ID K7YUQ7_BDEBC Unreviewed; 424 AA.
AC K7YUQ7;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN ORFNames=Bdt_0683 {ECO:0000313|EMBL:AFY00390.1};
OS Bdellovibrio bacteriovorus str. Tiberius.
OC Bacteria; Bdellovibrionota; Bdellovibrionia; Bdellovibrionales;
OC Pseudobdellovibrionaceae; Bdellovibrio.
OX NCBI_TaxID=1069642 {ECO:0000313|EMBL:AFY00390.1, ECO:0000313|Proteomes:UP000010074};
RN [1] {ECO:0000313|EMBL:AFY00390.1, ECO:0000313|Proteomes:UP000010074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tiberius {ECO:0000313|EMBL:AFY00390.1,
RC ECO:0000313|Proteomes:UP000010074};
RX PubMed=23181807; DOI=10.1186/1471-2164-13-670;
RA Hobley L., Lerner T.R., Williams L.E., Lambert C., Till R., Milner D.S.,
RA Basford S.M., Capeness M.J., Fenton A.K., Atterbury R.J., Harris M.A.,
RA Sockett R.E.;
RT "Genome analysis of a simultaneously predatory and prey-independent, novel
RT Bdellovibrio bacteriovorus from the River Tiber, supports in silico
RT predictions of both ancient and recent lateral gene transfer from diverse
RT bacteria.";
RL BMC Genomics 13:670-670(2012).
CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC {ECO:0000256|ARBA:ARBA00006382, ECO:0000256|PIRNR:PIRNR000185,
CC ECO:0000256|RuleBase:RU004417}.
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DR EMBL; CP002930; AFY00390.1; -; Genomic_DNA.
DR RefSeq; WP_015089866.1; NC_019567.1.
DR AlphaFoldDB; K7YUQ7; -.
DR STRING; 1069642.Bdt_0683; -.
DR KEGG; bbat:Bdt_0683; -.
DR PATRIC; fig|1069642.3.peg.676; -.
DR HOGENOM; CLU_025763_1_2_7; -.
DR Proteomes; UP000010074; Chromosome.
DR GO; GO:0004353; F:glutamate dehydrogenase [NAD(P)+] activity; IEA:UniProt.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR CDD; cd01076; NAD_bind_1_Glu_DH; 1.
DR Gene3D; 3.40.50.10860; Leucine Dehydrogenase, chain A, domain 1; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR InterPro; IPR006095; Glu/Leu/Phe/Val/Trp_DH.
DR InterPro; IPR006096; Glu/Leu/Phe/Val/Trp_DH_C.
DR InterPro; IPR006097; Glu/Leu/Phe/Val/Trp_DH_dimer.
DR InterPro; IPR033524; Glu/Leu/Phe/Val_DH_AS.
DR InterPro; IPR014362; Glu_DH.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR033922; NAD_bind_Glu_DH.
DR PANTHER; PTHR11606; GLUTAMATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11606:SF13; GLUTAMATE DEHYDROGENASE 1, MITOCHONDRIAL; 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 SMART; SM00839; ELFV_dehydrog; 1.
DR SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00074; GLFV_DEHYDROGENASE; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|PIRSR:PIRSR000185-2};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000185-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000185}.
FT DOMAIN 190..420
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 112
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT BINDING 76
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 197
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 228
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 356
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT SITE 152
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ SEQUENCE 424 AA; 46239 MW; 641A906E0C4A6BED CRC64;
MEHKIEPLYD GPLFRNAIQT LDEAAKIINC DPNILERLKR PRRCITVSVP VRMDDHSVKV
FTGYRVQYSP TLGPYKGGIR YHQNVDLSEV VGLAALMTFK NSVLGLPLGG AKGGITVDPT
KLSRTEKQNL TRRYASEIGP FVGPTKDIPA PDVGTDPQTM AWFMDTYSQE QGGFAQPGVV
TGKPVEIGGS LGRNHATGLG VVYVAEKAFE VCNMSMKGAS IAIQGFGNVG SFAAKFAHER
GARIVAVSDV SGGIFNGDGL DINEVNEYVK AHKFLKGYPK AQPISNEELL EVKCDALFPC
ALENQIDTHN AEKIQAKIIV EGANGPITNA GTKILHKRGV FIAPDVIANG GGVIVSYFEW
VQDTMSYFWD EEEVNGRLKG IITKAFDKGY SLAKEKNIDM RSAAMAVSVQ RLERAMLLRG
LYPR
//
