ID A0A1U9K0G2_9BURK Unreviewed; 429 AA.
AC A0A1U9K0G2;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN ORFNames=PAEH1_07515 {ECO:0000313|EMBL:AQS51439.1};
OS Paenalcaligenes hominis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Paenalcaligenes.
OX NCBI_TaxID=643674 {ECO:0000313|EMBL:AQS51439.1, ECO:0000313|Proteomes:UP000189369};
RN [1] {ECO:0000313|EMBL:AQS51439.1, ECO:0000313|Proteomes:UP000189369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=15S00501 {ECO:0000313|EMBL:AQS51439.1,
RC ECO:0000313|Proteomes:UP000189369};
RA Mukhopadhyay R., Joaquin J., Hogue R., Kilaru A., Jospin G., Mars K.,
RA Eisen J.A., Chaturvedi V.;
RT "Complete Genome Sequence of Paenalcaligenes hominis, Isolated from a
RT paraplegic Patient with neurogenic bladder.";
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
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; CP019697; AQS51439.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1U9K0G2; -.
DR STRING; 643674.PAEH1_07515; -.
DR KEGG; phn:PAEH1_07515; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000189369; 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; cd01076; NAD_bind_1_Glu_DH; 1.
DR Gene3D; 1.10.8.1210; -; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000189369}.
FT DOMAIN 196..426
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 119
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT BINDING 83
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 107
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 203
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 234
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 362
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT SITE 159
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ SEQUENCE 429 AA; 46400 MW; B20479F204406BB4 CRC64;
MNQPTQHDLP TYLNPDDLGP WGIYLEQVER VTPYLGKLGK WVETLKRPKR ILTVDVPVEL
DNGTIAHFEG YRVQHNMARG PGKGGVRYHQ DVTLSEVMAL SAWMSVKCAA VNVPFGGAKG
GIRINPRNYS QKELERVTRR YISEISLIIG PDQDIPAPDV NTNGQTMAWM MDTYAMKTGH
LATGVVTGKP ISLGGSLGRV EATGRGVFTV GVEAARELGL DLTGARVVVQ GCGNVGGIAA
LLFHEAGAKV IALQDHTASI YAENGLDVPT ILANNNPKIG LAGSNAGEII SADEFWELES
DILIPAALEN QITANNADRL RTKIVIEGAN GPTTPEADDI LASKGILVIP DVIANAGGVT
VSYFEWAQNF SSYFWEEDVI NERLGKMMRE AYQATAAVAK HHNVTLRTAA FISACSRILE
ARELRGLYP
//
