ID D3EDK3_GEOS4 Unreviewed; 493 AA.
AC D3EDK3;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|ARBA:ARBA00012896, ECO:0000256|PIRNR:PIRNR000185};
GN OrderedLocusNames=GYMC10_4994 {ECO:0000313|EMBL:ACX67208.1};
OS Geobacillus sp. (strain Y412MC10).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=481743 {ECO:0000313|EMBL:ACX67208.1, ECO:0000313|Proteomes:UP000002381};
RN [1] {ECO:0000313|Proteomes:UP000002381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y412MC10 {ECO:0000313|Proteomes:UP000002381};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA Brumm P., Mead D.;
RT "Complete sequence of Geobacillus sp. Y412MC10.";
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACX67208.1, ECO:0000313|Proteomes:UP000002381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y412MC10 {ECO:0000313|EMBL:ACX67208.1,
RC ECO:0000313|Proteomes:UP000002381};
RX PubMed=23408395; DOI=10.4056/sigs.2605792;
RA Mead D.A., Lucas S., Copeland A., Lapidus A., Cheng J.F., Bruce D.C.,
RA Goodwin L.A., Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C.S.,
RA Tapia R., Land M., Hauser L.J., Chang Y.J., Kyrpides N.C., Ivanova N.N.,
RA Ovchinnikova G., Woyke T., Brumm C., Hochstein R., Schoenfeld T., Brumm P.;
RT "Complete Genome Sequence of Paenibacillus strain Y4.12MC10, a Novel
RT Paenibacillus lautus strain Isolated from Obsidian Hot Spring in
RT Yellowstone National Park.";
RL Stand. Genomic Sci. 6:381-400(2012).
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; CP001793; ACX67208.1; -; Genomic_DNA.
DR AlphaFoldDB; D3EDK3; -.
DR STRING; 481743.GYMC10_4994; -.
DR KEGG; gym:GYMC10_4994; -.
DR HOGENOM; CLU_025763_2_1_9; -.
DR Proteomes; UP000002381; Chromosome.
DR GO; GO:0004352; F:glutamate dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR CDD; cd05313; NAD_bind_2_Glu_DH; 1.
DR Gene3D; 1.10.285.10; Glutamate Dehydrogenase, chain A, domain 3; 2.
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; PTHR43571; NADP-SPECIFIC GLUTAMATE DEHYDROGENASE 1-RELATED; 1.
DR PANTHER; PTHR43571:SF1; NADP-SPECIFIC GLUTAMATE DEHYDROGENASE 1-RELATED; 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 250..491
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 173
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT BINDING 137
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 158
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 161
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 212
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 257
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 288
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 425
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT SITE 213
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ SEQUENCE 493 AA; 53936 MW; F9FF185250C4997B CRC64;
MVLYKWFKTG VPFLKHQRFF SQFYFNDLKE CITKVTTNIS VTSPFTAAQE YVESIYNQVV
ARDPHESEFH QAVREFVDSL VPVLAQHPKY REHGILERLV EPERMVTFRV PWVDDQGKTQ
VNRGFRVQFN SALGPYKGGI RFHPSVYAGI VKFLGFEQIF KNSLTGQPIG GGKGGSDFDP
KGKSDQEVMR FTQSFMTELY RHIGPDSDVP AGDIGVGARE IGYMFGQYKR IRGGHEAGVL
TGKGVIYGGS LARTEATGYG CVYFVQEMLA AKGLSFQDSR VVVSGSGNVS IYAIEKAQQL
GAHVIACSDS NGYLYDPEGI NLETVKLLKE RDRLRISEYV KIHPHAVYTE GCTGIWSLPC
DIALPCATQN ELDADAAKTL ISNGVKAIGE GANMPSTLEA IELFISKGVL FGPAKAANAG
GVAVSALEMS QNSMRMSWTF EEVDAKLHQI MKNIYNSAVD AAEEYGVAGN LVAGANIAGF
IKVADAMIAQ GIV
//
