DHPH_THEIN
ID DHPH_THEIN Reviewed; 366 AA.
AC P22823;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Phenylalanine dehydrogenase {ECO:0000303|PubMed:1880121};
DE Short=PheDH {ECO:0000303|PubMed:1880121};
DE EC=1.4.1.20 {ECO:0000269|PubMed:1880121};
GN Name=pdh {ECO:0000303|PubMed:1880121};
OS Thermoactinomyces intermedius.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Thermoactinomycetaceae;
OC Thermoactinomyces.
OX NCBI_TaxID=2024;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-16, PATHWAY,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND FUNCTION.
RC STRAIN=ATCC 33205 / DSM 43846 / JCM 3312 / KCTC 9646 / NBRC 14230 / NRRL
RC B-16979 / VKM Ac-1427 / T-323;
RX PubMed=1880121; DOI=10.1093/oxfordjournals.jbchem.a123388;
RA Takada H., Yoshimura T., Ohshima T., Esaki N., Soda K.;
RT "Thermostable phenylalanine dehydrogenase of Thermoactinomyces intermedius:
RT cloning, expression, and sequencing of its gene.";
RL J. Biochem. 109:371-376(1991).
CC -!- FUNCTION: Catalyzes the reversible NAD(+)-dependent oxidative
CC deamination of L-phenylalanine to phenylpyruvate.
CC {ECO:0000269|PubMed:1880121}.
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:1880121};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Thermostable. {ECO:0000305|PubMed:1880121};
CC -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis; L-
CC phenylalanine from phenylpyruvate (PDH route): step 1/1.
CC {ECO:0000269|PubMed:1880121}.
CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC {ECO:0000305}.
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DR EMBL; D00631; BAA00524.1; -; Genomic_DNA.
DR PIR; JQ0513; JQ0513.
DR AlphaFoldDB; P22823; -.
DR SMR; P22823; -.
DR BRENDA; 1.4.1.20; 6278.
DR SABIO-RK; P22823; -.
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 Direct protein sequencing; NAD; Oxidoreductase.
FT CHAIN 1..366
FT /note="Phenylalanine dehydrogenase"
FT /id="PRO_0000182809"
FT ACT_SITE 81
FT /evidence="ECO:0000250|UniProtKB:Q59771,
FT ECO:0000255|PROSITE-ProRule:PRU10011"
FT BINDING 45
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q59771"
FT BINDING 69
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q59771"
FT BINDING 116
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q59771"
FT BINDING 151
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q59771"
FT BINDING 181..187
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q59771"
FT BINDING 204..205
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q59771"
FT BINDING 241..242
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q59771"
FT BINDING 262..264
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q59771"
FT BINDING 264
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q59771"
SQ SEQUENCE 366 AA; 40488 MW; 67DFDD87F439D72B CRC64;
MRDVFEMMDR YGHEQVIFCR HPQTGLKAII ALHNTTAGPA LGGCRMIPYA STDEALEDVL
RLSKGMTYKC SLADVDFGGG KMVIIGDPKK DKSPELFRVI GRFVGGLNGR FYTGTDMGTN
PEDFVHAARE SKSFAGLPKS YGGKGDTSIP TALGVFHGMR ATARFLWGTD QLKGRVVAIQ
GVGKVGERLL QLLVEVGAYC KIADIDSVRC EQLKEKYGDK VQLVDVNRIH KESCDIFSPC
AKGGVVNDDT IDEFRCLAIV GSANNQLVED RHGALLQKRS ICYAPDYLVN AGGLIQVADE
LEGFHEERVL AKTEAIYDMV LDIFHRAKNE NITTCEAADR IVMERLKKLT DIRRILLEDP
RNSARR
