HNL_MANES
ID HNL_MANES Reviewed; 258 AA.
AC P52705;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=(S)-hydroxynitrile lyase;
DE EC=4.1.2.47;
DE AltName: Full=(S)-acetone-cyanohydrin lyase;
DE AltName: Full=Oxynitrilase;
GN Name=HNL;
OS Manihot esculenta (Cassava) (Jatropha manihot).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Manihoteae;
OC Manihot.
OX NCBI_TaxID=3983;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 2-37 AND 169-192.
RC TISSUE=Cotyledon;
RX PubMed=8203915; DOI=10.1006/abbi.1994.1267;
RA Hughes J., Carvalho F.J.P.D.C., Hughes M.A.;
RT "Purification, characterization, and cloning of alpha-hydroxynitrile lyase
RT from cassava (Manihot esculenta Crantz).";
RL Arch. Biochem. Biophys. 311:496-502(1994).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX PubMed=11173464; DOI=10.1107/s0907444900015766;
RA Lauble H., Foerster S., Miehlich B., Wajant H., Effenberger F.;
RT "Structure of hydroxynitrile lyase from Manihot esculenta in complex with
RT substrates acetone and chloroacetone: implications for the mechanism of
RT cyanogenesis.";
RL Acta Crystallogr. D 57:194-200(2001).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), AND MUTAGENESIS OF SER-80.
RX PubMed=11316882; DOI=10.1110/ps.01301;
RA Lauble H., Miehlich B., Foerster S., Wajant H., Effenberger F.;
RT "Mechanistic aspects of cyanogenesis from active-site mutant Ser80Ala of
RT hydroxynitrile lyase from Manihot esculenta in complex with acetone
RT cyanohydrin.";
RL Protein Sci. 10:1015-1022(2001).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX PubMed=11742123; DOI=10.1110/ps.33702;
RA Lauble H., Miehlich B., Foerster S., Kobler C., Wajant H., Effenberger F.;
RT "Structure determinants of substrate specificity of hydroxynitrile lyase
RT from Manihot esculenta.";
RL Protein Sci. 11:65-71(2002).
CC -!- FUNCTION: Involved in cyanogenesis, the release of HCN from injured
CC tissues. Decomposes a varieties of (R) or (S) cyanohydrins into HCN and
CC the corresponding aldehydes and ketones. The natural substrate of this
CC enzyme is (S)-acetone cyanohydrin.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a monosubstituted aliphatic (S)-hydroxynitrile = an aldehyde +
CC hydrogen cyanide; Xref=Rhea:RHEA:56588, ChEBI:CHEBI:17478,
CC ChEBI:CHEBI:18407, ChEBI:CHEBI:140596; EC=4.1.2.47;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a disubstituted aliphatic (S)-hydroxynitrile = a ketone +
CC hydrogen cyanide; Xref=Rhea:RHEA:56592, ChEBI:CHEBI:17087,
CC ChEBI:CHEBI:18407, ChEBI:CHEBI:140597; EC=4.1.2.47;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aromatic (S)-hydroxynitrile = an aromatic aldehyde +
CC hydrogen cyanide; Xref=Rhea:RHEA:54660, ChEBI:CHEBI:18407,
CC ChEBI:CHEBI:33855, ChEBI:CHEBI:138306; EC=4.1.2.47;
CC -!- SUBUNIT: Homotrimer.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Hydroxynitrile
CC lyase family. {ECO:0000305}.
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DR EMBL; Z29091; CAA82334.1; -; mRNA.
DR PDB; 1DWO; X-ray; 2.20 A; A/B=2-258.
DR PDB; 1DWP; X-ray; 2.20 A; A/B=2-258.
DR PDB; 1DWQ; X-ray; 2.20 A; A/B=2-258.
DR PDB; 1E89; X-ray; 2.10 A; A/B=2-258.
DR PDB; 1E8D; X-ray; 2.20 A; A/B=2-258.
DR PDB; 1EB8; X-ray; 2.10 A; A/B=2-258.
DR PDB; 1EB9; X-ray; 2.10 A; A/B=2-258.
DR PDB; 3RKS; X-ray; 2.50 A; A/B/C/D=1-258.
DR PDB; 3X3H; X-ray; 2.88 A; A/B/C/D/E/F/G/H=1-258.
DR PDB; 4YK7; X-ray; 2.60 A; A/B/C/D=1-258.
DR PDBsum; 1DWO; -.
DR PDBsum; 1DWP; -.
DR PDBsum; 1DWQ; -.
DR PDBsum; 1E89; -.
DR PDBsum; 1E8D; -.
DR PDBsum; 1EB8; -.
DR PDBsum; 1EB9; -.
DR PDBsum; 3RKS; -.
DR PDBsum; 3X3H; -.
DR PDBsum; 4YK7; -.
DR AlphaFoldDB; P52705; -.
DR SMR; P52705; -.
DR STRING; 3983.cassava4.1_014330m; -.
DR ESTHER; manes-hnl; Hydroxynitrile_lyase.
DR EnsemblPlants; OAY33393; OAY33393; MANES_13G092100.
DR Gramene; OAY33393; OAY33393; MANES_13G092100.
DR KEGG; ag:CAA82334; -.
DR OrthoDB; 923240at2759; -.
DR BioCyc; MetaCyc:MON-6902; -.
DR BRENDA; 4.1.2.47; 3175.
DR SABIO-RK; P52705; -.
DR EvolutionaryTrace; P52705; -.
DR GO; GO:0052891; F:aliphatic (S)-hydroxynitrile lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0052892; F:aromatic (S)-hydroxynitrile lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0047606; F:hydroxynitrilase activity; IEA:UniProtKB-EC.
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; PF00561; Abhydrolase_1; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Lyase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8203915"
FT CHAIN 2..258
FT /note="(S)-hydroxynitrile lyase"
FT /id="PRO_0000084018"
FT DOMAIN 5..242
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 80
FT /evidence="ECO:0000250"
FT ACT_SITE 208
FT /evidence="ECO:0000250"
FT ACT_SITE 236
FT /evidence="ECO:0000250"
FT MUTAGEN 80
FT /note="S->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11316882"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:1E89"
FT HELIX 16..19
FT /evidence="ECO:0007829|PDB:1E89"
FT HELIX 22..28
FT /evidence="ECO:0007829|PDB:1E89"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:1E89"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:1E89"
FT HELIX 54..57
FT /evidence="ECO:0007829|PDB:1E89"
FT HELIX 59..67
FT /evidence="ECO:0007829|PDB:1E89"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:1E89"
FT HELIX 83..93
FT /evidence="ECO:0007829|PDB:1E89"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:1E89"
FT STRAND 97..105
FT /evidence="ECO:0007829|PDB:1E89"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:1E89"
FT HELIX 116..124
FT /evidence="ECO:0007829|PDB:1E89"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:1E89"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:1E89"
FT HELIX 151..157
FT /evidence="ECO:0007829|PDB:1E89"
FT HELIX 164..173
FT /evidence="ECO:0007829|PDB:1E89"
FT HELIX 181..185
FT /evidence="ECO:0007829|PDB:1E89"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:1E89"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:1E89"
FT STRAND 200..204
FT /evidence="ECO:0007829|PDB:1E89"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:1E89"
FT HELIX 213..222
FT /evidence="ECO:0007829|PDB:1E89"
FT STRAND 226..230
FT /evidence="ECO:0007829|PDB:1E89"
FT HELIX 238..241
FT /evidence="ECO:0007829|PDB:1E89"
FT HELIX 243..257
FT /evidence="ECO:0007829|PDB:1E89"
SQ SEQUENCE 258 AA; 29372 MW; 98ABA050AC8AF1C5 CRC64;
MVTAHFVLIH TICHGAWIWH KLKPALERAG HKVTALDMAA SGIDPRQIEQ INSFDEYSEP
LLTFLEKLPQ GEKVIIVGES CAGLNIAIAA DRYVDKIAAG VFHNSLLPDT VHSPSYTVEK
LLESFPDWRD TEYFTFTNIT GETITTMKLG FVLLRENLFT KCTDGEYELA KMVMRKGSLF
QNVLAQRPKF TEKGYGSIKK VYIWTDQDKI FLPDFQRWQI ANYKPDKVYQ VQGGDHKLQL
TKTEEVAHIL QEVADAYA
