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Protein
Submitted name:

Phenylacetaldehyde synthase

Gene

PAAS

Organism
Petunia hybrida (Petunia)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at transcript leveli

Functioni

Cofactori

pyridoxal 5'-phosphateUniRule annotation

GO - Molecular functioni

  1. carboxy-lyase activity Source: InterPro
  2. pyridoxal phosphate binding Source: InterPro

GO - Biological processi

  1. cellular amino acid metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

LyaseUniRule annotation

Keywords - Ligandi

Pyridoxal phosphateUniRule annotation

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13645.

Names & Taxonomyi

Protein namesi
Submitted name:
Phenylacetaldehyde synthaseImported
Gene namesi
Name:PAASImported
OrganismiPetunia hybrida (Petunia)Imported
Taxonomic identifieri4102 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaePetunioideaePetunia

Family & Domainsi

Sequence similaritiesi

Belongs to the group II decarboxylase family.UniRule annotation

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR010977. Aromatic_deC.
IPR002129. PyrdxlP-dep_de-COase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
IPR021115. Pyridoxal-P_BS.
[Graphical view]
PfamiPF00282. Pyridoxal_deC. 1 hit.
[Graphical view]
PRINTSiPR00800. YHDCRBOXLASE.
SUPFAMiSSF53383. SSF53383. 1 hit.
PROSITEiPS00392. DDC_GAD_HDC_YDC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q0ZQX0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDTIKINPEF DGQFCKTTSL LDPEEFRRNG HMMVDFLADY FHNIEKYPVR
60 70 80 90 100
SQVEPGYLER LLPDSAPIQP EPIEKILKDV RSDIFPGLTH WQSPNFFAYF
110 120 130 140 150
PCSSSTAGIL GEMLSAGLNV VGFSWIASPA ATELESIVMD WLGKLINLPK
160 170 180 190 200
TYLFSGGGGG VMQGTTCEVM LCTIVAARDK MLEKFGRENI DKLVVYASDQ
210 220 230 240 250
THFSFQKAVK ISGIKPENFR AIPTTKATEF SLNPESLRRA IQEDKKAGLI
260 270 280 290 300
PLFLCTSIGT TSTTAVDPLK PLCEIAEEYG IWVHVDAAYA GSACICPEFQ
310 320 330 340 350
HFLDGVEHAN SFSFNAHKWL FTTLDCCCLW LKDPSSLTKA LSTNPEVLRN
360 370 380 390 400
DATDSEQVVD YKDWQITLSR RFRSLKLWLV LKSYGVANLR NFIRSHIEMA
410 420 430 440 450
KHFEELVAMD ERFEIMAPRN FSLVCFRVSL LALEKKFNFV DETQVNEFNA
460 470 480 490 500
KLLESIISSG NVYMTHTVVE GVYMIRFAVG APLTDYPHID MAWNVVRNHA

TMMLNA
Length:506
Mass (Da):57,078
Last modified:August 22, 2006 - v1
Checksum:i605547DFA358C870
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ243784 mRNA. Translation: ABB72475.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ243784 mRNA. Translation: ABB72475.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13645.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR010977. Aromatic_deC.
IPR002129. PyrdxlP-dep_de-COase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
IPR021115. Pyridoxal-P_BS.
[Graphical view]
PfamiPF00282. Pyridoxal_deC. 1 hit.
[Graphical view]
PRINTSiPR00800. YHDCRBOXLASE.
SUPFAMiSSF53383. SSF53383. 1 hit.
PROSITEiPS00392. DDC_GAD_HDC_YDC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Plant phenylacetaldehyde synthase is a bifunctional homotetrameric enzyme that catalyzes phenylalanine decarboxylation and oxidation."
    Kaminaga Y., Schnepp J., Peel G., Kish C.M., Ben-Nissan G., Weiss D., Orlova I., Lavie O., Rhodes D., Wood K., Porterfield D.M., Cooper A.J., Schloss J.V., Pichersky E., Vainstein A., Dudareva N.
    J. Biol. Chem. 281:23357-23366(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.

Entry informationi

Entry nameiQ0ZQX0_PETHY
AccessioniPrimary (citable) accession number: Q0ZQX0
Entry historyi
Integrated into UniProtKB/TrEMBL: August 22, 2006
Last sequence update: August 22, 2006
Last modified: March 4, 2015
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

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 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.