ID A0A2S8B6Y3_9SPHN Unreviewed; 350 AA.
AC A0A2S8B6Y3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Amino acid dehydrogenase {ECO:0000313|EMBL:PQM28019.1};
GN ORFNames=CVO77_05685 {ECO:0000313|EMBL:PQM28019.1};
OS Sphingopyxis lindanitolerans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=2054227 {ECO:0000313|EMBL:PQM28019.1, ECO:0000313|Proteomes:UP000238954};
RN [1] {ECO:0000313|Proteomes:UP000238954}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WS5A3p {ECO:0000313|Proteomes:UP000238954};
RA Kaminski M.A.;
RT "The complete genome sequence of Sphingopyxis pomeranensis sp. nov. strain
RT WS5A3p.";
RL Submitted (NOV-2017) 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:PQM28019.1}.
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DR EMBL; PHFW01000002; PQM28019.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S8B6Y3; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000238954; 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:UP000238954}.
FT DOMAIN 144..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 350 AA; 36134 MW; 64056F8E27865950 CRC64;
MVARPTRLAP PVECVRLHDP ESGLDGVIAI HSTTLGPGAG GCRFWAYPGI DEALADALRL
AEGMSYKNAL AGLPLGGAKA VLRKPEGAFD RAKLFRAFGR AVEQLGGAYV TAEDVGTSVA
DMQEVARTTR HVAGLPPAAG RAGGDPSPWT ARGVFESMRA AARFALDTDL AGLTVAVQGT
GNVGADLCRH LADAGARLVI ADPNPARRDR LRAILGAEVV DVGEIASARA EIFAPCALGG
ALNRDSVRAM KAKLVCGAAN NQLASPEVAD MLRDRGIAYA PDYVVNAGGI ISVSAEYLGE
NESDVEARVA QIAPRVTALL DRAAREGRSP ALVADDMAEA VIAGGERVAA
//
