ID A0A1B0VM25_FERIS Unreviewed; 427 AA.
AC A0A1B0VM25;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN ORFNames=NA23_06835 {ECO:0000313|EMBL:AMW32992.1};
OS Fervidobacterium islandicum.
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Fervidobacteriaceae;
OC Fervidobacterium.
OX NCBI_TaxID=2423 {ECO:0000313|EMBL:AMW32992.1, ECO:0000313|Proteomes:UP000093740};
RN [1] {ECO:0000313|EMBL:AMW32992.1, ECO:0000313|Proteomes:UP000093740}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AW-1 {ECO:0000313|EMBL:AMW32992.1,
RC ECO:0000313|Proteomes:UP000093740};
RX PubMed=26421103; DOI=10.1186/s40793-015-0063-4;
RA Lee Y.J., Jeong H., Park G.S., Kwak Y., Lee S.J., Lee S.J., Park M.K.,
RA Kim J.Y., Kang H.K., Shin J.H., Lee D.W.;
RT "Genome sequence of a native-feather degrading extremely thermophilic
RT Eubacterium, Fervidobacterium islandicum AW-1.";
RL Stand. Genomic Sci. 10:71-71(2015).
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; CP014334; AMW32992.1; -; Genomic_DNA.
DR RefSeq; WP_052107200.1; NZ_CP014334.2.
DR AlphaFoldDB; A0A1B0VM25; -.
DR STRING; 2423.NA23_06835; -.
DR KEGG; fia:NA23_06835; -.
DR eggNOG; COG0334; Bacteria.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000093740; Chromosome.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
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: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; 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.
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 191..423
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 114
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT BINDING 78
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 102
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 198
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 229
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 359
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT SITE 154
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ SEQUENCE 427 AA; 46901 MW; A73FFDFBC7797063 CRC64;
MKLSTMGNLK PFGPLYENAQ KQFLKAADLM DLDPNIGNFL LWPQRILEVH FPVVMDDGRV
EIFEGYRVQH NTARGPAKGG IRYHPDTNLD EVASLAFWMT WKCAVMNLPY GGGKGGVRVD
VTQLSEKELE RLSRRFFSEI QVLVGPQKDI PAPDVNTNAK IMAWYMDTYS MNVGYTALGV
VTGKPLDLGG SEGRPEATGR GVAITANEAC KALGKDISKA TVAIQGFGNV GSYSAKILSE
EFGAKIVAVS DVSGGLYNEN GLDINDLIAY RDANKGLIKG YPKAKPITNE ELLELDVDIL
VPAALENAIT EKNASNIKAK IIVEGANGPT TPEAEEILIK KGVLIVPDIL ANAGGVTVSY
FEWVQDLQTF FWDIDDIRKK LTKMMVNAFA EVYKTKEKYN TDMRTAAYIV AINRVANAVK
ERGYYPM
//
