ID A0A1N6Z605_9BACI Unreviewed; 382 AA.
AC A0A1N6Z605;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Phenylalanine dehydrogenase {ECO:0000313|EMBL:SIR22282.1};
GN ORFNames=SAMN05443094_106111 {ECO:0000313|EMBL:SIR22282.1};
OS Domibacillus enclensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Domibacillus.
OX NCBI_TaxID=1017273 {ECO:0000313|EMBL:SIR22282.1, ECO:0000313|Proteomes:UP000186385};
RN [1] {ECO:0000313|EMBL:SIR22282.1, ECO:0000313|Proteomes:UP000186385}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIO-1016 {ECO:0000313|EMBL:SIR22282.1,
RC ECO:0000313|Proteomes:UP000186385};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-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}.
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DR EMBL; FTLX01000006; SIR22282.1; -; Genomic_DNA.
DR RefSeq; WP_045851169.1; NZ_MWSK01000006.1.
DR AlphaFoldDB; A0A1N6Z605; -.
DR STRING; 1017273.SAMN05443094_106111; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000186385; Unassembled WGS sequence.
DR GO; GO:0004353; F:glutamate dehydrogenase [NAD(P)+] activity; IEA:UniProt.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
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; 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.
DR PROSITE; PS00074; GLFV_DEHYDROGENASE; 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 159..364
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 92
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000188-1"
FT BINDING 192..197
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000188-2"
SQ SEQUENCE 382 AA; 41843 MW; 0BADE16FCEE94F84 CRC64;
MNKLPVAEQA PSLSFDLFEK MKDHEQVVFC NDPETGLKAI IAIHDTTLGP ALGGTRMRQY
ETMEDALEDA LRLSKGMTYK CAAADVDFGG GKAVIIGDPL KDKTPELFRA YGQFIETLNG
RFYTGTDMGT VLDDFVHAYK ETNCIAGLPE EYGGGGETSI PTALGVLYSI QAVAKTLWGH
EDLSGKKFAI QGLGKVGFKT AEHLLQAGAD LYVTDVDPCI VHVLTEKAEE MGRIAVSVSS
DDIYGVEADM FVPCAIGGII NDQTIDQLKV QAIVGAANNQ LLHESHAEKL KQKGILYAPD
YIVNGGGLIQ VADELYGPNR KRVLAKTEAI YRSLLEVFSQ SDALHVTTVE AANHICEKRM
DARKHRNSFF SPRKRNKWDV RL
//
