HNL_ARATH
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 03-AUG-2022, entry version 129.
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.AT5G10300.1; -.
DR ESTHER; arath-HNL; Hydroxynitrile_lyase.
DR PaxDb; Q9LFT6; -.
DR PRIDE; Q9LFT6; -.
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; locus:2145412; AT5G10300.
DR eggNOG; ENOG502QR2J; Eukaryota.
DR HOGENOM; CLU_046066_0_1_1; -.
DR InParanoid; Q9LFT6; -.
DR OMA; FSSHETK; -.
DR OrthoDB; 923240at2759; -.
DR PhylomeDB; Q9LFT6; -.
DR BioCyc; ARA:AT5G10300-MON; -.
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 Genevisible; Q9LFT6; AT.
DR GO; GO:0046593; F:mandelonitrile lyase activity; IDA:TAIR.
DR GO; GO:0080030; F:methyl indole-3-acetate esterase activity; IBA:GO_Central.
DR GO; GO:0080032; F:methyl jasmonate esterase activity; IBA:GO_Central.
DR GO; GO:0080031; F:methyl salicylate esterase activity; IBA:GO_Central.
DR GO; GO:0016139; P:glycoside catabolic process; IDA:TAIR.
DR GO; GO:0009694; P:jasmonic acid metabolic process; IBA:GO_Central.
DR GO; GO:0009611; P:response to wounding; IEP:TAIR.
DR GO; GO:0009696; P:salicylic acid metabolic process; IBA:GO_Central.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR045889; MES/HNL.
DR PANTHER; PTHR10992; PTHR10992; 1.
DR Pfam; PF12697; Abhydrolase_6; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
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 /evidence="ECO:0000250|UniProtKB:Q6RYA0"
FT ACT_SITE 208
FT /evidence="ECO:0000250|UniProtKB:Q6RYA0"
FT ACT_SITE 236
FT /evidence="ECO:0000250|UniProtKB:Q6RYA0"
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
