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Q9SSM2 (MDLL_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
(R)-mandelonitrile lyase-like

EC=4.1.2.10
Alternative name(s):
Hydroxynitrile lyase-like
Short name=(R)-oxynitrilase-like
Gene names
Ordered Locus Names:At1g73050
ORF Names:F3N23.25
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length552 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

(R)-mandelonitrile = cyanide + benzaldehyde.

Cofactor

FAD By similarity.

Subunit structure

Monomer By similarity.

Post-translational modification

Glycosylated By similarity.

Sequence similarities

Belongs to the GMC oxidoreductase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Potential
Chain29 – 552524(R)-mandelonitrile lyase-like
PRO_0000412562

Regions

Nucleotide binding55 – 8228FAD By similarity

Sites

Active site4921 By similarity

Amino acid modifications

Glycosylation441N-linked (GlcNAc...) Potential
Glycosylation1621N-linked (GlcNAc...) Potential
Glycosylation2591N-linked (GlcNAc...) Potential
Glycosylation4341N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict2571G → R in ABE65766. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9SSM2 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 7747A5D5C2DA7C7A

FASTA55260,783
        10         20         30         40         50         60 
MTKRIDSSLL YTALVVLLLL GVVHRSNARP RVNRPPGFMR FISNATDFAS EDYYDYIIVG 

        70         80         90        100        110        120 
GGTAGCPLAA TLSQSFRVLL LERGGVPYNR PNVMSHDGFL TTLTDVNNFD SPAQSFISEE 

       130        140        150        160        170        180 
GVPNARGRVL GGSSAINAGF YSRADKQFFE NSGLVWDLSS VNQSYEWVER AIVFRPQLRT 

       190        200        210        220        230        240 
WQTAIRDALL EVGVHPFNGF TLEHKVGTKI GGSTFDRTGR RHSSADLLRY ARSSNIRVAV 

       250        260        270        280        290        300 
YATVERVLLA SSPSVSGSNV SAIGVVYRDQ LGRFHHALIR DRGEVILSAG ALGSPQLLFL 

       310        320        330        340        350        360 
SGIGPRSYLS TWGIPVALDQ PHVGDFVYDN PRNGISIVPP VPMENSLIQV VGVTEDGAFL 

       370        380        390        400        410        420 
EAASNVIPFA SPLHSVFIRA PASPLYVPVT TIMEKILGPV SIGLLRLAST DVRINPVVRF 

       430        440        450        460        470        480 
NYFSDPQDLE RCVNGTRKIG EILRSRAMQD FMIREWFGNR RFRFVGAPLP VDQSNDLVMA 

       490        500        510        520        530        540 
DFCRRTVSTI WHYHGGAVVG KVVDSDLKVI GVNSLRLVDG STFNISPGTN PQATLMMLGR 

       550 
YMGLKMLRER MR 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. expand/collapse author list , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"Simultaneous high-throughput recombinational cloning of open reading frames in closed and open configurations."
Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.
Plant Biotechnol. J. 4:317-324(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC008017 Genomic DNA. Translation: AAD55652.1.
CP002684 Genomic DNA. Translation: AEE35408.1.
DQ446423 mRNA. Translation: ABE65766.1.
PIRA96756.
RefSeqNP_177448.1. NM_105963.1.
UniGeneAt.52489.

3D structure databases

ProteinModelPortalQ9SSM2.
SMRQ9SSM2. Positions 38-550.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT1G73050.1-P.

Proteomic databases

PRIDEQ9SSM2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G73050.1; AT1G73050.1; AT1G73050.
GeneID843636.
KEGGath:AT1G73050.

Organism-specific databases

TAIRAT1G73050.

Phylogenomic databases

eggNOGCOG2303.
HOGENOMHOG000239349.
InParanoidQ9SSM2.
KOK08248.
OMAWVERAIV.
PhylomeDBQ9SSM2.

Enzyme and pathway databases

BioCycARA:AT1G73050-MONOMER.

Gene expression databases

GenevestigatorQ9SSM2.

Family and domain databases

InterProIPR012132. GMC_OxRdtase.
IPR000172. GMC_OxRdtase_N.
IPR007867. GMC_OxRtase_C.
[Graphical view]
PfamPF05199. GMC_oxred_C. 1 hit.
PF00732. GMC_oxred_N. 1 hit.
[Graphical view]
PIRSFPIRSF000137. Alcohol_oxidase. 1 hit.
PROSITEPS00623. GMC_OXRED_1. 1 hit.
PS00624. GMC_OXRED_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROQ9SSM2.

Entry information

Entry nameMDLL_ARATH
AccessionPrimary (citable) accession number: Q9SSM2
Secondary accession number(s): Q1PFE0
Entry history
Integrated into UniProtKB/Swiss-Prot: September 21, 2011
Last sequence update: May 1, 2000
Last modified: May 14, 2014
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names