Q68G84 (Q68G84_TAXWC) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Phenylalanine ammonia-lyase RuleBase RU003955
EC=4.3.1.24 RuleBase RU003955

Gene names

Name:

pam EMBL AAU01182.1

Organism

Taxus wallichiana var. chinensis (Chinese yew) (Taxus chinensis) EMBL AAU01182.1

Taxonomic identifier

29808 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Coniferophyta › Coniferopsida › Coniferales › Taxaceae › Taxus › Taxus wallichiana

Protein attributes

Sequence length	687 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	L-phenylalanine = trans-cinnamate + ammonia. RuleBase RU003955 SAAS SAAS005922
Pathway	Phenylpropanoid metabolism; trans-cinnamate biosynthesis; trans-cinnamate from L-phenylalanine: step 1/1. RuleBase RU003955 SAAS SAAS005922
Subcellular location	Cytoplasm By similarity RuleBase RU003955 SAAS SAAS005922.
Sequence similarities	Belongs to the PAL/histidase family. RuleBase RU003954

Ontologies

Keywords
Biological process	Phenylpropanoid metabolism RuleBase RU003955 SAAS SAAS005922
Cellular component	Cytoplasm SAAS SAAS005922
Molecular function	Lyase RuleBase RU003954 SAAS SAAS005922
Technical term	3D-structure PDB 2YII PDB 4BAA PDB 4BAB
Gene Ontology (GO)
Biological_process	L-phenylalanine catabolic process Inferred from electronic annotation. Source: InterPro cinnamic acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	phenylalanine ammonia-lyase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Amino acid modifications
	Modified residue	175	1	MIO PDB 4BAA PDB 4BAB
	Modified residue	176	1	MIO PDB 4BAA PDB 4BAB
	Modified residue	177	1	MIO PDB 4BAA PDB 4BAB

Sequences

	Sequence		Length	Mass (Da)
	Q68G84 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: D9BC13C7C689A421	FASTA	687	75,332
	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

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), DEHYDRATION/CYCLIZATION AT ALA-175; SER-176 AND GLY-177.
[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), DEHYDRATION/CYCLIZATION AT ALA-175; SER-176 AND GLY-177.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AY724735 mRNA. Translation: AAU01182.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2YII	X-ray	2.18	A/B/C/D	1-687	[»]
4BAA	X-ray	2.50	A/B/C/D	1-687	[»]
4BAB	X-ray	2.56	A/B/C/D	1-687	[»]

ProteinModelPortal

Q68G84.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

UniPathway

UPA00713; UER00725.

Family and domain databases

Gene3D

1.10.274.20. 1 hit.
1.10.275.10. 1 hit.

InterPro

IPR001106. 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]

Pfam

PF00221. Lyase_aromatic. 1 hit.
[Graphical view]

SUPFAM

SSF48557. L-Aspartase-like. 1 hit.

TIGRFAMs

TIGR01226. phe_am_lyase. 1 hit.

PROSITE

PS00488. PAL_HISTIDASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

Q68G84_TAXWC

Accession

Primary (citable) accession number: Q68G84

Entry history

Integrated into UniProtKB/TrEMBL:	October 11, 2004
Last sequence update:	October 11, 2004
Last modified:	May 1, 2013
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)