ID   DHE4_PRERU              Reviewed;         444 AA.
AC   P95544;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=NAD(P)-specific glutamate dehydrogenase;
DE            Short=NAD(P)-GDH;
DE            EC=1.4.1.3;
DE   AltName: Full=NAD(P)H-dependent glutamate dehydrogenase;
GN   Name=gdhA;
OS   Prevotella ruminicola (Bacteroides ruminicola).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=839;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   SUBSTRATE SPECIFICITY.
RC   STRAIN=B14;
RX   PubMed=8837439; DOI=10.1128/aem.62.10.3826-3833.1996;
RA   Wen Z., Morrison M.;
RT   "The NAD(P)H-dependent glutamate dehydrogenase activities of Prevotella
RT   ruminicola B(1)4 can be attributed to one enzyme (GdhA), and gdhA
RT   expression is regulated in response to the nitrogen source available for
RT   growth.";
RL   Appl. Environ. Microbiol. 62:3826-3833(1996).
CC   -!- FUNCTION: Catalyzes the reversible oxidative deamination of glutamate
CC       to alpha-ketoglutarate and ammonia. P.ruminicola possess both
CC       NADP(H)- and NAD(H)-dependent activities on the same enzyme, suggesting
CC       that both anabolic and catabolic forms of the enzyme might occur.
CC       {ECO:0000269|PubMed:8837439}.
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=1.4.1.3;
CC         Evidence={ECO:0000269|PubMed:8837439};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-glutamate + NADP(+) = 2-oxoglutarate + H(+) + NADPH +
CC         NH4(+); Xref=Rhea:RHEA:11612, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.4.1.3;
CC         Evidence={ECO:0000269|PubMed:8837439};
CC   -!- SUBUNIT: Homohexamer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000305}.
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DR   EMBL; U82240; AAB40142.1; -; Genomic_DNA.
DR   PIR; T10487; T10487.
DR   AlphaFoldDB; P95544; -.
DR   SMR; P95544; -.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0004352; F:glutamate dehydrogenase (NAD+) activity; IEA:RHEA.
DR   GO; GO:0004354; F:glutamate dehydrogenase (NADP+) activity; IEA:RHEA.
DR   GO; GO:0004353; F:glutamate dehydrogenase [NAD(P)+] activity; IMP:UniProtKB.
DR   GO; GO:0006537; P:glutamate biosynthetic process; IMP:UniProtKB.
DR   CDD; cd05313; NAD_bind_2_Glu_DH; 1.
DR   InterPro; IPR046346; Aminiacid_DH-like_N_sf.
DR   InterPro; IPR006095; Glu/Leu/Phe/Val_DH.
DR   InterPro; IPR033524; Glu/Leu/Phe/Val_DH_AS.
DR   InterPro; IPR006096; Glu/Leu/Phe/Val_DH_C.
DR   InterPro; IPR006097; Glu/Leu/Phe/Val_DH_dimer_dom.
DR   InterPro; IPR014362; Glu_DH.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR033922; NAD_bind_Glu_DH.
DR   Pfam; PF00208; ELFV_dehydrog; 1.
DR   Pfam; PF02812; ELFV_dehydrog_N; 1.
DR   PIRSF; PIRSF000185; Glu_DH; 1.
DR   PRINTS; PR00082; GLFDHDRGNASE.
DR   SMART; SM00839; ELFV_dehydrog; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF53223; SSF53223; 1.
DR   PROSITE; PS00074; GLFV_DEHYDROGENASE; 1.
PE   1: Evidence at protein level;
KW   NAD; NADP; Oxidoreductase.
FT   CHAIN           1..444
FT                   /note="NAD(P)-specific glutamate dehydrogenase"
FT                   /id="PRO_0000182773"
FT   ACT_SITE        124
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
FT   BINDING         88
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         109
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         112
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         163
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         207
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         238
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         376
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            164
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   444 AA;  48878 MW;  32CAD7F278CF06A9 CRC64;
     MKATEVIEKL KAKFPGQPEY IQAVSQVLGT IEEEYNKHPE FEKANLIERL CVPDRILQFR
     VSWVDDNGNV QTNLGYRVQH NNAIGPYKGG LRFHKSVNAS ILKFLAFEQT FKNSLTTLPM
     GGAKGGSDFD PHGKSDMEVM RFCQAFMNEL YRLIGPDEDV PAGDIGVGGR EVGYMFGQYK
     KLTHQFQGIL TGKGLEFGGS LIRPEATGYG NVYFLEDMLK TRGESLEGKT VLVSGSGNVA
     QYTIEKLLQL GAKPVTCSDS NGYIYDPDGI DAEKLAFIME LKNVKRGRIK EYAEKYGVKY
     VENARPWGEK ADIATPCATQ DEINEAEAKT LIANGVFAVS EGANMPTEPA AIKVFQDAKI
     LYCPGKASNA GGVATSGLEM SQNSERLSWT REEVDTKLHN IMDEIHANCV KYGTEPDGYI
     NYVKGANVAG FMKVAKAMMA QGIY