ID   DHE41_HALSA             Reviewed;         435 AA.
AC   P29051;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   25-NOV-2008, entry version 49.
DE   RecName: Full=NAD-specific glutamate dehydrogenase A;
DE            Short=NAD-GDH A;
DE            EC=1.4.1.2;
GN   Name=gdhA; Synonyms=gdhX;
OS   Halobacterium salinarium (Halobacterium halobium).
OC   Archaea; Euryarchaeota; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=2242;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CCM 2090 / JCM 9120;
RX   MEDLINE=92114863; PubMed=1766432; DOI=10.1007/BF00280290;
RA   Benachenhou N., Baldacci G.;
RT   "The gene for a halophilic glutamate dehydrogenase: sequence,
RT   transcription analysis and phylogenetic implications.";
RL   Mol. Gen. Genet. 230:345-352(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NRC-36014;
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
RT   strain of Halobacterium salinarum.";
RL   Gene 349:237-244(2005).
RN   [3]
RP   PROTEIN SEQUENCE OF 119-128; 184-193 AND 268-276, AND
RP   CHARACTERIZATION.
RX   PubMed=12052548; DOI=10.1111/j.1574-6968.2002.tb11200.x;
RA   Hayden B.M., Bonete M.J., Brown P.E., Moir A.J., Engel P.C.;
RT   "Glutamate dehydrogenase of Halobacterium salinarum: evidence that the
RT   gene sequence currently assigned to the NADP+-dependent enzyme is in
RT   fact that of the NAD+-dependent glutamate dehydrogenase.";
RL   FEMS Microbiol. Lett. 211:37-41(2002).
CC   -!- CATALYTIC ACTIVITY: L-glutamate + H(2)O + NAD(+) = 2-oxoglutarate
CC       + NH(3) + NADH.
CC   -!- SUBUNIT: Homohexamer (By similarity).
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
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DR   EMBL; X63837; CAA45327.1; -; Genomic_DNA.
DR   EMBL; AY840088; AAW19068.1; -; Genomic_DNA.
DR   PIR; S18609; S18609.
DR   HSSP; P96110; 1B26.
DR   BioCyc; MetaCyc:MON-741; -.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0004352; F:glutamate dehydrogenase activity; IEA:EC.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR006095; Glu/Leu/Phe/Val_DHase.
DR   InterPro; IPR006096; Glu/Leu/Phe/Val_DHase_C.
DR   InterPro; IPR006097; Glu/Leu/Phe/Val_DHase_dimer.
DR   InterPro; IPR014362; Glu_DHase.
DR   InterPro; IPR016040; NAD(P)-bd.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   PANTHER; PTHR11606:SF2; GLFV_DH; 1.
DR   Pfam; PF00208; ELFV_dehydrog; 1.
DR   Pfam; PF02812; ELFV_dehydrog_N; 1.
DR   PIRSF; PIRSF000185; Glu_DH; 1.
DR   PRINTS; PR00082; GLFDHDRGNASE.
DR   PROSITE; PS00074; GLFV_DEHYDROGENASE; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; NAD; Oxidoreductase.
FT   CHAIN         1    435       NAD-specific glutamate dehydrogenase A.
FT                                /FTId=PRO_0000182779.
FT   ACT_SITE    126    126       By similarity.
SQ   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
//