ID DHE4_GORGO Reviewed; 558 AA. AC Q64I01; DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2004, sequence version 1. DT 25-NOV-2008, entry version 31. DE RecName: Full=Glutamate dehydrogenase 2, mitochondrial; DE Short=GDH; DE EC=1.4.1.3; DE Flags: Precursor; GN Name=GLUD2; OS Gorilla gorilla gorilla (Lowland gorilla). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Gorilla. OX NCBI_TaxID=9595; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=15378063; DOI=10.1038/ng1431; RA Burki F., Kaessmann H.; RT "Birth and adaptive evolution of a hominoid gene that supports high RT neurotransmitter flux."; RL Nat. Genet. 36:1061-1063(2004). CC -!- FUNCTION: Important for recycling the chief excitatory CC neurotransmitter, glutamate, during neurotransmission. CC -!- CATALYTIC ACTIVITY: L-glutamate + H(2)O + NAD(P)(+) = 2- CC oxoglutarate + NH(3) + NAD(P)H. CC -!- SUBUNIT: Homohexamer (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix (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; AY588267; AAU03133.1; -; Genomic_DNA. DR SMR; Q64I01; 58-558. DR HOVERGEN; Q64I01; -. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. 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_DHase. DR InterPro; IPR006096; Glu/Leu/Phe/Val_DHase_C. DR InterPro; IPR006097; Glu/Leu/Phe/Val_DHase_dimer. 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 PRINTS; PR00082; GLFDHDRGNASE. DR PROSITE; PS00074; GLFV_DEHYDROGENASE; 1. PE 3: Inferred from homology; KW Mitochondrion; NADP; Oxidoreductase; Transit peptide. FT TRANSIT 1 53 Mitochondrion (By similarity). FT CHAIN 54 558 Glutamate dehydrogenase 2, mitochondrial. FT /FTId=PRO_0000007207. FT ACT_SITE 183 183 By similarity. FT BINDING 84 84 Substrate (By similarity). SQ SEQUENCE 558 AA; 61559 MW; 1D63DDA43335A95A CRC64; MYRYLAKALL PSRAGTAALG SAANHSAALL GRSRGQPAAA SQPGLALAAR RHYSELVADR EDDPNFFKMV EGFFDRGASI VEDKLVKDLR TQESEEQKRN RVRGILRIIK PCNHVLSLCF PIRRDDGSWE VIEGYRAQHS QHRTPCKGGI RYSTDVSVDE VKALASLMTY KCAVVDVPFG GAKAGVKINP KNYTENELEK ITRRFTMELA KKGFIGPGVD VPAPDMNTGE REMSWIADTY ASTIGHYDIN AHACVTGKPI SQGGIHGRIS ATGRGVFHGI ENFINEASYM SILGMTPGFR DKTFVVQGFG NVGLHSMRYL HRFGAKCIAV GESDGSIWNP DGIDPKELED FRLQHGSILG FPKAKPYEGS ILEVDCDILI PAATEKQLTK SNAPRVKAKI IAEGANGPTT PEADRIFQER NILVIPDLYL NAGGVTVSYF EWLKNLNHVS YGRLTFKYER DSNYHLLMSV QESLERKFGK HGGTIPIVPT ADFQDSISGA SEKDIVHSAL AYTMERSARQ IMHTAMKYNL GLDLRTAAYV NAIEKVFKVY SEAGVTFT //