ID B2WN29_PYRTR Unreviewed; 1068 AA.
AC B2WN29;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=NAD-specific glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000184};
DE EC=1.4.1.2 {ECO:0000256|PIRNR:PIRNR000184};
GN ORFNames=PTRG_11478 {ECO:0000313|EMBL:EDU44528.1};
OS Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS (Drechslera tritici-repentis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=426418 {ECO:0000313|EMBL:EDU44528.1, ECO:0000313|Proteomes:UP000001471};
RN [1] {ECO:0000313|Proteomes:UP000001471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pt-1C-BFP {ECO:0000313|Proteomes:UP000001471};
RX PubMed=23316438; DOI=10.1534/g3.112.004044;
RA Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT repentis, reveals transduplication and the impact of repeat elements on
RT pathogenicity and population divergence.";
RL G3 (Bethesda) 3:41-63(2013).
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; DS231631; EDU44528.1; -; Genomic_DNA.
DR RefSeq; XP_001941809.1; XM_001941774.1.
DR AlphaFoldDB; B2WN29; -.
DR STRING; 426418.B2WN29; -.
DR EnsemblFungi; EDU44528; EDU44528; PTRG_11478.
DR GeneID; 6349794; -.
DR eggNOG; KOG2250; Eukaryota.
DR HOGENOM; CLU_005220_0_0_1; -.
DR InParanoid; B2WN29; -.
DR OMA; LYCLPQN; -.
DR OrthoDB; 89313at2759; -.
DR Proteomes; UP000001471; 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 Reference proteome {ECO:0000313|Proteomes:UP000001471}.
FT DOMAIN 695..959
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1068 AA; 120184 MW; 383A07D2B3A52DAC CRC64;
MASTPIDAAN GQPQNKQLDQ VVNQPDRRPS PLPTHLSLPG SGYSTPRTIP QEGSGGSGYV
APVFEGKEKQ MEAVMDGVEE KGFMPPELVE SETKWFYNEL GIDDMYFATE TVEAIISHIH
SLYAAKVAAY ARDDKRLEIR LEKEAADHAV YIDTSRPGVS VIDGPQYEQR LGKRYLAVSK
PGLAYRVESF RSESPLPGSE DQQLRCYFVY QCDFVEPNPS ETETDIEKIG DKRFLQKATA
NTKVIYQQIL QVAAERTGPV IDHFDIEGSR DKRLVVGFKR GSALGLFSAL SDLYHYYGLT
TSRKYVEQFS NGYTVMSLYL RPLPGAAGAK HPPIEASIHQ ITKEVSLLYC LPQNKFQTLF
ATSRLSLQET IYAHCVWVFI THFLNRLGSE YTALSAILDT ENSVHAELLS KLKRRLRAET
FTADYIYEII MTYPELVHTL YLPFAKTHYV QTRGQEDDFL PTLSYLRLQV DKVQTDKELT
DTINKAVVND HHEMVMTSFR VFNSSVLKTN FYTPTKVAIS FRMNPNFLPS SEYPQPLYGM
FLVIGSEFRG FHLRFRDIAR GGIRIVKSRS QEAYSINARS MFDENYNLAN TQQRKNKDIP
EGGSKGVVLL DFKHQDKARG AFEKYIDSIL DLLLPPTSPG IKDPIVDLHG KEEILFMGPD
ENTADLVDWA TEHARIRGAP WWKSFFTGKS PKLGGIPHDR YGMTTLSVRE YVLGIYRKLN
LDPSKVRKLQ TGGPDGDLGS NEILLSNEKY VAIIDGSGVL VDHKGINHPE LIRLAKGRKM
INEFDISKLS SEGYRVLVDD TNVRLPNGDL VYNGTTFRNT FHLRSDMHYD TFVPCGGRPE
SIDLSTASKL IVDGKSVIPY IVEGANLFIT QDAKLRLEKA GCILYKDASA NKGGVTSSSL
EVLASLSFDD ESFIKHMCVG EDGQAPEFYN NYVREVQKTI QNNARLEFEA IWREHQATGQ
PRSTLSDTLS TAITKLDEEL QNTDLWKNVE FRKSVLKEAL PNILLEKIGL DKIIERVPDN
YLRAIFGSYL ASRFVYEHGV SASQFAFFDF MSKRMQKGAA SAAAAAAH
//
