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Q9LFT6

- HNL_ARATH

UniProt

Q9LFT6 - HNL_ARATH

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Protein

Alpha-hydroxynitrile lyase

Gene

HNL

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Involved in cyanogenesis, the release of HCN from injured tissues (By similarity). Displays R-selective hydroxynitrile lyase activity. Also accepts nitromethane (MeNO2) as a donor in a reaction with aromatic aldehydes to yield (R)-beta-nitro alcohols.By similarity4 Publications

Catalytic activityi

(R)-mandelonitrile = cyanide + benzaldehyde.1 Publication

Kineticsi

  1. KM=1.4 mM for mandelonitrile1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei81 – 811
Active sitei208 – 2081
Active sitei236 – 2361

GO - Molecular functioni

  1. mandelonitrile lyase activity Source: TAIR

GO - Biological processi

  1. glycoside catabolic process Source: TAIR
  2. response to wounding Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Enzyme and pathway databases

BioCyciARA:AT5G10300-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-hydroxynitrile lyase (EC:4.1.2.10)
Short name:
AtHNL
Alternative name(s):
(R)-hydroxynitrile lyase
(R)-oxynitrilase
Methylesterase 5
Short name:
AtMES5
Gene namesi
Name:HNL
Synonyms:MES5
Ordered Locus Names:At5g10300
ORF Names:F18D22_70
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 5

Organism-specific databases

TAIRiAT5G10300.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi81 – 811S → A: Loss of activity. 1 Publication
Mutagenesisi208 – 2081D → N: Loss of activity. 1 Publication
Mutagenesisi236 – 2361H → F: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 258258Alpha-hydroxynitrile lyasePRO_0000418174Add
BLAST

Proteomic databases

PRIDEiQ9LFT6.

Expressioni

Gene expression databases

GenevestigatoriQ9LFT6.

Interactioni

Subunit structurei

Homodimer.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
MES9O231713EBI-4453194,EBI-4446268

Protein-protein interaction databases

IntActiQ9LFT6. 1 interaction.
STRINGi3702.AT5G10300.1-P.

Structurei

Secondary structure

1
258
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 105Combined sources
Helixi17 – 204Combined sources
Helixi23 – 297Combined sources
Beta strandi33 – 375Combined sources
Helixi49 – 513Combined sources
Helixi55 – 6713Combined sources
Beta strandi75 – 806Combined sources
Helixi83 – 919Combined sources
Helixi95 – 973Combined sources
Beta strandi98 – 1058Combined sources
Beta strandi111 – 1133Combined sources
Helixi117 – 1237Combined sources
Beta strandi133 – 1397Combined sources
Beta strandi142 – 1487Combined sources
Helixi151 – 1577Combined sources
Helixi164 – 17310Combined sources
Helixi181 – 1855Combined sources
Turni192 – 1943Combined sources
Helixi195 – 1973Combined sources
Beta strandi200 – 2056Combined sources
Beta strandi209 – 2113Combined sources
Helixi213 – 22210Combined sources
Beta strandi228 – 2314Combined sources
Helixi238 – 2414Combined sources
Helixi243 – 25614Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DQZX-ray2.50A/B/C/D1-258[»]
ProteinModelPortaliQ9LFT6.
SMRiQ9LFT6. Positions 3-258.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9LFT6.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG252413.
HOGENOMiHOG000133452.
InParanoidiQ9LFT6.
OMAiSHETRNG.
PhylomeDBiQ9LFT6.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q9LFT6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MERKHHFVLV HNAYHGAWIW YKLKPLLESA GHRVTAVELA ASGIDPRPIQ
60 70 80 90 100
AVETVDEYSK PLIETLKSLP ENEEVILVGF SFGGINIALA ADIFPAKIKV
110 120 130 140 150
LVFLNAFLPD TTHVPSHVLD KYMEMPGGLG DCEFSSHETR NGTMSLLKMG
160 170 180 190 200
PKFMKARLYQ NCPIEDYELA KMLHRQGSFF TEDLSKKEKF SEEGYGSVQR
210 220 230 240 250
VYVMSSEDKA IPCDFIRWMI DNFNVSKVYE IDGGDHMVML SKPQKLFDSL

SAIATDYM
Length:258
Mass (Da):29,217
Last modified:October 1, 2000 - v1
Checksum:i0CFA965320F1FD2E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti70 – 701P → Q in AAL25532. (PubMed:14593172)Curated
Sequence conflicti75 – 751V → G in AAL25532. (PubMed:14593172)Curated
Sequence conflicti177 – 1771G → R in AAK76689. (PubMed:14593172)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL360334 Genomic DNA. Translation: CAB96686.1.
CP002688 Genomic DNA. Translation: AED91518.1.
AY046015 mRNA. Translation: AAK76689.1.
AY058115 mRNA. Translation: AAL25532.1.
AY093714 mRNA. Translation: AAM10338.1.
AY142490 mRNA. Translation: AAN13041.1.
AK226255 mRNA. Translation: BAE98416.1.
PIRiT50818.
RefSeqiNP_196592.1. NM_121068.3.
UniGeneiAt.19934.

Genome annotation databases

EnsemblPlantsiAT5G10300.1; AT5G10300.1; AT5G10300.
GeneIDi830894.
KEGGiath:AT5G10300.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL360334 Genomic DNA. Translation: CAB96686.1 .
CP002688 Genomic DNA. Translation: AED91518.1 .
AY046015 mRNA. Translation: AAK76689.1 .
AY058115 mRNA. Translation: AAL25532.1 .
AY093714 mRNA. Translation: AAM10338.1 .
AY142490 mRNA. Translation: AAN13041.1 .
AK226255 mRNA. Translation: BAE98416.1 .
PIRi T50818.
RefSeqi NP_196592.1. NM_121068.3.
UniGenei At.19934.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3DQZ X-ray 2.50 A/B/C/D 1-258 [» ]
ProteinModelPortali Q9LFT6.
SMRi Q9LFT6. Positions 3-258.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9LFT6. 1 interaction.
STRINGi 3702.AT5G10300.1-P.

Proteomic databases

PRIDEi Q9LFT6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT5G10300.1 ; AT5G10300.1 ; AT5G10300 .
GeneIDi 830894.
KEGGi ath:AT5G10300.

Organism-specific databases

TAIRi AT5G10300.

Phylogenomic databases

eggNOGi NOG252413.
HOGENOMi HOG000133452.
InParanoidi Q9LFT6.
OMAi SHETRNG.
PhylomeDBi Q9LFT6.

Enzyme and pathway databases

BioCyci ARA:AT5G10300-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q9LFT6.

Gene expression databases

Genevestigatori Q9LFT6.

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

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
    Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.
    , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
    Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "Inactive methyl indole-3-acetic acid ester can be hydrolyzed and activated by several esterases belonging to the AtMES esterase family of Arabidopsis."
    Yang Y., Xu R., Ma C.J., Vlot A.C., Klessig D.F., Pichersky E.
    Plant Physiol. 147:1034-1045(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY, FUNCTION.
  6. "Uneven twins: comparison of two enantiocomplementary hydroxynitrile lyases with alpha/beta-hydrolase fold."
    Guterl J.K., Andexer J.N., Sehl T., von Langermann J., Frindi-Wosch I., Rosenkranz T., Fitter J., Gruber K., Kragl U., Eggert T., Pohl M.
    J. Biotechnol. 141:166-173(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
  7. "Synthesis of (R)-?-nitro alcohols catalyzed by R-selective hydroxynitrile lyase from Arabidopsis thaliana in the aqueous-organic biphasic system."
    Fuhshuku K., Asano Y.
    J. Biotechnol. 153:153-159(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "An R-selective hydroxynitrile lyase from Arabidopsis thaliana with an alpha/beta-hydrolase fold."
    Andexer J., von Langermann J., Mell A., Bocola M., Kragl U., Eggert T., Pohl M.
    Angew. Chem. Int. Ed. Engl. 46:8679-8681(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF SER-81; ASP-208 AND HIS-236.

Entry informationi

Entry nameiHNL_ARATH
AccessioniPrimary (citable) accession number: Q9LFT6
Secondary accession number(s): Q93Z57, Q94AI5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2012
Last sequence update: October 1, 2000
Last modified: November 26, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Caution

Was originally thought to belong to the methylesterase (MES) family.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3