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NAD-specific glutamate dehydrogenase A (NAD-GDH A) (EC 1.4.1.2)

 DHE2_HALSI              Reviewed;         435 AA.
P29051;
01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
01-DEC-1992, sequence version 1.
10-OCT-2018, entry version 85.
RecName: Full=NAD-specific glutamate dehydrogenase A;
Short=NAD-GDH A;
EC=1.4.1.2;
Name=gdhX; Synonyms=gdhA;
Halobacterium salinarum (Halobacterium halobium).
Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria;
Halobacteriales; Halobacteriaceae; Halobacterium.
NCBI_TaxID=2242;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=CCM 2090 / JCM 9120;
PubMed=1766432; DOI=10.1007/BF00280290;
Benachenhou N., Baldacci G.;
"The gene for a halophilic glutamate dehydrogenase: sequence,
transcription analysis and phylogenetic implications.";
Mol. Gen. Genet. 230:345-352(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=NRC-36014;
PubMed=15780999; DOI=10.1016/j.gene.2005.01.011;
Ingoldsby L.M., Geoghegan K.F., Hayden B.M., Engel P.C.;
"The discovery of four distinct glutamate dehydrogenase genes in a
strain of Halobacterium salinarum.";
Gene 349:237-244(2005).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 119-128;
184-193 AND 268-276, CHARACTERIZATION, AND CATALYTIC ACTIVITY.
STRAIN=NRC-36014;
PubMed=12052548; DOI=10.1111/j.1574-6968.2002.tb11200.x;
Hayden B.M., Bonete M.J., Brown P.E., Moir A.J., Engel P.C.;
"Glutamate dehydrogenase of Halobacterium salinarum: evidence that the
gene sequence currently assigned to the NADP+-dependent enzyme is in
fact that of the NAD+-dependent glutamate dehydrogenase.";
FEMS Microbiol. Lett. 211:37-41(2002).
[4]
CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
REGULATION.
STRAIN=NRC-36014;
PubMed=22527040; DOI=10.1007/s00792-012-0446-z;
Munawar N., Engel P.C.;
"Overexpression in a non-native halophilic host and biotechnological
potential of NAD+-dependent glutamate dehydrogenase from Halobacterium
salinarum strain NRC-36014.";
Extremophiles 16:463-476(2012).
-!- CATALYTIC ACTIVITY: L-glutamate + H(2)O + NAD(+) = 2-oxoglutarate
+ NH(3) + NADH. {ECO:0000269|PubMed:12052548,
ECO:0000269|PubMed:22527040}.
-!- ACTIVITY REGULATION: Inhibited by ethanol, acetone, acetonitrile
and 2-propanol (65 to 70% inhibition) and to a lesser extent by
methanol and dimethyl formamide (26 and 49 % inhibition
respectively). No effect of glycerol or DMSO.
{ECO:0000269|PubMed:22527040}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=14 mM for glutamate (for the recombinant enzyme, in the
presence of 3.2 M NaCl) {ECO:0000269|PubMed:22527040};
KM=0.35 mM for NAD(+) (for the recombinant enzyme, in the
presence of 3.2 M NaCl) {ECO:0000269|PubMed:22527040};
KM=3.4 mM for 2-oxoglutarate (for the recombinant enzyme, in the
presence of 3.2 M NaCl) {ECO:0000269|PubMed:22527040};
KM=118 mM for NH(4)(+) (for the recombinant enzyme, in the
presence of 3.2 M NaCl) {ECO:0000269|PubMed:22527040};
KM=0.011 mM for NADH (for the recombinant enzyme, in the
presence of 3.2 M NaCl) {ECO:0000269|PubMed:22527040};
KM=9 mM for glutamate (for the recombinant enzyme, in the
presence of 10% DMSO) {ECO:0000269|PubMed:22527040};
KM=0.13 mM for NAD(+) (for the recombinant enzyme, in the
presence of 10% DMSO) {ECO:0000269|PubMed:22527040};
KM=0.8 mM for 2-oxoglutarate (for the recombinant enzyme, in the
presence of 20% DMSO) {ECO:0000269|PubMed:22527040};
KM=112 mM for NH(4)(+) (for the recombinant enzyme, in the
presence of 20% DMSO) {ECO:0000269|PubMed:22527040};
KM=0.025 mM for NADH (for the recombinant enzyme, in the
presence of 20% DMSO) {ECO:0000269|PubMed:22527040};
Note=kcat is 24 sec(-1) for glutamate in the presence of 3.2 M
NaCl. kcat is 16 sec(-1) for NAD(+) in the presence of 3.2 M
NaCl. kcat is 56 sec(-1) for 2-oxoglutarate in the presence of
3.2 M NaCl. kcat is 85 sec(-1) for NH(4)(+) in the presence of
3.2 M NaCl. kcat is 39 sec(-1) for NADH in the presence of 3.2 M
NaCl. kcat is 17 sec(-1) for glutamate in the presence of 10%
DMSO. kcat is 15 sec(-1) for NAD(+) in the presence of 10% DMSO.
kcat is 46 sec(-1) for 2-oxoglutarate in the presence of 20%
DMSO. kcat is 84 sec(-1) for NH(4)(+) in the presence of 20%
DMSO. kcat is 47 sec(-1) for NADH in the presence of 20% DMSO.;
pH dependence:
Optimum pH for oxidative deamination is 9.2. Optimum pH for
reductive amination is 8.5. {ECO:0000269|PubMed:22527040};
Temperature dependence:
Optimum temperature is 70 degrees Celsius. The enzyme is
entirely stable from 50 to 70 degrees Celsius and 55 % activity
is retained after 30 min at 90 degrees Celsius.
{ECO:0000269|PubMed:22527040};
-!- SUBUNIT: Homohexamer. {ECO:0000250}.
-!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:12052548}.
-!- MISCELLANEOUS: Strain NRC-36014 contains 4 distinct glutamate
dehydrogenases while strain NRC-1 contains only 3. GdhX is only
present in strain NRC-36014 (PubMed:15780999).
{ECO:0000305|PubMed:15780999}.
-!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
{ECO:0000305}.
-!- CAUTION: Was initially thought to be a NADP-specific glutamate
dehydrogenase. {ECO:0000305|PubMed:1766432}.
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EMBL; X63837; CAA45327.1; -; Genomic_DNA.
EMBL; AY840088; AAW19068.1; -; Genomic_DNA.
PIR; S18609; S18609.
ProteinModelPortal; P29051; -.
SMR; P29051; -.
BioCyc; MetaCyc:MONOMER-741; -.
BRENDA; 1.4.1.2; 2552.
GO; GO:0004352; F:glutamate dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
CDD; cd01076; NAD_bind_1_Glu_DH; 1.
InterPro; IPR006095; Glu/Leu/Phe/Val_DH.
InterPro; IPR033524; Glu/Leu/Phe/Val_DH_AS.
InterPro; IPR006096; Glu/Leu/Phe/Val_DH_C.
InterPro; IPR006097; Glu/Leu/Phe/Val_DH_dimer_dom.
InterPro; IPR014362; Glu_DH.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR033922; NAD_bind_Glu_DH.
Pfam; PF00208; ELFV_dehydrog; 1.
Pfam; PF02812; ELFV_dehydrog_N; 1.
PIRSF; PIRSF000185; Glu_DH; 1.
PRINTS; PR00082; GLFDHDRGNASE.
SMART; SM00839; ELFV_dehydrog; 1.
SUPFAM; SSF51735; SSF51735; 1.
PROSITE; PS00074; GLFV_DEHYDROGENASE; 1.
1: Evidence at protein level;
Direct protein sequencing; NAD; Oxidoreductase.
CHAIN 1 435 NAD-specific glutamate dehydrogenase A.
/FTId=PRO_0000182779.
ACT_SITE 126 126 {ECO:0000255|PROSITE-ProRule:PRU10011}.
SEQUENCE 435 AA; 47459 MW; 0E4E940D2FF8B9D2 CRC64;
MTMASKSDST HDESGDEAAD STEPESALET ARRQLYHAAS YLDIDQNIVE RLKYPKKVHE
VTIPIERDDG TVEVFTGYRA QHDSVRGPYK GGLRYHPDVT RDECVGLGMW MTWKCAVMDL
PFGGAKGGVA VNPKELSPEE KERLTRRFTQ EIRDVIGPNQ DIPAPDMGTD PQTMAWLMDA
YSMQEGETTP GVVTGKPPVV GGSEGREEAP GRSVAIITQL VCEYYDQPLD ETTVAVQGYG
SVGANAARLL DKWGATIVAI SDVNGAMYEP DGIDTASVPS HDEEPEAVTT YADTVISNEE
LLTLDVDVLI PAALGNVITK ENAEAIAADL VVEGANGPTT STADSILADR DVAVIPDILA
NAGGVTVSYF EWLQDINRRA WSLERVNDEL EAEMQAAWRA VKDEYENRDV TWRDAAYIVA
LSRIAEAHEA RGLWP


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