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P52708

- HNLS_SORBI

UniProt

P52708 - HNLS_SORBI

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Protein

P-(S)-hydroxymandelonitrile lyase

Gene
N/A
Organism
Sorghum bicolor (Sorghum) (Sorghum vulgare)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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 – 3434 Reviewed predictionAdd
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...) Reviewed prediction

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.

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.

Miscellaneous databases

EvolutionaryTraceiP52708.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S10 family.

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

Sequence conflict

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

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: June 11, 2014
This is version 84 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

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