ID   B8YJM3_PICSP            Unreviewed;      1055 AA.
AC   B8YJM3;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=NAD-specific glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000184};
DE            EC=1.4.1.2 {ECO:0000256|PIRNR:PIRNR000184};
GN   Name=GDH2 {ECO:0000313|EMBL:ACL78797.1};
OS   Scheffersomyces stipitis (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX   NCBI_TaxID=4924 {ECO:0000313|EMBL:ACL78797.1};
RN   [1] {ECO:0000313|EMBL:ACL78797.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CBS 5774 {ECO:0000313|EMBL:ACL78797.1};
RX   PubMed=21360752; DOI=10.1002/yea.1845;
RA   Freese S., Vogts T., Speer F., Schafer B., Passoth V., Klinner U.;
RT   "C- and N-catabolic utilization of tricarboxylic acid cycle-related amino
RT   acids by Scheffersomyces stipitis and other yeasts.";
RL   Yeast 28:375-390(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; FJ540908; ACL78797.1; -; Genomic_DNA.
DR   AlphaFoldDB; B8YJM3; -.
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          674..946
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00839"
SQ   SEQUENCE   1055 AA;  119517 MW;  661D610F3552F61C CRC64;
     MSIQEPDIQR LTLERTASNS SSVLSLKHGY IDSPFSGKKD QYEQVLDILD STGFIPESLI
     ESEARWFYES LGIDDVFFAR ESPEGIAGHI HSLYSCKVQA YSGDGADFPL IQYKREADDH
     GVFFDSSDVS TSMYKNQFEE RIDDKYIDPS SSDSISYRVE YFSAPLNYKT DPILSGVFQN
     NKTLRDQLMR CYFVYKNQYD HLDVSADETD INKIGDSTFL KIASANTKQL YADIVKNVVT
     TTGPVIRHFP IEDSEEYRVV IGYRQKTSAR YNSALSDLAN YYKLQTTRKY VEQFANGVTI
     ISMYVTSKQK KLPVDLSIYQ VIKEASLLYC IPHNFFHDRF TKGELSLQES IYAQSGVIFV
     THFLNRLGPE YTKLATLLDA SKSLQNAEVL NSLKKRLRAE TYTQNFIQEV FDQRRDIVRK
     LYRQFADVHY IRSSMEKTLS YQRLSQITPV GTEEEFEQLL SRECSQNEHH AVVLRALFVF
     NKSILKTNFY TSTKVALSFR LDPSFLPSSE YPEKPYGMFF VVGSDFRGFH IRFRDIARGG
     IRIVRSRNLD AYNVNLRNLF DENYNLANTQ QRKNKDIPEG GSKGVILLDA GAAQERPKAC
     FEKYVDALID LLLKQHIPGV KDSYVDLYNK PEILFLGPDE GTAGYTDWAT LHARSRGAPW
     WKSFLTGKSP QIGGIPHDEY GMTTLSVRAY VNKIYEKLNI DNSKIRKFQT GGPDGDLGSN
     EIKLSRDEQY VGIVDGSGVI ADPNGLDKQE LLRLAHERKM IDHFDKSKLS KDGYIVLVDD
     VDVTLPNGHV VTSGVAFRNT FHLKLKEQYP DGVDLFVPCG GRPAAIDTNN VQELINEKTG
     KSILPYFLEG ANLFITQAAK LVLEQAGIVI FKDASTNKGG VTSSSLEVLA SLAFDDEGFL
     ANMCVDSKTH QKPLFYQEYV KNVQKIVVAN AENEFEALWK LKEETGISFT ELSDKLSVAI
     NKLGDELANS KELWNDDVDF RNAVLLDSLP PLLLEVVGID SVLTRVPEAY LRAIFATHLA
     SRFVYTRGID SNPAKFLEFI SSTRKEYVKK GLLKH
//