ID ARGC_ANAVT Reviewed; 322 AA. AC Q3MG30; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2005, sequence version 1. DT 16-JUN-2009, entry version 27. 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=Ava_0430; OS Anabaena variabilis (strain ATCC 29413 / PCC 7937). OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena. OX NCBI_TaxID=240292; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J., RA Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.; RT "Complete sequence of Anabaena variabilis ATCC 29413."; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. 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 (Probable). CC -!- SIMILARITY: Belongs to the NAGSA dehydrogenase family. Type 2 CC subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000117; ABA20056.1; -; Genomic_DNA. DR RefSeq; YP_320951.1; -. DR GeneID; 3682591; -. DR GenomeReviews; CP000117_GR; Ava_0430. DR KEGG; ava:Ava_0430; -. DR NMPDR; fig|240292.3.peg.1312; -. DR HOGENOM; Q3MG30; -. DR OMA; Q3MG30; FRQGMLV. DR BioCyc; AVAR240292:AVA_0430-MON; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase...; IEA:HAMAP. DR GO; GO:0051287; F:NAD or NADH binding; IEA:InterPro. DR GO; GO:0006526; P:arginine biosynthetic process; IEA:HAMAP. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR HAMAP; MF_01110; -; 1. DR InterPro; IPR000706; AGPR_act_site. DR InterPro; IPR010136; AGPR_subtype. DR InterPro; IPR000534; Semialdehyde_DH_NAD-bd. DR Pfam; PF01118; Semialdhyde_dh; 1. DR ProDom; PD003765; AGPR_act_site; 1. DR TIGRFAMs; TIGR01851; argC_other; 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 1 322 N-acetyl-gamma-glutamyl-phosphate FT reductase. FT /FTId=PRO_1000065137. FT ACT_SITE 117 117 By similarity. SQ SEQUENCE 322 AA; 34832 MW; A01B081ADD12A23C CRC64; MNKPKIFIDG EAGTTGLQIY SRLNERDDIE LVSIAASKRK DADERAKLLN SVDVAILCLP DDAAREAVSL VHSSQVKILD ASTAYRTAQG WVYGFPELNP GQREKIANAQ FVSNPGCYPT GFLACVRPLI AQGILPSSFP ITINAVSGYS GGGKSLIQKY DSFHEQQKGA TSDYPFGIYG LQFGHKHVKE MHQHSGLASP PLFIPAVGDF EQGMLVQIPL PLWTLDNPPS GEEIHQAIAQ YYQGEKFVQV ASFKDPSLLR DGTFLDATAV NGTNIVQVFV FANDNTKEAL LVARLDNLGK GASGAAVQNL NIMLGLPEEL GL //