Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P52705

- HNL_MANES

UniProt

P52705 - HNL_MANES

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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 – 801By similarity
Active sitei208 – 2081By similarity
Active sitei236 – 2361By 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 lyasePRO_0000084018Add
BLAST

Interactioni

Subunit structurei

Homotrimer.

Structurei

Secondary structure

1
258
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 95Combined sources
Helixi16 – 194Combined sources
Helixi22 – 287Combined sources
Beta strandi32 – 365Combined sources
Helixi48 – 503Combined sources
Helixi54 – 574Combined sources
Helixi59 – 679Combined sources
Beta strandi74 – 807Combined sources
Helixi83 – 9311Combined sources
Helixi94 – 963Combined sources
Beta strandi97 – 1059Combined sources
Beta strandi110 – 1123Combined sources
Helixi116 – 1249Combined sources
Beta strandi132 – 1376Combined sources
Beta strandi143 – 1486Combined sources
Helixi151 – 1577Combined sources
Helixi164 – 17310Combined sources
Helixi181 – 1855Combined sources
Turni192 – 1943Combined sources
Helixi195 – 1973Combined sources
Beta strandi200 – 2045Combined sources
Beta strandi209 – 2113Combined sources
Helixi213 – 22210Combined sources
Beta strandi226 – 2305Combined sources
Helixi238 – 2414Combined sources
Helixi243 – 25715Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

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

        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.

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
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: October 29, 2014
This is version 76 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