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Phenylalanine dehydrogenase (PheDH) (EC 1.4.1.20)

 DHPH_RHOSO              Reviewed;         356 AA.
Q59771;
11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 2.
10-MAY-2017, entry version 87.
RecName: Full=Phenylalanine dehydrogenase {ECO:0000303|PubMed:10029526, ECO:0000303|PubMed:10924111};
Short=PheDH;
EC=1.4.1.20 {ECO:0000269|PubMed:10924111, ECO:0000269|PubMed:8206922};
Name=pdh {ECO:0000303|PubMed:8206922, ECO:0000312|EMBL:AAA21461.1};
Rhodococcus sp.
Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
Rhodococcus.
NCBI_TaxID=1831 {ECO:0000312|EMBL:AAA21461.1};
[1] {ECO:0000312|EMBL:AAA21461.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-38; 90-95;
97-114 AND 300-312, FUNCTION, AND CATALYTIC ACTIVITY.
STRAIN=M4 {ECO:0000312|EMBL:AAA21461.1};
PubMed=8206922;
Brunhuber N.M., Banerjee A., Jacobs W.R. Jr., Blanchard J.S.;
"Cloning, sequencing, and expression of Rhodococcus L-phenylalanine
dehydrogenase. Sequence comparisons to amino-acid dehydrogenases.";
J. Biol. Chem. 269:16203-16211(1994).
[2] {ECO:0000244|PDB:1BW9, ECO:0000244|PDB:1BXG}
X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEXES WITH NAD;
PHENYLPROPIONATE AND KETO-PHENYLPYRUVATE, AND SUBUNIT.
PubMed=10029526; DOI=10.1021/bi982244q;
Vanhooke J.L., Thoden J.B., Brunhuber N.M., Blanchard J.S.,
Holden H.M.;
"Phenylalanine dehydrogenase from Rhodococcus sp. M4: high-resolution
X-ray analyses of inhibitory ternary complexes reveal key features in
the oxidative deamination mechanism.";
Biochemistry 38:2326-2339(1999).
[3] {ECO:0000244|PDB:1C1D, ECO:0000244|PDB:1C1X}
X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 2-356 IN COMPLEX WITH NAD
AND SUBSTRATE, FUNCTION, PATHWAY, CATALYTIC ACTIVITY, ENZYME
REGULATION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVE SITE.
PubMed=10924111; DOI=10.1021/bi000494c;
Brunhuber N.M., Thoden J.B., Blanchard J.S., Vanhooke J.L.;
"Rhodococcus L-phenylalanine dehydrogenase: kinetics, mechanism, and
structural basis for catalytic specificity.";
Biochemistry 39:9174-9187(2000).
-!- FUNCTION: Catalyzes the reversible, NAD-dependent deamination of
L-phenylalanine to phenyl pyruvate, ammonia and NADH.
{ECO:0000269|PubMed:10924111, ECO:0000269|PubMed:8206922}.
-!- CATALYTIC ACTIVITY: L-phenylalanine + H(2)O + NAD(+) =
phenylpyruvate + NH(3) + NADH. {ECO:0000269|PubMed:10924111,
ECO:0000269|PubMed:8206922}.
-!- ENZYME REGULATION: Subject to competitive inhibition by 3-
phenylpropionate for the conversion of L-phenylalanine to
phenylpyruvate. Subject to competitive inhibition by D-
phenylalanine for the conversion of phenylpyruvate to L-
phenylalanine. {ECO:0000269|PubMed:10924111}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1.4 mM for NAD in the forward reaction;
KM=0.03 mM for NADH in the reverse reaction;
KM=0.12 mM for phenylpyruvate in the reverse reaction;
KM=5.5 mM for L-phenylalanine in the forward reaction;
-!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis; L-
phenylalanine from phenylpyruvate (PDH route): step 1/1.
{ECO:0000305|PubMed:10924111}.
-!- SUBUNIT: Homotetramer, dimer of dimers.
{ECO:0000269|PubMed:10924111, ECO:0000305|PubMed:10029526}.
-!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
{ECO:0000255|RuleBase:RU004417}.
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EMBL; U08381; AAA21461.1; -; Genomic_DNA.
PIR; A54038; A54038.
PDB; 1BW9; X-ray; 1.50 A; A/B=1-356.
PDB; 1BXG; X-ray; 2.30 A; A/B=1-356.
PDB; 1C1D; X-ray; 1.25 A; A/B=2-356.
PDB; 1C1X; X-ray; 1.40 A; A/B=2-356.
PDBsum; 1BW9; -.
PDBsum; 1BXG; -.
PDBsum; 1C1D; -.
PDBsum; 1C1X; -.
ProteinModelPortal; Q59771; -.
SMR; Q59771; -.
DrugBank; DB03884; 3-Phenylpyruvic Acid.
DrugBank; DB02494; Alpha-Hydroxy-Beta-Phenyl-Propionic Acid.
UniPathway; UPA00121; UER00346.
EvolutionaryTrace; Q59771; -.
GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
GO; GO:0050175; F:phenylalanine dehydrogenase activity; IDA:UniProtKB.
GO; GO:0009094; P:L-phenylalanine biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0006559; P:L-phenylalanine catabolic process; IDA:UniProtKB.
InterPro; IPR006095; Glu/Leu/Phe/Val_DH.
InterPro; IPR006096; Glu/Leu/Phe/Val_DH_C.
InterPro; IPR006097; Glu/Leu/Phe/Val_DH_dimer_dom.
InterPro; IPR016211; Glu/Phe/Leu/Val_DH_bac/arc.
InterPro; IPR016040; NAD(P)-bd_dom.
PANTHER; PTHR42722:SF1; PTHR42722:SF1; 1.
Pfam; PF00208; ELFV_dehydrog; 1.
Pfam; PF02812; ELFV_dehydrog_N; 1.
PIRSF; PIRSF000188; Phe_leu_dh; 1.
PRINTS; PR00082; GLFDHDRGNASE.
SMART; SM00839; ELFV_dehydrog; 1.
SUPFAM; SSF51735; SSF51735; 1.
1: Evidence at protein level;
3D-structure; Direct protein sequencing; NAD; Nucleotide-binding;
Oxidoreductase.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:8206922}.
CHAIN 2 356 Phenylalanine dehydrogenase.
/FTId=PRO_0000434608.
NP_BIND 183 189 NAD. {ECO:0000244|PDB:1BW9,
ECO:0000244|PDB:1BXG,
ECO:0000244|PDB:1C1D,
ECO:0000269|PubMed:10924111,
ECO:0000305}.
NP_BIND 206 207 NAD. {ECO:0000244|PDB:1BW9,
ECO:0000244|PDB:1BXG,
ECO:0000244|PDB:1C1D,
ECO:0000269|PubMed:10924111}.
NP_BIND 240 241 NAD. {ECO:0000244|PDB:1BW9,
ECO:0000244|PDB:1BXG,
ECO:0000244|PDB:1C1D,
ECO:0000269|PubMed:10924111}.
NP_BIND 261 263 NAD. {ECO:0000244|PDB:1BW9,
ECO:0000244|PDB:1BXG,
ECO:0000244|PDB:1C1D,
ECO:0000269|PubMed:10924111}.
REGION 118 119 Substrate binding. {ECO:0000244|PDB:1C1D,
ECO:0000269|PubMed:10924111}.
ACT_SITE 79 79 Proton donor/acceptor.
{ECO:0000305|PubMed:10924111}.
BINDING 43 43 NAD. {ECO:0000244|PDB:1C1D,
ECO:0000269|PubMed:10924111}.
BINDING 67 67 Substrate. {ECO:0000244|PDB:1C1D,
ECO:0000269|PubMed:10924111}.
BINDING 119 119 NAD. {ECO:0000244|PDB:1BXG,
ECO:0000244|PDB:1C1D,
ECO:0000244|PDB:1C1X,
ECO:0000269|PubMed:10924111}.
BINDING 150 150 NAD. {ECO:0000244|PDB:1BXG,
ECO:0000244|PDB:1C1D,
ECO:0000244|PDB:1C1X,
ECO:0000269|PubMed:10924111}.
BINDING 154 154 NAD. {ECO:0000244|PDB:1BXG,
ECO:0000244|PDB:1C1D,
ECO:0000244|PDB:1C1X,
ECO:0000269|PubMed:10924111}.
BINDING 211 211 NAD. {ECO:0000244|PDB:1BW9,
ECO:0000244|PDB:1BXG,
ECO:0000244|PDB:1C1D,
ECO:0000269|PubMed:10924111}.
BINDING 263 263 Substrate. {ECO:0000244|PDB:1C1D,
ECO:0000269|PubMed:10924111}.
HELIX 3 7 {ECO:0000244|PDB:1C1D}.
STRAND 11 19 {ECO:0000244|PDB:1C1D}.
TURN 20 23 {ECO:0000244|PDB:1C1D}.
STRAND 24 32 {ECO:0000244|PDB:1C1D}.
STRAND 34 45 {ECO:0000244|PDB:1C1D}.
HELIX 50 70 {ECO:0000244|PDB:1C1D}.
STRAND 76 83 {ECO:0000244|PDB:1C1D}.
HELIX 88 90 {ECO:0000244|PDB:1C1D}.
HELIX 93 109 {ECO:0000244|PDB:1C1D}.
TURN 110 112 {ECO:0000244|PDB:1C1D}.
STRAND 113 118 {ECO:0000244|PDB:1C1D}.
HELIX 124 133 {ECO:0000244|PDB:1C1D}.
HELIX 142 144 {ECO:0000244|PDB:1C1D}.
HELIX 151 168 {ECO:0000244|PDB:1C1D}.
STRAND 178 182 {ECO:0000244|PDB:1C1D}.
HELIX 186 197 {ECO:0000244|PDB:1C1D}.
STRAND 201 205 {ECO:0000244|PDB:1C1D}.
HELIX 209 217 {ECO:0000244|PDB:1C1D}.
HELIX 225 230 {ECO:0000244|PDB:1C1D}.
STRAND 234 238 {ECO:0000244|PDB:1C1D}.
HELIX 247 252 {ECO:0000244|PDB:1C1D}.
STRAND 256 258 {ECO:0000244|PDB:1C1D}.
STRAND 266 268 {ECO:0000244|PDB:1C1X}.
HELIX 269 277 {ECO:0000244|PDB:1C1D}.
HELIX 285 288 {ECO:0000244|PDB:1C1D}.
HELIX 291 300 {ECO:0000244|PDB:1C1D}.
HELIX 306 314 {ECO:0000244|PDB:1C1D}.
HELIX 316 330 {ECO:0000244|PDB:1C1D}.
HELIX 334 348 {ECO:0000244|PDB:1C1D}.
SEQUENCE 356 AA; 36609 MW; A969C29E9466935E CRC64;
MSIDSALNWD GEMTVTRFDR ETGAHFVIRL DSTQLGPAAG GTRAAQYSQL ADALTDAGKL
AGAMTLKMAV SNLPMGGGKS VIALPAPRHS IDPSTWARIL RIHAENIDKL SGNYWTGPDV
NTNSADMDTL NDTTEFVFGR SLERGGAGSS AFTTAVGVFE AMKATVAHRG LGSLDGLTVL
VQGLGAVGGS LASLAAEAGA QLLVADTDTE RVAHAVALGH TAVALEDVLS TPCDVFAPCA
MGGVITTEVA RTLDCSVVAG AANNVIADEA ASDILHARGI LYAPDFVANA GGAIHLVGRE
VLGWSESVVH ERAVAIGDTL NQVFEISDND GVTPDEAART LAGRRAREAS TTTATA


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