ID DHE3_MAIZE Reviewed; 411 AA. AC Q43260; O04871; O04872; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 16-JUN-2009, entry version 56. DE RecName: Full=Glutamate dehydrogenase; DE Short=GDH; DE EC=1.4.1.3; GN Name=GDH1; OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Golden cross Bantam T51; TISSUE=Root; RX MEDLINE=96012931; PubMed=7551585; RA Sakakibara H., Fujii K., Sugiyama T.; RT "Isolation and characterization of a cDNA that encodes maize glutamate RT dehydrogenase."; RL Plant Cell Physiol. 36:789-797(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND MUTANT GDH1. RC STRAIN=cv. P-10 Inbred; TISSUE=Shoot; RA Ju G.C.; RT "Characterization of a GDH1-mutant in maize."; RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: L-glutamate + H(2)O + NAD(P)(+) = 2- CC oxoglutarate + NH(3) + NAD(P)H. 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; D49475; BAA08445.1; -; mRNA. DR EMBL; U93560; AAB51595.1; -; mRNA. DR EMBL; U93561; AAB51596.1; -; mRNA. DR PIR; T03294; T03294. DR PIR; T04342; T04342. DR RefSeq; NP_001105301.1; -. DR UniGene; Zm.44; -. DR HSSP; P96110; 1B26. DR GeneID; 542220; -. DR Gramene; Q43260; -. DR MaizeGDB; 12238; -. DR BRENDA; 1.4.1.3; 289. DR GO; GO:0005488; F:binding; IEA:InterPro. DR GO; GO:0004353; F:glutamate dehydrogenase [NAD(P)+] 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 NAD; Oxidoreductase. FT CHAIN 1 411 Glutamate dehydrogenase. FT /FTId=PRO_0000182749. FT ACT_SITE 102 102 By similarity. FT VARIANT 18 18 L -> V (in strain: cv. P-10 Inbred). FT VARIANT 370 370 I -> M (in strain: cv. P-10 Inbred). FT VARIANT 376 376 N -> D (in strain: cv. P-10 Inbred). FT MUTAGEN 188 188 G->R: In GDH1. FT MUTAGEN 246 246 D->G: In GDH1. FT MUTAGEN 252 253 QL->EV: In GDH1. FT MUTAGEN 367 367 R->Q: In GDH1. SQ SEQUENCE 411 AA; 44022 MW; 648C67A9338922CF CRC64; MNALAATSRN FKQAAKLLGL DSKLEKSLLI PFREIKVECT IPKDDGTLAS YVGFRVQHDN ARGPMKGGIR YHHEVDPDEV NALAQLMTWK TAVANIPYGG AKGGIGCSPG DLSISELERL TRVFTQKIHD LIGIHTDVPA PDMGTNSQTM AWILDEYSKF HGYSPAVVTG KPVDLGGSLG RDAATGRGVL FATEALLAEH GKGIAGQRFV IQGFGNVGSW AAQLISEAGG KVIAISDVTG AVKNVDGLDI AQLVKHSAEN KGIKGFKGGD AIAPDSLLTE ECDVLIPAAL GGVINKDNAN DIKAKYIIEA ANHPTDPEAD EILSKKGVLI LPDILANSGG VTVSYFEWVQ NIQGFMWDEE KVNAELRTYI TRAFGNVKQM CRSHSCDLRM GAFTLGVNRV ARATVLRGWE A //