ID   HNL_ARATH               Reviewed;         258 AA.
AC   Q9LFT6; Q93Z57; Q94AI5;
DT   11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 135.
DE   RecName: Full=Alpha-hydroxynitrile lyase {ECO:0000303|PubMed:17907254};
DE            Short=AtHNL {ECO:0000303|PubMed:17907254};
DE            EC=4.1.2.10 {ECO:0000269|PubMed:17907254};
DE   AltName: Full=(R)-hydroxynitrile lyase {ECO:0000303|PubMed:17907254};
DE   AltName: Full=(R)-oxynitrilase {ECO:0000303|PubMed:17907254};
DE   AltName: Full=Methylesterase 5 {ECO:0000303|PubMed:18467465};
DE            Short=AtMES5 {ECO:0000303|PubMed:18467465};
GN   Name=HNL {ECO:0000303|PubMed:17907254};
GN   Synonyms=MES5 {ECO:0000303|PubMed:18467465};
GN   OrderedLocusNames=At5g10300 {ECO:0000312|Araport:AT5G10300};
GN   ORFNames=F18D22_70 {ECO:0000312|EMBL:CAB96686.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   GENE FAMILY, AND FUNCTION.
RX   PubMed=18467465; DOI=10.1104/pp.108.118224;
RA   Yang Y., Xu R., Ma C.J., Vlot A.C., Klessig D.F., Pichersky E.;
RT   "Inactive methyl indole-3-acetic acid ester can be hydrolyzed and activated
RT   by several esterases belonging to the AtMES esterase family of
RT   Arabidopsis.";
RL   Plant Physiol. 147:1034-1045(2008).
RN   [6]
RP   FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=19433222; DOI=10.1016/j.jbiotec.2009.03.010;
RA   Guterl J.K., Andexer J.N., Sehl T., von Langermann J., Frindi-Wosch I.,
RA   Rosenkranz T., Fitter J., Gruber K., Kragl U., Eggert T., Pohl M.;
RT   "Uneven twins: comparison of two enantiocomplementary hydroxynitrile lyases
RT   with alpha/beta-hydrolase fold.";
RL   J. Biotechnol. 141:166-173(2009).
RN   [7]
RP   FUNCTION.
RX   PubMed=21439333; DOI=10.1016/j.jbiotec.2011.03.011;
RA   Fuhshuku K., Asano Y.;
RT   "Synthesis of (R)-?-nitro alcohols catalyzed by R-selective hydroxynitrile
RT   lyase from Arabidopsis thaliana in the aqueous-organic biphasic system.";
RL   J. Biotechnol. 153:153-159(2011).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, AND
RP   MUTAGENESIS OF SER-81; ASP-208 AND HIS-236.
RX   PubMed=17907254; DOI=10.1002/anie.200701455;
RA   Andexer J., von Langermann J., Mell A., Bocola M., Kragl U., Eggert T.,
RA   Pohl M.;
RT   "An R-selective hydroxynitrile lyase from Arabidopsis thaliana with an
RT   alpha/beta-hydrolase fold.";
RL   Angew. Chem. Int. Ed. Engl. 46:8679-8681(2007).
CC   -!- FUNCTION: Involved in cyanogenesis, the release of HCN from injured
CC       tissues (By similarity). Displays R-selective hydroxynitrile lyase
CC       activity. Also accepts nitromethane (MeNO2) as a donor in a reaction
CC       with aromatic aldehydes to yield (R)-beta-nitro alcohols. {ECO:0000250,
CC       ECO:0000269|PubMed:17907254, ECO:0000269|PubMed:18467465,
CC       ECO:0000269|PubMed:19433222, ECO:0000269|PubMed:21439333}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-mandelonitrile = benzaldehyde + hydrogen cyanide;
CC         Xref=Rhea:RHEA:18313, ChEBI:CHEBI:17169, ChEBI:CHEBI:18407,
CC         ChEBI:CHEBI:18450; EC=4.1.2.10;
CC         Evidence={ECO:0000269|PubMed:17907254};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.4 mM for mandelonitrile {ECO:0000269|PubMed:19433222};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q9LFT6; O23171: MES9; NbExp=3; IntAct=EBI-4453194, EBI-4446268;
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Hydroxynitrile
CC       lyase family. {ECO:0000305}.
CC   -!- CAUTION: Was originally thought to belong to the methylesterase (MES)
CC       family. {ECO:0000305|PubMed:19433222}.
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DR   EMBL; AL360334; CAB96686.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED91518.1; -; Genomic_DNA.
DR   EMBL; AY046015; AAK76689.1; -; mRNA.
DR   EMBL; AY058115; AAL25532.1; -; mRNA.
DR   EMBL; AY093714; AAM10338.1; -; mRNA.
DR   EMBL; AY142490; AAN13041.1; -; mRNA.
DR   EMBL; AK226255; BAE98416.1; -; mRNA.
DR   PIR; T50818; T50818.
DR   RefSeq; NP_196592.1; NM_121068.4.
DR   PDB; 3DQZ; X-ray; 2.50 A; A/B/C/D=1-258.
DR   PDB; 6COB; X-ray; 1.82 A; A/B=1-258.
DR   PDB; 6COC; X-ray; 1.93 A; A/B=1-258.
DR   PDB; 6COD; X-ray; 1.80 A; A/B=1-258.
DR   PDB; 6COE; X-ray; 1.84 A; A/B=1-258.
DR   PDB; 6COF; X-ray; 1.52 A; A/B=1-258.
DR   PDB; 6COG; X-ray; 1.80 A; A/B=1-258.
DR   PDB; 6COH; X-ray; 2.37 A; A/B=1-258.
DR   PDB; 6COI; X-ray; 2.02 A; A/B=1-258.
DR   PDBsum; 3DQZ; -.
DR   PDBsum; 6COB; -.
DR   PDBsum; 6COC; -.
DR   PDBsum; 6COD; -.
DR   PDBsum; 6COE; -.
DR   PDBsum; 6COF; -.
DR   PDBsum; 6COG; -.
DR   PDBsum; 6COH; -.
DR   PDBsum; 6COI; -.
DR   AlphaFoldDB; Q9LFT6; -.
DR   SMR; Q9LFT6; -.
DR   BioGRID; 16172; 1.
DR   IntAct; Q9LFT6; 1.
DR   STRING; 3702.Q9LFT6; -.
DR   ESTHER; arath-HNL; Hydroxynitrile_lyase.
DR   PaxDb; 3702-AT5G10300-1; -.
DR   ProteomicsDB; 230261; -.
DR   EnsemblPlants; AT5G10300.1; AT5G10300.1; AT5G10300.
DR   GeneID; 830894; -.
DR   Gramene; AT5G10300.1; AT5G10300.1; AT5G10300.
DR   KEGG; ath:AT5G10300; -.
DR   Araport; AT5G10300; -.
DR   TAIR; AT5G10300; MES5.
DR   eggNOG; ENOG502QR2J; Eukaryota.
DR   HOGENOM; CLU_046066_0_1_1; -.
DR   InParanoid; Q9LFT6; -.
DR   OMA; ECTVQDY; -.
DR   OrthoDB; 640126at2759; -.
DR   PhylomeDB; Q9LFT6; -.
DR   BioCyc; ARA:AT5G10300-MONOMER; -.
DR   BRENDA; 4.1.2.10; 399.
DR   SABIO-RK; Q9LFT6; -.
DR   EvolutionaryTrace; Q9LFT6; -.
DR   PRO; PR:Q9LFT6; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9LFT6; baseline and differential.
DR   GO; GO:0046593; F:mandelonitrile lyase activity; IDA:TAIR.
DR   GO; GO:0016139; P:glycoside catabolic process; IDA:TAIR.
DR   GO; GO:0009611; P:response to wounding; IEP:TAIR.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR045889; MES/HNL.
DR   PANTHER; PTHR10992:SF1013; ALPHA-HYDROXYNITRILE LYASE; 1.
DR   PANTHER; PTHR10992; METHYLESTERASE FAMILY MEMBER; 1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   Genevisible; Q9LFT6; AT.
PE   1: Evidence at protein level;
KW   3D-structure; Lyase; Reference proteome.
FT   CHAIN           1..258
FT                   /note="Alpha-hydroxynitrile lyase"
FT                   /id="PRO_0000418174"
FT   ACT_SITE        81
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P52704"
FT   ACT_SITE        236
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P52704"
FT   SITE            208
FT                   /note="Increases basicity of active site His"
FT                   /evidence="ECO:0000250|UniProtKB:P52704"
FT   MUTAGEN         81
FT                   /note="S->A: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:17907254"
FT   MUTAGEN         208
FT                   /note="D->N: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:17907254"
FT   MUTAGEN         236
FT                   /note="H->F: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:17907254"
FT   CONFLICT        70
FT                   /note="P -> Q (in Ref. 3; AAL25532)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        75
FT                   /note="V -> G (in Ref. 3; AAL25532)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        177
FT                   /note="G -> R (in Ref. 3; AAK76689)"
FT                   /evidence="ECO:0000305"
FT   STRAND          6..10
FT                   /evidence="ECO:0007829|PDB:6COF"
FT   HELIX           17..20
FT                   /evidence="ECO:0007829|PDB:6COF"
FT   HELIX           23..29
FT                   /evidence="ECO:0007829|PDB:6COF"
FT   STRAND          33..37
FT                   /evidence="ECO:0007829|PDB:6COF"
FT   HELIX           49..51
FT                   /evidence="ECO:0007829|PDB:6COF"
FT   HELIX           55..67
FT                   /evidence="ECO:0007829|PDB:6COF"
FT   STRAND          75..80
FT                   /evidence="ECO:0007829|PDB:6COF"
FT   HELIX           83..93
FT                   /evidence="ECO:0007829|PDB:6COF"
FT   HELIX           95..97
FT                   /evidence="ECO:0007829|PDB:6COF"
FT   STRAND          98..105
FT                   /evidence="ECO:0007829|PDB:6COF"
FT   STRAND          111..113
FT                   /evidence="ECO:0007829|PDB:6COF"
FT   HELIX           117..125
FT                   /evidence="ECO:0007829|PDB:6COF"
FT   STRAND          133..139
FT                   /evidence="ECO:0007829|PDB:6COF"
FT   STRAND          142..148
FT                   /evidence="ECO:0007829|PDB:6COF"
FT   HELIX           151..157
FT                   /evidence="ECO:0007829|PDB:6COF"
FT   HELIX           164..173
FT                   /evidence="ECO:0007829|PDB:6COF"
FT   HELIX           181..186
FT                   /evidence="ECO:0007829|PDB:6COF"
FT   TURN            192..194
FT                   /evidence="ECO:0007829|PDB:6COF"
FT   HELIX           195..197
FT                   /evidence="ECO:0007829|PDB:6COF"
FT   STRAND          200..205
FT                   /evidence="ECO:0007829|PDB:6COF"
FT   STRAND          209..211
FT                   /evidence="ECO:0007829|PDB:6COF"
FT   HELIX           213..222
FT                   /evidence="ECO:0007829|PDB:6COF"
FT   STRAND          228..231
FT                   /evidence="ECO:0007829|PDB:6COF"
FT   HELIX           238..241
FT                   /evidence="ECO:0007829|PDB:6COF"
FT   HELIX           243..256
FT                   /evidence="ECO:0007829|PDB:6COF"
SQ   SEQUENCE   258 AA;  29217 MW;  0CFA965320F1FD2E CRC64;
     MERKHHFVLV HNAYHGAWIW YKLKPLLESA GHRVTAVELA ASGIDPRPIQ AVETVDEYSK
     PLIETLKSLP ENEEVILVGF SFGGINIALA ADIFPAKIKV LVFLNAFLPD TTHVPSHVLD
     KYMEMPGGLG DCEFSSHETR NGTMSLLKMG PKFMKARLYQ NCPIEDYELA KMLHRQGSFF
     TEDLSKKEKF SEEGYGSVQR VYVMSSEDKA IPCDFIRWMI DNFNVSKVYE IDGGDHMVML
     SKPQKLFDSL SAIATDYM
//