ID   DHE4_PYRCJ              Reviewed;         421 AA.
AC   A3MWK6;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=NADP(+)-dependent glutamate dehydrogenase {ECO:0000303|PubMed:23508687};
DE            Short=NADP-GDH;
DE            EC=1.4.1.4 {ECO:0000269|PubMed:23508687};
GN   OrderedLocusNames=Pcal_1606 {ECO:0000312|EMBL:ABO09023.1};
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. Shows a
CC       high preference for NADP(+)/NADPH as the acceptor/donor over
CC       NAD(+)/NADH. May function in vivo in the synthetic direction. Also
CC       catalyzes at very low rates the oxidative deamination of L-2-
CC       aminobutyrate, and the reductive amination of 2-oxovalerate and 2-
CC       oxobutyrate. {ECO:0000269|PubMed:23508687}.
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=1.4.1.4;
CC         Evidence={ECO:0000269|PubMed:23508687};
CC   -!- ACTIVITY REGULATION: Is not regulated allosterically. Activity is
CC       inhibited in the presence of high ionic strength; the inhibitory effect
CC       of KCl is slightly higher than that of NaCl.
CC       {ECO:0000269|PubMed:23508687}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.035 mM for NADP(+) (at 50 degrees Celsius)
CC         {ECO:0000269|PubMed:23508687};
CC         KM=3.4 mM for L-glutamate (at 50 degrees Celsius)
CC         {ECO:0000269|PubMed:23508687};
CC         KM=0.017 mM for NADPH (at 50 degrees Celsius)
CC         {ECO:0000269|PubMed:23508687};
CC         KM=1.7 mM for 2-oxoglutarate (at 50 degrees Celsius)
CC         {ECO:0000269|PubMed:23508687};
CC         KM=2.2 mM for ammonia (at 50 degrees Celsius)
CC         {ECO:0000269|PubMed:23508687};
CC         Note=kcat is 13 sec(-1) for oxidative deamination of L-glutamate, and
CC         95 sec(-1) for reductive amination of 2-oxoglutarate (at 50 degrees
CC         Celsius). {ECO:0000269|PubMed:23508687};
CC       pH dependence:
CC         Optimum pH is 9.5 for oxidative deamination, and 9.0 for reductive
CC         amination. Retains more than 80% of its activity after incubation for
CC         30 minutes at pH 4.5-9.5. {ECO:0000269|PubMed:23508687};
CC       Temperature dependence:
CC         Optimum temperature is 90 degrees Celsius for oxidative deamination.
CC         Retains full activity after incubation for 10 minutes at temperatures
CC         up to 90 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000561; ABO09023.1; -; Genomic_DNA.
DR   AlphaFoldDB; A3MWK6; -.
DR   SMR; A3MWK6; -.
DR   STRING; 410359.Pcal_1606; -.
DR   EnsemblBacteria; ABO09023; ABO09023; Pcal_1606.
DR   KEGG; pcl:Pcal_1606; -.
DR   eggNOG; arCOG01352; Archaea.
DR   HOGENOM; CLU_025763_1_2_2; -.
DR   OMA; PCFAAFP; -.
DR   BRENDA; 1.4.1.4; 7282.
DR   Proteomes; UP000001431; Chromosome.
DR   GO; GO:0004354; F:glutamate dehydrogenase (NADP+) activity; IDA:UniProtKB.
DR   GO; GO:0070401; F:NADP+ binding; IDA:UniProtKB.
DR   GO; GO:0070402; F:NADPH 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   NADP; Oxidoreductase.
FT   CHAIN           1..421
FT                   /note="NADP(+)-dependent glutamate dehydrogenase"
FT                   /id="PRO_0000432228"
FT   ACT_SITE        106
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P24295"
FT   BINDING         70
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P24295"
FT   BINDING         94
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P24295"
FT   BINDING         190
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P24295"
FT   BINDING         221
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P24295"
FT   BINDING         354
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P24295"
FT   SITE            146
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   421 AA;  46610 MW;  DECEAEB7942AE122 CRC64;
     MSQNGQFLEY TLQVIRRGVE MGGFPEDFYK LLSRPKRIIQ VSIPVKMDNG SYEVFEGYRV
     QHNDALGPFK GGIRFHPEVT LADDIALAML MTLKNSLAGL PYGGAKGAVR VDPRRLSRRE
     LEELARGYAR AVAPLIGEQL DIPAPDVGTD SQVMAWMVDE YSKLAGRNAP AVFTSKPPEL
     WGNPVREYST GFGVAVAARE VAKRLWGGIE GKTVAVHGAG NTGAWAAYWL EKMGAKVVAI
     SDTRGTVVNK AGIPGEQILK VYMEKKRDKS ATVLALEGEK IADSNASLYQ DVDILVPAAI
     ENVVREDNVG LVRARLVVEG ANGPTTPGAE RRLYERGVVV VPDILANAGG VIMSYLEWVE
     NLQWLFWDEE ETRRRLEAIM SNNVARVYAR WEKEKSWTMR DAAVVTALER IYNAMKTRGW
     I