Adenosylhomocysteinase 2 - Arabidopsis thaliana (Mouse-ear cress)

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Q9LK36 (SAHH2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 81. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Adenosylhomocysteinase 2
Short name=AdoHcyase 2
EC=3.3.1.1

Alternative name(s):
S-adenosyl-L-homocysteine hydrolase 1
SAH hydrolase 2

Gene names

Name:	SAHH2
Ordered Locus Names:	At3g23810
ORF Names:	MYM9_15, MYM9.16

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	485 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Adenosylhomocysteine is a competitive inhibitor of S-adenosyl-L-methinine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine By similarity.
Catalytic activity	S-adenosyl-L-homocysteine + H₂O = L-homocysteine + adenosine.
Cofactor	NAD By similarity.
Pathway	Amino-acid biosynthesis; L-homocysteine biosynthesis; L-homocysteine from S-adenosyl-L-homocysteine: step 1/1.
Miscellaneous	In contrast to SAHH1, a mutation in the C-terminus of this protein is not sufficient to abolish transcriptional gene silencing.
Sequence similarities	Belongs to the adenosylhomocysteinase family.

Ontologies

Keywords
Biological process	One-carbon metabolism
Ligand	NAD
Molecular function	Hydrolase
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	one-carbon metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from direct assay. Source: TAIR plasma membrane Inferred from direct assay. Source: TAIR vacuole Inferred from direct assay. Source: TAIR
Molecular function	adenosylhomocysteinase 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

Chain

1 – 485

485

Adenosylhomocysteinase 2

PRO_0000116921

Regions

Nucleotide binding

206 – 208

NAD By similarity

Nucleotide binding

269 – 274

NAD By similarity

Nucleotide binding

348 – 350

NAD By similarity

Sites

Binding site

Substrate By similarity

Binding site

139

Substrate By similarity

Binding site

205

Substrate By similarity

Binding site

235

Substrate By similarity

Binding site

239

Substrate By similarity

Binding site

240

NAD By similarity

Binding site

292

NAD By similarity

Binding site

327

NAD By similarity

Binding site

397

NAD By similarity

Amino acid modifications

Modified residue

219

Phosphothreonine Ref.6

Cross-link

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.5

Experimental info

Sequence conflict

T → A in AAL16259. Ref.3

Sequence conflict

155

E → A in AAM19782. Ref.3

Sequence conflict

442

H → R in AAK92718. Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

Q9LK36 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 876079E944DC3732
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FASTA

485

53,159

        10         20         30         40         50         60 
MALLVEKTSS GREYKVKDMS QADFGRLEIE LAEVEMPGLV SCVTEFGPSQ PLKGARITGS 

        70         80         90        100        110        120 
LHMTIQTAVL IETLTALGAE VRWCSCNIFS TQDHAAAAIA RDSAAVFAWK GETLQEYWWC 

       130        140        150        160        170        180 
TERALDWGPG GGPDLIVDDG GDATLLIHEG VKAEEIFAKN GTFPDPTSTD NPEFQIVLSI 

       190        200        210        220        230        240 
IKDGLQVDPK KYHKMKERLV GVSEETTTGV KRLYQMQETG ALLFPAINVN DSVTKSKFDN 

       250        260        270        280        290        300 
LYGCRHSLPD GLMRATDVMI AGKVAVICGY GDVGKGCAAA MKTAGARVIV TEIDPICALQ 

       310        320        330        340        350        360 
ALMEGLQVLT LEDVVSEADI FCTTTGNKDI IMVDHMRKMK NNAIVCNIGH FDNEIDMLGL 

       370        380        390        400        410        420 
ETYPGVKRIT IKPQTDRWVF PDTNSGIIVL AEGRLMNLGC ATGHPSFVMS CSFTNQVIAQ 

       430        440        450        460        470        480 
LELWNEKSSG KYEKKVYVLP KHLDEKVAAL HLGKLGARLT KLTKDQSDYV SIPVEGPYKP 


VHYRY

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC clones." Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S. DNA Res. 7:217-221(2000) [PubMed: 10907853] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[3]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"The Arabidopsis HOMOLOGY-DEPENDENT GENE SILENCING1 gene codes for an S-adenosyl-L-homocysteine hydrolase required for DNA methylation-dependent gene silencing." Rocha P.S., Sheikh M., Melchiorre R., Fagard M., Boutet S., Loach R., Moffatt B., Wagner C., Vaucheret H., Furner I. Plant Cell 17:404-417(2005) [PubMed: 15659630] [Abstract] Cited for: ABSENCE OF EFFECT ON TRANSCRIPTIONAL GENE SILENCING.
[5]	"Multidimensional protein identification technology (MudPIT) analysis of ubiquitinated proteins in plants." Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K. Mol. Cell. Proteomics 6:601-610(2007) [PubMed: 17272265] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-15, MASS SPECTROMETRY. Strain: cv. Landsberg erecta.
[6]	"Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks." Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S. Plant Physiol. 150:889-903(2009) [PubMed: 19376835] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-219, MASS SPECTROMETRY. Strain: cv. Columbia. Tissue: Seedling.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AP000377 Genomic DNA. Translation: BAB01858.1. CP002686 Genomic DNA. Translation: AEE76817.1. AY059888 mRNA. Translation: AAL24370.1. AY093385 mRNA. Translation: AAM13384.1. AY150471 mRNA. Translation: AAN12996.1. AF428329 mRNA. Translation: AAL16259.1. AY094404 mRNA. Translation: AAM19782.1. AY050783 mRNA. Translation: AAK92718.1.
IPI	IPI00527089.
RefSeq	NP_189023.1. NM_113286.2.
UniGene	At.24845. At.67005.
3D structure databases
ProteinModelPortal	Q9LK36.
SMR	Q9LK36. Positions 1-485.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9LK36.
Proteomic databases
PRIDE	Q9LK36.
ProMEX	Q9LK36.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT3G23810.1; AT3G23810.1; AT3G23810.
GeneID	821964.
GenomeReviews	Gene locus AT3G23810 in contig BA000014_GR.
KEGG	ath:AT3G23810.
NMPDR	fig\|3702.1.peg.14638.
Organism-specific databases
TAIR	At3g23810.
Phylogenomic databases
GeneTree	EPGT00050000017198.
HOGENOM	HBG352029.
InParanoid	Q9LK36.
OMA	MKEDAIV.
PhylomeDB	Q9LK36.
ProtClustDB	PLN02494.
Gene expression databases
Genevestigator	Q9LK36.
GermOnline	AT3G23810. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR000043. Adenosylhomocysteinase. IPR015878. Ado_hCys_hydrolase_NAD-bd. IPR020082. S-Ado-L-homoCys_hydrolase_CS. [Graphical view]
KO	K01251.
PANTHER	PTHR23420. Ad_hcy_hydrolase. 1 hit.
Pfam	PF05221. AdoHcyase. 1 hit. PF00670. AdoHcyase_NAD. 1 hit. [Graphical view]
PIRSF	PIRSF001109. Ad_hcy_hydrolase. 1 hit.
SMART	SM00996. AdoHcyase. 1 hit. SM00997. AdoHcyase_NAD. 1 hit. [Graphical view]
TIGRFAMs	TIGR00936. AhcY. 1 hit.
PROSITE	PS00738. ADOHCYASE_1. 1 hit. PS00739. ADOHCYASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SAHH2_ARATH

Accession

Primary (citable) accession number: Q9LK36
Secondary accession number(s): Q8LPS8, Q944K5, Q949Z9

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	October 1, 2000
Last modified:	January 25, 2012
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents