ID W7MU24_GIBM7 Unreviewed; 1050 AA.
AC W7MU24;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=NAD-specific glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000184};
DE EC=1.4.1.2 {ECO:0000256|PIRNR:PIRNR000184};
GN ORFNames=FVEG_10303 {ECO:0000313|EMBL:EWG51269.1};
OS Gibberella moniliformis (strain M3125 / FGSC 7600) (Maize ear and stalk rot
OS fungus) (Fusarium verticillioides).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=334819 {ECO:0000313|EMBL:EWG51269.1, ECO:0000313|Proteomes:UP000009096};
RN [1] {ECO:0000313|EMBL:EWG51269.1, ECO:0000313|Proteomes:UP000009096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M3125 / FGSC 7600 {ECO:0000313|Proteomes:UP000009096};
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.B., Woloshuk C., Xie X., Xu J.R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M.,
RA Park G., Park J., Park S.Y., Proctor R.H., Regev A., Ruiz-Roldan M.C.,
RA Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G.,
RA Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A.,
RA Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
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; DS022255; EWG51269.1; -; Genomic_DNA.
DR RefSeq; XP_018757460.1; XM_018899400.1.
DR AlphaFoldDB; W7MU24; -.
DR EnsemblFungi; FVEG_10303T0; FVEG_10303T0; FVEG_10303.
DR GeneID; 30067900; -.
DR VEuPathDB; FungiDB:FVEG_10303; -.
DR HOGENOM; CLU_005220_0_0_1; -.
DR OMA; LYCLPQN; -.
DR OrthoDB; 89313at2759; -.
DR Proteomes; UP000009096; Chromosome 9.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000009096}.
FT DOMAIN 685..949
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT REGION 16..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1050 AA; 117673 MW; 2C7B6EB0652DA417 CRC64;
MTAISANPVA NVKAVEASRG PSPQPTHFSV PLQNGNGGNG HRILRSATVG YIAPEFTGKP
EQKKTVKSII SAAGFVPEPQ IDEQIEWFYE KLGIDDVYFE LETPDVISSH ITSLYAAKVA
SFAREDKQEE IRLDMEANDH AIYIDTSVAG KTNTAGPRYE ERLEAKYIDH PGSSKYRVET
FRSPAVVSPS SKATLRCYFV YQCQFATPPE HTDPKETNLE LIADNGFLRK ATDNTKQIYQ
DIIELAVNRA GPVIEVFDIE NTDEKRMVVA FRARTAQGLF SALSDLYHYY GVTSSRKYLE
QFSNGITVMS VYLRPASDAV ESSGQFPSLE ESIDQISKEV SLLYCLPHNK FHNLFLDGQL
SLQESVYAHS AWVFVQHFLN RLGPEYSTLA ELLDVKNNAQ QALLSNLKRR LRSETFTPEY
IYEIIQNYPG LVRALYASFA NIHLVKDQED PVKVVSSSLS VEVLSDDALK DKIAKNVNNE
HDEMVLTAFR VFNNAILKTN YFTPTKVALS FRLDPSFLPE VEYPKPLYGM FLVISSESRG
FHLRFKDISR GGIRIVKSRN KEAYGINARS IFDENYGLAS TQQRKNKDIP EGGSKGVILL
DPKQQNRARE AFEKYIDSIL DLLLPAETPG IKNPIVDLYG KEEIIFMGPD ENTAELVDWA
TEHARSRGAP WWKSFFTGKS PKLGGIPHDT YGMTTLSVRE YVKGIYRKLE LDPSAIRKMQ
TGGPDGDLGS NEIKLGNEKY TAIVDGSGVL ADPNGLDRDE LLRLANGRKM IIEYDVSKLS
PEGYRVLCDD VNITLPNGEV INNGTSFRNT FHLRDTGSVD CFVPCGGRPA SIDLISVNRL
IKDGKCIIPY LVEGANLFIT QEAKLRLEAA GCILYKDASA NKGGVTSSSL EVLASLSFDD
EGFVENMCHN AQGEAPQFYQ DYVKQVQLKI QENARLEFEA IWREHEQTGT PRSILSDKLS
VAITDLDEKL QHSDLWDNEK IRRSVLQDAL PRLLLEKIGL DTLIARIPDS YLRSIFGSYL
ASRFVYEFGS SPSQFAFYDF MSKRMAQIAN
//
