ID ARGC_BACTN Reviewed; 322 AA. AC Q8A1A7; DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 16-JUN-2009, entry version 51. 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=BT_3759; OS Bacteroides thetaiotaomicron. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=818; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482; RX MEDLINE=22550858; PubMed=12663928; DOI=10.1126/science.1080029; RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., RA Chiang H.C., Hooper L.V., Gordon J.I.; RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis."; RL Science 299:2074-2076(2003). 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 1 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; AE015928; AAO78864.1; -; Genomic_DNA. DR RefSeq; NP_812670.1; -. DR GeneID; 1076380; -. DR GenomeReviews; AE015928_GR; BT_3759. DR KEGG; bth:BT_3759; -. DR NMPDR; fig|226186.1.peg.3757; -. DR HOGENOM; Q8A1A7; -. DR OMA; Q8A1A7; TSHFSWR. DR BioCyc; BTHE226186:BT_3759-MON; -. DR BRENDA; 1.2.1.38; 21018. 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:0046983; F:protein dimerization activity; 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_00150; -; 1. DR InterPro; IPR000706; AGPR_act_site. DR InterPro; IPR000534; Semialdehyde_DH_NAD-bd. DR InterPro; IPR012280; Semialdhyde_DH_C. DR Pfam; PF01118; Semialdhyde_dh; 1. DR Pfam; PF02774; Semialdhyde_dhC; 1. DR ProDom; PD003765; AGPR_act_site; 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 1 322 N-acetyl-gamma-glutamyl-phosphate FT reductase. FT /FTId=PRO_0000112386. FT ACT_SITE 132 132 By similarity. SQ SEQUENCE 322 AA; 35838 MW; 074D784C4F7AB7F7 CRC64; MIKAGIIGGA GYTAGELIRL LLNHPETEIV FINSSSNAGN RITDVHEGLY GETDLRFTDQ LPLDAIDVLF FCTAHGDTKK FMESHNVPED LKIIDLSMDY RIKSDDHDFI YGLPELNRRA TCTAKHVANP GCFATCIQLG LLPLAKNLML TGDVSVNAIT GSTGAGVKPG ATSHFSWRNN NISIYKAFDH QHVPEIKQSL KQLQNSFDSE IDFIPYRGDF PRGIFATLVV KTKVALEEIV RMYEEYYAKD SFVHIVDKNI DLKQVVNTNK CLIHLEKHGD KLLIISCIDN LLKGASGQAV HNMNLMFNLE ETVGLRLKPS AF //