| Gene | T32N15.11 |
| Putative Identification | prephenate dehydratase |
| Position | 87366 to 88640, from initial methionine to termination codon |
| Strand | - |
| EST match | T42435, N96431, H74930, N96696 |
| Database match | bacterial PheA proteins (prephenate dehydratase) |
CDS: The table below lists the coordinates of the single T32N15.11 exon and which exon prediction algorithms selected the termini (Gr = GRAIL)
| Exon | Range | 3' | 5' |
|---|---|---|---|
| 1 | 87366 - 88640 | Gr | Gr |
Complete CDS of T32N15.11
ATGCAAGCCGCAACGTCGTGTGATCTCAAGTTCCGATCAACAGATCCGACGTCTAGGAAC AAATGTTTCTCCCACGCGATTCCAAAGCGCGTGGCTGTTACGTGCGGTTATAGGTCGGAG TCGTTTAGCTTCCCTAACGGTGTCTCCGTGAGTCGATCTGATTGGCAAAGCTCATGTGCC ATTTTATCTAGTAAAGTTGCTTCTGTTGAAAATACCGGTGGTTTAGCGGACAAAATCGCC GCCGTTAATGGTCACACGAACGGCTCTGTGAATCTTGGTCTCGTCGCCGTTGAGTCAACT AACGGAAAGTTAGCTCCTGCTCAGCCGTTGACTATTACTGATCTATCTCCGGCACCGTTG CATGGTTCTAGTCTACGTGTAGCTTACCAAGGCGTTCCCGGAGCTTACTCGGAAGCAGCT GCCGGAAAAGCTTATCCCAATTGCGACGCCATTCCTTGTGACCAGTTTGACGTTGCTTTT CAGGCGGTGGAGCTTTGGATCGCTGATCGAGCTGTGCTTCCGGTGGAGAACTCACTCGGT GGTTCGATCCATCGAAACTATGATCTTCTTCTCCGTCACCGTCTTCACATCGTTGGAGAA GTTCAGATTCCGGTCCACCATTGCCTCCTCGCACTCCCGGGAGTCCGAACTGACTGTGTT TCGCGGGTGATCTCTCACCCGCAAGCCCTAGCGCAGACGGAACACTCCCTCGACGTCCTT ACACCACATGCAGCGCGTGAGGCTTTCCATGACACAGCGGCTGCTGCGGAGTATATCTCA GCTAACGACCTACATGACACGGCGGCTGTGGCGAGCGCACGCGCCGCTGAGCTTTACAAC CTCCAGATATTAGCGGATGGGATTCAAGACGACCCGGGGAACGTCACTCGTTTCCTAATG TTGGCGCGTGAGCCTATAATCCCACGCACGGACCGGCCATTCAAGACTAGCATCGTCTTT GCTGCCCAAGAGCACAAAGGAACTAGCGTCCTCTTTAAAGTCCTCTCGGCTTTCGCTTTC AGAGACATTAGCCTGACCAAGATCGAGTCCCGGCCTCACCATAACCGCCCGCTTAGGGTT GTTGGTGACGGGAGCTTTGGGACGTCGAAGAACTTCGAGTACATGTTTTACGTGGATTTT GAGGCATCGATGGCTGAGCCGCGTGCACAGAACGCGCTTGCGGAGGTTCAAGAGTACACG TCGTTCCTAAGGGTGCTGGGAAGTTACCCCATGGATATGACACCATGGTCCATGACATCC ACAGAAGAAGCATGA
Protein translation:
MQAATSCDLKFRSTDPTSRNKCFSHAIPKRVAVTCGYRSESFSFPNGVSVSRSDWQSSCA ILSSKVASVENTGGLADKIAAVNGHTNGSVNLGLVAVESTNGKLAPAQPLTITDLSPAPL HGSSLRVAYQGVPGAYSEAAAGKAYPNCDAIPCDQFDVAFQAVELWIADRAVLPVENSLG GSIHRNYDLLLRHRLHIVGEVQIPVHHCLLALPGVRTDCVSRVISHPQALAQTEHSLDVL TPHAAREAFHDTAAAAEYISANDLHDTAAVASARAAELYNLQILADGIQDDPGNVTRFLM LAREPIIPRTDRPFKTSIVFAAQEHKGTSVLFKVLSAFAFRDISLTKIESRPHHNRPLRV VGDGSFGTSKNFEYMFYVDFEASMAEPRAQNALAEVQEYTSFLRVLGSYPMDMTPWSMTS TEEA*
Biochemical reaction catalyzed prephanate dehydratase:
COO- COO- COO-
| | |
C=O C=O H-C-NH3+
| | |
CH2 CH2 CH2
| | |
(C6H5OH)-COO- (C6H5) (C6H5)
PheA
Prephenate -------> Phenylpyruvate -------> Phenylalanine
In E. coli, the decarboxylation of prephanate to
phenylpyruvate is catalyzed by prephenate dehydratase.
Transamination of phenylpyruvate yields phenylalanine.
Alignment of bacterial PheA proteins and T32N15.11. The alignment contains the proteins encoded by the PheA genes of E. coli (M10431), E. herbicola (X60420), and P. stutzeri (M73971) with T32N15.11. The PROSITE Dictionary states that prephenate dehydratase (PDT, EC 4.2.1.51) catalyzes the decarboxylation of prephenate into phenylpyruvate. In microorganisms PDT is involved in the terminal pathway of the biosynthesis of phenylalanine. Signature sequences for prephenate dehydratase are centered around a conserved threonine which has been said to be essential for the activity of the enzyme in E. coli; the second region includes a conserved glutamate. These regions are highlighted in red.
1 60
EcoliPheA ~~~~~~~~~~MTSENPLLALREKISALDEKLLALLAERREL.....AVEVGKAKLLSHRP
EherbPheA ~~~~~~~~~~MNPDNPLLALRDKISAVDKKLLTLLAERRLL.....AVEVAQAKLATHRP
PstutzPheA ~~~~~~~~~~MSEADQLKALRVRIDSLDERILDLISERARC.....AQEVARVKTASWPK
T32N15.11 MQAATSCDLKFRSTDPTSRNKCFSHAIPKRVAVTCGYRSESFSFPNGVSVSRSDWQSSCA
61 120
EcoliPheA VRDI.....DRERDLLERLITLGKAHHLDAHYITRLFQLIIEDSVLTQQALLQQHLNKIN
EherbPheA IRDV.....ERERALLENLIVLGKAHNLDAHYITRLFQLVIEDSVLTQQALLQKNLNHPH
PstutzPheA AEEAVFYRPEREAWVLKHIMELNKG.PLDNEEMARLFREIMSSCLALEQPL.........
T32N15.11 ILSSKVASVENTGGLADKIAAVN.GHTNGSVNLGLVAVESTNGKLAPAQPLTITDLSPAP
121 180
EcoliPheA PH..SARIAFLGPKGSYSHLAARQYAARHFEQFIESGCAKFADIFNQVETGQADYAVVPI
EherbPheA AH..AARIAFLGPKGSYSHLAARNYASRHFDSMVECGCLKFHDIIKQVENGVADYAVMPI
PstutzPheA ......RVAYLGPEGTFSQAAALKHFGH...SVISKPMAAIDEVFREVVAGAVNFGVVPV
T32N15.11 LHGSSLRVAYQGVPGAYSEAAA....GKAYPNCDAIPCDQFDVAFQAVELWIADRAVLPV
181 240
EcoliPheA ENTSSGAINDVYDLLQHTSLSIVGEMTLTIDHCLLVSGTTDLSTINTVYSHPQPFQQCSK
EherbPheA ENTSSGSINDVYDLLQQTSLSIVGELTLPIDHCVLVNGPTDLQQIETVYSHPQPFQQCSQ
PstutzPheA ENSTEGAVNHTLDSFLEHDIVICGEVELRIHHHLLVGETTKTDRITRIYSHAQSLAQCRK
T32N15.11 ENSLGGSIHRNYDLLLRHRLHIVGEVQIPVHHCLLALPGVRTDCVSRVISHPQALAQTEH
241 300
EcoliPheA FLN.RYPHWKIEYTESTSAAMEKVAQAKSPHVAALGSEAGGTLYGLQVLERIEANQRQNF
EherbPheA FIN.RFPHWKIEYTESTAAAMEKVAALNSPKVAALGSEAGGELYQLQVLERNLANQQQNH
PstutzPheA WLDAHYPNVERVAVSSNADAAKRVK..SEWNSAAIAGDMAAQLYGLSKLAEKIEDRPDNS
T32N15.11 SLDVLTPHAAREAFHDTAAAAEYISANDLHDTAAVASARAAELYNLQILADGIQDDPGNV
301 360
EcoliPheA TRFVVLARKAINVSDQVPAKTTLLMATGQQAG..ALVEALLVLRNHNLIMTRLESRPIHG
EherbPheA TRFIVLARKAIEVSDQVPAKTTLIMATGQQAG..ALVDALLVLRQHNLIMSKLESRPING
PstutzPheA TRFLIIGSQ..EVPPTGDDKTSIIVSMRNKPG..ALHELLMPFHSNGIDLTRIETRPSRS
T32N15.11 TRFLMLAREPIIPRTDRPFKTSIVFAAQEHKGTSVLFKVLSAFAFRDISLTKIESRPHHN
361 420
EcoliPheA NP..............WEEMFYLDIQANLESAEMQKALKELGEITRSMKVLGCYPSENVV
EherbPheA NP..............WEEMFYIDVQGNLQSERMQQALQELQTMTRSLKVLGCYPSENVV
PstutzPheA GK..............WTYVFFIDCMGHYQDPLIKDVLEKIDHEAVALKVLGSYPKAVL*
T32N15.11 RPLRVVGDGSFGTSKNFEYMFYVDFEASMAEPRAQNALAEVQEYTSFLRVLGSYPMDMTP
421
EcoliPheA PVDPT*~~~~
EherbPheA PAEPGR*~~~
PstutzPheA ~~~~~~~~~~
T32N15.11 WSMTSTEEA*
written 28 Aug 97
Larry Parnell