ID A0A395LQG3_9SPHN Unreviewed; 354 AA.
AC A0A395LQG3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Glu/Leu/Phe/Val dehydrogenase {ECO:0000313|EMBL:RDS78687.1};
GN ORFNames=DL238_12235 {ECO:0000313|EMBL:RDS78687.1};
OS Alteriqipengyuania lutimaris.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Alteriqipengyuania.
OX NCBI_TaxID=1538146 {ECO:0000313|EMBL:RDS78687.1, ECO:0000313|Proteomes:UP000254101};
RN [1] {ECO:0000313|EMBL:RDS78687.1, ECO:0000313|Proteomes:UP000254101}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S-5 {ECO:0000313|EMBL:RDS78687.1,
RC ECO:0000313|Proteomes:UP000254101};
RA Chen X., Liu J.;
RT "Erythrobacter nanhaiensis sp. nov., a novel member of the genus
RT Erythrobacter isolated from the South China Sea.";
RL Submitted (JUL-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}.
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:RDS78687.1}.
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DR EMBL; QRBB01000001; RDS78687.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395LQG3; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000254101; 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}.
FT DOMAIN 146..354
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 81
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000188-1"
FT BINDING 182..187
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000188-2"
SQ SEQUENCE 354 AA; 37168 MW; 1E8468AD5FE93E63 CRC64;
MNAFWTEPDF DDHEVVHFVR DEKRGLTAII ALHSTHLGPA AGGTRFWHYA KPGDAMRDAL
RLSRGMSYKN AMAGLPMGGG KAVILADEDR RKTPEMLAAF GDAVNGLGGK YVTAEDVGIT
VADMVAVNQR TDHVSGLPVA EGEAGGNPGP FTALGIYLGI KAAVQHKLGT DSVEGVHVAM
QGIGSVGGGV ARLLAKDGAK LTLADIDADE VEALAQELGA DTVAPDAIMS VGCDVFSPNA
LGAILDEEGI ARLDCKIVAG GANNQLARPG NGTTLAQRGI LYAPDYVINA GGIISVTMEY
LCRRDDAPCD INEVRKRIAL IPERLTKIWQ DSEASGSSPD RVADAMAQEL IGRK
//
