ID   DHPH_LYSSH              Reviewed;         381 AA.
AC   P23307;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Phenylalanine dehydrogenase {ECO:0000303|PubMed:2838396};
DE            Short=PheDH {ECO:0000303|PubMed:2838396};
DE            EC=1.4.1.20 {ECO:0000269|PubMed:2838396};
GN   Name=pdh {ECO:0000303|PubMed:2838396};
OS   Lysinibacillus sphaericus (Bacillus sphaericus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX   NCBI_TaxID=1421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, AND FUNCTION.
RX   PubMed=2838396; DOI=10.1016/0378-1119(88)90537-9;
RA   Okazaki N., Hibino Y., Asano Y., Ohmori M., Numao N., Kondo K.;
RT   "Cloning and nucleotide sequencing of phenylalanine dehydrogenase gene of
RT   Bacillus sphaericus.";
RL   Gene 63:337-341(1988).
CC   -!- FUNCTION: Catalyzes the reversible NAD(+)-dependent oxidative
CC       deamination of L-phenylalanine to phenylpyruvate.
CC       {ECO:0000269|PubMed:2838396}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-phenylalanine + NAD(+) = 3-phenylpyruvate + H(+) +
CC         NADH + NH4(+); Xref=Rhea:RHEA:21408, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:18005, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58095; EC=1.4.1.20;
CC         Evidence={ECO:0000269|PubMed:2838396};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis; L-
CC       phenylalanine from phenylpyruvate (PDH route): step 1/1.
CC       {ECO:0000269|PubMed:2838396}.
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000305}.
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DR   EMBL; M26661; AAA22646.1; -; Genomic_DNA.
DR   PIR; I39939; I39939.
DR   AlphaFoldDB; P23307; -.
DR   SMR; P23307; -.
DR   SABIO-RK; P23307; -.
DR   UniPathway; UPA00121; UER00346.
DR   GO; GO:0050175; F:phenylalanine dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009094; P:L-phenylalanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR046346; Aminiacid_DH-like_N_sf.
DR   InterPro; IPR006095; Glu/Leu/Phe/Val_DH.
DR   InterPro; IPR033524; Glu/Leu/Phe/Val_DH_AS.
DR   InterPro; IPR006096; Glu/Leu/Phe/Val_DH_C.
DR   InterPro; IPR006097; Glu/Leu/Phe/Val_DH_dimer_dom.
DR   InterPro; IPR016211; Glu/Phe/Leu/Val_DH_bac/arc.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR42722; PTHR42722; 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; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF53223; SSF53223; 1.
DR   PROSITE; PS00074; GLFV_DEHYDROGENASE; 1.
PE   1: Evidence at protein level;
KW   NAD; Oxidoreductase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000305|PubMed:2838396"
FT   CHAIN           2..381
FT                   /note="Phenylalanine dehydrogenase"
FT                   /id="PRO_0000182807"
FT   ACT_SITE        91
FT                   /evidence="ECO:0000250|UniProtKB:Q59771,
FT                   ECO:0000255|PROSITE-ProRule:PRU10011"
FT   BINDING         55
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q59771"
FT   BINDING         79
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q59771"
FT   BINDING         126
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q59771"
FT   BINDING         157
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q59771"
FT   BINDING         161
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q59771"
FT   BINDING         191..197
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q59771"
FT   BINDING         214..215
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q59771"
FT   BINDING         254..255
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q59771"
FT   BINDING         275..277
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q59771"
FT   BINDING         277
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q59771"
SQ   SEQUENCE   381 AA;  41578 MW;  D32450CE397ACA67 CRC64;
     MAKQLEKSSK IGNEDVFQKI ANHEQIVFCN DPVSGLQAII AIHDTTLGPA LGGTRMYPYK
     NVDEALEDVL RLSEGMTYKC AAADIDFGGG KAVIIGDPEK DKSPALFRAF GQFVESLNGR
     FYTGTDMGTT MDDFVHAQKE TNFINGIPEQ YGGSGDSSIP TAQGVIYALK ATNQYLFGSD
     SLSGKTYAIQ GLGKVGYKVA EQLLKAGADL FVTDIHENVL NSIKQKSEEL GGSVTIVKSD
     DIYSVQADIF VPCAMGGIIN DKTIPKLKVK AVVGSANNQL KDLRHANVLN EKGILYAPDY
     IVNAGGLIQV ADELYGPNKE RVLLKTKEIY RSLLEIFNQA ALDCITTVEA ANRKCQKTIE
     GQQTRNSFFS RGRRPKWNIK E