ID B0DSY6_LACBS Unreviewed; 1077 AA.
AC B0DSY6;
DT 26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=NAD-specific glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000184};
DE EC=1.4.1.2 {ECO:0000256|PIRNR:PIRNR000184};
GN ORFNames=LACBIDRAFT_309733 {ECO:0000313|EMBL:EDR02399.1};
OS Laccaria bicolor (strain S238N-H82 / ATCC MYA-4686) (Bicoloured deceiver)
OS (Laccaria laccata var. bicolor).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Hydnangiaceae; Laccaria.
OX NCBI_TaxID=486041 {ECO:0000313|Proteomes:UP000001194};
RN [1] {ECO:0000313|EMBL:EDR02399.1, ECO:0000313|Proteomes:UP000001194}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 / ATCC MYA-4686 {ECO:0000313|Proteomes:UP000001194};
RX PubMed=18322534; DOI=10.1038/nature06556;
RA Martin F., Aerts A., Ahren D., Brun A., Danchin E.G.J., Duchaussoy F.,
RA Gibon J., Kohler A., Lindquist E., Pereda V., Salamov A., Shapiro H.J.,
RA Wuyts J., Blaudez D., Buee M., Brokstein P., Canbaeck B., Cohen D.,
RA Courty P.E., Coutinho P.M., Delaruelle C., Detter J.C., Deveau A.,
RA DiFazio S., Duplessis S., Fraissinet-Tachet L., Lucic E., Frey-Klett P.,
RA Fourrey C., Feussner I., Gay G., Grimwood J., Hoegger P.J., Jain P.,
RA Kilaru S., Labbe J., Lin Y.C., Legue V., Le Tacon F., Marmeisse R.,
RA Melayah D., Montanini B., Muratet M., Nehls U., Niculita-Hirzel H.,
RA Oudot-Le Secq M.P., Peter M., Quesneville H., Rajashekar B., Reich M.,
RA Rouhier N., Schmutz J., Yin T., Chalot M., Henrissat B., Kuees U.,
RA Lucas S., Van de Peer Y., Podila G.K., Polle A., Pukkila P.J.,
RA Richardson P.M., Rouze P., Sanders I.R., Stajich J.E., Tunlid A.,
RA Tuskan G., Grigoriev I.V.;
RT "The genome of Laccaria bicolor provides insights into mycorrhizal
RT symbiosis.";
RL Nature 452:88-92(2008).
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; DS547131; EDR02399.1; -; Genomic_DNA.
DR RefSeq; XP_001887076.1; XM_001887041.1.
DR AlphaFoldDB; B0DSY6; -.
DR STRING; 486041.B0DSY6; -.
DR GeneID; 6082706; -.
DR KEGG; lbc:LACBIDRAFT_309733; -.
DR HOGENOM; CLU_005220_0_0_1; -.
DR InParanoid; B0DSY6; -.
DR OrthoDB; 89313at2759; -.
DR Proteomes; UP000001194; Unassembled WGS sequence.
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; 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.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|PIRNR:PIRNR000184};
KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR000184,
KW ECO:0000313|EMBL:EDR02399.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001194}.
FT DOMAIN 715..977
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
SQ SEQUENCE 1077 AA; 120044 MW; 2B4D98B0F4CBC57D CRC64;
MEHPIIAPNG NSKHGLYIRT PNFILSSHYP LKHSSFMSTP EPTVNTAQLP LNGAKKLTQA
LFGEGFTNGG ESHCAKASHG YTTPVFEGKK AQRASVEIDV ASKGFIPHNL IAGEVDWFYF
NLGIDDSYFQ KESSEIISDH IIALFGAKIV AYTKRDPTKF IIDLERIDDQ GKGGTFIHTS
APGLTSAEGP GASCEKRIDE LFLDKSTPTN AYRLETFRSA GSISATASQQ LRCYFVTKCN
FPKNPSILAG KTDIRSVSDS YFLEKATGAV LDIYQQILWK VESKLGPVIE VHDGEASREK
WLVIGYKMGS TSRFFSALSN LYHFYSLYSS RKYVEQFSNG VTIISLYLNP LPNTNAPPIE
NSIFQVMKEA SLLFCLPDNP YFLPKISGSH AVQEATYAYC GWIFAQHFCN RLGPAYLQLK
NVLNEDDPIH AEVLSDIKRR FREETFTPES IAQVIHAHPD LISLLYVNFA MTHYPPSDDA
SKLMPTLSYQ RLHTVQPLDD AQLYEKIRRT APNKHVLQVL GSFLVFNKHV LKTNFYQPTK
VALSFRLAPE FLPEVEYPKK PYGMFIVIGN EFRGFHIRFR DVARGGIRIV LSRNKDNYSV
NQRMLVDENY GLAATQSLKN KDIPEGGAKG TILPSLGASP RRCFEKYVDA MIDLLIPGVK
EPVVDLYGIP ELLFFGPDEG TADLMDWAAI HARSRGAETW WKSFTTGKSA ETLGGIPHDV
YGMTSLSIRQ FVLGLYKQLG LRERDITKVQ TGGPDGDLGS NEILLSSDKT VAVIDGSGVL
SDPVGIDREE LVRLAKLRVP VSHFNTAKLS KNGYLVKLED QDFKLPSGEV VPDGTDFRNT
AHLRFKADLF VPCGGRPEAV NISNMAALVD SEGKPHFKYI VEGANLFITQ QARLYLEKRK
VVLFKDSSAN KGGVTSSSLE VLAGLALSTQ EYLDLMVFKD GKPSEFYQNY VKDVQTKITE
NAADEFQCIW REHSRSQGTK SRTLISDELS LTLNNLQADL ESSALFDDLP SRKGVIGRAI
PKTLVDQVGL ETLLQRLPEP YQRALFSSWV ASHFIYKCGV KGSTVDFFHF ARDLANL
//
