Q9SSM2 (MDLL_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	552 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Domain	Signal
Ligand	FAD Flavoprotein
Molecular function	Lyase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	alcohol metabolic process Inferred from electronic annotation. Source: InterPro
Molecular_function	choline dehydrogenase activity Inferred from electronic annotation. Source: InterPro flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro mandelonitrile lyase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 28	28	Potential
	Chain	29 – 552	524	(R)-mandelonitrile lyase-like		PRO_0000412562
Regions
	Nucleotide binding	55 – 82	28	FAD By similarity
Sites
	Active site	492	1	By similarity
Amino acid modifications
	Glycosylation	44	1	N-linked (GlcNAc...) Potential
	Glycosylation	162	1	N-linked (GlcNAc...) Potential
	Glycosylation	259	1	N-linked (GlcNAc...) Potential
	Glycosylation	434	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	257	1	G → R in ABE65766. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q9SSM2 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 7747A5D5C2DA7C7A	FASTA	552	60,783
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
IPI	IPI00545440.
PIR	A96756.
RefSeq	NP_177448.1. NM_105963.1.
UniGene	At.52489.
3D structure databases
HSSP	HSSP built from PDB template 1JU2 based on UniProtKB Q945K2.
ProteinModelPortal	Q9SSM2.
SMR	Q9SSM2. Positions 38-550.
ModBase	Search...
Protein-protein interaction databases
STRING	3702.AT1G73050.1-P.
Proteomic databases
PRIDE	Q9SSM2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT1G73050.1; AT1G73050.1; AT1G73050.
GeneID	843636.
KEGG	ath:AT1G73050.
Organism-specific databases
TAIR	At1g73050.
Phylogenomic databases
eggNOG	COG2303.
HOGENOM	HOG000239349.
InParanoid	Q9SSM2.
KO	K08248.
OMA	INAREDG.
PhylomeDB	Q9SSM2.
ProtClustDB	CLSN2679835.
Gene expression databases
ArrayExpress	Q9SSM2.
Genevestigator	Q9SSM2.
Family and domain databases
InterPro	IPR012132. GMC_OxRdtase. IPR000172. GMC_OxRdtase_N. IPR007867. GMC_OxRtase_C. [Graphical view]
Pfam	PF05199. GMC_oxred_C. 1 hit. PF00732. GMC_oxred_N. 1 hit. [Graphical view]
PIRSF	PIRSF000137. Alcohol_oxidase. 1 hit.
PROSITE	PS00623. GMC_OXRED_1. 1 hit. PS00624. GMC_OXRED_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MDLL_ARATH

Accession

Primary (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 1, 2013
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program