ID DHE4_HELPY Reviewed; 448 AA. AC P55990; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 16-JUN-2009, entry version 50. DE RecName: Full=NADP-specific glutamate dehydrogenase; DE Short=NADP-GDH; DE EC=1.4.1.4; GN Name=gdhA; OrderedLocusNames=HP_0380; OS Helicobacter pylori (Campylobacter pylori). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=210; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700392 / 26695; RX MEDLINE=97394467; PubMed=9252185; DOI=10.1038/41483; RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G., RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., RA Dougherty B.A., Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., RA Peterson S.N., Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., RA Glodek A., McKenney K., FitzGerald L.M., Lee N., Adams M.D., RA Hickey E.K., Berg D.E., Gocayne J.D., Utterback T.R., Peterson J.D., RA Kelley J.M., Cotton M.D., Weidman J.F., Fujii C., Bowman C., RA Watthey L., Wallin E., Hayes W.S., Borodovsky M., Karp P.D., RA Smith H.O., Fraser C.M., Venter J.C.; RT "The complete genome sequence of the gastric pathogen Helicobacter RT pylori."; RL Nature 388:539-547(1997). CC -!- CATALYTIC ACTIVITY: L-glutamate + H(2)O + NADP(+) = 2-oxoglutarate CC + NH(3) + NADPH. CC -!- SUBUNIT: Homohexamer (By similarity). 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; AE000511; AAD07448.1; -; Genomic_DNA. DR PIR; D64567; D64567. DR RefSeq; NP_207178.1; -. DR HSSP; P24295; 1AUP. DR GeneID; 898871; -. DR GenomeReviews; AE000511_GR; HP_0380. DR KEGG; hpy:HP0380; -. DR NMPDR; fig|85962.1.peg.376; -. DR TIGR; HP_0380; -. DR HOGENOM; P55990; -. DR OMA; P55990; EMAQNAS. DR BRENDA; 1.4.1.4; 1131. DR GO; GO:0005488; F:binding; IEA:InterPro. DR GO; GO:0004354; F:glutamate dehydrogenase (NADP+) 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 3: Inferred from homology; KW Complete proteome; NADP; Oxidoreductase. FT CHAIN 1 448 NADP-specific glutamate dehydrogenase. FT /FTId=PRO_0000182771. FT ACT_SITE 124 124 By similarity. SQ SEQUENCE 448 AA; 49379 MW; 1044636E2F696A43 CRC64; MYVEKILQSL QKKYPYQKEF HQAVYEAITS LKPLLDSDKS YEKHAILERL IEPEREIFFR VCWLDDNNQI QVNRGCRVEF NSAIGPYKGG LRFHPSVNES VIKFLGFEQV LKNSLTTLAM GGAKGGSDFD PKGKSEHEIM RFCQAFMNEL YRHIGATTDV PAGDIGVGER EIGYLFGQYK KLVNRFEGVL TGKGLTYGGS LCRKEATGYG CVYFAEEMLQ ERNSSLEGKV CSVSGSGNVA IYTIEKLLQI GAKPVTASDS NGMIYDKDGI DLELLKEIKE VRRGRIKEYA LEKKSAEYTP TENYPKGGNA VWHVPCFAAF PSATENELSV LDAKTLLSNG CKCVAEGANM PSSNEAIGLF LQAKISYGIG KAANAGGVSV SGLEMAQNAS MHPWSFEVVD AKLHHIMKEI YKNVSQTAKE FKDPTNFVLG ANIAGFRKVA SAMIAQGV //