O23255 (SAHH1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Adenosylhomocysteinase 1
Short name=AdoHcyase 1
EC=3.3.1.1

Alternative name(s):
Protein EMBRYO DEFECTIVE 1395
Protein HOMOLOGY-DEPENDENT GENE SILENCING 1
S-adenosyl-L-homocysteine hydrolase 1
Short name=SAH hydrolase 1

Gene names

Name:	SAHH1
Synonyms:	EMB1395, HOG1
Ordered Locus Names:	At4g13940
ORF Names:	dl3010w

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. Required for DNA methylation-dependent gene silencing.
Catalytic activity	S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine.
Cofactor	Binds 1 NAD per subunit.
Pathway	Amino-acid biosynthesis; L-homocysteine biosynthesis; L-homocysteine from S-adenosyl-L-homocysteine: step 1/1.
Subunit structure	Homotetramer By similarity.
Miscellaneous	Null mutations are homozygous lethal.
Sequence similarities	Belongs to the adenosylhomocysteinase family.

Ontologies

Keywords
Biological process	One-carbon metabolism
Coding sequence diversity	Alternative splicing
Ligand	NAD
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	embryo development ending in seed dormancy Inferred from mutant phenotype. Source: TAIR methylation-dependent chromatin silencing Inferred from mutant phenotype Ref.2. Source: TAIR one-carbon metabolic process Inferred from electronic annotation. Source: UniProtKB-KW posttranscriptional gene silencing Inferred from mutant phenotype. Source: TAIR
Cellular component	cytosol Inferred from direct assay. Source: TAIR plasma membrane Inferred from direct assay. Source: TAIR plasmodesma Inferred from direct assay. Source: TAIR vacuolar membrane Inferred from direct assay. Source: TAIR
Molecular function	adenosylhomocysteinase activity Inferred from mutant phenotype Ref.2. Source: TAIR copper ion binding Inferred from direct assay. Source: TAIR
Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: O23255-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 485	485	Adenosylhomocysteinase 1		PRO_0000116920
Regions
	Nucleotide binding	206 – 208	3	NAD By similarity
	Nucleotide binding	269 – 274	6	NAD By similarity
	Nucleotide binding	348 – 350	3	NAD By similarity
Sites
	Binding site	64	1	Substrate By similarity
	Binding site	139	1	Substrate By similarity
	Binding site	205	1	Substrate By similarity
	Binding site	235	1	Substrate By similarity
	Binding site	239	1	Substrate By similarity
	Binding site	240	1	NAD By similarity
	Binding site	292	1	NAD By similarity
	Binding site	327	1	NAD By similarity
	Binding site	397	1	NAD By similarity
Experimental info
	Mutagenesis	386	1	G → E in hog1-2; genome-wide demethylation and loss of transcriptional gene silencing. Ref.2
	Mutagenesis	414	1	T → I in hog1-1; genome-wide demethylation and loss of transcriptional gene silencing. Ref.2
	Mutagenesis	444	1	D → N in hog1-3; genome-wide demethylation and loss of transcriptional gene silencing. Ref.2
	Sequence conflict	80	1	E → Q in CAB09795. Ref.8
	Sequence conflict	96	1	A → R in CAB09795. Ref.8
	Sequence conflict	392	1	E → Q in CAB09795. Ref.8
	Sequence conflict	460	1	T → R in CAB09795. Ref.8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 1113270A0F46C86C	FASTA	485	53,379
	10 20 30 40 50 60 MALLVEKTSS GREYKVKDMS QADFGRLELE LAEVEMPGLM ACRTEFGPSQ PFKGARITGS 70 80 90 100 110 120 LHMTIQTAVL IETLTALGAE VRWCSCNIFS TQDHAAAAIA RDSAAVFAWK GETLQEYWWC 130 140 150 160 170 180 TERALDWGPG GGPDLIVDDG GDATLLIHEG VKAEEIFEKT GQVPDPTSTD NPEFQIVLSI 190 200 210 220 230 240 IKEGLQVDPK KYHKMKERLV GVSEETTTGV KRLYQMQQNG TLLFPAINVN DSVTKSKFDN 250 260 270 280 290 300 LYGCRHSLPD GLMRATDVMI AGKVAVICGY GDVGKGCAAA MKTAGARVIV TEIDPICALQ 310 320 330 340 350 360 ALMEGLQVLT LEDVVSEADI FVTTTGNKDI IMVDHMRKMK NNAIVCNIGH FDNEIDMLGL 370 380 390 400 410 420 ETYPGVKRIT IKPQTDRWVF PETKAGIIVL AEGRLMNLGC ATGHPSFVMS CSFTNQVIAQ 430 440 450 460 470 480 LELWNEKASG KYEKKVYVLP KHLDEKVALL HLGKLGARLT KLSKDQSDYV SIPIEGPYKP PHYRY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The isolation of an Arabidopsis thaliana cDNA clone encoding S-adenosyl-L-homocysteine hydrolase." Belbahri L., Elleuch H., Villarroel R., Inze D., Thomas D., Thomasset B. Plant Gene Register PGR99-139 Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Landsberg erecta.
[2]	"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: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF GLY-386; THR-414 AND ASP-444.
[3]	"Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis thaliana." Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C., Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P., Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E. , Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R., De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M., Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M., Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A., Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D., Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A., Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S., Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G., Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N. Nature 391:485-488(1998) [PubMed: 9461215] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [PubMed: 10617198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[5]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[6]	"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. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[7]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[8]	"Identification of novel nitrate-inducible genes from Arabidopsis." Zhang H., Forde B.G. Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE OF 19-485. Strain: cv. Landsberg erecta.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF059581 mRNA. Translation: AAC14714.1. Z97335 Genomic DNA. Translation: CAB10173.1. AL161537 Genomic DNA. Translation: CAB78436.1. CP002687 Genomic DNA. Translation: AEE83345.1. AF325037 mRNA. Translation: AAG40389.1. AY042866 mRNA. Translation: AAK68806.1. AY049279 mRNA. Translation: AAK83621.1. AY081468 mRNA. Translation: AAM10030.1. AY090284 mRNA. Translation: AAL90945.1. BT002404 mRNA. Translation: AAO00764.1. AY085669 mRNA. Translation: AAM62888.1. Z97059 mRNA. Translation: CAB09795.1.
IPI	IPI00527713.
PIR	C71400.
RefSeq	NP_193130.1. NM_117468.2.
UniGene	At.24056. At.24845. At.71469. At.71956. At.74987. At.74988.
3D structure databases
ProteinModelPortal	O23255.
SMR	O23255. Positions 1-485.
ModBase	Search...
Protein-protein interaction databases
IntAct	O23255. 1 interaction.
STRING	O23255.
Proteomic databases
PRIDE	O23255.
ProMEX	O23255.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT4G13940.1; AT4G13940.1; AT4G13940.
GeneID	827028.
GenomeReviews	Gene locus AT4G13940 in contig CT486007_GR.
KEGG	ath:AT4G13940.
NMPDR	fig|3702.1.peg.19089.
Organism-specific databases
TAIR	At4g13940.
Phylogenomic databases
HOGENOM	HBG352029.
InParanoid	O23255.
OMA	ELFTKTE.
PhylomeDB	O23255.
ProtClustDB	PLN02494.
Gene expression databases
ArrayExpress	O23255.
Genevestigator	O23255.
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

SAHH1_ARATH

Accession

Primary (citable) accession number: O23255
Secondary accession number(s): O81847, Q8LE20

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	January 1, 1998
Last modified:	January 25, 2012
This is version 104 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program