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 03-SEP-2014, entry version 62. DE RecName: Full=N-acetyl-gamma-glutamyl-phosphate reductase; DE Short=AGPR; DE EC=1.2.1.38; DE AltName: Full=N-acetyl-glutamate semialdehyde dehydrogenase; DE Short=NAGSA dehydrogenase; GN Name=argC; OrderedLocusNames=SUN_1304; OS Sulfurovum sp. (strain NBC37-1). OC Bacteria; Proteobacteria; Epsilonproteobacteria; 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 -!- CATALYTIC ACTIVITY: N-acetyl-L-glutamate 5-semialdehyde + NADP(+) CC + phosphate = N-acetyl-5-glutamyl phosphate + NADPH. CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)- CC acetyl-L-ornithine from L-glutamate: step 3/4. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the NAGSA dehydrogenase family. Type 1 CC subfamily. 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 RefSeq; WP_011980990.1; NC_009663.1. DR RefSeq; YP_001358614.1; NC_009663.1. DR ProteinModelPortal; A6Q9U8; -. DR STRING; 387093.SUN_1304; -. DR EnsemblBacteria; BAF72257; BAF72257; SUN_1304. DR GeneID; 5363920; -. DR KEGG; sun:SUN_1304; -. DR PATRIC; 23775593; VBISulSp49917_1324. DR eggNOG; COG0002; -. DR HOGENOM; HOG000254902; -. DR KO; K00145; -. DR OMA; NHRHHPE; -. DR OrthoDB; EOG6XSZS3; -. DR BioCyc; SSP387093:GH25-1320-MONOMER; -. DR UniPathway; UPA00068; UER00108. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.720; -; 1. DR HAMAP; MF_00150; ArgC_type1; 1. DR InterPro; IPR023013; AGPR_AS. DR InterPro; IPR000706; AGPR_type-1. DR InterPro; IPR016040; NAD(P)-bd_dom. 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 TIGRFAMs; TIGR01850; argC; 1. DR PROSITE; PS01224; ARGC; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Arginine biosynthesis; Complete proteome; KW Cytoplasm; NADP; Oxidoreductase. FT CHAIN 1 335 N-acetyl-gamma-glutamyl-phosphate FT reductase. FT /FTId=PRO_1000118064. FT ACT_SITE 147 147 By similarity. 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 //