ID A0A2S0I0K7_9FLAO Unreviewed; 365 AA.
AC A0A2S0I0K7;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Leucine dehydrogenase {ECO:0000313|EMBL:AVI52398.1};
GN ORFNames=C5O00_09910 {ECO:0000313|EMBL:AVI52398.1};
OS Pukyongia salina.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Pukyongia.
OX NCBI_TaxID=2094025 {ECO:0000313|EMBL:AVI52398.1, ECO:0000313|Proteomes:UP000238442};
RN [1] {ECO:0000313|EMBL:AVI52398.1, ECO:0000313|Proteomes:UP000238442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RR4-38 {ECO:0000313|EMBL:AVI52398.1,
RC ECO:0000313|Proteomes:UP000238442};
RA Kim Y.-S., Jang Y.H., Kim K.-H.;
RT "Genomic analysis of the strain RR4-38 isolated from a seawater
RT recirculating aquaculture system.";
RL Submitted (FEB-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; CP027062; AVI52398.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S0I0K7; -.
DR KEGG; aue:C5O00_09910; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000238442; Chromosome.
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:UP000238442}.
FT DOMAIN 158..365
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 94
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000188-1"
FT BINDING 194..199
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000188-2"
SQ SEQUENCE 365 AA; 40111 MW; 61DC847574CBAF94 CRC64;
MVTDLVNTNE LTKIDPVFGQ LSFDNHEQVV FCNDKDTGLR AIIGIHNTVL GPALGGTRMW
NYSSEWEALN DVLRLSRGMT FKSAITGLNL GGGKAVILGD ARTQKTPELM KRFGEFVHSL
SGKYITAEDV GMETADMDLV RTVTPYVTGI SEEKGGAGNP SPITAYGVFM GMKAAAKYAF
GTELLEDRTV YVQGIGNVGE ALVENLTNEG AKVFITDINS ERLEYVRDKY NVNIYEGENL
YSEEMDIYAP CALGATINDE TIDQLKAKVI AGAANNQLAN ELKHGLLLRE RGIVYAPDFL
INAGGIINVY AELENYGKQE IVRKTENIYN TTLEILQNAE TNDITTHQAA FEIAQSRIDA
RKTEK
//
