ID F0NJL9_SULIH Unreviewed; 419 AA.
AC F0NJL9;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN OrderedLocusNames=SiH_0598 {ECO:0000313|EMBL:ADX81956.1};
OS Sulfolobus islandicus (strain HVE10/4).
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=930943 {ECO:0000313|EMBL:ADX81956.1, ECO:0000313|Proteomes:UP000006395};
RN [1] {ECO:0000313|EMBL:ADX81956.1, ECO:0000313|Proteomes:UP000006395}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HVE10/4 {ECO:0000313|EMBL:ADX81956.1,
RC ECO:0000313|Proteomes:UP000006395};
RX PubMed=21278296; DOI=10.1128/JB.01487-10;
RA Guo L., Brugger K., Liu C., Shah S.A., Zheng H., Zhu Y., Wang S.,
RA Lillestol R.K., Chen L., Frank J., Prangishvili D., Paulin L., She Q.,
RA Huang L., Garrett R.A.;
RT "Genome analyses of icelandic strains of Sulfolobus islandicus, model
RT organisms for genetic and virus-host interaction studies.";
RL J. Bacteriol. 193:1672-1680(2011).
CC -!- SUBUNIT: Homohexamer. {ECO:0000256|ARBA:ARBA00011643}.
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; CP002426; ADX81956.1; -; Genomic_DNA.
DR RefSeq; WP_014512154.1; NC_017275.1.
DR AlphaFoldDB; F0NJL9; -.
DR GeneID; 78426920; -.
DR KEGG; sih:SiH_0598; -.
DR HOGENOM; CLU_025763_1_2_2; -.
DR Proteomes; UP000006395; 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; 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 186..417
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 108
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT BINDING 72
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 96
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 192
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 223
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 351
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT SITE 148
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ SEQUENCE 419 AA; 45415 MW; 0733158886709815 CRC64;
MEELLTSNLF VQQVKKLYKV GELLGLDIDT LEALSQPERV IQVKIQIRGS DGKLRTFVGW
RSQHNSALGP YKGGVRYSPN VTQEEVIALS MIMTWKNSLL LLPYGGGKGG IRVDPKKLTL
KELEDLSRKY IQLIHNYLGS NVDIPAPDIN TNPQTMAWFL DEYIKITGEV DFAVFTGKPS
ELGGIGVRLY STGLGVATIA REAANKFIGG IEGSRVIIQG FGNVGSFTAK FLSEMGAKII
GVSDIGGGVI NENGIDVNKA LEVAQRTGSV VNYPEGKKVT NEELLISDCD ILIPAAVENV
INKFNAPKVK AKLIVEGANG PLTADADDVI KQRGIVVIPD ILANAGGVVG SYVEWANNKS
GGIISDEEAK KLIIDRMTNA FNALYDFHKR KFADQDLRTV AMALAVDRVV KAMKARGLL
//
