ID A0A0B1ZRU6_9SPHN Unreviewed; 350 AA.
AC A0A0B1ZRU6;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Amino acid dehydrogenase {ECO:0000313|EMBL:KHK93306.1};
GN ORFNames=LK12_03090 {ECO:0000313|EMBL:KHK93306.1};
OS Novosphingobium malaysiense.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1348853 {ECO:0000313|EMBL:KHK93306.1, ECO:0000313|Proteomes:UP000031057};
RN [1] {ECO:0000313|EMBL:KHK93306.1, ECO:0000313|Proteomes:UP000031057}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUSC 273 {ECO:0000313|EMBL:KHK93306.1,
RC ECO:0000313|Proteomes:UP000031057};
RA Lee L.-H.;
RT "Genome sequence of Novosphingobium malaysiense MUSC 273(T).";
RL Submitted (OCT-2014) 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:KHK93306.1}.
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DR EMBL; JTDI01000001; KHK93306.1; -; Genomic_DNA.
DR RefSeq; WP_039279186.1; NZ_JTDI01000001.1.
DR AlphaFoldDB; A0A0B1ZRU6; -.
DR STRING; 1348853.LK12_03090; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000031057; 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; 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.
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:UP000031057}.
FT DOMAIN 144..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 350 AA; 36723 MW; EE38222675585E5D CRC64;
MVTAAHRMMP PMEYVRLHDE AAGLDGVIAI HSTARGPAAG GCRLWTYPDA NAAMVDAFRL
AEGMSYKNAM AELPFGGGKA VLRKPEGKFD RRALFEAFGA AIEKLDGRYV TAEDVGTSVA
DMEFVANKTR HVAGRTSRPG FAGGDPSPWT ALGVFEAMKA AVQFRFGSGL SGVTVAVQGV
GNVGGDLCRR LHEAGARLIL ADIDAERCTA LAREFDADVA SIDDIAQADA DVFAPCALGG
ALNEKSVASL KAGLVCGAAN NQLAEPGIAK TLLERGIAYA PDYVVNAGGI INVSAEYLGE
SVEDVRTRTM KIGPRTAGIL EEAARDNLPP SVVADRMAER LMSRPIADVA
//
