ID A0A370KB85_9GAMM Unreviewed; 367 AA.
AC A0A370KB85;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Glu/Leu/Phe/Val dehydrogenase {ECO:0000313|EMBL:RDI99915.1};
GN ORFNames=DVT68_03560 {ECO:0000313|EMBL:RDI99915.1};
OS Dyella solisilvae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Dyella.
OX NCBI_TaxID=1920168 {ECO:0000313|EMBL:RDI99915.1, ECO:0000313|Proteomes:UP000254711};
RN [1] {ECO:0000313|EMBL:RDI99915.1, ECO:0000313|Proteomes:UP000254711}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DHG54 {ECO:0000313|EMBL:RDI99915.1,
RC ECO:0000313|Proteomes:UP000254711};
RA Gao Z., Qiu L.;
RT "Dyella solisilvae sp. nov., isolated from the pine and broad-leaved mixed
RT forest soil.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reversible oxidative deamination of glutamate
CC to alpha-ketoglutarate and ammonia. {ECO:0000256|ARBA:ARBA00003868}.
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:RDI99915.1}.
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DR EMBL; QQSY01000001; RDI99915.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A370KB85; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000254711; 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; IPR033524; Glu/Leu/Phe/Val_DH_AS.
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; 1.
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.
DR PROSITE; PS00074; GLFV_DEHYDROGENASE; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000188-2};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000188-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU004417}.
FT DOMAIN 143..350
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 79
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000188-1"
FT BINDING 179..184
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000188-2"
SQ SEQUENCE 367 AA; 39938 MW; 0A5EB24D98642BE5 CRC64;
MIFETIANTG HEEVVFCHNK DAGLKAIIAI HNTVLGPSLG GLRMWPYKSE QDAVNDVLRL
SRGMTYKNAV AGLNLGGGKA VIIGDPSKDK SEALFRAFGR FVNSLNGRYI TAEDVGIDVN
DMEYVFRETE YVTGVHQVHG GSGDPSPFTA FGTLQGLMAA LQVKHGNEDV GKYSYAVQGC
GHVGSEFIKL LREQGAKVFV TDINKDAVQR CVDELGCEAV GLDEIYDVDA DVYSPCALGG
TLNEQTIDRI KAKIICGAAN NQLATDAIGD ELQRRGVLYA PDYAVNAGGV MNVSLEIDGY
NRERAMRMMR TIYYNLGRIF EISKTQGVPT YKAADRLAEE RIDAIGKIKL PSMGNHGPRF
AGRMRGQ
//