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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: 4 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 – 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 – 634Combined sources
Beta strandi79 – 879Combined sources
Turni88 – 914Combined sources
Beta strandi92 – 998Combined sources
Helixi106 – 1083Combined sources
Beta strandi111 – 1166Combined sources
Turni118 – 1203Combined sources
Helixi124 – 1329Combined sources
Beta strandi133 – 1375Combined sources
Beta strandi144 – 1463Combined sources
Helixi151 – 1533Combined sources
Beta strandi155 – 1606Combined sources
Beta strandi170 – 1734Combined sources
Helixi174 – 1774Combined sources
Helixi181 – 19818Combined sources
Helixi200 – 2023Combined sources
Beta strandi205 – 2128Combined sources
Helixi216 – 22611Combined sources
Turni227 – 2304Combined sources
Beta strandi235 – 2439Combined sources
Helixi248 – 26114Combined sources
Helixi267 – 27610Combined sources
Beta strandi282 – 2843Combined sources
Helixi287 – 29913Combined sources
Turni300 – 3023Combined sources
Turni343 – 3453Combined sources
Helixi346 – 3538Combined sources
Helixi356 – 3627Combined sources
Helixi366 – 3683Combined sources
Helixi379 – 3835Combined sources
Helixi393 – 4019Combined sources
Beta strandi405 – 4117Combined sources
Beta strandi415 – 4173Combined sources
Helixi419 – 4279Combined sources
Beta strandi433 – 44311Combined sources
Beta strandi448 – 4569Combined sources
Beta strandi459 – 4646Combined sources
Helixi471 – 4744Combined sources
Helixi476 – 48813Combined sources

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

        10         20         30         40         50
MAVFISSSGS PGRATATTTT TTTLLLAVLA AAAAAGLLLA PVAARGSPPE
60 70 80 90 100
HDKQLQLQQQ EDDRIPGLPG QPNGVAFGMY GGYVTIDDNN GRALYYWFQE
110 120 130 140 150
ADTADPAAAP LVLWLNGGPG CSSIGLGAMQ ELGPFRVHTN GESLLLNEYA
160 170 180 190 200
WNKAANILFA ESPAGVVFSY SNTSSDLSMG DDKMAQDTYT FLVKWFERFP
210 220 230 240 250
HYNYREFYIA GESGHFIPQL SQVVYRNRNN SPFINFQGLL VSSGLTNDHE
260 270 280 290 300
DMIGMFELWW HHGLISDETR DSGLKVCPGT SFMHPTPECT EVWNKALAEQ
310 320 330 340 350
GNINPYTIYT PTCDREPSPY QRRFWAPHGR AAPPPLMLPP YDPCAVFNSI
360 370 380 390 400
NYLNLPEVQT ALHANVSGIV EYPWTVCSNT IFDQWGQAAD DLLPVYRELI
410 420 430 440 450
QAGLRVWVYS GDTDSVVPVS STRRSLAALE LPVKTSWYPW YMAPTEREVG
460 470 480 490 500
GWSVQYEGLT YVSPSGAGHL VPVHRPAQAF LLFKQFLKGE PMPAEEKNDI
510
LLPSEKAPFY
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 29, 2014
This is version 86 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