HNLS_SORBI
ID HNLS_SORBI Reviewed; 510 AA.
AC P52708; Q8W4X3;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=P-(S)-hydroxymandelonitrile lyase;
DE Short=HNL;
DE Short=Hydroxynitrile lyase;
DE EC=4.1.2.11;
DE Contains:
DE RecName: Full=P-(S)-hydroxymandelonitrile lyase chain A;
DE Contains:
DE RecName: Full=P-(S)-hydroxymandelonitrile lyase chain B;
DE Flags: Precursor;
OS Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX NCBI_TaxID=4558;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS)
RP OF 56-325 AND 338-495 IN COMPLEX WITH INHIBITOR, GLYCOSYLATION AT ASN-172
RP AND ASN-365, AND DISULFIDE BONDS.
RX PubMed=12356304; DOI=10.1021/bi020300o;
RA Lauble H., Miehlich B., Forster S., Wajant H., Effenberger F.;
RT "Crystal structure of hydroxynitrile lyase from Sorghum bicolor in complex
RT with the inhibitor benzoic acid: a novel cyanogenic enzyme.";
RL Biochemistry 41:12043-12050(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 145-510, AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=cv. Sordan 79; TISSUE=Seedling;
RX PubMed=7948927; DOI=10.1007/bf00013758;
RA Wajant H., Mundry K.-W., Pfizenmaier K.;
RT "Molecular cloning of hydroxynitrile lyase from Sorghum bicolor (L.).
RT Homologies to serine carboxypeptidases.";
RL Plant Mol. Biol. 26:735-746(1994).
RN [3]
RP PROTEIN SEQUENCE OF 185-220; 285-311 AND 339-358.
RA Jansen J., Woker J., Kula M.-R.;
RT "Purification and protein characterisation of hydroxynitrile lyases from
RT sorghum and almond.";
RL Biotechnol. Appl. Biochem. 15:90-99(1992).
CC -!- FUNCTION: Involved in cyanogenesis, the release of HCN from injured
CC tissues. Is involved in the catabolism of the cyanogenic glycoside
CC dhurrin. {ECO:0000269|PubMed:12356304}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-4-hydroxymandelonitrile = 4-hydroxybenzaldehyde + hydrogen
CC cyanide; Xref=Rhea:RHEA:15977, ChEBI:CHEBI:16660, ChEBI:CHEBI:17597,
CC ChEBI:CHEBI:18407; EC=4.1.2.11;
CC -!- SUBUNIT: Heterotetramer of two A and two B chains. The A and B chains
CC are linked by a disulfide bond. {ECO:0000269|PubMed:12356304}.
CC -!- TISSUE SPECIFICITY: Primary leaves of seedlings.
CC -!- PTM: The N-terminus of chain A is blocked.
CC -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR EMBL; AJ421152; CAD12888.1; -; mRNA.
DR EMBL; X84057; CAA58876.1; -; mRNA.
DR PIR; S53311; S53311.
DR PDB; 1GXS; X-ray; 2.30 A; A/C=56-325, B/D=338-495.
DR PDBsum; 1GXS; -.
DR AlphaFoldDB; P52708; -.
DR SMR; P52708; -.
DR STRING; 4558.Sb04g036350.1; -.
DR ESTHER; sorbi-hnl; Carboxypeptidase_S10.
DR MEROPS; S10.005; -.
DR iPTMnet; P52708; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_13_0_1; -.
DR BioCyc; MetaCyc:MON-14084; -.
DR BRENDA; 4.1.2.11; 5768.
DR EvolutionaryTrace; P52708; -.
DR ExpressionAtlas; P52708; baseline and differential.
DR GO; GO:0050419; F:hydroxymandelonitrile lyase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001563; Peptidase_S10.
DR InterPro; IPR033124; Ser_caboxypep_his_AS.
DR PANTHER; PTHR11802; PTHR11802; 1.
DR Pfam; PF00450; Peptidase_S10; 1.
DR PRINTS; PR00724; CRBOXYPTASEC.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00560; CARBOXYPEPT_SER_HIS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Lyase; Signal.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT CHAIN 35..338
FT /note="P-(S)-hydroxymandelonitrile lyase chain A"
FT /id="PRO_0000004341"
FT CHAIN 339..510
FT /note="P-(S)-hydroxymandelonitrile lyase chain B"
FT /id="PRO_0000004342"
FT ACT_SITE 213
FT /evidence="ECO:0000269|PubMed:12356304,
FT ECO:0007744|PDB:1GXS"
FT ACT_SITE 414
FT /evidence="ECO:0000250|UniProtKB:P08819"
FT ACT_SITE 469
FT /evidence="ECO:0000250|UniProtKB:P08819"
FT BINDING 116..118
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P08819"
FT BINDING 212..213
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P08819"
FT BINDING 465..469
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P08819"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:12356304, ECO:0007744|PDB:1GXS"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:12356304, ECO:0007744|PDB:1GXS"
FT DISULFID 121..377
FT /note="Interchain (between A and B chains)"
FT /evidence="ECO:0000269|PubMed:12356304,
FT ECO:0007744|PDB:1GXS"
FT DISULFID 277..289
FT /evidence="ECO:0000269|PubMed:12356304,
FT ECO:0007744|PDB:1GXS"
FT DISULFID 313..344
FT /note="Interchain (between A and B chains)"
FT /evidence="ECO:0000269|PubMed:12356304,
FT ECO:0007744|PDB:1GXS"
FT CONFLICT 289
FT /note="C -> E (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="Q -> E (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="P -> S (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 342
FT /note="D -> E (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 344
FT /note="C -> V (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 357..358
FT /note="EV -> PL (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 60..63
FT /evidence="ECO:0007829|PDB:1GXS"
FT STRAND 79..87
FT /evidence="ECO:0007829|PDB:1GXS"
FT TURN 88..91
FT /evidence="ECO:0007829|PDB:1GXS"
FT STRAND 92..99
FT /evidence="ECO:0007829|PDB:1GXS"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:1GXS"
FT STRAND 111..116
FT /evidence="ECO:0007829|PDB:1GXS"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:1GXS"
FT HELIX 124..132
FT /evidence="ECO:0007829|PDB:1GXS"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:1GXS"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:1GXS"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:1GXS"
FT STRAND 155..160
FT /evidence="ECO:0007829|PDB:1GXS"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:1GXS"
FT HELIX 174..177
FT /evidence="ECO:0007829|PDB:1GXS"
FT HELIX 181..198
FT /evidence="ECO:0007829|PDB:1GXS"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:1GXS"
FT STRAND 205..212
FT /evidence="ECO:0007829|PDB:1GXS"
FT HELIX 216..226
FT /evidence="ECO:0007829|PDB:1GXS"
FT TURN 227..230
FT /evidence="ECO:0007829|PDB:1GXS"
FT STRAND 235..243
FT /evidence="ECO:0007829|PDB:1GXS"
FT HELIX 248..261
FT /evidence="ECO:0007829|PDB:1GXS"
FT HELIX 267..276
FT /evidence="ECO:0007829|PDB:1GXS"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:1GXS"
FT HELIX 287..299
FT /evidence="ECO:0007829|PDB:1GXS"
FT TURN 300..302
FT /evidence="ECO:0007829|PDB:1GXS"
FT TURN 343..345
FT /evidence="ECO:0007829|PDB:1GXS"
FT HELIX 346..353
FT /evidence="ECO:0007829|PDB:1GXS"
FT HELIX 356..362
FT /evidence="ECO:0007829|PDB:1GXS"
FT HELIX 366..368
FT /evidence="ECO:0007829|PDB:1GXS"
FT HELIX 379..383
FT /evidence="ECO:0007829|PDB:1GXS"
FT HELIX 393..401
FT /evidence="ECO:0007829|PDB:1GXS"
FT STRAND 405..411
FT /evidence="ECO:0007829|PDB:1GXS"
FT STRAND 415..417
FT /evidence="ECO:0007829|PDB:1GXS"
FT HELIX 419..427
FT /evidence="ECO:0007829|PDB:1GXS"
FT STRAND 433..443
FT /evidence="ECO:0007829|PDB:1GXS"
FT STRAND 448..456
FT /evidence="ECO:0007829|PDB:1GXS"
FT STRAND 459..464
FT /evidence="ECO:0007829|PDB:1GXS"
FT HELIX 471..474
FT /evidence="ECO:0007829|PDB:1GXS"
FT HELIX 476..488
FT /evidence="ECO:0007829|PDB:1GXS"
SQ SEQUENCE 510 AA; 56319 MW; 5BAD268ADFA42A8C CRC64;
MAVFISSSGS PGRATATTTT TTTLLLAVLA AAAAAGLLLA PVAARGSPPE HDKQLQLQQQ
EDDRIPGLPG QPNGVAFGMY GGYVTIDDNN GRALYYWFQE ADTADPAAAP LVLWLNGGPG
CSSIGLGAMQ ELGPFRVHTN GESLLLNEYA WNKAANILFA ESPAGVVFSY SNTSSDLSMG
DDKMAQDTYT FLVKWFERFP HYNYREFYIA GESGHFIPQL SQVVYRNRNN SPFINFQGLL
VSSGLTNDHE DMIGMFELWW HHGLISDETR DSGLKVCPGT SFMHPTPECT EVWNKALAEQ
GNINPYTIYT PTCDREPSPY QRRFWAPHGR AAPPPLMLPP YDPCAVFNSI NYLNLPEVQT
ALHANVSGIV EYPWTVCSNT IFDQWGQAAD DLLPVYRELI QAGLRVWVYS GDTDSVVPVS
STRRSLAALE LPVKTSWYPW YMAPTEREVG GWSVQYEGLT YVSPSGAGHL VPVHRPAQAF
LLFKQFLKGE PMPAEEKNDI LLPSEKAPFY
