P52705 (HNL_MANES) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
(S)-hydroxynitrile lyase
EC=4.1.2.47

Alternative name(s):
(S)-acetone-cyanohydrin lyase
Oxynitrilase

Gene names

Name:

HNL

Organism

Manihot esculenta (Cassava) (Jatropha manihot)

Taxonomic identifier

3983 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Malpighiales › Euphorbiaceae › Crotonoideae › Manihoteae › Manihot

Protein attributes

Sequence length	258 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	Involved in cyanogenesis, the release of HCN from injured tissues. Decomposes a varieties of (R) or (S) cyanohydrins into HCN and the corresponding aldehydes and ketones. The natural substrate of this enzyme is (S)-acetone cyanohydrin.
Catalytic activity	An aliphatic (S)-hydroxynitrile = cyanide + an aliphatic aldehyde or ketone. An aromatic (S)-hydroxynitrile = cyanide + an aromatic aldehyde.
Subunit structure	Homotrimer.
Sequence similarities	Belongs to the AB hydrolase superfamily. Hydroxynitrile lyase family.

Ontologies

Keywords
Molecular function	Lyase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Molecular_function	aliphatic (S)-hydroxynitrile lyase activity Inferred from electronic annotation. Source: EC aromatic (S)-hydroxynitrile lyase 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

Initiator methionine

1

1

Removed Ref.1

Chain

2 – 258

257

(S)-hydroxynitrile lyase

PRO_0000084018

Sites

Active site

80

1

By similarity

Active site

208

1

By similarity

Active site

236

1

By similarity

Experimental info

Mutagenesis

80

1

S → A: Loss of activity. Ref.3

Secondary structure

1

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258

Helix Strand Turn

Details...

Beta strand

5 – 9

5

Helix

16 – 19

4

Helix

22 – 28

7

Beta strand

32 – 36

5

Helix

48 – 50

3

Helix

54 – 57

4

Helix

59 – 67

9

Beta strand

74 – 80

7

Helix

83 – 93

11

Helix

94 – 96

3

Beta strand

97 – 105

9

Beta strand

110 – 112

3

Helix

116 – 124

9

Beta strand

132 – 137

6

Beta strand

143 – 148

6

Helix

151 – 157

7

Helix

164 – 173

10

Helix

181 – 185

5

Turn

192 – 194

3

Helix

195 – 197

3

Beta strand

200 – 204

5

Beta strand

209 – 211

3

Helix

213 – 222

10

Beta strand

226 – 230

5

Helix

238 – 241

4

Helix

243 – 257

15

Sequences

	Sequence		Length	Mass (Da)
	P52705 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 98ABA050AC8AF1C5	FASTA	258	29,372
	10 20 30 40 50 60 MVTAHFVLIH TICHGAWIWH KLKPALERAG HKVTALDMAA SGIDPRQIEQ INSFDEYSEP 70 80 90 100 110 120 LLTFLEKLPQ GEKVIIVGES CAGLNIAIAA DRYVDKIAAG VFHNSLLPDT VHSPSYTVEK 130 140 150 160 170 180 LLESFPDWRD TEYFTFTNIT GETITTMKLG FVLLRENLFT KCTDGEYELA KMVMRKGSLF 190 200 210 220 230 240 QNVLAQRPKF TEKGYGSIKK VYIWTDQDKI FLPDFQRWQI ANYKPDKVYQ VQGGDHKLQL 250 TKTEEVAHIL QEVADAYA

References

[1]	"Purification, characterization, and cloning of alpha-hydroxynitrile lyase from cassava (Manihot esculenta Crantz)." Hughes J., Carvalho F.J.P.D.C., Hughes M.A. Arch. Biochem. Biophys. 311:496-502(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-37 AND 169-192. Tissue: Cotyledon.
[2]	"Structure of hydroxynitrile lyase from Manihot esculenta in complex with substrates acetone and chloroacetone: implications for the mechanism of cyanogenesis." Lauble H., Foerster S., Miehlich B., Wajant H., Effenberger F. Acta Crystallogr. D 57:194-200(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[3]	"Mechanistic aspects of cyanogenesis from active-site mutant Ser80Ala of hydroxynitrile lyase from Manihot esculenta in complex with acetone cyanohydrin." Lauble H., Miehlich B., Foerster S., Wajant H., Effenberger F. Protein Sci. 10:1015-1022(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), MUTAGENESIS OF SER-80.
[4]	"Structure determinants of substrate specificity of hydroxynitrile lyase from Manihot esculenta." Lauble H., Miehlich B., Foerster S., Kobler C., Wajant H., Effenberger F. Protein Sci. 11:65-71(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z29091 mRNA. Translation: CAA82334.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DWO	X-ray	2.20	A/B	1-258	[»]
1DWP	X-ray	2.20	A/B	1-258	[»]
1DWQ	X-ray	2.20	A/B	1-258	[»]
1E89	X-ray	2.10	A/B	1-258	[»]
1E8D	X-ray	2.20	A/B	1-258	[»]
1EB8	X-ray	2.10	A/B	1-258	[»]
1EB9	X-ray	2.10	A/B	1-258	[»]
3RKS	X-ray	2.50	A/B/C/D	1-258	[»]
3RKT	X-ray	2.91	A/B/C/D/E/F/G/H	1-258	[»]

ProteinModelPortal

P52705.

SMR

P52705. Positions 1-258.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-6902.

Family and domain databases

InterPro

IPR000073. AB_hydrolase_1.
[Graphical view]

Pfam

PF00561. Abhydrolase_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P52705.

Entry information

Entry name

HNL_MANES

Accession

Primary (citable) accession number: P52705

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 69 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program