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 24-JAN-2024, entry version 124. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 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:MONOMER-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; 3.40.50.11320; -; 1. DR Gene3D; 6.10.250.940; -; 1. DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR001563; Peptidase_S10. DR InterPro; IPR033124; Ser_caboxypep_his_AS. DR PANTHER; PTHR11802:SF219; CARBOXYPEPTIDASE; 1. DR PANTHER; PTHR11802; SERINE PROTEASE FAMILY S10 SERINE CARBOXYPEPTIDASE; 1. DR Pfam; PF00450; Peptidase_S10; 1. DR PRINTS; PR00724; CRBOXYPTASEC. DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 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 //