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Database: UniProt
Entry: A0A370KB85_9GAMM
LinkDB: A0A370KB85_9GAMM
Original site: A0A370KB85_9GAMM 
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
//
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