DHE2_PYRCJ
ID DHE2_PYRCJ Reviewed; 424 AA.
AC A3MUY9;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=NAD(+)-dependent glutamate dehydrogenase {ECO:0000303|PubMed:23508687};
DE Short=NAD-GDH;
DE EC=1.4.1.2 {ECO:0000269|PubMed:23508687};
DE AltName: Full=NAD-specific glutamate dehydrogenase {ECO:0000303|PubMed:23508687};
GN OrderedLocusNames=Pcal_1031 {ECO:0000312|EMBL:ABO08456.1};
OS Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=410359;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21063 / JCM 11548 / VA1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Cozen A.E.,
RA Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.;
RT "Complete sequence of Pyrobaculum calidifontis JCM 11548.";
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, ACTIVITY REGULATION, SUBUNIT, AND INDUCTION.
RC STRAIN=DSM 21063 / JCM 11548 / VA1;
RX PubMed=23508687; DOI=10.1007/s00792-013-0527-7;
RA Wakamatsu T., Higashi C., Ohmori T., Doi K., Ohshima T.;
RT "Biochemical characterization of two glutamate dehydrogenases with
RT different cofactor specificities from a hyperthermophilic archaeon
RT Pyrobaculum calidifontis.";
RL Extremophiles 17:379-389(2013).
CC -!- FUNCTION: Catalyzes the reversible oxidative deamination of L-glutamate
CC to 2-oxoglutarate and ammonia, thereby playing a key role at the
CC intersection of the carbon and nitrogen metabolic pathways. Is strictly
CC specific for NAD(+)/NADH as the acceptor/donor, since it cannot use
CC NADP(+)/NADPH. May function in vivo in the catabolic direction. Also
CC catalyzes at low rates the oxidative deamination of L-norvaline, L-2-
CC aminobutyrate, L-valine and L-isoleucine, and the reductive amination
CC of 2-oxovalerate and 2-oxobutyrate. {ECO:0000269|PubMed:23508687}.
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:0000269|PubMed:23508687};
CC -!- ACTIVITY REGULATION: Is not regulated allosterically.
CC {ECO:0000269|PubMed:23508687}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.028 mM for NAD(+) (at 50 degrees Celsius)
CC {ECO:0000269|PubMed:23508687};
CC KM=5.3 mM for L-glutamate (at 50 degrees Celsius)
CC {ECO:0000269|PubMed:23508687};
CC KM=0.010 mM for NADH (at 50 degrees Celsius)
CC {ECO:0000269|PubMed:23508687};
CC KM=0.92 mM for 2-oxoglutarate (at 50 degrees Celsius)
CC {ECO:0000269|PubMed:23508687};
CC KM=9.8 mM for ammonia (at 50 degrees Celsius)
CC {ECO:0000269|PubMed:23508687};
CC Note=kcat is 17 sec(-1) for oxidative deamination of L-glutamate, and
CC 65 sec(-1) for reductive amination of 2-oxoglutarate (at 50 degrees
CC Celsius). {ECO:0000269|PubMed:23508687};
CC pH dependence:
CC Optimum pH is 10.5 for oxidative deamination, and 9.5 for reductive
CC amination. Retains more than 80% of its activity after incubation for
CC 30 minutes at pH 4.0-10.5. {ECO:0000269|PubMed:23508687};
CC Temperature dependence:
CC Optimum temperature is 80 degrees Celsius for oxidative deamination.
CC Retains full activity after incubation for 10 minutes at temperatures
CC up to 105 degrees Celsius. {ECO:0000269|PubMed:23508687};
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:23508687}.
CC -!- INDUCTION: Is constitutively expressed. {ECO:0000269|PubMed:23508687}.
CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC {ECO:0000305}.
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DR EMBL; CP000561; ABO08456.1; -; Genomic_DNA.
DR AlphaFoldDB; A3MUY9; -.
DR SMR; A3MUY9; -.
DR STRING; 410359.Pcal_1031; -.
DR EnsemblBacteria; ABO08456; ABO08456; Pcal_1031.
DR KEGG; pcl:Pcal_1031; -.
DR eggNOG; arCOG01352; Archaea.
DR HOGENOM; CLU_025763_1_2_2; -.
DR OMA; TNAWWWW; -.
DR BRENDA; 1.4.1.2; 7282.
DR Proteomes; UP000001431; Chromosome.
DR GO; GO:0004352; F:glutamate dehydrogenase (NAD+) activity; IDA:UniProtKB.
DR GO; GO:0070403; F:NAD+ binding; IDA:UniProtKB.
DR GO; GO:0070404; F:NADH binding; IDA:UniProtKB.
DR GO; GO:0006103; P:2-oxoglutarate metabolic process; IDA:UniProtKB.
DR GO; GO:0006536; P:glutamate metabolic process; IDA:UniProtKB.
DR CDD; cd01076; NAD_bind_1_Glu_DH; 1.
DR InterPro; IPR046346; Aminiacid_DH-like_N_sf.
DR InterPro; IPR006095; Glu/Leu/Phe/Val_DH.
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.
PE 1: Evidence at protein level;
KW NAD; Oxidoreductase.
FT CHAIN 1..424
FT /note="NAD(+)-dependent glutamate dehydrogenase"
FT /id="PRO_0000432227"
FT ACT_SITE 109
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P24295"
FT BINDING 73
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P24295"
FT BINDING 97
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P24295"
FT BINDING 193
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P24295"
FT BINDING 224
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P24295"
FT BINDING 357
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P24295"
FT SITE 149
FT /note="Important for catalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 424 AA; 47118 MW; B476BF6088C17DC1 CRC64;
MSTTYIVSDF LINTLLTIKR GVELAGLPPE FYEALEKPKR ILVVNIPVKM DDGKIKYFEG
YRVQHNDALG PFKGGIRFHP EVTLADDIAL AMLMTLKNSL AGLPYGGAKG AVRVDPRRLS
RRELEELARG YARAVAPLIG EQLDIPAPDV GTDSQVMAWM VDEYSRLVGR NAPAVFTSKP
PELWGNPVRE YSTGFGVAVA AREVAKRLWG GIVGKTAAVQ GLGNVGRWAA YWLEKMGAKV
VAVSDVNGVV YRERGLDVDL IRETKAKGPQ LLEMISQKNG VEIVKNPDQI FSLDVDILVP
AAIENVVRED NVDGVRARLV VEGANGPTTP GAERRLYERG VVVVPDILAN AGGVIMSYLE
WVENLQWLFW DEEETRRRLE AIMSNNVARV YARWEKEKSW TMRDAAVVTA LERIYNAMKT
RGWI
