ID E4ZWH2_LEPMJ Unreviewed; 1071 AA.
AC E4ZWH2;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=NAD-specific glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000184};
DE EC=1.4.1.2 {ECO:0000256|PIRNR:PIRNR000184};
GN ORFNames=LEMA_P031000.1 {ECO:0000313|EMBL:CBX95948.1};
OS Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS (Blackleg fungus) (Phoma lingam).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC Plenodomus; Plenodomus lingam/Leptosphaeria maculans species complex.
OX NCBI_TaxID=985895 {ECO:0000313|Proteomes:UP000002668};
RN [1] {ECO:0000313|Proteomes:UP000002668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8
RC {ECO:0000313|Proteomes:UP000002668};
RX PubMed=21326234; DOI=10.1038/ncomms1189;
RA Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT "Effector diversification within compartments of the Leptosphaeria maculans
RT genome affected by Repeat-Induced Point mutations.";
RL Nat. Commun. 2:202-202(2011).
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; FP929127; CBX95948.1; -; Genomic_DNA.
DR RefSeq; XP_003839427.1; XM_003839379.1.
DR AlphaFoldDB; E4ZWH2; -.
DR STRING; 985895.E4ZWH2; -.
DR EnsemblFungi; CBX95948; CBX95948; LEMA_P031000.1.
DR GeneID; 13281402; -.
DR eggNOG; KOG2250; Eukaryota.
DR HOGENOM; CLU_005220_0_0_1; -.
DR InParanoid; E4ZWH2; -.
DR OMA; LYCLPQN; -.
DR OrthoDB; 89313at2759; -.
DR Proteomes; UP000002668; Genome.
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 Reference proteome {ECO:0000313|Proteomes:UP000002668}.
FT DOMAIN 699..963
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1071 AA; 120461 MW; 22EB5600119D9A38 CRC64;
MASTPLNGAN GPQQPHHKQL EQVLNTPDRR PSPLPTHLST PASGSGHSTP RIIPQEGSGG
SGYVAPVFTG KEKQMEAVMD GVEEKGFMPP ELVESETKWF YNELGIDDMY FATETVDAIV
SHVHSLYAAK VAAYARDDKR LEIRLDKEAA DHAVYIDTSR PGVSVIAGPQ YEQRIGKKYL
AVSKPGLAYR VESFRSESPL PGSDDQQLRC YFVYQCDFVD PNPKETETDI EKIGDKRFLQ
KATDNTKAIY QQILKVAVER TGPVIEYFDI EGSRDKRLVV GFKRGSALGL FSALSDLYHY
YGLTTSRKYV EQFSNGYTCM SLYLRPLLGA AGAKHPPIEA SIHQITKEVS LLYCLPQNRF
QTLFATGRLS LQETIYAHCV WVFITHFLNR LGNEYTALAA ILDPENSAHA ELLSKLKRRL
RAETFTADYI SEIIFTYPEL VHTLYLPFAK THYVQTRGQA DDFLPTLSYL RLQVDRVQTD
SELTETINKA VANDHHVMVM NSFRIFNNSV LKTNFYTPTK VAVSFRLNPN FLPPSEYPQP
LYGMFLVIGS EFRGFHLRFR DIARGGIRIV KSRSQEAYSI NARSMFDENY NLANTQQRKN
KDIPEGGSKG VVLLDYKHQD KARGAFEKYI DSILDLLLPP SSPGIKDPIV DLHGKEEILF
MGPDENTADL VDWATEHARV RGAPWWKSFF TGKSPKLGGI PHDRYGMTTL SVREYVLGIY
RKLNLDPSKV RKLQTGGPDG DLGSNEILLS NEKYISIVDG SGVLVDPKGI NHEELLRLAK
SRKMIGEFDI SKLSPEGYRV LVDDSNVRLP NGDLVYNGTT FRNTFHLRSD IHYDTFVPCG
GRPESIDLTS ANKLIVDGKS VIPYIVEGAN LFITQDAKLK LEKAGCILYK DASANKGGVT
SSSLEVLASL SFDDESFIKH MCVGEDGQAP EFYNAYVREV QKTIQNNARL EFEAIWREHQ
NTGQPRSILS DVLSNAITKL DEELQNTDLW KDIEFRKSVL KEALPNILLQ QIGLEKIMER
VPDNYLRAIF GSYLASRFVY EYGVSTSQFA FFDFMSRRKN SGSNGATNNA K
//
