ID ARGC_AQUAE Reviewed; 340 AA. AC O67724; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 16-JUN-2009, entry version 65. 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=aq_1879; OS Aquifex aeolicus. OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex. OX NCBI_TaxID=63363; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VF5; RX MEDLINE=98196666; PubMed=9537320; DOI=10.1038/32831; RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.; RT "The complete genome of the hyperthermophilic bacterium Aquifex RT aeolicus."; RL Nature 392:353-358(1998). 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; AE000657; AAC07684.1; -; Genomic_DNA. DR PIR; B70462; B70462. DR RefSeq; NP_214292.1; -. DR GeneID; 1193531; -. DR GenomeReviews; AE000657_GR; aq_1879. DR KEGG; aae:aq_1879; -. DR NMPDR; fig|224324.1.peg.1307; -. DR HOGENOM; O67724; -. DR OMA; O67724; VCRIAVH. DR BioCyc; AAEO224324:AQ_1879-MON; -. DR BRENDA; 1.2.1.38; 189781. 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 1 340 N-acetyl-gamma-glutamyl-phosphate FT reductase. FT /FTId=PRO_0000112375. FT ACT_SITE 151 151 By similarity. SQ SEQUENCE 340 AA; 38958 MW; A7BADB7A186AB653 CRC64; MEQTLRVSVF GATGYTGIEL LRSLLTHPHF EVKNLISQSY KGKKVREVLP FFSNTYISEI EFLEEPVEDY ELAFLCLPHE VSYEIVPKLL SQGKKVVDLS GAYRIKSPKA YEEFYGFKHE REDILQRAVY GLPEVFREEI KNSDLVANPG CYPTATLLAI YPFLKERVGI ESVIVHALSG VSGAGRKPKQ QFHFPEMTEN FFNYAVEKHR HTPEMEDVIR RVYGREVKVR FTPTVVPTSR GMISTVYLKS EKLNVKELFK EVYEDEIFVK VVDEPPQTKW VLGTNYCFIY PHYDERTGYY VIISAIDNLG KGASLQAVQN ANLMFGLAED DGLLQLPVFP //