ID   DHEB_HALSI              Reviewed;         429 AA.
AC   P0DMG3; Q5MBG0; Q9HSM4;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 30.
DE   RecName: Full=Glutamate dehydrogenase B;
DE            Short=GDH B;
DE            EC=1.4.1.-;
GN   Name=gdhB;
OS   Halobacterium salinarum (Halobacterium halobium).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=2242;
RN   [1]
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 strain
RT   of Halobacterium salinarum.";
RL   Gene 349:237-244(2005).
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; AY840087; AAW19067.1; -; Genomic_DNA.
DR   RefSeq; WP_010902074.1; NZ_CP038631.1.
DR   AlphaFoldDB; P0DMG3; -.
DR   SMR; P0DMG3; -.
DR   GeneID; 5952406; -.
DR   GeneID; 62885895; -.
DR   OMA; PCFAAFP; -.
DR   GO; GO:0016639; F:oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
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   Oxidoreductase.
FT   CHAIN           1..429
FT                   /note="Glutamate dehydrogenase B"
FT                   /id="PRO_0000182780"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        119
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
SQ   SEQUENCE   429 AA;  45968 MW;  A344F09C60BE60A6 CRC64;
     MAQTPPPESA PSTDSEPETA LETARRQLQA AAEHVDIADG VIERLTHPTR VVQVSVPVER
     DDGTVTVYDG YRAQHDDVRG PYKGGLRYHP GVSAEECVGL SMWMTWKCAV MDLPFGGAKG
     GVVVDPKTLS ADEHERLTRR FAAELRDEVG PSQDIPAPDM GTDAQTMAWF MDAYSMQQGE
     TVPGVVTGKP PVAGGSHGRA EAPGRSVAIA TREAINYYDI PIDDATVAVQ GYGSVGANAA
     LLLDDWGARV VAVSDVNGGV LDTDGLDTHA IPSHGNQPAA VMRHDAPNTL TNEELLELDV
     DVVIPAAVGN VITAANADRI QADIVVEGAN GPTTSAADRI LEERAVPVIP DILANAGGVT
     VSYFEWLQDI NRRTWSPERV RDELESEMLS AWNAVRSEVD DGDLSWRDAA YVVALQRIGR
     AKEARGLWP