ID A0A1G4KLB3_9SACH Unreviewed; 1059 AA.
AC A0A1G4KLB3;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=NAD-specific glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000184};
DE EC=1.4.1.2 {ECO:0000256|PIRNR:PIRNR000184};
GN ORFNames=LANO_0H03906G {ECO:0000313|EMBL:SCV05275.1};
OS Lachancea nothofagi CBS 11611.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=1266666 {ECO:0000313|EMBL:SCV05275.1};
RN [1] {ECO:0000313|EMBL:SCV05275.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Ploux O.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: NAD(+)-dependent glutamate dehydrogenase which degrades
CC glutamate to ammonia and alpha-ketoglutarate.
CC {ECO:0000256|PIRNR:PIRNR000184}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamate + NAD(+) = 2-oxoglutarate + H(+) + NADH +
CC NH4(+); 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 Evidence={ECO:0000256|PIRNR:PIRNR000184};
CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC {ECO:0000256|ARBA:ARBA00006382, ECO:0000256|PIRNR:PIRNR000184}.
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DR EMBL; LT598447; SCV05275.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4KLB3; -.
DR OrthoDB; 89313at2759; -.
DR Proteomes; UP000189911; Chromosome h.
DR GO; GO:0004352; F:glutamate dehydrogenase (NAD+) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019551; P:glutamate catabolic process to 2-oxoglutarate; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR InterPro; IPR006096; Glu/Leu/Phe/Val/Trp_DH_C.
DR InterPro; IPR033524; Glu/Leu/Phe/Val_DH_AS.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR016210; NAD-GDH_euk.
DR PANTHER; PTHR11606; GLUTAMATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11606:SF42; NAD-SPECIFIC GLUTAMATE DEHYDROGENASE; 1.
DR Pfam; PF00208; ELFV_dehydrog; 1.
DR PIRSF; PIRSF000184; GDH_NAD; 1.
DR SMART; SM00839; ELFV_dehydrog; 1.
DR SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00074; GLFV_DEHYDROGENASE; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|PIRNR:PIRNR000184};
KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR000184}.
FT DOMAIN 682..953
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
SQ SEQUENCE 1059 AA; 119128 MW; D352F16F50A2FD2D CRC64;
MLSVNKSQLP DISSLSISSM SDYHNFDFPG KDAQREAVLD LIDQQGFIPD DVVEHEVEWL
YDALGIDDLF FSKESPEMIA NIIHTLYAAK IESFARINIA GDTSDESATP LAAAEAAVAA
AAVTEAKPTG FSVKTQVVTD GHSVFMETGH ELDEQIDSML LDSPDHRYRL ISYTAENALK
LTFVYRTAFA QGSPAYPTLT SEQLSNGDID SISDVTMSQV TSNENKRLYG LIMDQMRQRE
GPIIKTMHSV ADQDEVRIVI GFKRGTTKSY YTALSSLLQY YDLKPSKIYL ETFANDVMIY
SLYLKQSQQT EKVLNSLPMS ILQIEREASL LYAIPSNFFQ DLYQQKSFSP QEAIYAHIGS
IFINNFINRL GEEYQDLIGQ VNTSFSSNNN SMLEVLASLK KKLRNETYTQ QMIIEVLHKY
KDIVSKLYKN FAQVHYVSSM STKFGKTLSY QRLSKLEPFE DDNEFEQYVN KFIPNDSPDM
LILQTLATFN KAILKTNFFM TRKVAISFRL DPALIMPKVE FPETPFGIFF VVGNTFKAFH
IRFRDIARGG IRIVCSKTQD IYEVNSRMAI DENYQLASTQ QRKNKDIPEG GSKGVILLNP
TLTTQQQTFV AFSQYVDAII DILIQDPLKE KYVDLLKQEE ILFFGPDEGT AGFVNWATSH
AKSRGCPWWK SFLTGKSPTM GGIPHDVYGM TSLSVRAFVN ALYETLGLQE TTINKFQTGG
PDGDLGSNEI LLSSVNERYI GLVDGSGVLC DPKGLDQDEL RRLAVERKMS SFYNKSKLSN
EGFFVSVDEI EVQLPNGVTV ANGTTFRNKF HLEIFKFVDK VDLFVPCGGR PNSIDINVLK
YFVDEKTNKC KIPYIVEGAN LFITQPAKIA LENLGCVLFK DASTNKGGVT SSSMEVLASL
ALNDHDFIHE FVAKESNKTT ALYDNYVQII QDRVVKNARA EFAQLWQLNQ ATGTPISELS
NVLSQTINKL NDELIISNEL WANDLELRNY LLLKKIIPKL LIDVAGPSNI LENIPESYLK
ALLSSYLSST YVYTYGIDVN IGKFLEYVGE LKREAKGFN
//
