ID DHE2_STAAM Reviewed; 414 AA. AC Q99VD0; DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 16-JUN-2009, entry version 47. DE RecName: Full=NAD-specific glutamate dehydrogenase; DE Short=NAD-GDH; DE EC=1.4.1.2; GN Name=gluD; Synonyms=gudB; OrderedLocusNames=SAV0958; OS Staphylococcus aureus (strain Mu50 / ATCC 700699). OC Bacteria; Firmicutes; Bacillales; Staphylococcus. OX NCBI_TaxID=158878; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=21311952; PubMed=11418146; DOI=10.1016/S0140-6736(00)04403-2; RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., RA Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y., RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., RA Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M., RA Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M., RA Ogasawara N., Hayashi H., Hiramatsu K.; RT "Whole genome sequencing of meticillin-resistant Staphylococcus RT aureus."; RL Lancet 357:1225-1240(2001). CC -!- CATALYTIC ACTIVITY: L-glutamate + H(2)O + NAD(+) = 2-oxoglutarate CC + NH(3) + NADH. CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family. 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; BA000017; BAB57120.1; -; Genomic_DNA. DR RefSeq; NP_371482.1; -. DR HSSP; P80319; 1GTM. DR World-2DPAGE; 0002:Q99VD0; -. DR GeneID; 1120933; -. DR GenomeReviews; BA000017_GR; SAV0958. DR KEGG; sav:SAV0958; -. DR HOGENOM; Q99VD0; -. DR OMA; Q99VD0; REMAWMM. DR BioCyc; SAUR158878:SAV0958-MON; -. DR GO; GO:0005488; F:binding; IEA:InterPro. DR GO; GO:0004352; F:glutamate dehydrogenase activity; IEA:EC. DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR006095; Glu/Leu/Phe/Val_DH. DR InterPro; IPR006096; Glu/Leu/Phe/Val_DH_C. DR InterPro; IPR006097; Glu/Leu/Phe/Val_DH_dimer. DR InterPro; IPR014362; Glu_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR PANTHER; PTHR11606:SF2; GLFV_DH; 1. DR Pfam; PF00208; ELFV_dehydrog; 1. DR Pfam; PF02812; ELFV_dehydrog_N; 1. DR PIRSF; PIRSF000185; Glu_DH; 1. DR PRINTS; PR00082; GLFDHDRGNASE. DR PROSITE; PS00074; GLFV_DEHYDROGENASE; 1. PE 1: Evidence at protein level; KW Complete proteome; NAD; Oxidoreductase. FT CHAIN 1 414 NAD-specific glutamate dehydrogenase. FT /FTId=PRO_0000223327. FT ACT_SITE 106 106 By similarity. SQ SEQUENCE 414 AA; 45760 MW; F79290751F6312C7 CRC64; MTENNNLVTS TQGIIKEALH KLGFDEGMYD LIKEPLRMLQ VRIPVRMDDG TVKTFTGYRA QHNDAVGPTK GGVRFHPDVD EEEVKALSMW MTLKCGIVNL PYGGGKGGIV CDPRQMSIHE VERLSRGYVR AISQFVGPNK DIPAPDVFTN SQIMAWMMDE YSALDKFNSP GFITGKPIVL GGSHGRDRST ALGVVIAIEQ AAKRRNMQIE GAKVVIQGFG NAGSFLAKFL YDLGAKIVGI SDAYGALHDP NGLDIDYLLD RRDSFGTVTN LFEETISNKE LFELDCDILV PAAISNQITE DNAHDIKASI VVEAANGPTT PEATRILTER GILLVPDVLA SAGGVTVSYF EWVQNNQGYY WSEEEVNEKL REKLEAAFDT IYELSQNRKI DMRLAAYIIG IKRTAEAARY RGWA //