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Q68G84

- PAM_TAXWC

UniProt

Q68G84 - PAM_TAXWC

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Protein

Phenylalanine aminomutase (L-beta-phenylalanine forming)

Gene

pam

Organism
Taxus wallichiana var. chinensis (Chinese yew) (Taxus chinensis)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Phenylalanine aminomutase that catalyzes the rearrangement of L-phenylalanine to R-beta-phenylalanine. Catalyzes the first commited step in the biosynthesis of the side chain of the alkaloid taxol (paclitaxel), a widely-used compound with antitumor activity. Has also low phenylalanine ammonia-lyase activity and can catalyze the amination of trans-cinnamate.3 Publications

Catalytic activityi

L-phenylalanine = L-beta-phenylalanine.
L-phenylalanine = trans-cinnamate + ammonia.

Kineticsi

  1. KM=1.1 mM for L-Phe2 Publications

Vmax=110 µmol/min/mg enzyme with L-Phe as substrate2 Publications

pH dependencei

Optimum pH is 7.5-8.0.2 Publications

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei80 – 801Proton donor/acceptor2 Publications
Binding sitei231 – 2311Substrate
Binding sitei319 – 3191Substrate
Binding sitei325 – 3251Substrate
Binding sitei355 – 3551Substrate
Binding sitei458 – 4581Substrate

GO - Molecular functioni

  1. intramolecular transferase activity, transferring amino groups Source: UniProtKB
  2. phenylalanine ammonia-lyase activity Source: UniProtKB-EC

GO - Biological processi

  1. alkaloid biosynthetic process Source: UniProtKB
  2. cinnamic acid biosynthetic process Source: UniProtKB-UniPathway
  3. L-phenylalanine catabolic process Source: InterPro
  4. L-phenylalanine metabolic process Source: UniProtKB
  5. paclitaxel biosynthetic process Source: UniProtKB
  6. protein homotetramerization Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Lyase

Keywords - Biological processi

Alkaloid metabolism, Phenylpropanoid metabolism, Taxol biosynthesis

Enzyme and pathway databases

UniPathwayiUPA00713; UER00725.
UPA00842.

Names & Taxonomyi

Protein namesi
Recommended name:
Phenylalanine aminomutase (L-beta-phenylalanine forming) (EC:5.4.3.10)
Alternative name(s):
Phenylalanine ammonia-lyase (EC:4.3.1.24)
Gene namesi
Name:pam
OrganismiTaxus wallichiana var. chinensis (Chinese yew) (Taxus chinensis)
Taxonomic identifieri29808 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaPinidaeCupressalesTaxaceaeTaxus

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Biotechnological usei

Could be used for the stereoselective biosynthesis of beta-amino acids via amination of cinnamic acid derivatives.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi80 – 801Y → A or F: Abolishes enzyme activity. 1 Publication
Mutagenesisi231 – 2311N → A: Abolishes the formation of the MIO cofactor and thereby abolishes enzyme activity. 2 Publications
Mutagenesisi231 – 2311N → X: Abolishes enzyme activity; when associated with X-355. 2 Publications
Mutagenesisi319 – 3191Q → M: Increases deamination activity with beta-Phe. Increases beta-regioselectivity in the amination of cinnamate. Abolishes enzyme activity; when associated with K-325. 1 Publication
Mutagenesisi322 – 3221Y → A: Abolishes the formation of the MIO cofactor and thereby abolishes enzyme activity. 2 Publications
Mutagenesisi322 – 3221Y → X: Abolishes enzyme activity; when associated with X-371. 2 Publications
Mutagenesisi325 – 3251R → K: Increases deamination activity with beta-Phe. Increases beta-regioselectivity in the amination of cinnamate. Abolishes enzyme activity; when associated with M-319. 1 Publication
Mutagenesisi355 – 3551N → X: Abolishes enzyme activity; when associated with X-231. 1 Publication
Mutagenesisi371 – 3711F → X: Abolishes enzyme activity; when associated with X-322. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 687687Phenylalanine aminomutase (L-beta-phenylalanine forming)PRO_0000429970Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki175 ↔ 1775-imidazolinone (Ala-Gly)
Modified residuei176 – 17612,3-didehydroalanine (Ser)

Post-translational modificationi

Contains an active site 4-methylidene-imidazol-5-one (MIO), which is formed autocatalytically by cyclization and dehydration of residues Ala-Ser-Gly.

Interactioni

Subunit structurei

Homodimer (PubMed:15878763). Homotetramer, dimer of dimers (PubMed:24786474).2 Publications

Structurei

Secondary structure

1
687
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 2314Combined sources
Beta strandi26 – 338Combined sources
Helixi37 – 459Combined sources
Beta strandi50 – 534Combined sources
Helixi55 – 7420Combined sources
Turni80 – 823Combined sources
Helixi87 – 893Combined sources
Helixi97 – 10812Combined sources
Helixi126 – 14015Combined sources
Helixi149 – 16012Combined sources
Beta strandi163 – 1653Combined sources
Beta strandi174 – 1774Combined sources
Helixi179 – 18911Combined sources
Beta strandi196 – 2027Combined sources
Beta strandi204 – 2063Combined sources
Helixi207 – 2137Combined sources
Helixi225 – 2306Combined sources
Helixi234 – 26532Combined sources
Helixi269 – 2724Combined sources
Helixi274 – 2785Combined sources
Helixi283 – 29614Combined sources
Helixi300 – 31011Combined sources
Helixi313 – 3153Combined sources
Helixi322 – 3254Combined sources
Helixi327 – 34923Combined sources
Beta strandi355 – 3595Combined sources
Helixi360 – 3623Combined sources
Beta strandi364 – 3663Combined sources
Helixi374 – 40229Combined sources
Turni404 – 4096Combined sources
Helixi412 – 4143Combined sources
Helixi420 – 4223Combined sources
Helixi427 – 44317Combined sources
Helixi448 – 4503Combined sources
Turni455 – 4584Combined sources
Beta strandi459 – 4613Combined sources
Helixi465 – 51753Combined sources
Helixi522 – 53413Combined sources
Helixi537 – 5393Combined sources
Turni540 – 5423Combined sources
Helixi550 – 56516Combined sources
Helixi576 – 60429Combined sources
Helixi619 – 6224Combined sources
Helixi626 – 6338Combined sources
Turni634 – 6374Combined sources
Beta strandi642 – 6443Combined sources
Helixi649 – 66113Combined sources
Turni662 – 6654Combined sources
Helixi666 – 6727Combined sources
Turni673 – 6753Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliQ68G84.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PAL/histidase family.Curated

Family and domain databases

Gene3Di1.10.274.20. 1 hit.
1.10.275.10. 1 hit.
InterProiIPR001106. 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]
PfamiPF00221. Lyase_aromatic. 1 hit.
[Graphical view]
SUPFAMiSSF48557. SSF48557. 1 hit.
TIGRFAMsiTIGR01226. phe_am_lyase. 1 hit.
PROSITEiPS00488. PAL_HISTIDASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q68G84-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGFAVESRSH VKDILGLINA FNEVKKITVD GTTPITVAHV AALARRHDVK
60 70 80 90 100
VALEAEQCRA RVETCSSWVQ RKAEDGADIY GVTTGFGACS SRRTNRLSEL
110 120 130 140 150
QESLIRCLLA GVFTKGCAPS VDELPATATR SAMLLRLNSF TYGCSGIRWE
160 170 180 190 200
VMEALEKLLN SNVSPKVPLR GSVSASGDLI PLAYIAGLLI GKPSVIARIG
210 220 230 240 250
DDVEVPAPEA LSRVGLRPFK LQAKEGLALV NGTSFATAVA STVMYDANVL
260 270 280 290 300
LLLVETLCGM FCEVIFGREE FAHPLIHKVK PHPGQIESAE LLEWLLRSSP
310 320 330 340 350
FQELSREYYS IDKLKKPKQD RYALRSSPQW LAPLVQTIRD ATTTVETEVN
360 370 380 390 400
SANDNPIIDH ANDRALHGAN FQGSAVGFYM DYVRIAVAGL GKLLFAQFTE
410 420 430 440 450
LMIEYYSNGL PGNLSLGPDL SVDYGLKGLD IAMAAYSSEL QYLANPVTTH
460 470 480 490 500
VHSAEQHNQD INSLALISAR KTEEALDILK LMIASHLTAM CQAVDLRQLE
510 520 530 540 550
EALVKVVENV VSTLADECGL PNDTKARLLY VAKAVPVYTY LESPCDPTLP
560 570 580 590 600
LLLGLKQSCF DTILALHKKD GIETDTLVDR LAEFEKRLSD RLENEMTAVR
610 620 630 640 650
VLYEKKGHKT ADNNDALVRI QGSKFLPFYR FVREELDTGV MSARREQTPQ
660 670 680
EDVQKVFDAI ADGRITVPLL HCLQGFLGQP NGCANGV
Length:687
Mass (Da):75,332
Last modified:October 11, 2004 - v1
Checksum:iD9BC13C7C689A421
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY724735 mRNA. Translation: AAU01182.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY724735 mRNA. Translation: AAU01182.1 .

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 [» ]
4C5R X-ray 2.14 A/B/C/D 1-687 [» ]
4C5S X-ray 1.85 A/B/C/D 1-79 [» ]
A/B/C/D 81-687 [» ]
4C5U X-ray 2.19 A/B/C/D 1-687 [» ]
4C6G X-ray 2.10 A/B/C/D 1-687 [» ]
4CQ5 X-ray 1.90 A/B/C/D 1-687 [» ]
ProteinModelPortali Q68G84.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00713 ; UER00725 .
UPA00842 .

Family and domain databases

Gene3Di 1.10.274.20. 1 hit.
1.10.275.10. 1 hit.
InterProi 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 ]
Pfami PF00221. Lyase_aromatic. 1 hit.
[Graphical view ]
SUPFAMi SSF48557. SSF48557. 1 hit.
TIGRFAMsi TIGR01226. phe_am_lyase. 1 hit.
PROSITEi PS00488. PAL_HISTIDASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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 [MRNA], PARTIAL PROTEIN SEQUENCE, CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
  2. "Mechanism-inspired engineering of phenylalanine aminomutase for enhanced beta-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), FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, BIOTECHNOLOGY, MUTAGENESIS OF ASN-231; GLN-319; TYR-322; ARG-325; ASN-355 AND PHE-371, ACTIVE SITE, PTM.
  3. "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 53:3187-3198(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH TRANS-CINNAMATE, CATALYTIC ACTIVITY, FUNCTION, ACTIVE SITE, PTM, SUBUNIT, MUTAGENESIS OF TYR-80; ASN-231 AND TYR-322.

Entry informationi

Entry nameiPAM_TAXWC
AccessioniPrimary (citable) accession number: Q68G84
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 3, 2014
Last sequence update: October 11, 2004
Last modified: November 26, 2014
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3