HNL_HEVBR
ID HNL_HEVBR Reviewed; 257 AA.
AC P52704;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 98.
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 Hevea brasiliensis (Para rubber tree) (Siphonia brasiliensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Micrandreae;
OC Hevea.
OX NCBI_TaxID=3981;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 121-126; 176-181; 200-204
RP AND 244-253, AND MUTAGENESIS OF CYS-81.
RC TISSUE=Leaf;
RX PubMed=8621461; DOI=10.1074/jbc.271.10.5884;
RA Hasslacher M., Schall M., Hayn M., Griengl H., Kohlwein S.D., Schwab H.;
RT "Molecular cloning of the full-length cDNA of (S)-hydroxynitrile lyase from
RT Hevea brasiliensis. Functional expression in Escherichia coli and
RT Saccharomyces cerevisiae and identification of an active site residue.";
RL J. Biol. Chem. 271:5884-5891(1996).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), AND MUTAGENESIS OF SER-80 AND
RP HIS-235.
RX PubMed=8805565; DOI=10.1016/s0969-2126(96)00088-3;
RA Wagner U.G., Hasslacher M., Griengl H., Schwab H., Kratky C.;
RT "Mechanism of cyanogenesis: the crystal structure of hydroxynitrile lyase
RT from Hevea brasiliensis.";
RL Structure 4:811-822(1996).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS).
RX PubMed=10494852; DOI=10.1515/bc.1999.123;
RA Gruber K., Gugganig M., Wagner U.G., Kratky C.;
RT "Atomic resolution crystal structure of hydroxynitrile lyase from Hevea
RT brasiliensis.";
RL Biol. Chem. 380:993-1000(1999).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS).
RX PubMed=10548044; DOI=10.1110/ps.8.10.1990;
RA Zuegg J., Gruber K., Gugganig M., Wagner U.G., Kratky C.;
RT "Three-dimensional structures of enzyme-substrate complexes of the
RT hydroxynitrile lyase from Hevea brasiliensis.";
RL Protein Sci. 8:1990-2000(1999).
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: Homodimer.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Hydroxynitrile
CC lyase family. {ECO:0000305}.
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DR EMBL; U40402; AAC49184.1; -; mRNA.
DR PIR; T10758; T10758.
DR PDB; 1QJ4; X-ray; 1.10 A; A=1-257.
DR PDB; 1SC9; X-ray; 1.80 A; A=1-257.
DR PDB; 1SCI; X-ray; 2.18 A; A=1-257.
DR PDB; 1SCK; X-ray; 1.70 A; A=1-257.
DR PDB; 1SCQ; X-ray; 2.90 A; A=1-257.
DR PDB; 1YAS; X-ray; 1.90 A; A=1-257.
DR PDB; 1YB6; X-ray; 1.54 A; A=2-257.
DR PDB; 1YB7; X-ray; 1.76 A; A=2-257.
DR PDB; 2G4L; X-ray; 1.84 A; A=1-257.
DR PDB; 2YAS; X-ray; 1.72 A; A=1-257.
DR PDB; 3C6X; X-ray; 1.05 A; A=1-257.
DR PDB; 3C6Y; X-ray; 1.25 A; A=1-257.
DR PDB; 3C6Z; X-ray; 1.05 A; A=1-257.
DR PDB; 3C70; X-ray; 1.05 A; A=1-257.
DR PDB; 3YAS; X-ray; 1.85 A; A=1-257.
DR PDB; 4YAS; X-ray; 2.00 A; A=1-257.
DR PDB; 5YAS; X-ray; 2.20 A; A=1-257.
DR PDB; 6YAS; X-ray; 2.20 A; A=1-257.
DR PDB; 7YAS; X-ray; 1.75 A; A=1-257.
DR PDBsum; 1QJ4; -.
DR PDBsum; 1SC9; -.
DR PDBsum; 1SCI; -.
DR PDBsum; 1SCK; -.
DR PDBsum; 1SCQ; -.
DR PDBsum; 1YAS; -.
DR PDBsum; 1YB6; -.
DR PDBsum; 1YB7; -.
DR PDBsum; 2G4L; -.
DR PDBsum; 2YAS; -.
DR PDBsum; 3C6X; -.
DR PDBsum; 3C6Y; -.
DR PDBsum; 3C6Z; -.
DR PDBsum; 3C70; -.
DR PDBsum; 3YAS; -.
DR PDBsum; 4YAS; -.
DR PDBsum; 5YAS; -.
DR PDBsum; 6YAS; -.
DR PDBsum; 7YAS; -.
DR AlphaFoldDB; P52704; -.
DR SMR; P52704; -.
DR ESTHER; hevbr-hnl; Hydroxynitrile_lyase.
DR KEGG; ag:AAC49184; -.
DR OrthoDB; 923240at2759; -.
DR BRENDA; 4.1.2.47; 2665.
DR SABIO-RK; P52704; -.
DR EvolutionaryTrace; P52704; -.
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 CHAIN 1..257
FT /note="(S)-hydroxynitrile lyase"
FT /id="PRO_0000084017"
FT DOMAIN 5..241
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 80
FT ACT_SITE 207
FT ACT_SITE 235
FT MUTAGEN 80
FT /note="S->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:8805565"
FT MUTAGEN 81
FT /note="C->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:8621461"
FT MUTAGEN 235
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:8805565"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:3C6X"
FT HELIX 16..19
FT /evidence="ECO:0007829|PDB:3C6X"
FT HELIX 22..28
FT /evidence="ECO:0007829|PDB:3C6X"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:3C6X"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:3C6X"
FT HELIX 54..57
FT /evidence="ECO:0007829|PDB:3C6X"
FT HELIX 59..66
FT /evidence="ECO:0007829|PDB:3C6X"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:3C6X"
FT HELIX 82..93
FT /evidence="ECO:0007829|PDB:3C6X"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:3C6X"
FT STRAND 97..105
FT /evidence="ECO:0007829|PDB:3C6X"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:3C6X"
FT HELIX 116..124
FT /evidence="ECO:0007829|PDB:3C6X"
FT STRAND 132..138
FT /evidence="ECO:0007829|PDB:3C6X"
FT STRAND 141..147
FT /evidence="ECO:0007829|PDB:3C6X"
FT HELIX 150..156
FT /evidence="ECO:0007829|PDB:3C6X"
FT HELIX 163..172
FT /evidence="ECO:0007829|PDB:3C6X"
FT HELIX 180..185
FT /evidence="ECO:0007829|PDB:3C6X"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:3C6X"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:3C6X"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:3C6X"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:3C6X"
FT HELIX 212..221
FT /evidence="ECO:0007829|PDB:3C6X"
FT STRAND 225..229
FT /evidence="ECO:0007829|PDB:3C6X"
FT HELIX 237..240
FT /evidence="ECO:0007829|PDB:3C6X"
FT HELIX 242..255
FT /evidence="ECO:0007829|PDB:3C6X"
SQ SEQUENCE 257 AA; 29228 MW; EF4AE88717279CEB CRC64;
MAFAHFVLIH TICHGAWIWH KLKPLLEALG HKVTALDLAA SGVDPRQIEE IGSFDEYSEP
LLTFLEALPP GEKVILVGES CGGLNIAIAA DKYCEKIAAA VFHNSVLPDT EHCPSYVVDK
LMEVFPDWKD TTYFTYTKDG KEITGLKLGF TLLRENLYTL CGPEEYELAK MLTRKGSLFQ
NILAKRPFFT KEGYGSIKKI YVWTDQDEIF LPEFQLWQIE NYKPDKVYKV EGGDHKLQLT
KTKEIAEILQ EVADTYN
