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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: 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.2 Publications
L-phenylalanine = trans-cinnamate + ammonia.By similarity

Kineticsi

  1. KM=1.1 mM for L-phenylalanine2 Publications
  1. Vmax=110 µmol/min/mg enzyme with L-phenylalanine as substrate2 Publications

pH dependencei

Optimum pH is 7.5-8.0.2 Publications

Pathwayi: taxol biosynthesis

This protein is involved in the pathway taxol biosynthesis, which is part of Alkaloid biosynthesis.
View all proteins of this organism that are known to be involved in the pathway taxol biosynthesis and in Alkaloid biosynthesis.

Pathwayi: trans-cinnamate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes trans-cinnamate from L-phenylalanine.
Proteins known to be involved in this subpathway in this organism are:
  1. Phenylalanine ammonia-lyase (pam), Phenylalanine aminomutase (L-beta-phenylalanine forming) (pam)
This subpathway is part of the pathway trans-cinnamate biosynthesis, which is itself part of Phenylpropanoid metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes trans-cinnamate from L-phenylalanine, the pathway trans-cinnamate biosynthesis and in Phenylpropanoid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei80Proton donor/acceptor2 Publications1
Binding sitei231Substrate1
Binding sitei319Substrate1
Binding sitei325Substrate1
Binding sitei355Substrate1
Binding sitei458Substrate1

GO - Molecular functioni

GO - Biological processi

  • alkaloid biosynthetic process Source: UniProtKB
  • cinnamic acid biosynthetic process Source: UniProtKB-UniPathway
  • L-phenylalanine catabolic process Source: InterPro
  • L-phenylalanine metabolic process Source: UniProtKB
  • paclitaxel biosynthetic process Source: UniProtKB
  • 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

BRENDAi5.4.3.11. 9720.
UniPathwayiUPA00713; UER00725.
UPA00842.

Names & Taxonomyi

Protein namesi
Recommended name:
Phenylalanine aminomutase (L-beta-phenylalanine forming) (EC:5.4.3.102 Publications)
Alternative name(s):
Phenylalanine ammonia-lyase (EC:4.3.1.24By similarity)
Gene namesi
Name:pam
OrganismiTaxus wallichiana var. chinensis (Chinese yew) (Taxus chinensis)
Taxonomic identifieri29808 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaPinidaeCupressalesTaxaceaeTaxus

Subcellular locationi

GO - Cellular componenti

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)DescriptionActionsGraphical viewLength
Mutagenesisi80Y → A or F: Abolishes enzyme activity. 1 Publication1
Mutagenesisi231N → A: Abolishes the formation of the MIO cofactor and thereby abolishes enzyme activity. 2 Publications1
Mutagenesisi231N → X: Abolishes enzyme activity; when associated with X-355. 2 Publications1
Mutagenesisi319Q → M: Increases deamination activity with beta-Phe. Increases beta-regioselectivity in the amination of cinnamate. Abolishes enzyme activity; when associated with K-325. 1 Publication1
Mutagenesisi322Y → A: Abolishes the formation of the MIO cofactor and thereby abolishes enzyme activity. 2 Publications1
Mutagenesisi322Y → X: Abolishes enzyme activity; when associated with X-371. 2 Publications1
Mutagenesisi325R → K: Increases deamination activity with beta-Phe. Increases beta-regioselectivity in the amination of cinnamate. Abolishes enzyme activity; when associated with M-319. 1 Publication1
Mutagenesisi355N → X: Abolishes enzyme activity; when associated with X-231. 1 Publication1
Mutagenesisi371F → X: Abolishes enzyme activity; when associated with X-322. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004299701 – 687Phenylalanine aminomutase (L-beta-phenylalanine forming)Add BLAST687

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki175 ↔ 1775-imidazolinone (Ala-Gly)
Modified residuei1762,3-didehydroalanine (Ser)1

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

1687
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi10 – 23Combined sources14
Beta strandi26 – 33Combined sources8
Helixi37 – 45Combined sources9
Beta strandi50 – 53Combined sources4
Helixi55 – 74Combined sources20
Turni80 – 82Combined sources3
Helixi87 – 89Combined sources3
Helixi97 – 108Combined sources12
Helixi126 – 140Combined sources15
Helixi149 – 160Combined sources12
Beta strandi163 – 165Combined sources3
Beta strandi174 – 177Combined sources4
Helixi179 – 189Combined sources11
Beta strandi196 – 199Combined sources4
Turni200 – 202Combined sources3
Beta strandi203 – 206Combined sources4
Helixi207 – 213Combined sources7
Helixi225 – 230Combined sources6
Beta strandi231 – 233Combined sources3
Helixi234 – 265Combined sources32
Helixi269 – 272Combined sources4
Helixi274 – 278Combined sources5
Helixi283 – 296Combined sources14
Helixi300 – 310Combined sources11
Helixi313 – 315Combined sources3
Helixi322 – 325Combined sources4
Helixi327 – 349Combined sources23
Beta strandi355 – 359Combined sources5
Helixi360 – 362Combined sources3
Beta strandi364 – 366Combined sources3
Helixi374 – 402Combined sources29
Helixi404 – 406Combined sources3
Turni407 – 409Combined sources3
Helixi412 – 414Combined sources3
Helixi420 – 422Combined sources3
Helixi427 – 443Combined sources17
Helixi448 – 450Combined sources3
Turni455 – 458Combined sources4
Beta strandi459 – 461Combined sources3
Helixi465 – 517Combined sources53
Helixi522 – 534Combined sources13
Helixi537 – 539Combined sources3
Turni540 – 542Combined sources3
Helixi550 – 565Combined sources16
Helixi575 – 603Combined sources29
Beta strandi613 – 615Combined sources3
Helixi619 – 622Combined sources4
Helixi626 – 633Combined sources8
Turni634 – 637Combined sources4
Beta strandi642 – 644Combined sources3
Helixi649 – 661Combined sources13
Turni662 – 665Combined sources4
Helixi666 – 672Combined sources7
Turni673 – 675Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4V2QX-ray1.95A/B1-687[»]
4V2RX-ray2.20A/B1-687[»]
ProteinModelPortaliQ68G84.
SMRiQ68G84.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PAL/histidase family.Curated

Family and domain databases

CDDicd00332. PAL-HAL. 1 hit.
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.
IPR031008. Taxol_Phe_23mut.
[Graphical view]
PfamiPF00221. Lyase_aromatic. 1 hit.
[Graphical view]
SUPFAMiSSF48557. SSF48557. 1 hit.
TIGRFAMsiTIGR01226. phe_am_lyase. 1 hit.
TIGR04473. taxol_Phe_23mut. 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
PDB 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[»]
4V2QX-ray1.95A/B1-687[»]
4V2RX-ray2.20A/B1-687[»]
ProteinModelPortaliQ68G84.
SMRiQ68G84.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00713; UER00725.
UPA00842.
BRENDAi5.4.3.11. 9720.

Family and domain databases

CDDicd00332. PAL-HAL. 1 hit.
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.
IPR031008. Taxol_Phe_23mut.
[Graphical view]
PfamiPF00221. Lyase_aromatic. 1 hit.
[Graphical view]
SUPFAMiSSF48557. SSF48557. 1 hit.
TIGRFAMsiTIGR01226. phe_am_lyase. 1 hit.
TIGR04473. taxol_Phe_23mut. 1 hit.
PROSITEiPS00488. PAL_HISTIDASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

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 2, 2016
This is version 87 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.