ID A0A0K1NDC8_9BURK Unreviewed; 448 AA.
AC A0A0K1NDC8;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN ORFNames=ADJ79_05960 {ECO:0000313|EMBL:AKU66883.1};
OS Ottowia sp. oral taxon 894.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Ottowia.
OX NCBI_TaxID=1658672 {ECO:0000313|EMBL:AKU66883.1, ECO:0000313|Proteomes:UP000056623};
RN [1] {ECO:0000313|Proteomes:UP000056623}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W10237 {ECO:0000313|Proteomes:UP000056623};
RA Holder M.E., Ajami N.J., Petrosino J.F.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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; CP012073; AKU66883.1; -; Genomic_DNA.
DR RefSeq; WP_050715192.1; NZ_CP012073.1.
DR AlphaFoldDB; A0A0K1NDC8; -.
DR STRING; 1658672.ADJ79_05960; -.
DR KEGG; oto:ADJ79_05960; -.
DR PATRIC; fig|1658672.3.peg.1577; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000056623; 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 204..446
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 128
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT BINDING 92
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 113
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 167
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 211
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 242
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 380
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT SITE 168
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ SEQUENCE 448 AA; 48525 MW; 83ED07113145BC67 CRC64;
MTATTSLEDF LRNVQRRDPD QPEFLQAVRE VLTSLWPFLE KNPQYREYAL LERLCEPDRV
VQFRVSWTDD QGRTQVNRAF RIQHSKAIGP YKGGMRFHPS VNLSILKFLA FEQSFKNALT
TLPMGGGKGG SDFDPKGKSD AEVMRFCQAL VQELFRHIGP DTDVPAGDIG VGAREVGYMA
GMMKKLSNSA ACVFTGKGMS FGGSLMRPEA TGYGVAYFAQ EMLARKSEGF EGKRVSISGS
GNVAQYAAEK ALEMGAKVIT LSDSGGTLVH EAGLSREQVL AVMELKNVQR GRLADFAARH
GLTFLPGSRP WHVKTDIALP CATQNELDGE DAKTLVKNGV LCVAEGANMP STLEAVDVFL
AAGTLYAPGK ASNAGGVATS GLEMSQNAMR LGWTAQEVDE RLHAIMKDIH QNCVRYGERA
QGAVNYVEGA NIAGFVKLAD AMLAQGVV
//
