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Protein

(S)-hydroxynitrile lyase

Gene

HNL

Organism
Manihot esculenta (Cassava) (Jatropha manihot)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

An aliphatic (S)-hydroxynitrile = cyanide + an aliphatic aldehyde or ketone.
An aromatic (S)-hydroxynitrile = cyanide + an aromatic aldehyde.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei80By similarity1
Active sitei208By similarity1
Active sitei236By similarity1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-6902.
BRENDAi4.1.2.47. 3175.

Protein family/group databases

ESTHERimanes-hnl. Hydroxynitrile_lyase.

Names & Taxonomyi

Protein namesi
Recommended name:
(S)-hydroxynitrile lyase (EC:4.1.2.47)
Alternative name(s):
(S)-acetone-cyanohydrin lyase
Oxynitrilase
Gene namesi
Name:HNL
OrganismiManihot esculenta (Cassava) (Jatropha manihot)
Taxonomic identifieri3983 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsMalpighialesEuphorbiaceaeCrotonoideaeManihoteaeManihot

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi80S → A: Loss of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000840182 – 258(S)-hydroxynitrile lyaseAdd BLAST257

Interactioni

Subunit structurei

Homotrimer.

Structurei

Secondary structure

1258
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 9Combined sources5
Helixi16 – 19Combined sources4
Helixi22 – 28Combined sources7
Beta strandi32 – 36Combined sources5
Helixi48 – 50Combined sources3
Helixi54 – 57Combined sources4
Helixi59 – 67Combined sources9
Beta strandi74 – 80Combined sources7
Helixi83 – 93Combined sources11
Helixi94 – 96Combined sources3
Beta strandi97 – 105Combined sources9
Beta strandi110 – 112Combined sources3
Helixi116 – 124Combined sources9
Beta strandi132 – 137Combined sources6
Beta strandi143 – 148Combined sources6
Helixi151 – 157Combined sources7
Helixi164 – 173Combined sources10
Helixi181 – 185Combined sources5
Turni192 – 194Combined sources3
Helixi195 – 197Combined sources3
Beta strandi200 – 204Combined sources5
Beta strandi209 – 211Combined sources3
Helixi213 – 222Combined sources10
Beta strandi226 – 230Combined sources5
Helixi238 – 241Combined sources4
Helixi243 – 257Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DWOX-ray2.20A/B2-258[»]
1DWPX-ray2.20A/B2-258[»]
1DWQX-ray2.20A/B2-258[»]
1E89X-ray2.10A/B2-258[»]
1E8DX-ray2.20A/B2-258[»]
1EB8X-ray2.10A/B2-258[»]
1EB9X-ray2.10A/B2-258[»]
3RKSX-ray2.50A/B/C/D1-258[»]
3X3HX-ray2.88A/B/C/D/E/F/G/H1-258[»]
4YK7X-ray2.60A/B/C/D1-258[»]
ProteinModelPortaliP52705.
SMRiP52705.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP52705.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini5 – 242AB hydrolase-1Sequence analysisAdd BLAST238

Sequence similaritiesi

Phylogenomic databases

KOiK13033.

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.

P52705-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVTAHFVLIH TICHGAWIWH KLKPALERAG HKVTALDMAA SGIDPRQIEQ
60 70 80 90 100
INSFDEYSEP LLTFLEKLPQ GEKVIIVGES CAGLNIAIAA DRYVDKIAAG
110 120 130 140 150
VFHNSLLPDT VHSPSYTVEK LLESFPDWRD TEYFTFTNIT GETITTMKLG
160 170 180 190 200
FVLLRENLFT KCTDGEYELA KMVMRKGSLF QNVLAQRPKF TEKGYGSIKK
210 220 230 240 250
VYIWTDQDKI FLPDFQRWQI ANYKPDKVYQ VQGGDHKLQL TKTEEVAHIL

QEVADAYA
Length:258
Mass (Da):29,372
Last modified:January 23, 2007 - v3
Checksum:i98ABA050AC8AF1C5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z29091 mRNA. Translation: CAA82334.1.

Genome annotation databases

KEGGiag:CAA82334.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z29091 mRNA. Translation: CAA82334.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DWOX-ray2.20A/B2-258[»]
1DWPX-ray2.20A/B2-258[»]
1DWQX-ray2.20A/B2-258[»]
1E89X-ray2.10A/B2-258[»]
1E8DX-ray2.20A/B2-258[»]
1EB8X-ray2.10A/B2-258[»]
1EB9X-ray2.10A/B2-258[»]
3RKSX-ray2.50A/B/C/D1-258[»]
3X3HX-ray2.88A/B/C/D/E/F/G/H1-258[»]
4YK7X-ray2.60A/B/C/D1-258[»]
ProteinModelPortaliP52705.
SMRiP52705.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

ESTHERimanes-hnl. Hydroxynitrile_lyase.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:CAA82334.

Phylogenomic databases

KOiK13033.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-6902.
BRENDAi4.1.2.47. 3175.

Miscellaneous databases

EvolutionaryTraceiP52705.

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 nameiHNL_MANES
AccessioniPrimary (citable) accession number: P52705
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 86 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.