ID DHE2_ACHKL Reviewed; 1063 AA. AC P41755; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 02-SEP-2026, entry version 55. DE RecName: Full=NAD-specific glutamate dehydrogenase; DE Short=NAD-GDH; DE EC=1.4.1.2; OS Achlya klebsiana. OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniomycetes; OC Saprolegniales; Achlyaceae; Achlya. OX NCBI_TaxID=4767; RN [1] RP NUCLEOTIDE SEQUENCE. RX PubMed=8308022; DOI=10.1016/s0021-9258(17)41809-6; RA Lejohn H.B., Cameron L.E., Yang B., Rennie S.L.; RT "Molecular characterization of an NAD-specific glutamate dehydrogenase gene RT inducible by L-glutamine. Antisense gene pair arrangement with L-glutamine- RT inducible heat shock 70-like protein gene."; RL J. Biol. Chem. 269:4523-4531(1994). CC -!- CATALYTIC ACTIVITY: CC Reaction=L-glutamate + NAD(+) + H2O = 2-oxoglutarate + NH4(+) + NADH + CC H(+); Xref=Rhea:RHEA:15133, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16810, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.4.1.2; CC -!- ACTIVITY REGULATION: Allosterically activated by NADP(+). CC -!- SUBUNIT: Homotetramer. CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family. CC Highly divergent. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U02505; AAA17563.1; -; Unassigned_DNA. DR PIR; A53164; A53164. DR AlphaFoldDB; P41755; -. DR GO; GO:0004352; F:L-glutamate dehydrogenase (NAD+) activity; IEA:UniProtKB-EC. DR InterPro; IPR019651; Glutamate_DH_NAD-spec. DR Pfam; PF10712; NAD-GH; 1. PE 3: Inferred from homology; KW Allosteric enzyme; NAD; Oxidoreductase. FT CHAIN 1..1063 FT /note="NAD-specific glutamate dehydrogenase" FT /id="PRO_0000182731" SQ SEQUENCE 1063 AA; 118741 MW; 4EAC1E2C36674860 CRC64; MLLCIVLFLI FHILINQAGI VHVLYNASFV ASSSRFILFC EELFKATPQY WQWGNSIVQN GDASIASTLY LTMRTFIKHW KYTLLIMINQ SISYSCYSTN EASHLLFTNL PKVAPYTLGP LNFECCLLSS HHIRHIVLMF YGANIDHGLT KYELYTVCRP SSDEKLCNKI LNSPRLHTHN RYLYLTEVRI VGAFYLIKQV GARMVGLLVH LAFMVLQNLP KLIWPLDLVH VRQKGTCTAH IAYHPLAQKH FPPYFTHFYL NVTIYAVVKN ILDNISSSFT LQSNRVRPRP DVAGFDFFHR FDAFEQSLTY GGDTGITSSN EKVALCFEAT YTDIFFTVEI IDSTSVDSGA IMLPILVDAY TAVARNFCSV SMVISPLVTL VVYDIYTCSF IGLCTQRRTI NCTRILDAIS SVGNSHTFLP RYKSPRELTT RQPSGSSVIL LIFLLLGFEF FLFSGLVVVE PVNDVGDLVV NDLLVAFIDL ALELFVVEGV AEVVGVVFKT VLGFNADVVG FIFRLVLFSF LHHAFNIILG EATLVVGNGN LVFFTSRLFD GRHVQDTVGI NVEGDINLWN TTRHWRNTIE GELPEQVVVT GHRTLTFKHL NQHTRLVVSV GGESLRLLGW HSSVTLDEGS HDTTSSFQTK RERSDIKKQQ VLELFRRVVT AQNGSLDCGT ESNSFIRVDR LAWFLAVEEV RKQLLDLWDT GGTTDKDDFM DLALGELRVT EDLFNRFHSL AEVVTAHVFE TGTGDGGVEI NTIEERVDFN VSLGRRRKST LGTFTSGTKT AKGTLVLGHI LAVLALEFSG KVVDEAVIEI FTTQVGITSS SLDFEDTFFN GQKRHIEGTT TKIENENIAF TTLLVKTVGN GGTSRFVNDT KDVKTSNGTS ILGSLTLRVV EISWDGNDSV VNSSTNEGFS NFLHLDQNHR GNFFRLESLS FTLEFDGDLW LVTSTRGNLE WPVLNIGLSS WVVEFTTDQT LSIEHSVGRV HGNLVLSGIT NKTFAVSESN VRWGGTVTLI VGNNFNTIVL PDTDTRISRT EIDTDGSSLD TRHACSKFKN EVDSPPHLTS AFI //