ID   G3JUB5_CORMM            Unreviewed;      1125 AA.
AC   G3JUB5;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=NAD-specific glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000184};
DE            EC=1.4.1.2 {ECO:0000256|PIRNR:PIRNR000184};
GN   ORFNames=CCM_09444 {ECO:0000313|EMBL:EGX87822.1};
OS   Cordyceps militaris (strain CM01) (Caterpillar fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Cordyceps.
OX   NCBI_TaxID=983644 {ECO:0000313|EMBL:EGX87822.1, ECO:0000313|Proteomes:UP000001610};
RN   [1] {ECO:0000313|EMBL:EGX87822.1, ECO:0000313|Proteomes:UP000001610}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CM01 {ECO:0000313|EMBL:EGX87822.1,
RC   ECO:0000313|Proteomes:UP000001610};
RX   PubMed=22112802; DOI=10.1186/gb-2011-12-11-r116;
RA   Zheng P., Xia Y., Xiao G., Xiong C., Hu X., Zhang S., Zheng H., Huang Y.,
RA   Zhou Y., Wang S., Zhao G.P., Liu X., St Leger R.J., Wang C.;
RT   "Genome sequence of the insect pathogenic fungus Cordyceps militaris, a
RT   valued traditional Chinese medicine.";
RL   Genome Biol. 12:RESEARCH116.1-RESEARCH116.21(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; JH126407; EGX87822.1; -; Genomic_DNA.
DR   RefSeq; XP_006674641.1; XM_006674578.1.
DR   AlphaFoldDB; G3JUB5; -.
DR   STRING; 983644.G3JUB5; -.
DR   GeneID; 18171447; -.
DR   KEGG; cmt:CCM_09444; -.
DR   VEuPathDB; FungiDB:CCM_09444; -.
DR   eggNOG; KOG2250; Eukaryota.
DR   HOGENOM; CLU_005220_0_0_1; -.
DR   InParanoid; G3JUB5; -.
DR   OMA; LYCLPQN; -.
DR   OrthoDB; 89313at2759; -.
DR   Proteomes; UP000001610; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001610}.
FT   DOMAIN          741..1006
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00839"
FT   REGION          76..100
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1125 AA;  126518 MW;  F2D2E49FF8F03967 CRC64;
     MASPFCSGLP SLCRSYLDLP LSRLSLVSSF PFPRRTSPPL GAASRMKLAS TAQSHNPYLP
     ATMPTSANKV LADIASQDSS RLPSPQPTHM SSHNSNGHRK LRSATVGYVA PEFTGKTEQM
     KTVHKLIHDN GWIPEALIDE QIRWFYEQLG IDDVYFRIET PDVIANQITS LYAAKVAANS
     REDKREEIRL DMEAEDHAIY IDTSEPGQSH VFGPRYEGRL EAKYLDHSER TKYRVETFRS
     PAVIGASPNS KATLRCYFVY KCDFKQSVED TDPKETNIEL ISDTGFWQKA TENTKQIYQE
     IIELAVARTG PVIEIFDIED SVEKRLVVAF RTRTARGMFS SLSDLYHYYG VTSSRKYVEQ
     FSNGISVMSI YLRPASTEGG YFPPMEESIH QITKEISLLY CLPQNKFHNL FATGELSLQE
     AVYAHSTWVF VQHFLNRLGP EYVSLSEIID HNDSAQAALL SKLKRRLRTE TFTPDYIYEI
     IQSYPELVRS LYASFANIHL SVGPDYDRAY LAPTPKVEVL SDEKLKDKIS KTVANEHDEM
     VMTAFRVFNN AILKTNYFTP TKVALSFRLD PSFLPMAEYP RRLYGMFLVI GAESRGFHLR
     FREISRGGIR IVKSRSKEAY GINVRNLFDE NYGLASTQQR KNKDIPEGGS KGVILLDPKQ
     QDRAQEAFEK YIDSILDLLL PAETPGIKNP VVDLYGKQEI LFMGPDENTA GLVDWATEHA
     RIRGAPWWKS FFTGKSQKLG GIPHDKYGMT TLSVREYVKG IYRKLNLDPS TVRKMQTGGP
     DGDLGSNEIL LGNEKWTAIV DGSGVLADPN GLDRDELVRL ATKRAMISEY DLSKVSKDGY
     RVLCEDTNVT LPNGEVISNG TSFRNTYHLR DTGMTDVFVP CGGRPESIDL ISVNRLIKDG
     KAVIPYIVEG ANLFITQDAK LRLEAAGCVL YKDASANKGG VTSSSLEVLA SLSFDDAGFV
     ENMCCDAKTG EPPQFYNDYV RSVQAKIQEN AALEFEAIWR EHEKTGEPRS ILSDKLSIAI
     TDLDEKLQKS DLWTNKEIRF GILKDALPKL LLDKIGLETI MQRVPESYLR SIFGSYLASR
     FVYEFGAEPS QFAFFDFMSK RMAAIGGDAN ANGTERLRRA SISQH
//