ID A0A3D8L8Q6_9BACT Unreviewed; 366 AA.
AC A0A3D8L8Q6;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Glu/Leu/Phe/Val dehydrogenase {ECO:0000313|EMBL:RDV13790.1};
GN ORFNames=DXT99_17290 {ECO:0000313|EMBL:RDV13790.1};
OS Pontibacter diazotrophicus.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Pontibacter.
OX NCBI_TaxID=1400979 {ECO:0000313|EMBL:RDV13790.1, ECO:0000313|Proteomes:UP000256708};
RN [1] {ECO:0000313|Proteomes:UP000256708}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H4X {ECO:0000313|Proteomes:UP000256708};
RA Liu Z.-W., Du Z.-J.;
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC {ECO:0000256|ARBA:ARBA00006382, ECO:0000256|RuleBase:RU004417}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RDV13790.1}.
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DR EMBL; QRGR01000020; RDV13790.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D8L8Q6; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000256708; Unassembled WGS sequence.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0016639; F:oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR CDD; cd01075; NAD_bind_Leu_Phe_Val_DH; 1.
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; IPR016211; Glu/Phe/Leu/Val/Trp_DH_bac/arc.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR42722; LEUCINE DEHYDROGENASE; 1.
DR PANTHER; PTHR42722:SF1; VALINE DEHYDROGENASE; 1.
DR Pfam; PF00208; ELFV_dehydrog; 2.
DR Pfam; PF02812; ELFV_dehydrog_N; 1.
DR PIRSF; PIRSF000188; Phe_leu_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:PIRSR000188-2};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000188-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU004417};
KW Reference proteome {ECO:0000313|Proteomes:UP000256708}.
FT DOMAIN 156..364
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 92
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000188-1"
FT BINDING 192..197
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000188-2"
SQ SEQUENCE 366 AA; 40083 MW; 5856E607F3382EBE CRC64;
MVELKEVKRK KDKSVFDLVS EHNHEKVVFC HDKDTGLKAI IGVHNTVLGP ALGGTRMWSY
ASEAEALDDV LRLSRAMTYK AAISGLNLGG GKAVIIGDAK KDKNEALLRR FGRFIKNLNG
SFITAEDVGM TTKDMEYIRM ETEHVCGLPE SRGGGGDPSP VSAYGTYMGM KAAAKKAFGS
DSLEGKRIAV QGVGHVGAYL VELLTKENVE IFVTDIYEDR LREVAKKFGA KVVGMDELYD
LDVDIYAPCG LGGTINDITI DRLKCKVIAG CANNQLRDEQ VHGPALVKKG IVYAPDFLIN
AGGLINVYSE LVGYNRDNAY AQTERIYGYT LDIFALAEKE GLHNQQAAMR LAEKRIESIG
KMRSTF
//
