ID L7WAV9_NONDD Unreviewed; 447 AA.
AC L7WAV9;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN Name=gdhA2 {ECO:0000313|EMBL:AGC76048.1};
GN OrderedLocusNames=DDD_0921 {ECO:0000313|EMBL:AGC76048.1};
OS Nonlabens dokdonensis (strain DSM 17205 / KCTC 12402 / DSW-6) (Donghaeana
OS dokdonensis).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Nonlabens.
OX NCBI_TaxID=592029 {ECO:0000313|EMBL:AGC76048.1, ECO:0000313|Proteomes:UP000011173};
RN [1] {ECO:0000313|EMBL:AGC76048.1, ECO:0000313|Proteomes:UP000011173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17205 / KCTC 12402 / DSW-6
RC {ECO:0000313|Proteomes:UP000011173};
RX PubMed=23292138; DOI=10.1093/gbe/evs134;
RA Kwon S.K., Kim B.K., Song J.Y., Kwak M.J., Lee C.H., Yoon J.H., Oh T.K.,
RA Kim J.F.;
RT "Genomic makeup of the marine flavobacterium Nonlabens (Donghaeana)
RT dokdonensis DSW-6 and identification of a novel class of rhodopsins.";
RL Genome Biol. Evol. 5:187-187(2013).
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; CP001397; AGC76048.1; -; Genomic_DNA.
DR RefSeq; WP_015361545.1; NC_020156.1.
DR AlphaFoldDB; L7WAV9; -.
DR STRING; 592029.DDD_0921; -.
DR KEGG; ndo:DDD_0921; -.
DR PATRIC; fig|592029.3.peg.913; -.
DR eggNOG; COG0334; Bacteria.
DR HOGENOM; CLU_025763_2_1_10; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000011173; 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; 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; 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; 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.
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 202..445
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 126
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 114
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 165
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 209
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 240
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 379
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT SITE 166
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ SEQUENCE 447 AA; 49256 MW; 1438F92233711083 CRC64;
MEKNIQSFID LIKKKNPNEP EFIQAVEEVA EAVIPFIEEN KKYQSDKLLE RMAEPERVTM
FRVPWTDDNN EVHVNRGYRI QMNSAIGPYK GGLRFHPSVN LSILKFLAFE QVFKNSLTTL
PMGGGKGGSD FDPKGKSDRE VMRFCQSFMV ELQRVIGADT DVPAGDIGVG GREIGYLFGY
YKKLRNEFTG ILTGKGRSYG GSLIRPEATG YGNVYFAQNM LKTRGEEIKG KTTVISGSGN
VAQYAAEKIL QLGGKVVTMS DSGGYIYDEE GIDADKLAFI MDLKNNRRGR ISEYVDQYSN
ATYHDGERPW SVKCDIALPC ATQNELNGEE AKTLVSNGCI CVGEGANMPC TPEAIEHFLD
NKILFSPGKA SNAGGVATSG LEMSQNSMRY SWTAEEVDSK LHSIMNDIHE ACVEYGKDED
GFVDYVKGAN IAGFVKVADA MLAQGIV
//
