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Database: UniProt
Entry: A0A2R8B7P1_9RHOB
LinkDB: A0A2R8B7P1_9RHOB
Original site: A0A2R8B7P1_9RHOB 
ID   A0A2R8B7P1_9RHOB        Unreviewed;       349 AA.
AC   A0A2R8B7P1;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Leucine dehydrogenase {ECO:0000313|EMBL:SPH18618.1};
DE            EC=1.4.1.9 {ECO:0000313|EMBL:SPH18618.1};
GN   Name=ldh {ECO:0000313|EMBL:SPH18618.1};
GN   ORFNames=DEA8626_02158 {ECO:0000313|EMBL:SPH18618.1};
OS   Defluviimonas aquaemixtae.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Defluviimonas.
OX   NCBI_TaxID=1542388 {ECO:0000313|EMBL:SPH18618.1, ECO:0000313|Proteomes:UP000244924};
RN   [1] {ECO:0000313|EMBL:SPH18618.1, ECO:0000313|Proteomes:UP000244924}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 8626 {ECO:0000313|EMBL:SPH18618.1,
RC   ECO:0000313|Proteomes:UP000244924};
RA   Keele B.F.;
RL   Submitted (MAR-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}.
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DR   EMBL; OMOQ01000001; SPH18618.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2R8B7P1; -.
DR   OrthoDB; 9803297at2; -.
DR   Proteomes; UP000244924; 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; 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.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000244924}.
FT   DOMAIN          143..348
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   349 AA;  36440 MW;  AED749A34CFE3148 CRC64;
     MRITAIDAEE HEEVYRVEDA EAGLKGFIAV HSTRLGPAAG GLRMRVYRCD DEALRDVLNL
     SRGMTFKNAA ADLPLGGGKA VIIGDPSHDK TPAILRAMGR AIGQLEGRYW TAEDMGMTPD
     DMAVIAAETP FVAGLAGGDF ASGDPSPVTA LGVFNAVRRA TRHRLGYDSL YGLTVSVQGL
     GNVGRHLAQL VHGDGAHLVV TDIDPARVAA AIAEWGAEAA AEDDIYKTGA DIFAPCAIGG
     VLNAETIPQL RARVVVGAAN NQLATPADGD RMAQRGILYA PDFVANGGGI INVAAEILKV
     ADRPSWVASK LTALDATMEA ILVAARTEGV SPNAVAERIV AERMSRAAA
//
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