DHPH_SPOUR
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 03-AUG-2022, entry version 84.
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; Firmicutes; Bacilli; Bacillales; Planococcaceae; 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=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: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: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 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="substrate"
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="substrate"
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
