ID X0ID59_FUSOX Unreviewed; 1078 AA.
AC X0ID59;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=NAD-specific glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000184};
DE EC=1.4.1.2 {ECO:0000256|PIRNR:PIRNR000184};
GN ORFNames=FOPG_05138 {ECO:0000313|EMBL:EXL81825.1};
OS Fusarium oxysporum f. sp. conglutinans race 2 54008.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1089457 {ECO:0000313|EMBL:EXL81825.1};
RN [1] {ECO:0000313|EMBL:EXL81825.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=54008 {ECO:0000313|EMBL:EXL81825.1};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum PHW808.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EXL81825.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=54008 {ECO:0000313|EMBL:EXL81825.1};
RG The Broad Institute Genomics Platform;
RA Ma L.-J., Corby-Kistler H., Broz K., Gale L.R., Jonkers W., O'Donnell K.,
RA Ploetz R., Steinberg C., Schwartz D.C., VanEtten H., Zhou S., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Annotation of Fusarium oxysporum PHW808.";
RL Submitted (MAY-2012) 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; JH658822; EXL81825.1; -; Genomic_DNA.
DR AlphaFoldDB; X0ID59; -.
DR Proteomes; UP000030676; 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; 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 713..977
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1078 AA; 120981 MW; EFD79547F5A72871 CRC64;
MAPITESPTN MLPSQTFPDY TDPYQKSNMT AISANPVANV KATEASRGPS PQPTHFSVPL
QNGNGGNGHR ILRSATVGYI APEFTGKPEQ KKTVKSIISA AGFVPEPQID EQIEWFYEKL
GIDDVYFELE TPDVISSHIT SLYAAKVASF AREDKQEEIR LDMEANDHAI YIDTSVAGKT
NTAGPRYEER LEAKYIDHPG HSKYRVETFR SPAVVSPSSK ATLRCYFVYQ CQFATPPEQT
DPKETNLELI ADNGFLRKAT DNTKQIYQDI IELAVNRAGP VIEVFDIENT DEKRMVVAFR
SRTAQGLFSA LSDLYHYYGV TSSRKYLEQF SNGITVMSVY LRPTSDTVES SGQFPSIEES
IDQISKEVSL LYCLPHNKFH NLFLDGQLSL QESVYAHSAW VFVQHFLNRL GPEYSTLAEL
LDVKNNAQQA LLSNLKRRLR SETFTPEYIY EIIQNYPGLV RALYASFANI HLVKDQEDPV
KVVSSSLSVE VLSDDALKDK ISKNVNNEHD EMVLTAFRVF NNAILKTNYF TPTKVALSFR
LDPSFLPEVE YPKPLYGMFL VISSESRGFH LRFKDISRGG IRIVKSRNKE AYGINARSIF
DENYGLASTQ QRKNKDIPEG GSKGVILLDP KQQNRAREAF EKYIDSILDL LLPAETPGIK
NPVVDLYGKE EIIFMGPDEN TAELVDWATE HARSRGAPWW KSFFTGKSPK LGGIPHDTYG
MTTLSVREYV KGIYRKLELD PSTIRKMQTG GPDGDLGSNE IKLGNEKYTA IVDGSGVLAD
PNGLDRDELL RLANGRKMII EYDVSKLSPE GYRVLCDDVN ITLPNGEVIN NGTSFRNTFH
LRDTGSVDCF VPCGGRPASI DLISVNRLIK DGKCIIPYLV EGANLFITQE AKLRLEAAGC
ILYKDASANK GGVTSSSLEV LASLSFDDEG FVENMCHNAQ GEAPQFYKDY VKQVQLKIQE
NARLEFEAIW REHEQTGTPR SILSDKLSVA ITDLDEKLQH SDLWDNEKIR RSVLQDALPR
LLLEKIGLDT LIARIPDSYL RSIFGSYLAS RFVYEFGSSP SQFAFYDFMS KRMAQIAN
//
