ID DHE4_HAEIN Reviewed; 449 AA. AC P43793; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 25-NOV-2008, entry version 52. DE RecName: Full=NADP-specific glutamate dehydrogenase; DE Short=NADP-GDH; DE EC=1.4.1.4; GN Name=gdhA; OrderedLocusNames=HI0189; OS Haemophilus influenzae. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=727; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX MEDLINE=95350630; PubMed=7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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; L42023; AAC21858.1; -; Genomic_DNA. DR PIR; A64053; A64053. DR RefSeq; NP_438358.1; -. DR HSSP; P24295; 1AUP. DR GeneID; 951095; -. DR GenomeReviews; L42023_GR; HI0189. DR KEGG; hin:HI0189; -. DR NMPDR; fig|71421.1.peg.179; -. DR TIGR; HI0189; -. DR HOGENOM; P43793; -. DR BioCyc; HINF71421:HI_0189-MON; -. 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_DHase. DR InterPro; IPR006096; Glu/Leu/Phe/Val_DHase_C. DR InterPro; IPR006097; Glu/Leu/Phe/Val_DHase_dimer. DR InterPro; IPR014362; Glu_DHase. DR InterPro; IPR016040; NAD(P)-bd. 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 1 449 NADP-specific glutamate dehydrogenase. FT /FTId=PRO_0000182770. FT ACT_SITE 128 128 By similarity. SQ SEQUENCE 449 AA; 48660 MW; 4698E0CD6C665A34 CRC64; MSKVASLDAF LTKVAQRDGY QPEFLQAVRE VFTSIWPFLE ANPKYRSEAL LERLVEPERA FQFRVAWTDD KGQVQVNRAF RVQFNSAIGP FKGGMRFHPS VNLSILKFLG FEQIFKNALT TLPMGGAKGG SDFDPKGKSD AEVMRFCQAL MAELYRHVGA DTDVPAGDIG VGGREVGYLA GYMKKLSNQS ACVFTGRGLS FGGSLIRPEA TGYGLIYFAQ AMLAEKGDSF AGKVVSVSGS GNVAQYAIEK ALSLGAKVVT CSDSSGYVYD PNGFTTEKLA ALFDIKNTKR GRVKDYAEQF GLQYFEGKRP WEVQVDIALP CATQNELELS DAQRLIKNGV KLVAEGANMP TTIEATEALL AADVLFGPGK AANAGGVATS GLEMAQSSQR LYWTAEEVDA QLHRIMLDIH ANCKKYGTIE GQENINYVVG ANVAGFVKVA DAMLAQGVY //