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P52708

- HNLS_SORBI

UniProt

P52708 - HNLS_SORBI

Protein

P-(S)-hydroxymandelonitrile lyase

Gene
N/A
Organism
Sorghum bicolor (Sorghum) (Sorghum vulgare)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 85 (01 Oct 2014)
      Sequence version 2 (28 Jul 2009)
      Previous versions | rss
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    Functioni

    Involved in cyanogenesis, the release of HCN from injured tissues. Is involved in the catabolism of the cyanogenic glycoside dhurrin.1 Publication

    Catalytic activityi

    (S)-4-hydroxymandelonitrile = cyanide + 4-hydroxybenzaldehyde.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei213 – 2131
    Active sitei414 – 4141
    Active sitei469 – 4691

    GO - Molecular functioni

    1. hydroxymandelonitrile lyase activity Source: UniProtKB-EC
    2. serine-type carboxypeptidase activity Source: InterPro

    Keywords - Molecular functioni

    Lyase

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-14084.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    P-(S)-hydroxymandelonitrile lyase (EC:4.1.2.11)
    Short name:
    HNL
    Short name:
    Hydroxynitrile lyase
    Cleaved into the following 2 chains:
    OrganismiSorghum bicolor (Sorghum) (Sorghum vulgare)
    Taxonomic identifieri4558 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogoneaeSorghum

    Organism-specific databases

    GrameneiP52708.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3434Sequence AnalysisAdd
    BLAST
    Chaini35 – 338304P-(S)-hydroxymandelonitrile lyase chain APRO_0000004341Add
    BLAST
    Chaini339 – 510172P-(S)-hydroxymandelonitrile lyase chain BPRO_0000004342Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi121 ↔ 377Interchain (between A and B chains)
    Glycosylationi172 – 1721N-linked (GlcNAc...)1 Publication
    Disulfide bondi277 ↔ 289
    Disulfide bondi313 ↔ 344Interchain (between A and B chains)
    Glycosylationi365 – 3651N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    The N-terminus of chain A is blocked.

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Expressioni

    Tissue specificityi

    Primary leaves of seedlings.

    Interactioni

    Subunit structurei

    Heterotetramer of two A and two B chains. The A and B chains are linked by a disulfide bond.1 Publication

    Protein-protein interaction databases

    STRINGi4558.Sb04g036350.1.

    Structurei

    Secondary structure

    1
    510
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi60 – 634
    Beta strandi79 – 879
    Turni88 – 914
    Beta strandi92 – 998
    Helixi106 – 1083
    Beta strandi111 – 1166
    Turni118 – 1203
    Helixi124 – 1329
    Beta strandi133 – 1375
    Beta strandi144 – 1463
    Helixi151 – 1533
    Beta strandi155 – 1606
    Beta strandi170 – 1734
    Helixi174 – 1774
    Helixi181 – 19818
    Helixi200 – 2023
    Beta strandi205 – 2128
    Helixi216 – 22611
    Turni227 – 2304
    Beta strandi235 – 2439
    Helixi248 – 26114
    Helixi267 – 27610
    Beta strandi282 – 2843
    Helixi287 – 29913
    Turni300 – 3023
    Turni343 – 3453
    Helixi346 – 3538
    Helixi356 – 3627
    Helixi366 – 3683
    Helixi379 – 3835
    Helixi393 – 4019
    Beta strandi405 – 4117
    Beta strandi415 – 4173
    Helixi419 – 4279
    Beta strandi433 – 44311
    Beta strandi448 – 4569
    Beta strandi459 – 4646
    Helixi471 – 4744
    Helixi476 – 48813

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GXSX-ray2.30A/C56-325[»]
    B/D338-495[»]
    ProteinModelPortaliP52708.
    SMRiP52708. Positions 59-325, 338-495.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP52708.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase S10 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG2939.
    HOGENOMiHOG000198295.

    Family and domain databases

    Gene3Di3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR001563. Peptidase_S10.
    IPR018202. Peptidase_S10_AS.
    [Graphical view]
    PANTHERiPTHR11802. PTHR11802. 1 hit.
    PfamiPF00450. Peptidase_S10. 1 hit.
    [Graphical view]
    PRINTSiPR00724. CRBOXYPTASEC.
    SUPFAMiSSF53474. SSF53474. 1 hit.
    PROSITEiPS00560. CARBOXYPEPT_SER_HIS. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P52708-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAVFISSSGS PGRATATTTT TTTLLLAVLA AAAAAGLLLA PVAARGSPPE    50
    HDKQLQLQQQ EDDRIPGLPG QPNGVAFGMY GGYVTIDDNN GRALYYWFQE 100
    ADTADPAAAP LVLWLNGGPG CSSIGLGAMQ ELGPFRVHTN GESLLLNEYA 150
    WNKAANILFA ESPAGVVFSY SNTSSDLSMG DDKMAQDTYT FLVKWFERFP 200
    HYNYREFYIA GESGHFIPQL SQVVYRNRNN SPFINFQGLL VSSGLTNDHE 250
    DMIGMFELWW HHGLISDETR DSGLKVCPGT SFMHPTPECT EVWNKALAEQ 300
    GNINPYTIYT PTCDREPSPY QRRFWAPHGR AAPPPLMLPP YDPCAVFNSI 350
    NYLNLPEVQT ALHANVSGIV EYPWTVCSNT IFDQWGQAAD DLLPVYRELI 400
    QAGLRVWVYS GDTDSVVPVS STRRSLAALE LPVKTSWYPW YMAPTEREVG 450
    GWSVQYEGLT YVSPSGAGHL VPVHRPAQAF LLFKQFLKGE PMPAEEKNDI 500
    LLPSEKAPFY 510
    Length:510
    Mass (Da):56,319
    Last modified:July 28, 2009 - v2
    Checksum:i5BAD268ADFA42A8C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti289 – 2891C → E AA sequence 1 PublicationCurated
    Sequence conflicti300 – 3001Q → E AA sequence 1 PublicationCurated
    Sequence conflicti339 – 3391P → S AA sequence 1 PublicationCurated
    Sequence conflicti342 – 3421D → E AA sequence 1 PublicationCurated
    Sequence conflicti344 – 3441C → V AA sequence 1 PublicationCurated
    Sequence conflicti357 – 3582EV → PL AA sequence 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ421152 mRNA. Translation: CAD12888.1.
    X84057 mRNA. Translation: CAA58876.1.
    PIRiS53311.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ421152 mRNA. Translation: CAD12888.1 .
    X84057 mRNA. Translation: CAA58876.1 .
    PIRi S53311.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GXS X-ray 2.30 A/C 56-325 [» ]
    B/D 338-495 [» ]
    ProteinModelPortali P52708.
    SMRi P52708. Positions 59-325, 338-495.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 4558.Sb04g036350.1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    Gramenei P52708.

    Phylogenomic databases

    eggNOGi COG2939.
    HOGENOMi HOG000198295.

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-14084.

    Miscellaneous databases

    EvolutionaryTracei P52708.

    Family and domain databases

    Gene3Di 3.40.50.1820. 1 hit.
    InterProi IPR029058. AB_hydrolase.
    IPR001563. Peptidase_S10.
    IPR018202. Peptidase_S10_AS.
    [Graphical view ]
    PANTHERi PTHR11802. PTHR11802. 1 hit.
    Pfami PF00450. Peptidase_S10. 1 hit.
    [Graphical view ]
    PRINTSi PR00724. CRBOXYPTASEC.
    SUPFAMi SSF53474. SSF53474. 1 hit.
    PROSITEi PS00560. CARBOXYPEPT_SER_HIS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Crystal structure of hydroxynitrile lyase from Sorghum bicolor in complex with the inhibitor benzoic acid: a novel cyanogenic enzyme."
      Lauble H., Miehlich B., Forster S., Wajant H., Effenberger F.
      Biochemistry 41:12043-12050(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 56-325 IN COMPLEX WITH INHIBITOR, GLYCOSYLATION AT ASN-172.
    2. "Molecular cloning of hydroxynitrile lyase from Sorghum bicolor (L.). Homologies to serine carboxypeptidases."
      Wajant H., Mundry K.-W., Pfizenmaier K.
      Plant Mol. Biol. 26:735-746(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 145-510, PARTIAL PROTEIN SEQUENCE.
      Strain: cv. Sordan 79.
      Tissue: Seedling.
    3. "Purification and protein characterisation of hydroxynitrile lyases from sorghum and almond."
      Jansen J., Woker J., Kula M.-R.
      Biotechnol. Appl. Biochem. 15:90-99(1992)
      Cited for: PROTEIN SEQUENCE OF 185-220; 285-311 AND 339-358.

    Entry informationi

    Entry nameiHNLS_SORBI
    AccessioniPrimary (citable) accession number: P52708
    Secondary accession number(s): Q8W4X3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: July 28, 2009
    Last modified: October 1, 2014
    This is version 85 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3