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Q68G84 (Q68G84_TAXWC) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein attributes

Sequence length687 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Sequence similarities

Belongs to the PAL/histidase family. RuleBase RU003954

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Amino acid modifications

Modified residue1751MIO PDB 2YII PDB 4BAA PDB 4BAB
Modified residue1761MIO PDB 2YII PDB 4BAA PDB 4BAB
Modified residue1771MIO PDB 2YII PDB 4BAA PDB 4BAB

Sequences

Sequence LengthMass (Da)Tools
Q68G84 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: D9BC13C7C689A421

FASTA68775,332
        10         20         30         40         50         60 
MGFAVESRSH VKDILGLINA FNEVKKITVD GTTPITVAHV AALARRHDVK VALEAEQCRA 

        70         80         90        100        110        120 
RVETCSSWVQ RKAEDGADIY GVTTGFGACS SRRTNRLSEL QESLIRCLLA GVFTKGCAPS 

       130        140        150        160        170        180 
VDELPATATR SAMLLRLNSF TYGCSGIRWE VMEALEKLLN SNVSPKVPLR GSVSASGDLI 

       190        200        210        220        230        240 
PLAYIAGLLI GKPSVIARIG DDVEVPAPEA LSRVGLRPFK LQAKEGLALV NGTSFATAVA 

       250        260        270        280        290        300 
STVMYDANVL LLLVETLCGM FCEVIFGREE FAHPLIHKVK PHPGQIESAE LLEWLLRSSP 

       310        320        330        340        350        360 
FQELSREYYS IDKLKKPKQD RYALRSSPQW LAPLVQTIRD ATTTVETEVN SANDNPIIDH 

       370        380        390        400        410        420 
ANDRALHGAN FQGSAVGFYM DYVRIAVAGL GKLLFAQFTE LMIEYYSNGL PGNLSLGPDL 

       430        440        450        460        470        480 
SVDYGLKGLD IAMAAYSSEL QYLANPVTTH VHSAEQHNQD INSLALISAR KTEEALDILK 

       490        500        510        520        530        540 
LMIASHLTAM CQAVDLRQLE EALVKVVENV VSTLADECGL PNDTKARLLY VAKAVPVYTY 

       550        560        570        580        590        600 
LESPCDPTLP LLLGLKQSCF DTILALHKKD GIETDTLVDR LAEFEKRLSD RLENEMTAVR 

       610        620        630        640        650        660 
VLYEKKGHKT ADNNDALVRI QGSKFLPFYR FVREELDTGV MSARREQTPQ EDVQKVFDAI 

       670        680 
ADGRITVPLL HCLQGFLGQP NGCANGV 

« Hide

References

[1]"Purification, cloning, and functional expression of phenylalanine aminomutase: the first committed step in Taxol side-chain biosynthesis."
Steele C.L., Chen Y., Dougherty B.A., Li W., Hofstead S., Lam K.S., Xing Z., Chiang S.J.
Arch. Biochem. Biophys. 438:1-10(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
[2]"Mechanism-inspired engineering of phenylalanine aminomutase for enhanced ?-regioselective asymmetric amination of cinnamates."
Wu B., Szymanski W., Wybenga G.G., Heberling M.M., Bartsch S., de Wildeman S., Poelarends G.J., Feringa B.L., Dijkstra B.W., Janssen D.B.
Angew. Chem. Int. Ed. 51:482-486(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS).
[3]"Redesign of a Phenylalanine Aminomutase Into a Phenylalanine Ammonia Lyase."
Bartsch S., Wybenga G.G., Jansen M., Heberling M.M., Wu B., Dijkstra B.W., Janssen D.B.
Submitted (SEP-2012) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS).
[4]"Structural Investigations into the Stereochemistry and Activity of a Phenylalanine-2,3-aminomutase from Taxus chinensis."
Wybenga G.G., Szymanski W., Wu B., Feringa B.L., Janssen D.B., Dijkstra B.W.
Biochemistry 0:0-0(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1-79 AND 81-687.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY724735 mRNA. Translation: AAU01182.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2YIIX-ray2.18A/B/C/D1-687[»]
4BAAX-ray2.50A/B/C/D1-687[»]
4BABX-ray2.56A/B/C/D1-687[»]
4C5RX-ray2.14A/B/C/D1-687[»]
4C5SX-ray1.85A/B/C/D1-79[»]
A/B/C/D81-687[»]
4C5UX-ray2.19A/B/C/D1-687[»]
4C6GX-ray2.10A/B/C/D1-687[»]
4CQ5X-ray1.90A/B/C/D1-687[»]
ProteinModelPortalQ68G84.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D1.10.274.20. 1 hit.
1.10.275.10. 1 hit.
InterProIPR001106. Aromatic_Lyase.
IPR024083. Fumarase/histidase_N.
IPR008948. L-Aspartase-like.
IPR022313. Phe/His_NH3-lyase_AS.
IPR005922. Phe_NH3-lyase.
IPR023144. Phe_NH3-lyase_shielding_dom.
[Graphical view]
PfamPF00221. Lyase_aromatic. 1 hit.
[Graphical view]
SUPFAMSSF48557. SSF48557. 1 hit.
TIGRFAMsTIGR01226. phe_am_lyase. 1 hit.
PROSITEPS00488. PAL_HISTIDASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameQ68G84_TAXWC
AccessionPrimary (citable) accession number: Q68G84
Entry history
Integrated into UniProtKB/TrEMBL: October 11, 2004
Last sequence update: October 11, 2004
Last modified: July 9, 2014
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)