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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)DescriptionActionsGraphical viewLength
Active sitei871
Active sitei2161
Active sitei2441

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)DescriptionActionsGraphical viewLength
Mutagenesisi17H → A: No effect. 1 Publication1
Mutagenesisi20C → A: Loss of function. 1 Publication1
Mutagenesisi86H → A: Loss of function. 1 Publication1
Mutagenesisi87S → A: Loss of function. 1 Publication1
Mutagenesisi132C → A: No effect. 1 Publication1
Mutagenesisi152G → Q: No effect; when associated with S-213. 1 Publication1
Mutagenesisi170C → A: No effect. 1 Publication1
Mutagenesisi213C → S: No effect; when associated with Q-152. 1 Publication1
Mutagenesisi216D → A: Loss of function. 1 Publication1
Mutagenesisi244H → A: Loss of function. 1 Publication1
Mutagenesisi257C → A: No effect. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000220771 – 61 Publication6
ChainiPRO_00000220787 – 264Polyneuridine-aldehyde esteraseAdd BLAST258

Interactioni

Subunit structurei

Homodimer; homodimerizes in aqueous solutions at pH 7.0.

Structurei

Secondary structure

1264
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi12 – 16Combined sources5
Helixi23 – 26Combined sources4
Helixi29 – 35Combined sources7
Beta strandi39 – 43Combined sources5
Helixi55 – 57Combined sources3
Helixi61 – 74Combined sources14
Beta strandi81 – 86Combined sources6
Helixi89 – 99Combined sources11
Helixi101 – 103Combined sources3
Beta strandi104 – 112Combined sources9
Helixi123 – 131Combined sources9
Turni134 – 139Combined sources6
Beta strandi141 – 146Combined sources6
Beta strandi152 – 156Combined sources5
Helixi159 – 165Combined sources7
Helixi172 – 181Combined sources10
Helixi189 – 192Combined sources4
Turni200 – 202Combined sources3
Helixi203 – 205Combined sources3
Beta strandi208 – 213Combined sources6
Beta strandi217 – 219Combined sources3
Helixi221 – 231Combined sources11
Beta strandi234 – 239Combined sources6
Helixi246 – 249Combined sources4
Helixi251 – 262Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
SMRiQ9SE93.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9SE93.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini12 – 122AB hydrolase-1Sequence analysisAdd BLAST111

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
PDB 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.
SMRiQ9SE93.
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...

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: November 2, 2016
This is version 66 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.