Reviewed, UniProtKB/Swiss-Prot Q9SE93 (PNAE_RAUSE)

Names and origin

Protein names

Recommended name:
    Polyneuridine-aldehyde esterase
    EC=3.1.1.78
Alternative name(s):
    Polyneuridine aldehyde esterase

Gene names

Name:

PNAE

Organism

Rauvolfia serpentina (Serpentwood) (Devilpepper)

Taxonomic identifier

4060 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Gentianales › Apocynaceae › Rauvolfioideae › Vinceae › Rauvolfia

Protein attributes

Sequence length	264 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the hydrolysis of polyneuridine aldehyde into epi-vellosimine, which is the immediate precursor for the synthesis of the ajmaline. Ref.1
Catalytic activity	Polyneuridine aldehyde + H2O = 16-epivellosimine + CO2 + methanol.
Enzyme regulation	Inhibited by DEPC and HgCl2.
Pathway	Alkaloid biosynthesis; ajmaline biosynthesis.
Subunit structure	Homodimer; homodimerizes in aqueous solutions at pH 7.0. Ref.2
Miscellaneous	Ajmaline is an anti-arrhythmic alkaloid commercially used as an efficient drug for the treatment of arrhythmic heart disorder.
Sequence similarities	Belongs to the AB hydrolase superfamily.

Ontologies

Keywords
Biological process	Alkaloid metabolism
Molecular function	Hydrolase Serine esterase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	alkaloid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	polyneuridine-aldehyde esterase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Propeptide	1 – 6	6			PRO_0000022077
	Chain	7 – 264	258	Polyneuridine-aldehyde esterase		PRO_0000022078
Sites
	Active site	87	1
	Active site	216	1
	Active site	244	1
Experimental info
	Mutagenesis	17	1	H → A: No effect. Ref.2
	Mutagenesis	20	1	C → A: Loss of function. Ref.2
	Mutagenesis	86	1	H → A: Loss of function. Ref.2
	Mutagenesis	87	1	S → A: Loss of function. Ref.2
	Mutagenesis	132	1	C → A: No effect. Ref.2
	Mutagenesis	152	1	G → Q: No effect; when associated with S-213. Ref.2
	Mutagenesis	170	1	C → A: No effect. Ref.2
	Mutagenesis	213	1	C → S: No effect; when associated with Q-152. Ref.2
	Mutagenesis	216	1	D → A: Loss of function. Ref.2
	Mutagenesis	244	1	H → A: Loss of function. Ref.2
	Mutagenesis	257	1	C → A: No effect. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9SE93-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 3836517100C6E2DD	FASTA	264	29,655
	10 20 30 40 50 60 MHSAANAKQQ KHFVLVHGGC LGAWIWYKLK PLLESAGHKV TAVDLSAAGI NPRRLDEIHT 70 80 90 100 110 120 FRDYSEPLME VMASIPPDEK VVLLGHSFGG MSLGLAMETY PEKISVAVFM SAMMPDPNHS 130 140 150 160 170 180 LTYPFEKYNE KCPADMMLDS QFSTYGNPEN PGMSMILGPQ FMALKMFQNC SVEDLELAKM 190 200 210 220 230 240 LTRPGSLFFQ DLAKAKKFST ERYGSVKRAY IFCNEDKSFP VEFQKWFVES VGADKVKEIK 250 260 EADHMGMLSQ PREVCKCLLD ISDS

References

[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: 10691977] [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: 12071952] [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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AF178576 mRNA. Translation: AAF22288.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2WFL	X-ray	2.10	A	1-264	[»]
			B	1-264	[»]
3GZJ	X-ray	2.19	A/B/C/D/E	7-264	[»]

ModBase

Search...

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-7725.

BRENDA

3.1.1.78. 257570.

Family and domain databases

InterPro

IPR000073. AB_hydrolase_1.
[Graphical view]

Pfam

PF00561. Abhydrolase_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

PNAE_RAUSE

Accession

Primary (citable) accession number: Q9SE93

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	May 1, 2000
Last modified:	November 24, 2009
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)