ID   DHPH_SPOUR              Reviewed;         379 AA.
AC   P97014;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   02-SEP-2026, entry version 93.
DE   RecName: Full=Phenylalanine dehydrogenase {ECO:0000303|Ref.1};
DE            Short=PheDH;
DE            EC=1.4.1.20 {ECO:0000250|UniProtKB:Q59771};
GN   Name=pdh;
OS   Sporosarcina ureae.
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Caryophanaceae;
OC   Sporosarcina.
OX   NCBI_TaxID=1571;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=R04;
RA   Asano Y.;
RT   "Phenylalanine dehydrogenase.";
RL   Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible NAD(+)-dependent oxidative
CC       deamination of L-phenylalanine to phenylpyruvate.
CC       {ECO:0000250|UniProtKB:Q59771}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-phenylalanine + NAD(+) + H2O = 3-phenylpyruvate + NH4(+) +
CC         NADH + H(+); 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:0000250|UniProtKB:Q59771};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis; L-
CC       phenylalanine from phenylpyruvate (PDH route): step 1/1.
CC       {ECO:0000250|UniProtKB:Q59771}.
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000305}.
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DR   EMBL; AB001031; BAA19221.1; -; Genomic_DNA.
DR   AlphaFoldDB; P97014; -.
DR   SMR; P97014; -.
DR   eggNOG; COG0334; Bacteria.
DR   UniPathway; UPA00121; UER00346.
DR   GO; GO:0050175; F:L-phenylalanine dehydrogenase (NAD+) activity; ISS:UniProtKB.
DR   GO; GO:0009094; P:L-phenylalanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd01075; NAD_bind_Leu_Phe_Val_DH; 1.
DR   FunFam; 3.40.50.10860:FF:000010; Leucine dehydrogenase; 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; Oxidoreductase.
FT   CHAIN           1..379
FT                   /note="Phenylalanine dehydrogenase"
FT                   /id="PRO_0000182808"
FT   ACT_SITE        92
FT                   /evidence="ECO:0000250|UniProtKB:Q59771,
FT                   ECO:0000255|PROSITE-ProRule:PRU10011"
FT   BINDING         56
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q59771"
FT   BINDING         80
FT                   /ligand="L-phenylalanine"
FT                   /ligand_id="ChEBI:CHEBI:58095"
FT                   /evidence="ECO:0000250|UniProtKB:Q59771"
FT   BINDING         127
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q59771"
FT   BINDING         158
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q59771"
FT   BINDING         162
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q59771"
FT   BINDING         192..198
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q59771"
FT   BINDING         215..216
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q59771"
FT   BINDING         252..253
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q59771"
FT   BINDING         273..275
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q59771"
FT   BINDING         275
FT                   /ligand="L-phenylalanine"
FT                   /ligand_id="ChEBI:CHEBI:58095"
FT                   /evidence="ECO:0000250|UniProtKB:Q59771"
SQ   SEQUENCE   379 AA;  41329 MW;  3764391A07B4C0A8 CRC64;
     MILVTLEQTL QDDKASVLDK MVEHEQILFC HDKATGLQAI IAVHDTTMGP ALGGCRMAPY
     KTMDLALKDV LRLSKGMTYK CAAADVDFGG GKSVIIGDPL KDKTPEKFRA FGQFIESLNG
     RFYTGTDMGT TLEDFVHAMK ETNYIVGKPV EYGGGGDSSI PTALGVFYGI KATNQNLFGD
     DKVEGRKYSI QGLGKVGYKV AEHIINEGGN VIVTDINEQA IADIQKLGGS AVRVVSSEEI
     YSQQADVFVP CAFGGVINDD TLKVLKVRGI SGSANNQLAE SRHGELLREK GILYAPDYIV
     NGGGLIQVAD ELYGTNPARV LAKTENIYTS LLEVFHQAEQ DHMTTATAAD RMCEKRIADA
     KNRNSFFTQS NRPKWNFHQ
//