ID G7DWZ6_MIXOS Unreviewed; 1034 AA.
AC G7DWZ6;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=NAD-specific glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000184};
DE EC=1.4.1.2 {ECO:0000256|PIRNR:PIRNR000184};
GN Name=Mo01748 {ECO:0000313|EMBL:GAA95093.1};
GN ORFNames=E5Q_01748 {ECO:0000313|EMBL:GAA95093.1};
OS Mixia osmundae (strain CBS 9802 / IAM 14324 / JCM 22182 / KY 12970).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina; Mixiomycetes;
OC Mixiales; Mixiaceae; Mixia.
OX NCBI_TaxID=764103 {ECO:0000313|EMBL:GAA95093.1, ECO:0000313|Proteomes:UP000009131};
RN [1] {ECO:0000313|Proteomes:UP000009131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 9802 / IAM 14324 / JCM 22182 / KY 12970
RC {ECO:0000313|Proteomes:UP000009131};
RX PubMed=21478649; DOI=10.2323/jgam.57.63;
RA Nishida H., Nagatsuka Y., Sugiyama J.;
RT "Draft genome sequencing of the enigmatic basidiomycete Mixia osmundae.";
RL J. Gen. Appl. Microbiol. 57:63-67(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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAA95093.1}.
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DR EMBL; BABT02000054; GAA95093.1; -; Genomic_DNA.
DR RefSeq; XP_014566667.1; XM_014711181.1.
DR AlphaFoldDB; G7DWZ6; -.
DR STRING; 764103.G7DWZ6; -.
DR GeneID; 26265277; -.
DR eggNOG; KOG2250; Eukaryota.
DR HOGENOM; CLU_005220_0_0_1; -.
DR InParanoid; G7DWZ6; -.
DR OMA; LYCLPQN; -.
DR OrthoDB; 89313at2759; -.
DR Proteomes; UP000009131; 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:UP000009131}.
FT DOMAIN 671..934
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
SQ SEQUENCE 1034 AA; 115846 MW; 8F1235254F52B6EA CRC64;
MSTSATASAS MNGMPAMTIK PSLSPGLNHL SVPGTPHRVV SNSSGYHQSV FKAADKKLQA
TRVEELVREK GFIPEALVHS EVSWYTQDLG IDDAYFKTES VETIASHIIS LYGSKILAYA
RGDGTLDINL EKIHDDGAVF IHTSNPGVSD PHGPLIEQRI DEKYLDVSTP KEAYRLETYR
SAGHVSSSIS QQLRCYFLAR CNFVEPNPDA EETDITKLGD RAFLETVSEN TLEIYQEVML
ATLERTGPVV EAFDVENSQE KRLVIGYRMG STSHFFSAIS DLYHWYGIYS SRKYVEHFSN
GVSIVSLYLN PLRGPPINQA ILQITREISL IFCLPSNPFF VAGSGHAVQE SSYAYAAAVF
CQHFLNRLGP SFLNLKNQLD ENDPTQANIL ADIRKRLREQ TFTRQSIRDS IEAYPELVRL
LYVNFAMTHY ISGRSQLMPT LSYQRIQTNA ALNDEELYTR IKKTTQNAHD FEVFESMLSF
NKSILKTNFY QPTKVSLSFR LDPAFLPEAE YPTRPYGLIL VVGPDFRGFH VRFSDVARGG
IRIIRSRDRE TFSVNQRNLF DENYALALTQ HLKNKDIPEG GSKGTILPDL GADPRAVFEK
YIDSILDLLI PGNSPGVKEQ IVDLYQKEEI LFFGPDENTA GFMDWACLHA RERGYGTWKS
ITTGKSSLLG GVAHDIFGMT SLSVRQYVIG IYQQLGLREE EITKMQTGGP DGDLGSNEIL
LSKDKTIAII DGSGVLHDPS GLNREELTRL AKERKMVTHF DRSLLSSEGY LVLVEDQDFT
LPSGEIVNDG TSFRNSAHLR YKADIFVPCG GRPESINMGN IKQLFDADGK PNFKYVVEGA
NLFISPQARL ALEKRGVVVF KDASANKGGV TSSSLEVLSG LGLDDQEFLE LMTNNGHEGF
SEFYRNYVQE IQKIISYNAA QEFNCIWKDH AISKKPRPNI TDELSRAIVQ LQADLEQSNL
WDDLGVRRAV ISRAVPKTLL KQVGLDKLIS RLPPTYLRSL FADFVASHYV YEYGLQSSLV
AFYSFVSKFK EAQA
//
