DHPH_CALTT
ID DHPH_CALTT Reviewed; 370 AA.
AC F5L9G2;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Phenylalanine dehydrogenase {ECO:0000303|Ref.2};
DE Short=PheDH {ECO:0000303|Ref.2};
DE EC=1.4.1.20 {ECO:0000269|Ref.2};
GN ORFNames=CathTA2_2466 {ECO:0000312|EMBL:EGL81949.1};
OS Caldalkalibacillus thermarum (strain TA2.A1).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Caldalkalibacillus.
OX NCBI_TaxID=986075;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TA2.A1;
RX PubMed=21685297; DOI=10.1128/jb.05035-11;
RA Kalamorz F., Keis S., McMillan D.G., Olsson K., Stanton J.A., Stockwell P.,
RA Black M.A., Klingeman D.M., Land M.L., Han C.S., Martin S.L., Becher S.A.,
RA Peddie C.J., Morgan H.W., Matthies D., Preiss L., Meier T., Brown S.D.,
RA Cook G.M.;
RT "Draft genome sequence of the thermoalkaliphilic Caldalkalibacillus
RT thermarum strain TA2.A1.";
RL J. Bacteriol. 193:4290-4291(2011).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PROTEIN
RP ENGINEERING, AND BIOTECHNOLOGY.
RX DOI=10.1021/acscatal.7b00516;
RA Pushpanath A., Siirola E., Bornadel A., Woodlock D., Schell U.;
RT "Understanding and overcoming the limitations of Bacillus badius and
RT Caldalkalibacillus thermarum amine dehydrogenases for biocatalytic
RT reductive amination.";
RL ACS Catal. 7:3204-3209(2017).
CC -!- FUNCTION: Catalyzes the reversible NAD(+)-dependent oxidative
CC deamination of L-phenylalanine to phenylpyruvate. {ECO:0000269|Ref.2}.
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|Ref.2};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.71 mM for phenylpyruvate {ECO:0000269|Ref.2};
CC KM=10.24 mM for ketoleucine {ECO:0000269|Ref.2};
CC KM=0.88 mM for 2-oxo-4-phenylbutyrate {ECO:0000269|Ref.2};
CC KM=38.2 uM for NADH {ECO:0000269|Ref.2};
CC KM=157.9 mM for NH(3) {ECO:0000269|Ref.2};
CC Note=kcat is 74.8 sec(-1) with phenylpyruvate as substrate. kcat is
CC 56.2 sec(-1) with ketoleucine as substrate. kcat is 2.2 sec(-1) with
CC 2-oxo-4-phenylbutyrate as substrate. {ECO:0000269|Ref.2};
CC Temperature dependence:
CC Thermostable. Has a melting point (Tm) of 85.5 degrees Celsius.
CC {ECO:0000269|Ref.2};
CC -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis; L-
CC phenylalanine from phenylpyruvate (PDH route): step 1/1. {ECO:0000305}.
CC -!- BIOTECHNOLOGY: This enzyme has been engineered to lead to an amine
CC dehydrogenase able to catalyze the direct asymmetric reductive
CC amination of ketones using ammonia as the sole amino donor. This
CC reaction is a highly desirable transformation for the synthesis of
CC chiral amine intermediates, particularly for the pharmaceuticals
CC industry. {ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC {ECO:0000305}.
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DR EMBL; AFCE01000158; EGL81949.1; -; Genomic_DNA.
DR RefSeq; WP_007505854.1; NZ_AFCE01000158.1.
DR AlphaFoldDB; F5L9G2; -.
DR SMR; F5L9G2; -.
DR STRING; 986075.CathTA2_2466; -.
DR EnsemblBacteria; EGL81949; EGL81949; CathTA2_2466.
DR eggNOG; COG0334; Bacteria.
DR OrthoDB; 1184827at2; -.
DR UniPathway; UPA00121; UER00346.
DR Proteomes; UP000010716; Unassembled WGS sequence.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
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; Nucleotide-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..370
FT /note="Phenylalanine dehydrogenase"
FT /id="PRO_0000445469"
FT ACT_SITE 80
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q59771"
FT BINDING 44
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q59771"
FT BINDING 68
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q59771"
FT BINDING 114..115
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q59771"
FT BINDING 115
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q59771"
FT BINDING 146
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q59771"
FT BINDING 150
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q59771"
FT BINDING 180..186
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q59771"
FT BINDING 203..204
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q59771"
FT BINDING 243..244
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q59771"
FT BINDING 264..266
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q59771"
FT BINDING 266
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q59771"
SQ SEQUENCE 370 AA; 40555 MW; 33B892C39148301B CRC64;
MSTVTFDQIS EHEQVMFCND PHTGLKAIIA IHNTTLGPAL GGCRMLPYKS EEEALTDVLR
LSKGMTYKCV AADVDFGGGK AVIIGDPRKD KTPELFRAFG QFVQSLNGRF YTGTDMGTTP
EDFVQAYKET SFIVGLPEEY GGNGDSSVTT AFGVMQGLRA VSQFLWGTDV LTERVFAVQG
LGKVGFKVAE GLLKEGANVY VTDVDPETIA KLEEKAYQYP GHVQAVTADD IYGVGADVFV
PCAIGGIIND ETIERLKVKA VCGAANNQLL EDRHGKVLQA KNILYAPDYI VNAGGLIQVS
DELYGPNKAR VLKKTRALYD TLFEIFQSAE KKAVSTVEAA NQFVEERLQK RARLNSFFSP
DNPPKWRVRR
