ID M7XRK5_RHOT1 Unreviewed; 1043 AA.
AC M7XRK5;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=NAD-specific glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000184};
DE EC=1.4.1.2 {ECO:0000256|PIRNR:PIRNR000184};
GN ORFNames=RHTO_07718 {ECO:0000313|EMBL:EMS22848.1};
OS Rhodotorula toruloides (strain NP11) (Yeast) (Rhodosporidium toruloides).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1130832 {ECO:0000313|EMBL:EMS22848.1, ECO:0000313|Proteomes:UP000016926};
RN [1] {ECO:0000313|EMBL:EMS22848.1, ECO:0000313|Proteomes:UP000016926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NP11 {ECO:0000313|EMBL:EMS22848.1,
RC ECO:0000313|Proteomes:UP000016926};
RX PubMed=23047670; DOI=10.1038/ncomms2112;
RA Zhu Z., Zhang S., Liu H., Shen H., Lin X., Yang F., Zhou Y.J., Jin G.,
RA Ye M., Zou H., Zou H., Zhao Z.K.;
RT "A multi-omic map of the lipid-producing yeast Rhodosporidium toruloides.";
RL Nat. Commun. 3:1112-1112(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; KB722649; EMS22848.1; -; Genomic_DNA.
DR RefSeq; XP_016273967.1; XM_016421374.1.
DR AlphaFoldDB; M7XRK5; -.
DR GeneID; 27371731; -.
DR eggNOG; KOG2250; Eukaryota.
DR HOGENOM; CLU_005220_0_0_1; -.
DR OrthoDB; 89313at2759; -.
DR Proteomes; UP000016926; 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}.
FT DOMAIN 680..943
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1043 AA; 116517 MW; DF08A911494F9848 CRC64;
MPSAMLSPPS PLEHLKDRLD VPRTPSPAHG TIKHNDLGYR KASFAGKDKH KEAVVDIVAS
NGFLPELLVQ PEVDWFYSQL GIDDGYFSLT SPQEVADHVE SLYGAKVQAH ASHQDYLEIK
LEKEGDSSAV YIFTSPPGVS LANGPQYEQR IDSQYLDNSN PTDAWRLESY RAVPPVTTNG
DDANGHAPIE SVAAQLRSYF VSKCDFVDTK LDEQELVKPG VNIREVGDKT FLEKATDNTL
EIYQELMDEA LRRMGPVVAA YDVENSRERR IVLAYKQGGT RSFFSALSDL YHSYGFYSTR
KYVENLRNGV TIISLYLHPL QGIPNEGNIL QIIKESSLIY VLPNNPLFTG SQLSVQESTY
AYSAWVFAQH FLNRLGPSYA ALKNILDEND SVQAGVLSDI RARFRQETFT RASILECLQQ
YPDVIRLAYI SFAYTHYYSN YGNNLVPTLS YARLQTAEVL TSDQLKAHIR KNVLNKHDAQ
ILESLVTFNN AILKTNFFTS TKVALSFRLD PDFLPESEYP VRAYGLFLVV GDGFRGFHLR
FKDVARGGLR MIMSRNREAY SVNQRSLFDE VYGLASTQAL KNKDIPEGGS KGAILPDLGA
NPQTCFCKFV DSIFDLLLPG RTPGVKDKII DLYGKEEILF FGPDEGTANY MAWVADHARA
RGAPWWKASS TGKPASTHGG IPHDIYGMTS LSVRGYTTGI YRKLGLKEEE ITKVQTGGPD
GDLGSNEILL SKDKTITIID GSGTLHDPHG INREELIRLA KARKMVVNFD RSKLSKDGYL
ILVDDRDVTL PNGDVVADGT DFRNTAHLHY KADILVPCGG RPESVNVNNV SKLWDADGVT
NFKYIVEGAN LFITQGARLQ LEKKGVVLFR DASANKGGVT SSSLEVLSGM ALDDAQFIDL
MTSAGKDRLP EFYQQYARSI QETIFKNATA EFETIWAAHE KTGRPFTLLS DDLSRKLVQL
QAEMEESTLY DDQQMRRAVM ERALPKLLID TAGLDKILAR LPEAYKHSVF SCYVASHFVY
TYGIDASPID FYRFLRSLTQ DEN
//
