ID F4GDP5_ALIDK Unreviewed; 430 AA.
AC F4GDP5;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 61.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN OrderedLocusNames=Alide2_0190 {ECO:0000313|EMBL:AEB82628.1};
OS Alicycliphilus denitrificans (strain DSM 14773 / CIP 107495 / K601).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Alicycliphilus.
OX NCBI_TaxID=596154 {ECO:0000313|EMBL:AEB82628.1, ECO:0000313|Proteomes:UP000007938};
RN [1] {ECO:0000313|EMBL:AEB82628.1, ECO:0000313|Proteomes:UP000007938}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14773 / CIP 107495 / K601
RC {ECO:0000313|Proteomes:UP000007938};
RX PubMed=21742888; DOI=10.1128/JB.00365-11;
RA Oosterkamp M.J., Veuskens T., Plugge C.M., Langenhoff A.A., Gerritse J.,
RA van Berkel W.J., Pieper D.H., Junca H., Goodwin L.A., Daligault H.E.,
RA Bruce D.C., Detter J.C., Tapia R., Han C.S., Land M.L., Hauser L.J.,
RA Smidt H., Stams A.J.;
RT "Genome Sequences of Alicycliphilus denitrificans Strains BC and K601T.";
RL J. Bacteriol. 193:5028-5029(2011).
RN [2] {ECO:0000313|EMBL:AEB82628.1, ECO:0000313|Proteomes:UP000007938}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14773 / CIP 107495 / K601
RC {ECO:0000313|Proteomes:UP000007938};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Zeytun A., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Oosterkamp M.,
RA Pieper D., van Berkel W., Langenhoff A., Smidt H., Stams A., Woyke T.;
RT "Complete sequence of chromosome of Alicycliphilus denitrificans K601.";
RL Submitted (APR-2011) 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; CP002657; AEB82628.1; -; Genomic_DNA.
DR RefSeq; WP_013517124.1; NC_015422.1.
DR AlphaFoldDB; F4GDP5; -.
DR STRING; 596154.Alide2_0190; -.
DR KEGG; adk:Alide2_0190; -.
DR eggNOG; COG0334; Bacteria.
DR HOGENOM; CLU_025763_1_2_4; -.
DR OMA; WLQNRNG; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000007938; 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:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
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 NADP {ECO:0000256|ARBA:ARBA00022857};
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:UP000007938}.
FT DOMAIN 197..427
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 120
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT BINDING 84
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 108
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 204
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 235
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 363
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT SITE 160
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ SEQUENCE 430 AA; 46047 MW; 6F6284740C8E1671 CRC64;
MTSPSGTHPL PSYLDPNHLG PWGVYLQQVD RVTPYLGNLA RWVETLKRPK RALIVDVPIE
LDNGTIAHFE GYRVQHNVSR GPGKGGVRFH QDVTLSEVMA LSAWMSIKNA AVNVPYGGAK
GGIRVDPKTL SRGELERLTR RYTSEIGIII GPSKDIPAPD VNTNAQVMAW MMDTYSMNVG
TTATGVVTGK PVDLGGSLGR VEATGRGVFT VGVEAARLTG MPIEGARVAV QGFGNVGGTA
GRLFSEAGAK VVAVQDHTGT IHNDKGLDVP ALLAHVQQTG GVAGFAGAEP MADDAFWGVA
CDILIPAALE SQITKDNAGR IQARMVIEGA NGPTTPEADD ILHDKGVLVL PDVIANAGGV
TVSYFEWVQD FSSFFWTEDE INARLVRIMK EAFAGVWNVA QENKVSLRTA TFIVACKRIL
HAREMRGLYP
//