SAHH2_ARATH
ID SAHH2_ARATH Reviewed; 485 AA.
AC Q9LK36; Q8LPS8; Q944K5; Q949Z9;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Adenosylhomocysteinase 2;
DE Short=AdoHcyase 2;
DE EC=3.3.1.1;
DE AltName: Full=S-adenosyl-L-homocysteine hydrolase 1;
DE AltName: Full=SAH hydrolase 2;
GN Name=SAHH2; OrderedLocusNames=At3g23810; ORFNames=MYM9.16, MYM9_15;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP ABSENCE OF EFFECT ON TRANSCRIPTIONAL GENE SILENCING.
RX PubMed=15659630; DOI=10.1105/tpc.104.028332;
RA Rocha P.S., Sheikh M., Melchiorre R., Fagard M., Boutet S., Loach R.,
RA Moffatt B., Wagner C., Vaucheret H., Furner I.;
RT "The Arabidopsis HOMOLOGY-DEPENDENT GENE SILENCING1 gene codes for an S-
RT adenosyl-L-homocysteine hydrolase required for DNA methylation-dependent
RT gene silencing.";
RL Plant Cell 17:404-417(2005).
CC -!- FUNCTION: Adenosylhomocysteine is a competitive inhibitor of S-
CC adenosyl-L-methionine-dependent methyl transferase reactions; therefore
CC adenosylhomocysteinase may play a key role in the control of
CC methylations via regulation of the intracellular concentration of
CC adenosylhomocysteine. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + S-adenosyl-L-homocysteine = adenosine + L-homocysteine;
CC Xref=Rhea:RHEA:21708, ChEBI:CHEBI:15377, ChEBI:CHEBI:16335,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:58199; EC=3.3.1.1;
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-homocysteine biosynthesis; L-
CC homocysteine from S-adenosyl-L-homocysteine: step 1/1.
CC -!- MISCELLANEOUS: In contrast to SAHH1, a mutation in the C-terminus of
CC this protein is not sufficient to abolish transcriptional gene
CC silencing.
CC -!- SIMILARITY: Belongs to the adenosylhomocysteinase family.
CC {ECO:0000305}.
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DR EMBL; AP000377; BAB01858.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76817.1; -; Genomic_DNA.
DR EMBL; AY059888; AAL24370.1; -; mRNA.
DR EMBL; AY093385; AAM13384.1; -; mRNA.
DR EMBL; AY150471; AAN12996.1; -; mRNA.
DR EMBL; AF428329; AAL16259.1; -; mRNA.
DR EMBL; AY094404; AAM19782.1; -; mRNA.
DR EMBL; AY050783; AAK92718.1; -; mRNA.
DR RefSeq; NP_189023.1; NM_113286.3.
DR AlphaFoldDB; Q9LK36; -.
DR SMR; Q9LK36; -.
DR BioGRID; 7296; 5.
DR IntAct; Q9LK36; 1.
DR STRING; 3702.AT3G23810.1; -.
DR iPTMnet; Q9LK36; -.
DR MetOSite; Q9LK36; -.
DR PaxDb; Q9LK36; -.
DR PRIDE; Q9LK36; -.
DR ProteomicsDB; 232837; -.
DR EnsemblPlants; AT3G23810.1; AT3G23810.1; AT3G23810.
DR GeneID; 821964; -.
DR Gramene; AT3G23810.1; AT3G23810.1; AT3G23810.
DR KEGG; ath:AT3G23810; -.
DR Araport; AT3G23810; -.
DR TAIR; locus:2095193; AT3G23810.
DR eggNOG; KOG1370; Eukaryota.
DR HOGENOM; CLU_025194_2_1_1; -.
DR InParanoid; Q9LK36; -.
DR OMA; CLHVEAK; -.
DR OrthoDB; 371693at2759; -.
DR PhylomeDB; Q9LK36; -.
DR BioCyc; ARA:AT3G23810-MON; -.
DR UniPathway; UPA00314; UER00076.
DR PRO; PR:Q9LK36; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LK36; baseline and differential.
DR Genevisible; Q9LK36; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0004013; F:adenosylhomocysteinase activity; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0033353; P:S-adenosylmethionine cycle; IBA:GO_Central.
DR CDD; cd00401; SAHH; 1.
DR Gene3D; 3.40.50.1480; -; 1.
DR HAMAP; MF_00563; AdoHcyase; 1.
DR InterPro; IPR042172; Adenosylhomocyst_ase-like_sf.
DR InterPro; IPR000043; Adenosylhomocysteinase-like.
DR InterPro; IPR015878; Ado_hCys_hydrolase_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020082; S-Ado-L-homoCys_hydrolase_CS.
DR PANTHER; PTHR23420; PTHR23420; 1.
DR Pfam; PF05221; AdoHcyase; 1.
DR Pfam; PF00670; AdoHcyase_NAD; 1.
DR PIRSF; PIRSF001109; Ad_hcy_hydrolase; 1.
DR SMART; SM00996; AdoHcyase; 1.
DR SMART; SM00997; AdoHcyase_NAD; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR00936; ahcY; 1.
DR PROSITE; PS00738; ADOHCYASE_1; 1.
DR PROSITE; PS00739; ADOHCYASE_2; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; NAD; One-carbon metabolism; Reference proteome.
FT CHAIN 1..485
FT /note="Adenosylhomocysteinase 2"
FT /id="PRO_0000116921"
FT BINDING 64
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 205
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 206..208
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 235
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 239
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 240
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 269..274
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 292
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 327
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 348..350
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 397
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT CONFLICT 44
FT /note="T -> A (in Ref. 3; AAL16259)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="E -> A (in Ref. 3; AAM19782)"
FT /evidence="ECO:0000305"
FT CONFLICT 442
FT /note="H -> R (in Ref. 3; AAK92718)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 485 AA; 53159 MW; 876079E944DC3732 CRC64;
MALLVEKTSS GREYKVKDMS QADFGRLEIE LAEVEMPGLV SCVTEFGPSQ PLKGARITGS
LHMTIQTAVL IETLTALGAE VRWCSCNIFS TQDHAAAAIA RDSAAVFAWK GETLQEYWWC
TERALDWGPG GGPDLIVDDG GDATLLIHEG VKAEEIFAKN GTFPDPTSTD NPEFQIVLSI
IKDGLQVDPK KYHKMKERLV GVSEETTTGV KRLYQMQETG ALLFPAINVN DSVTKSKFDN
LYGCRHSLPD GLMRATDVMI AGKVAVICGY GDVGKGCAAA MKTAGARVIV TEIDPICALQ
ALMEGLQVLT LEDVVSEADI FCTTTGNKDI IMVDHMRKMK NNAIVCNIGH FDNEIDMLGL
ETYPGVKRIT IKPQTDRWVF PDTNSGIIVL AEGRLMNLGC ATGHPSFVMS CSFTNQVIAQ
LELWNEKSSG KYEKKVYVLP KHLDEKVAAL HLGKLGARLT KLTKDQSDYV SIPVEGPYKP
VHYRY
