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EBI DbfetchID U08381; SV 1; linear; genomic DNA; STD; PRO; 1294 BP. XX AC U08381; XX DT 25-MAY-1994 (Rel. 39, Created) DT 27-OCT-2001 (Rel. 69, Last updated, Version 6) XX DE Rhodococcus sp. M4 L-phenylalanine dehydrogenase precursor (pdh) gene, DE complete cds. XX KW . XX OS Rhodococcus sp. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Nocardiaceae; Rhodococcus. XX RN [1] RP 1-1294 RX PUBMED; 8206922. RA Brunhuber N.M., Banerjee A., Jacobs W.R.Jr., Blanchard J.S.; RT "Cloning, sequencing, and expression of Rhodococcus L-phenylalanine RT dehydrogenase. Sequence comparisons to amino-acid dehydrogenases"; RL J. Biol. Chem. 269(23):16203-16211(1994). XX RN [2] RA Brunhuber N.M.W., Hummel W., Blanchard J.S.; RT "Purification, characterization, and kinetic mechanism of L-phenylalanine RT dehydrogenase"; RL Unpublished. XX RN [3] RP 1-1294 RA Brunhuber N.M.W.; RT ; RL Submitted (06-APR-1994) to the EMBL/GenBank/DDBJ databases. RL Norbert M. W. Brunhuber, Albert Einstein College of Medicine, Biochemistry, RL 1300 Morris Park Ave., Bronx, NY 10461, USA XX FH Key Location/Qualifiers FH FT source 1..1294 FT /organism="Rhodococcus sp." FT /strain="M4" FT /mol_type="genomic DNA" FT /clone_lib="library pYUB18-RhM4" FT /clone="pKSII-1B" FT /db_xref="taxon:1831" FT RBS 117..122 FT /gene="pdh" FT CDS 129..1199 FT /codon_start=1 FT /transl_table=11 FT /gene="pdh" FT /product="L-phenylalanine dehydrogenase precursor" FT /function="Oxidative deamination of L-phenylalanine with FT reduction of NAD" FT /EC_number="1.4.1.20" FT /note="L-phenylalanine:NAD oxidoreductase, deaminating" FT /db_xref="GOA:Q59771" FT /db_xref="InterPro:IPR016211" FT /db_xref="PDB:1BW9" FT /db_xref="UniProtKB/TrEMBL:Q59771" FT /citation=[2] FT /citation=[1] FT /experiment="experimental evidence, no additional details FT recorded" FT /protein_id="AAA21461.1" FT /translation="MSIDSALNWDGEMTVTRFDRETGAHFVIRLDSTQLGPAAGGTRAA FT QYSQLADALTDAGKLAGAMTLKMAVSNLPMGGGKSVIALPAPRHSIDPSTWARILRIHA FT ENIDKLSGNYWTGPDVNTNSADMDTLNDTTEFVFGRSLERGGAGSSAFTTAVGVFEAMK FT ATVAHRGLGSLDGLTVLVQGLGAVGGSLASLAAEAGAQLLVADTDTERVAHAVALGHTA FT VALEDVLSTPCDVFAPCAMGGVITTEVARTLDCSVVAGAANNVIADEAASDILHARGIL FT YAPDFVANAGGAIHLVGREVLGWSESVVHERAVAIGDTLNQVFEISDNDGVTPDEAART FT LAGRRAREASTTTATA" FT mat_peptide 132..1196 FT /gene="pdh" FT /product="L-phenylalanine dehydrogenase" FT /note="initiator methionine is removed posttranslationally" XX SQ Sequence 1294 BP; 243 A; 426 C; 402 G; 223 T; 0 other; ctgcagagac gttttcgcca aagactggtc acactatgaa gacgcaccct ccgtcgccgc 60 ggacccgaat cgggactgct cggagttgtc tgcgtccact gcatccatcg aacatcaagg 120 ggtacatcat gagtatcgac agcgcactga actgggacgg ggaaatgacg gtcacccgat 180 tcgaccggga gactggtgcc catttcgtca ttcgactcga ttcgacccaa ctcggaccgg 240 cggccggagg caccagagcc gcacagtact cacagctggc ggacgccctc accgacgccg 300 gcaaattggc gggggcgatg acgttgaaga tggcagtgag caaccttccg atgggcgggg 360 gcaaatccgt cattgcgctt cctgcgccgc gtcattcgat cgatccgagc acgtgggcac 420 gcatcctccg aatccacgcc gagaacatcg acaagttgtc cggcaactac tggaccggac 480 cggacgtcaa caccaattcg gcagacatgg atactctgaa cgacaccacc gagttcgtgt 540 tcggacggtc gctcgaacgc ggcggcgcgg gttcgagcgc gttcaccacc gccgttggcg 600 tgttcgaggc gatgaaggcg accgtcgcgc accgtgggct gggctcactc gacggtttga 660 cggtcctggt ccaaggactg ggggcagtcg gaggatcatt ggcatccctg gccgccgaag 720 cgggtgcgca actcctggtg gcagacaccg acaccgagcg agtagcgcac gctgttgcgt 780 tgggccacac agcggttgcc ctcgaggacg ttctgtccac cccgtgtgat gtcttcgcac 840 cctgcgcaat gggcggcgtc atcaccaccg aggtggcgcg aacactcgac tgttccgtcg 900 tggccggtgc cgccaacaac gtcatcgccg acgaggccgc ctcggacatc ctgcacgcac 960 gcggaattct gtacgctccc gacttcgtgg ccaacgccgg cggtgccatc cacctcgtag 1020 gccgggaggt tctcggttgg tccgagtcgg ttgtccacga acgagcagtt gccataggcg 1080 acaccctgaa tcaggtcttc gagatctccg acaacgacgg cgtcaccccg gacgaggccg 1140 cccgcactct cgctggacgg cgcgcccgcg aggcctcgac aacgacagcg actgcctagt 1200 aatcgatctc ggagtctggc gatcgaccat cggtccccat ctggcacgga cggtcatgcg 1260 agggtcggcg tcccgtccag tccgcctcgg tcct 1294 // ![]() |