..335 FT /note="N-acetyl-gamma-glutamyl-phosphate reductase" FT /id="PRO_1000118064" FT ACT_SITE 147 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00150" SQ SEQUENCE 335 AA; 36561 MW; D50D2832D87449DB CRC64; MIKVGVVGAS GYTGLELVKM LITHPGFELT YLATTQGDTT IEALHPSLEG VVTLEVEKAD VNAVADACEL VFLALPHKAS MGFAKGLIEK GVKVVDLSAD YRLELDTYEA HYCEHEDKEH LDESVYALIE YYREELKEAE LAAGPGCYPT ATLLGILPFI PYIDTSAPLF VDAKSGVSGA GKKLSETTHF VTVNDNIFAY NPLKHRHAPE IAEKIEKVHG AKMNVNFVPH LIPATRGELV SVYATLKEDI DPLEVLRKHY ANDRFIRIRE KPVDIKSTAG THFCDIYAAK NGHALFVSSA IDNLLRGASS QALAAANLMC GYDEGMGLPV IPYMP //