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Protein

P-(S)-hydroxymandelonitrile lyase

Gene
N/A
Organism
Sorghum bicolor (Sorghum) (Sorghum vulgare)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Active sitei2131
Active sitei4141
Active sitei4691

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14084.
BRENDAi4.1.2.11. 5768.

Protein family/group databases

ESTHERisorbi-hnl. Carboxypeptidase_S10.
MEROPSiS10.005.

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 cladePanicoideaeAndropogonodaeAndropogoneaeSorghinaeSorghum

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 34Sequence analysisAdd BLAST34
ChainiPRO_000000434135 – 338P-(S)-hydroxymandelonitrile lyase chain AAdd BLAST304
ChainiPRO_0000004342339 – 510P-(S)-hydroxymandelonitrile lyase chain BAdd BLAST172

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi121 ↔ 377Interchain (between A and B chains)
Glycosylationi172N-linked (GlcNAc...)1 Publication1
Disulfide bondi277 ↔ 289
Disulfide bondi313 ↔ 344Interchain (between A and B chains)
Glycosylationi365N-linked (GlcNAc...)Sequence analysis1

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

1510
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi60 – 63Combined sources4
Beta strandi79 – 87Combined sources9
Turni88 – 91Combined sources4
Beta strandi92 – 99Combined sources8
Helixi106 – 108Combined sources3
Beta strandi111 – 116Combined sources6
Turni118 – 120Combined sources3
Helixi124 – 132Combined sources9
Beta strandi133 – 137Combined sources5
Beta strandi144 – 146Combined sources3
Helixi151 – 153Combined sources3
Beta strandi155 – 160Combined sources6
Beta strandi170 – 173Combined sources4
Helixi174 – 177Combined sources4
Helixi181 – 198Combined sources18
Helixi200 – 202Combined sources3
Beta strandi205 – 212Combined sources8
Helixi216 – 226Combined sources11
Turni227 – 230Combined sources4
Beta strandi235 – 243Combined sources9
Helixi248 – 261Combined sources14
Helixi267 – 276Combined sources10
Beta strandi282 – 284Combined sources3
Helixi287 – 299Combined sources13
Turni300 – 302Combined sources3
Turni343 – 345Combined sources3
Helixi346 – 353Combined sources8
Helixi356 – 362Combined sources7
Helixi366 – 368Combined sources3
Helixi379 – 383Combined sources5
Helixi393 – 401Combined sources9
Beta strandi405 – 411Combined sources7
Beta strandi415 – 417Combined sources3
Helixi419 – 427Combined sources9
Beta strandi433 – 443Combined sources11
Beta strandi448 – 456Combined sources9
Beta strandi459 – 464Combined sources6
Helixi471 – 474Combined sources4
Helixi476 – 488Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GXSX-ray2.30A/C56-325[»]
B/D338-495[»]
ProteinModelPortaliP52708.
SMRiP52708.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP52708.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S10 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1282. Eukaryota.
COG2939. LUCA.
HOGENOMiHOG000198295.
OrthoDBiEOG09360880.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR001563. Peptidase_S10.
IPR033124. Ser_caboxypep_his_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)DescriptionActionsGraphical viewLength
Sequence conflicti289C → E AA sequence (Ref. 3) Curated1
Sequence conflicti300Q → E AA sequence (Ref. 3) Curated1
Sequence conflicti339P → S AA sequence (Ref. 3) Curated1
Sequence conflicti342D → E AA sequence (Ref. 3) Curated1
Sequence conflicti344C → V AA sequence (Ref. 3) Curated1
Sequence conflicti357 – 358EV → PL AA sequence (Ref. 3) Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ421152 mRNA. Translation: CAD12888.1.
X84057 mRNA. Translation: CAA58876.1.
PIRiS53311.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ421152 mRNA. Translation: CAD12888.1.
X84057 mRNA. Translation: CAA58876.1.
PIRiS53311.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GXSX-ray2.30A/C56-325[»]
B/D338-495[»]
ProteinModelPortaliP52708.
SMRiP52708.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi4558.Sb04g036350.1.

Protein family/group databases

ESTHERisorbi-hnl. Carboxypeptidase_S10.
MEROPSiS10.005.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG1282. Eukaryota.
COG2939. LUCA.
HOGENOMiHOG000198295.
OrthoDBiEOG09360880.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14084.
BRENDAi4.1.2.11. 5768.

Miscellaneous databases

EvolutionaryTraceiP52708.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR001563. Peptidase_S10.
IPR033124. Ser_caboxypep_his_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]
ProtoNetiSearch...

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: November 2, 2016
This is version 97 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.