ID M2RLB9_CERS8 Unreviewed; 1069 AA.
AC M2RLB9;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=NAD-specific glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000184};
DE EC=1.4.1.2 {ECO:0000256|PIRNR:PIRNR000184};
GN ORFNames=CERSUDRAFT_111938 {ECO:0000313|EMBL:EMD39631.1};
OS Ceriporiopsis subvermispora (strain B) (White-rot fungus) (Gelatoporia
OS subvermispora).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Gelatoporiaceae; Gelatoporia.
OX NCBI_TaxID=914234 {ECO:0000313|EMBL:EMD39631.1, ECO:0000313|Proteomes:UP000016930};
RN [1] {ECO:0000313|EMBL:EMD39631.1, ECO:0000313|Proteomes:UP000016930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B {ECO:0000313|EMBL:EMD39631.1,
RC ECO:0000313|Proteomes:UP000016930};
RX PubMed=22434909; DOI=10.1073/pnas.1119912109;
RA Fernandez-Fueyo E., Ruiz-Duenas F.J., Ferreira P., Floudas D.,
RA Hibbett D.S., Canessa P., Larrondo L.F., James T.Y., Seelenfreund D.,
RA Lobos S., Polanco R., Tello M., Honda Y., Watanabe T., Watanabe T.,
RA Ryu J.S., Kubicek C.P., Schmoll M., Gaskell J., Hammel K.E., St John F.J.,
RA Vanden Wymelenberg A., Sabat G., Splinter BonDurant S., Syed K.,
RA Yadav J.S., Doddapaneni H., Subramanian V., Lavin J.L., Oguiza J.A.,
RA Perez G., Pisabarro A.G., Ramirez L., Santoyo F., Master E., Coutinho P.M.,
RA Henrissat B., Lombard V., Magnuson J.K., Kuees U., Hori C., Igarashi K.,
RA Samejima M., Held B.W., Barry K.W., LaButti K.M., Lapidus A.,
RA Lindquist E.A., Lucas S.M., Riley R., Salamov A.A., Hoffmeister D.,
RA Schwenk D., Hadar Y., Yarden O., de Vries R.P., Wiebenga A., Stenlid J.,
RA Eastwood D., Grigoriev I.V., Berka R.M., Blanchette R.A., Kersten P.,
RA Martinez A.T., Vicuna R., Cullen D.;
RT "Comparative genomics of Ceriporiopsis subvermispora and Phanerochaete
RT chrysosporium provide insight into selective ligninolysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:5458-5463(2012).
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; KB445793; EMD39631.1; -; Genomic_DNA.
DR AlphaFoldDB; M2RLB9; -.
DR STRING; 914234.M2RLB9; -.
DR HOGENOM; CLU_005220_0_0_1; -.
DR OrthoDB; 89313at2759; -.
DR Proteomes; UP000016930; 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:UP000016930}.
FT DOMAIN 692..970
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1069 AA; 119718 MW; 69B4BED18874DDEF CRC64;
MSTPASSTPN SGASTPAFLA DPSKQHLHVP GLQPSSSEQS VHKIKNVPGY TTPVFKEKEE
QRAKVQSTVA AKGFIPRELV ANEVNWFYGH LGIDDTYFAN ESVEVISDHI IALFGAKVLA
YTKHDPSKLV IDLENIDPNG KGATFIHTSP PGLTITEGPG STCEARIDEL YLDKSTPTNA
YRLETYRSQG SISATASQQL RCYFVDKCNF PQNPPPSTRT DGKTDIRTVS DPVFLEKASE
NTLEIYQRVM WHVETRYGPV IEVFEVEGSR ERRLVIGYKM GGTNKFFSAL SNLYHFYSLY
SARKYVEQFS NGITIISLYL NPLPGANAPP IEHSIFQVMK EASLLYCLPD NPFFYPGAGP
RNGHAVQEAT YAYCGWVFAQ HFCNRLGASY LALKNILDES NPSHAEVLND IKRRFREETF
TRESIAQVIH AHADLINLLY VNFAMVHYPT DSASQLMPTL SYQRLQTQVP LSDQELYDKI
RRSVHNKHEL QVLESFLIFN KHVLKTNFYQ PTKVALSFRL APDFLPEVEY PKKPFGMFFV
IGGEFRGFHI RFRDVARGGI RIVMSRNREN YSINQRMLFD ENYGLASTQS LKNKDIPEGG
AKGTILPSLG ASPRLAFEKY VDAVIDLLIP GRSPGIKEQL VDLYGKPEML FFGPDEGTAD
MMDWAALHAR ARGAETWWKS FTTGKSAETL GGIPHDRFGM TSLSIRQYVL GIYKQLGLRE
KDITKVQTGG PDGDLGSNEI LLSSDKTVAV IDGSGVLADP NGIDREELIR LAKLRVPVGN
FDKSKLSKDG YLVRVEDQDV KLPSGEVIID GTDFRNSAHL RFKADLFVPC GGRPEAVNIS
NVATLVDAEG KPHFKYVVEG ANLFLTQQAR LFLEKRKVVL FKDSSTNKGK CLQMYKSPAL
TLALGGVTSS SLEVLAGLAL STQEYVDLMI FKDGKPSEFY ENYVRDIQQK ITENAAAEFH
CIWREHVRSQ GAKPRTLISD ELSSTLNNLQ EELESSDLYG DITNRKAVMR RAIPKTLVDQ
IGLDTLLQRL PESYQRALFS SWVASHFIYK YGVNASSVDF YHFIRDLSL
//
