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Protein

Polyneuridine-aldehyde esterase

Gene

PNAE

Organism
Rauvolfia serpentina (Serpentine wood) (Ophioxylon serpentinum)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the hydrolysis of polyneuridine aldehyde into epi-vellosimine, which is the immediate precursor for the synthesis of the ajmaline.1 Publication

Catalytic activityi

Polyneuridine aldehyde + H2O = 16-epivellosimine + CO2 + methanol.

Enzyme regulationi

Inhibited by DEPC and HgCl2.

Pathwayi: ajmaline biosynthesis

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei87 – 871
Active sitei216 – 2161
Active sitei244 – 2441

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Keywords - Biological processi

Alkaloid metabolism

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-7725.
BRENDAi3.1.1.78. 5309.
UniPathwayiUPA00310.

Protein family/group databases

ESTHERirause-pnae. Hydroxynitrile_lyase.

Names & Taxonomyi

Protein namesi
Recommended name:
Polyneuridine-aldehyde esterase (EC:3.1.1.78)
Alternative name(s):
Polyneuridine aldehyde esterase
Gene namesi
Name:PNAE
OrganismiRauvolfia serpentina (Serpentine wood) (Ophioxylon serpentinum)
Taxonomic identifieri4060 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsGentianalesApocynaceaeRauvolfioideaeVinceaeRauvolfiinaeRauvolfia

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi17 – 171H → A: No effect. 1 Publication
Mutagenesisi20 – 201C → A: Loss of function. 1 Publication
Mutagenesisi86 – 861H → A: Loss of function. 1 Publication
Mutagenesisi87 – 871S → A: Loss of function. 1 Publication
Mutagenesisi132 – 1321C → A: No effect. 1 Publication
Mutagenesisi152 – 1521G → Q: No effect; when associated with S-213. 1 Publication
Mutagenesisi170 – 1701C → A: No effect. 1 Publication
Mutagenesisi213 – 2131C → S: No effect; when associated with Q-152. 1 Publication
Mutagenesisi216 – 2161D → A: Loss of function. 1 Publication
Mutagenesisi244 – 2441H → A: Loss of function. 1 Publication
Mutagenesisi257 – 2571C → A: No effect. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 661 PublicationPRO_0000022077
Chaini7 – 264258Polyneuridine-aldehyde esterasePRO_0000022078Add
BLAST

Interactioni

Subunit structurei

Homodimer; homodimerizes in aqueous solutions at pH 7.0.

Structurei

Secondary structure

1
264
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi12 – 165Combined sources
Helixi23 – 264Combined sources
Helixi29 – 357Combined sources
Beta strandi39 – 435Combined sources
Helixi55 – 573Combined sources
Helixi61 – 7414Combined sources
Beta strandi81 – 866Combined sources
Helixi89 – 9911Combined sources
Helixi101 – 1033Combined sources
Beta strandi104 – 1129Combined sources
Helixi123 – 1319Combined sources
Turni134 – 1396Combined sources
Beta strandi141 – 1466Combined sources
Beta strandi152 – 1565Combined sources
Helixi159 – 1657Combined sources
Helixi172 – 18110Combined sources
Helixi189 – 1924Combined sources
Turni200 – 2023Combined sources
Helixi203 – 2053Combined sources
Beta strandi208 – 2136Combined sources
Beta strandi217 – 2193Combined sources
Helixi221 – 23111Combined sources
Beta strandi234 – 2396Combined sources
Helixi246 – 2494Combined sources
Helixi251 – 26212Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WFLX-ray2.10A/B1-264[»]
2WFMX-ray2.20A/B/C/D/E1-264[»]
3GZJX-ray2.19A/B/C/D/E7-264[»]
ProteinModelPortaliQ9SE93.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9SE93.

Family & Domainsi

Sequence similaritiesi

Belongs to the AB hydrolase superfamily.Curated

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9SE93-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHSAANAKQQ KHFVLVHGGC LGAWIWYKLK PLLESAGHKV TAVDLSAAGI
60 70 80 90 100
NPRRLDEIHT FRDYSEPLME VMASIPPDEK VVLLGHSFGG MSLGLAMETY
110 120 130 140 150
PEKISVAVFM SAMMPDPNHS LTYPFEKYNE KCPADMMLDS QFSTYGNPEN
160 170 180 190 200
PGMSMILGPQ FMALKMFQNC SVEDLELAKM LTRPGSLFFQ DLAKAKKFST
210 220 230 240 250
ERYGSVKRAY IFCNEDKSFP VEFQKWFVES VGADKVKEIK EADHMGMLSQ
260
PREVCKCLLD ISDS
Length:264
Mass (Da):29,655
Last modified:May 1, 2000 - v1
Checksum:i3836517100C6E2DD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF178576 mRNA. Translation: AAF22288.1.

Genome annotation databases

KEGGiag:AAF22288.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF178576 mRNA. Translation: AAF22288.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WFLX-ray2.10A/B1-264[»]
2WFMX-ray2.20A/B/C/D/E1-264[»]
3GZJX-ray2.19A/B/C/D/E7-264[»]
ProteinModelPortaliQ9SE93.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

ESTHERirause-pnae. Hydroxynitrile_lyase.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAF22288.

Enzyme and pathway databases

UniPathwayiUPA00310.
BioCyciMetaCyc:MONOMER-7725.
BRENDAi3.1.1.78. 5309.

Miscellaneous databases

EvolutionaryTraceiQ9SE93.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The gene encoding polyneuridine aldehyde esterase of monoterpenoid indole alkaloid biosynthesis in plants is an ortholog of the a/b hydrolase super family."
    Dogru E., Warzecha H., Seibel F., Haebel S., Lottspeich F., Stoeckigt J.
    Eur. J. Biochem. 267:1397-1406(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 7-23; 104-149; 208-217 AND 226-235, FUNCTION.
  2. "Potential active-site residues in polyneuridine aldehyde esterase, a central enzyme of indole alkaloid biosynthesis, by modelling and site-directed mutagenesis."
    Mattern-Dogru E., Ma X., Hartmann J., Decker H., Stoeckigt J.
    Eur. J. Biochem. 269:2889-2896(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: HOMODIMERIZATION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-17; CYS-20; HIS-86; SER-87; CYS-132; GLY-152; CYS-170; CYS-213; ASP-216; HIS-244 AND CYS-257.

Entry informationi

Entry nameiPNAE_RAUSE
AccessioniPrimary (citable) accession number: Q9SE93
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: May 1, 2000
Last modified: May 11, 2016
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Ajmaline is an anti-arrhythmic alkaloid commercially used as an efficient drug for the treatment of arrhythmic heart disorder.

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.