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Entry version 100 (02 Jun 2021)
Sequence version 1 (11 Oct 2004)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Phenylalanine aminomutase that catalyzes the rearrangement of L-phenylalanine to R-beta-phenylalanine. Catalyzes the first committed 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

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>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. 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
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei80Proton donor/acceptor2 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei231SubstrateCombined sources1 Publication1
Binding sitei319SubstrateCombined sources1 Publication1
Binding sitei325SubstrateCombined sources1 Publication1
Binding sitei355SubstrateCombined sources1 Publication1
Binding sitei458SubstrateCombined sources1 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionIsomerase, Lyase
Biological processAlkaloid metabolism, Phenylpropanoid metabolism, Taxol biosynthesis

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
5.4.3.10, 9720
5.4.3.11, 9720

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00713;UER00725
UPA00842

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:pam
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiTaxus wallichiana var. chinensis (Chinese yew) (Taxus chinensis)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri29808 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaPinopsidaPinidaeCupressalesTaxaceaeTaxus

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004299701 – 687Phenylalanine aminomutase (L-beta-phenylalanine forming)Add BLAST687

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki175 ↔ 1775-imidazolinone (Ala-Gly)1 Publication
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei1762,3-didehydroalanine (Ser)1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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.1 Publication

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

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

2 Publications

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1687
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q68G84

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the PAL/histidase family.Curated

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00332, PAL-HAL, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.274.20, 1 hit
1.10.275.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in 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_sf
IPR031008, Taxol_Phe_23mut

The PANTHER Classification System

More...
PANTHERi
PTHR10362, PTHR10362, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00221, Lyase_aromatic, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48557, SSF48557, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01226, phe_am_lyase, 1 hit
TIGR04473, taxol_Phe_23mut, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00488, PAL_HISTIDASE, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iD9BC13C7C689A421
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AY724735 mRNA Translation: AAU01182.1

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
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/D1-687[»]
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[»]
SMRiQ68G84
ModBaseiSearch...
PDBe-KBiSearch...

Enzyme and pathway databases

UniPathwayiUPA00713;UER00725
UPA00842
BRENDAi5.4.3.10, 9720
5.4.3.11, 9720

Family and domain databases

CDDicd00332, PAL-HAL, 1 hit
Gene3Di1.10.274.20, 1 hit
1.10.275.10, 1 hit
InterProiView protein in 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_sf
IPR031008, Taxol_Phe_23mut
PANTHERiPTHR10362, PTHR10362, 1 hit
PfamiView protein in Pfam
PF00221, Lyase_aromatic, 1 hit
SUPFAMiSSF48557, SSF48557, 1 hit
TIGRFAMsiTIGR01226, phe_am_lyase, 1 hit
TIGR04473, taxol_Phe_23mut, 1 hit
PROSITEiView protein in PROSITE
PS00488, PAL_HISTIDASE, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPAM_TAXWC
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q68G84
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 3, 2014
Last sequence update: October 11, 2004
Last modified: June 2, 2021
This is version 100 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>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
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