DHE4_HALSA
ID DHE4_HALSA Reviewed; 417 AA.
AC Q9HRM7;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 2.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=NADP-specific glutamate dehydrogenase A1;
DE EC=1.4.1.4;
GN Name=gdhA1; OrderedLocusNames=VNG_0628G;
OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS (Halobacterium halobium).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=64091;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX PubMed=11016950; DOI=10.1073/pnas.190337797;
RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA DasSarma S.;
RT "Genome sequence of Halobacterium species NRC-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
RN [2]
RP IDENTIFICATION.
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX PubMed=15780999; DOI=10.1016/j.gene.2005.01.011;
RA Ingoldsby L.M., Geoghegan K.F., Hayden B.M., Engel P.C.;
RT "The discovery of four distinct glutamate dehydrogenase genes in a strain
RT of Halobacterium salinarum.";
RL Gene 349:237-244(2005).
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 -!- SUBUNIT: Homohexamer. {ECO:0000250}.
CC -!- MISCELLANEOUS: Strain NRC-36014 contains 4 distinct glutamate
CC dehydrogenases while strain NRC-1 contains only 3.
CC {ECO:0000305|PubMed:15780999}.
CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC {ECO:0000305}.
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DR EMBL; AE004437; AAG19131.1; -; Genomic_DNA.
DR PIR; G84220; G84220.
DR RefSeq; WP_012289198.1; NC_002607.1.
DR AlphaFoldDB; Q9HRM7; -.
DR SMR; Q9HRM7; -.
DR STRING; 64091.VNG_0628G; -.
DR PaxDb; Q9HRM7; -.
DR EnsemblBacteria; AAG19131; AAG19131; VNG_0628G.
DR GeneID; 5953644; -.
DR GeneID; 62886255; -.
DR KEGG; hal:VNG_0628G; -.
DR PATRIC; fig|64091.14.peg.478; -.
DR HOGENOM; CLU_025763_1_2_2; -.
DR InParanoid; Q9HRM7; -.
DR OrthoDB; 40988at2157; -.
DR PhylomeDB; Q9HRM7; -.
DR Proteomes; UP000000554; Chromosome.
DR GO; GO:0004352; F:glutamate dehydrogenase (NAD+) activity; IBA:GO_Central.
DR GO; GO:0004354; F:glutamate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0006538; P:glutamate catabolic process; IBA:GO_Central.
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; 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 3: Inferred from homology;
KW NADP; Oxidoreductase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..417
FT /note="NADP-specific glutamate dehydrogenase A1"
FT /id="PRO_0000428791"
FT ACT_SITE 105
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
SQ SEQUENCE 417 AA; 45008 MW; C18FA67CA33E81A1 CRC64;
MPEANPFESL QEQLDDAGEF LDVNADVLER LKHPERVLET TLSVEMDDGT IETFKAFRSQ
FNGDRGPYKG GIRYHPGVTR DEVKALSGWM VYKTAVADIP YGGGKGGIIL DPEEYSDSEL
ERITRAFATE LRPFIGEDKD VPAPDVNTGQ REMNWIKDTY ETLEDTTAPG VITGKALENG
GSEGRVNATG RSTMFAAREV FDYLDRDLSD ATVAVQGYGN AGSVAAKLIA DQGADVVAVS
DSSGAVHNPD GLDTRAVKAF KTETGSVSGY EGATEELSNE ALLTMDVDLL VPAALENAID
EDLAHDVDAD VVVEAANGPL TPDADDVLTE RGVTVVPDIL ANAGGVTVSY FEWVQNRQRF
QWTEDRVNEE LEAIITDAFD AMTDAHEDAG TPNLRTAAYV VAVQRVVDAY EGSGSWP