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P52705

- HNL_MANES

UniProt

P52705 - HNL_MANES

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Protein
(S)-hydroxynitrile lyase
Gene
HNL
Organism
Manihot esculenta (Cassava) (Jatropha manihot)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei80 – 801 By similarity
Active sitei208 – 2081 By similarity
Active sitei236 – 2361 By similarity

GO - Molecular functioni

  1. aliphatic (S)-hydroxynitrile lyase activity Source: UniProtKB-EC
  2. aromatic (S)-hydroxynitrile lyase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-6902.

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi80 – 801S → A: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 258257(S)-hydroxynitrile lyase
PRO_0000084018Add
BLAST

Interactioni

Subunit structurei

Homotrimer.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 95
Helixi16 – 194
Helixi22 – 287
Beta strandi32 – 365
Helixi48 – 503
Helixi54 – 574
Helixi59 – 679
Beta strandi74 – 807
Helixi83 – 9311
Helixi94 – 963
Beta strandi97 – 1059
Beta strandi110 – 1123
Helixi116 – 1249
Beta strandi132 – 1376
Beta strandi143 – 1486
Helixi151 – 1577
Helixi164 – 17310
Helixi181 – 1855
Turni192 – 1943
Helixi195 – 1973
Beta strandi200 – 2045
Beta strandi209 – 2113
Helixi213 – 22210
Beta strandi226 – 2305
Helixi238 – 2414
Helixi243 – 25715

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
3RKTX-ray2.91A/B/C/D/E/F/G/H1-258[»]
ProteinModelPortaliP52705.
SMRiP52705. Positions 1-258.

Miscellaneous databases

EvolutionaryTraceiP52705.

Family & Domainsi

Sequence similaritiesi

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

MVTAHFVLIH TICHGAWIWH KLKPALERAG HKVTALDMAA SGIDPRQIEQ    50
INSFDEYSEP LLTFLEKLPQ GEKVIIVGES CAGLNIAIAA DRYVDKIAAG 100
VFHNSLLPDT VHSPSYTVEK LLESFPDWRD TEYFTFTNIT GETITTMKLG 150
FVLLRENLFT KCTDGEYELA KMVMRKGSLF QNVLAQRPKF TEKGYGSIKK 200
VYIWTDQDKI FLPDFQRWQI ANYKPDKVYQ VQGGDHKLQL TKTEEVAHIL 250
QEVADAYA 258
Length:258
Mass (Da):29,372
Last modified:January 23, 2007 - v3
Checksum:i98ABA050AC8AF1C5
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z29091 mRNA. Translation: CAA82334.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z29091 mRNA. Translation: CAA82334.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DWO X-ray 2.20 A/B 2-258 [» ]
1DWP X-ray 2.20 A/B 2-258 [» ]
1DWQ X-ray 2.20 A/B 2-258 [» ]
1E89 X-ray 2.10 A/B 2-258 [» ]
1E8D X-ray 2.20 A/B 2-258 [» ]
1EB8 X-ray 2.10 A/B 2-258 [» ]
1EB9 X-ray 2.10 A/B 2-258 [» ]
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 [» ]
ProteinModelPortali P52705.
SMRi P52705. Positions 1-258.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-6902.

Miscellaneous databases

EvolutionaryTracei P52705.

Family and domain databases

Gene3Di 3.40.50.1820. 1 hit.
InterProi IPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
[Graphical view ]
Pfami PF00561. Abhydrolase_1. 1 hit.
[Graphical view ]
SUPFAMi SSF53474. SSF53474. 1 hit.
ProtoNeti Search...

Publicationsi

  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).

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: July 9, 2014
This is version 74 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

External Data

Dasty 3

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