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P52704

- HNL_HEVBR

UniProt

P52704 - HNL_HEVBR

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Protein

(S)-hydroxynitrile lyase

Gene

HNL

Organism
Hevea brasiliensis (Para rubber tree) (Siphonia brasiliensis)
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
Active sitei207 – 2071
Active sitei235 – 2351

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

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
OrganismiHevea brasiliensis (Para rubber tree) (Siphonia brasiliensis)
Taxonomic identifieri3981 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsMalpighialesEuphorbiaceaeCrotonoideaeMicrandreaeHevea

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi80 – 801S → A: Loss of activity. 1 Publication
Mutagenesisi81 – 811C → S: Loss of activity. 1 Publication
Mutagenesisi235 – 2351H → A: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 257257(S)-hydroxynitrile lyasePRO_0000084017Add
BLAST

Post-translational modificationi

The N-terminus is blocked.

Proteomic databases

PRIDEiP52704.

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1
257
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 – 668Combined sources
Beta strandi74 – 807Combined sources
Helixi82 – 9312Combined sources
Helixi94 – 963Combined sources
Beta strandi97 – 1059Combined sources
Beta strandi110 – 1123Combined sources
Helixi116 – 1249Combined sources
Beta strandi132 – 1387Combined sources
Beta strandi141 – 1477Combined sources
Helixi150 – 1567Combined sources
Helixi163 – 17210Combined sources
Helixi180 – 1856Combined sources
Turni191 – 1933Combined sources
Helixi194 – 1963Combined sources
Beta strandi199 – 2035Combined sources
Beta strandi208 – 2103Combined sources
Helixi212 – 22110Combined sources
Beta strandi225 – 2295Combined sources
Helixi237 – 2404Combined sources
Helixi242 – 25514Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QJ4X-ray1.10A1-257[»]
1SC9X-ray1.80A1-257[»]
1SCIX-ray2.18A1-257[»]
1SCKX-ray1.70A1-257[»]
1SCQX-ray2.90A1-257[»]
1YASX-ray1.90A1-257[»]
1YB6X-ray1.54A2-257[»]
1YB7X-ray1.76A2-257[»]
2G4LX-ray1.84A1-257[»]
2YASX-ray1.72A1-257[»]
3C6XX-ray1.05A1-257[»]
3C6YX-ray1.25A1-257[»]
3C6ZX-ray1.05A1-257[»]
3C70X-ray1.05A1-257[»]
3YASX-ray1.85A1-257[»]
4YASX-ray2.00A1-257[»]
5YASX-ray2.20A1-257[»]
6YASX-ray2.20A1-257[»]
7YASX-ray1.75A1-257[»]
ProteinModelPortaliP52704.
SMRiP52704. Positions 2-257.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP52704.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequencei

Sequence statusi: Complete.

P52704-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAFAHFVLIH TICHGAWIWH KLKPLLEALG HKVTALDLAA SGVDPRQIEE
60 70 80 90 100
IGSFDEYSEP LLTFLEALPP GEKVILVGES CGGLNIAIAA DKYCEKIAAA
110 120 130 140 150
VFHNSVLPDT EHCPSYVVDK LMEVFPDWKD TTYFTYTKDG KEITGLKLGF
160 170 180 190 200
TLLRENLYTL CGPEEYELAK MLTRKGSLFQ NILAKRPFFT KEGYGSIKKI
210 220 230 240 250
YVWTDQDEIF LPEFQLWQIE NYKPDKVYKV EGGDHKLQLT KTKEIAEILQ

EVADTYN
Length:257
Mass (Da):29,228
Last modified:October 1, 1996 - v1
Checksum:iEF4AE88717279CEB
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U40402 mRNA. Translation: AAC49184.1.
PIRiT10758.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U40402 mRNA. Translation: AAC49184.1 .
PIRi T10758.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1QJ4 X-ray 1.10 A 1-257 [» ]
1SC9 X-ray 1.80 A 1-257 [» ]
1SCI X-ray 2.18 A 1-257 [» ]
1SCK X-ray 1.70 A 1-257 [» ]
1SCQ X-ray 2.90 A 1-257 [» ]
1YAS X-ray 1.90 A 1-257 [» ]
1YB6 X-ray 1.54 A 2-257 [» ]
1YB7 X-ray 1.76 A 2-257 [» ]
2G4L X-ray 1.84 A 1-257 [» ]
2YAS X-ray 1.72 A 1-257 [» ]
3C6X X-ray 1.05 A 1-257 [» ]
3C6Y X-ray 1.25 A 1-257 [» ]
3C6Z X-ray 1.05 A 1-257 [» ]
3C70 X-ray 1.05 A 1-257 [» ]
3YAS X-ray 1.85 A 1-257 [» ]
4YAS X-ray 2.00 A 1-257 [» ]
5YAS X-ray 2.20 A 1-257 [» ]
6YAS X-ray 2.20 A 1-257 [» ]
7YAS X-ray 1.75 A 1-257 [» ]
ProteinModelPortali P52704.
SMRi P52704. Positions 2-257.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi P52704.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P52704.

Family and domain databases

Gene3Di 3.40.50.1820. 1 hit.
InterProi IPR029058. AB_hydrolase.
[Graphical view ]
SUPFAMi SSF53474. SSF53474. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Molecular cloning of the full-length cDNA of (S)-hydroxynitrile lyase from Hevea brasiliensis. Functional expression in Escherichia coli and Saccharomyces cerevisiae and identification of an active site residue."
    Hasslacher M., Schall M., Hayn M., Griengl H., Kohlwein S.D., Schwab H.
    J. Biol. Chem. 271:5884-5891(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 121-126; 176-181; 200-204 AND 244-253, MUTAGENESIS OF CYS-81.
    Tissue: Leaf.
  2. "Mechanism of cyanogenesis: the crystal structure of hydroxynitrile lyase from Hevea brasiliensis."
    Wagner U.G., Hasslacher M., Griengl H., Schwab H., Kratky C.
    Structure 4:811-822(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), MUTAGENESIS OF SER-80 AND HIS-235.
  3. "Atomic resolution crystal structure of hydroxynitrile lyase from Hevea brasiliensis."
    Gruber K., Gugganig M., Wagner U.G., Kratky C.
    Biol. Chem. 380:993-1000(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS).
  4. "Three-dimensional structures of enzyme-substrate complexes of the hydroxynitrile lyase from Hevea brasiliensis."
    Zuegg J., Gruber K., Gugganig M., Wagner U.G., Kratky C.
    Protein Sci. 8:1990-2000(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS).

Entry informationi

Entry nameiHNL_HEVBR
AccessioniPrimary (citable) accession number: P52704
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: October 29, 2014
This is version 78 of the entry and version 1 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