T3DB: Phenylalanine dehydrogenase

Name	Phenylalanine dehydrogenase
Synonyms	1.4.1.20 PheDH
Gene Name	pdh
Organism	Rhodococcus sp.
Amino acid sequence	>lcl\|BSEQ0012865\|Phenylalanine dehydrogenase MSIDSALNWDGEMTVTRFDRETGAHFVIRLDSTQLGPAAGGTRAAQYSQLADALTDAGKL AGAMTLKMAVSNLPMGGGKSVIALPAPRHSIDPSTWARILRIHAENIDKLSGNYWTGPDV NTNSADMDTLNDTTEFVFGRSLERGGAGSSAFTTAVGVFEAMKATVAHRGLGSLDGLTVL VQGLGAVGGSLASLAAEAGAQLLVADTDTERVAHAVALGHTAVALEDVLSTPCDVFAPCA MGGVITTEVARTLDCSVVAGAANNVIADEAASDILHARGILYAPDFVANAGGAIHLVGRE VLGWSESVVHERAVAIGDTLNQVFEISDNDGVTPDEAARTLAGRRAREASTTTATA
Number of residues	356
Molecular Weight	36608.615
Theoretical pI	4.55
GO Classification	Functions nucleotide binding phenylalanine dehydrogenase activity Processes L-phenylalanine catabolic process L-phenylalanine biosynthetic process
General Function	Phenylalanine dehydrogenase activity
Specific Function	Catalyzes the reversible, NAD-dependent deamination of L-phenylalanine to phenyl pyruvate, ammonia and NADH.
Pfam Domain Function	ELFV_dehydrog (PF00208 ) ELFV_dehydrog_N (PF02812 )
Transmembrane Regions	Not Available
GenBank Protein ID	475596
UniProtKB ID	Q59771
UniProtKB Entry Name	DHPH_RHOSO
Cellular Location	Not Available
Gene sequence	>lcl\|BSEQ0007840\|1071 bp ATGAGTATCGACAGCGCACTGAACTGGGACGGGGAAATGACGGTCACCCGATTCGACCGG GAGACTGGTGCCCATTTCGTCATTCGACTCGATTCGACCCAACTCGGACCGGCGGCCGGA GGCACCAGAGCCGCACAGTACTCACAGCTGGCGGACGCCCTCACCGACGCCGGCAAATTG GCGGGGGCGATGACGTTGAAGATGGCAGTGAGCAACCTTCCGATGGGCGGGGGCAAATCC GTCATTGCGCTTCCTGCGCCGCGTCATTCGATCGATCCGAGCACGTGGGCACGCATCCTC CGAATCCACGCCGAGAACATCGACAAGTTGTCCGGCAACTACTGGACCGGACCGGACGTC AACACCAATTCGGCAGACATGGATACTCTGAACGACACCACCGAGTTCGTGTTCGGACGG TCGCTCGAACGCGGCGGCGCGGGTTCGAGCGCGTTCACCACCGCCGTTGGCGTGTTCGAG GCGATGAAGGCGACCGTCGCGCACCGTGGGCTGGGCTCACTCGACGGTTTGACGGTCCTG GTCCAAGGACTGGGGGCAGTCGGAGGATCATTGGCATCCCTGGCCGCCGAAGCGGGTGCG CAACTCCTGGTGGCAGACACCGACACCGAGCGAGTAGCGCACGCTGTTGCGTTGGGCCAC ACAGCGGTTGCCCTCGAGGACGTTCTGTCCACCCCGTGTGATGTCTTCGCACCCTGCGCA ATGGGCGGCGTCATCACCACCGAGGTGGCGCGAACACTCGACTGTTCCGTCGTGGCCGGT GCCGCCAACAACGTCATCGCCGACGAGGCCGCCTCGGACATCCTGCACGCACGCGGAATT CTGTACGCTCCCGACTTCGTGGCCAACGCCGGCGGTGCCATCCACCTCGTAGGCCGGGAG GTTCTCGGTTGGTCCGAGTCGGTTGTCCACGAACGAGCAGTTGCCATAGGCGACACCCTG AATCAGGTCTTCGAGATCTCCGACAACGACGGCGTCACCCCGGACGAGGCCGCCCGCACT CTCGCTGGACGGCGCGCCCGCGAGGCCTCGACAACGACAGCGACTGCCTAG
GenBank Gene ID	U08381
GeneCard ID	Not Available
GenAtlas ID	Not Available
HGNC ID	Not Available
Chromosome Location	Not Available
Locus	Not Available
References	Brunhuber NM, Banerjee A, Jacobs WR Jr, Blanchard JS: Cloning, sequencing, and expression of Rhodococcus L-phenylalanine dehydrogenase. Sequence comparisons to amino-acid dehydrogenases. J Biol Chem. 1994 Jun 10;269(23):16203-11. 8206922 Vanhooke JL, Thoden JB, Brunhuber NM, Blanchard JS, Holden HM: Phenylalanine dehydrogenase from Rhodococcus sp. M4: high-resolution X-ray analyses of inhibitory ternary complexes reveal key features in the oxidative deamination mechanism. Biochemistry. 1999 Feb 23;38(8):2326-39. 10029526 Brunhuber NM, Thoden JB, Blanchard JS, Vanhooke JL: Rhodococcus L-phenylalanine dehydrogenase: kinetics, mechanism, and structural basis for catalytic specificity. Biochemistry. 2000 Aug 8;39(31):9174-87. 10924111