SAHH1_ARATH
ID SAHH1_ARATH Reviewed; 485 AA.
AC O23255; O81847; Q8LE20;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Adenosylhomocysteinase 1 {ECO:0000303|PubMed:15659630};
DE Short=AdoHcyase 1 {ECO:0000303|PubMed:15659630};
DE EC=3.3.1.1 {ECO:0000269|PubMed:15659630};
DE AltName: Full=Protein EMBRYO DEFECTIVE 1395 {ECO:0000303|PubMed:15266054};
DE AltName: Full=Protein HOMOLOGY-DEPENDENT GENE SILENCING 1 {ECO:0000303|PubMed:15659630};
DE AltName: Full=S-adenosyl-L-homocysteine hydrolase 1 {ECO:0000303|PubMed:15659630, ECO:0000303|Ref.1};
DE Short=SAH hydrolase 1 {ECO:0000303|PubMed:15659630, ECO:0000303|Ref.1};
GN Name=SAHH1 {ECO:0000303|PubMed:15659630, ECO:0000303|Ref.1};
GN Synonyms=EMB1395, HOG1 {ECO:0000303|PubMed:15659630};
GN OrderedLocusNames=At4g13940 {ECO:0000312|Araport:AT4G13940};
GN ORFNames=dl3010w {ECO:0000312|EMBL:CAB10173.1};
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 [MRNA].
RC STRAIN=cv. Landsberg erecta;
RA Belbahri L., Elleuch H., Villarroel R., Inze D., Thomas D., Thomasset B.;
RT "The isolation of an Arabidopsis thaliana cDNA clone encoding S-adenosyl-L-
RT homocysteine hydrolase.";
RL (er) Plant Gene Register PGR99-139(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF GLY-386; THR-414 AND ASP-444,
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE OF 19-485.
RC STRAIN=cv. Landsberg erecta;
RA Zhang H., Forde B.G.;
RT "Identification of novel nitrate-inducible genes from Arabidopsis.";
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
RX PubMed=15266054; DOI=10.1104/pp.104.045179;
RA Tzafrir I., Pena-Muralla R., Dickerman A., Berg M., Rogers R., Hutchens S.,
RA Sweeney T.C., McElver J., Aux G., Patton D., Meinke D.;
RT "Identification of genes required for embryo development in Arabidopsis.";
RL Plant Physiol. 135:1206-1220(2004).
CC -!- FUNCTION: Essential protein during embryogenesis (PubMed:15266054).
CC Adenosylhomocysteine is a competitive inhibitor of S-adenosyl-L-
CC 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 (PubMed:15659630). Required for DNA methylation-
CC dependent gene silencing (PubMed:15659630).
CC {ECO:0000269|PubMed:15266054, ECO:0000269|PubMed:15659630}.
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 Evidence={ECO:0000269|PubMed:15659630};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000250|UniProtKB:P23526};
CC Note=Binds 1 NAD(+) per subunit. {ECO:0000250|UniProtKB:P23526};
CC -!- PATHWAY: Amino-acid biosynthesis; L-homocysteine biosynthesis; L-
CC homocysteine from S-adenosyl-L-homocysteine: step 1/1.
CC {ECO:0000269|PubMed:15659630}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P23526}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=O23255-1; Sequence=Displayed;
CC -!- DISRUPTION PHENOTYPE: Embryo defective arrested at the globular stage
CC (PubMed:15266054). Null mutations are homozygous lethal
CC (PubMed:15266054). {ECO:0000269|PubMed:15266054}.
CC -!- SIMILARITY: Belongs to the adenosylhomocysteinase family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Seed defective Arabidopsis mutants;
CC URL="http://seedgenes.org/MutantList";
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DR EMBL; AF059581; AAC14714.1; -; mRNA.
DR EMBL; Z97335; CAB10173.1; -; Genomic_DNA.
DR EMBL; AL161537; CAB78436.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83345.1; -; Genomic_DNA.
DR EMBL; AF325037; AAG40389.1; -; mRNA.
DR EMBL; AY042866; AAK68806.1; -; mRNA.
DR EMBL; AY049279; AAK83621.1; -; mRNA.
DR EMBL; AY081468; AAM10030.1; -; mRNA.
DR EMBL; AY090284; AAL90945.1; -; mRNA.
DR EMBL; BT002404; AAO00764.1; -; mRNA.
DR EMBL; AY085669; AAM62888.1; -; mRNA.
DR EMBL; Z97059; CAB09795.1; -; mRNA.
DR PIR; C71400; C71400.
DR RefSeq; NP_193130.1; NM_117468.3. [O23255-1]
DR AlphaFoldDB; O23255; -.
DR SMR; O23255; -.
DR BioGRID; 12325; 13.
DR IntAct; O23255; 2.
DR STRING; 3702.AT4G13940.1; -.
DR iPTMnet; O23255; -.
DR PaxDb; O23255; -.
DR PRIDE; O23255; -.
DR EnsemblPlants; AT4G13940.1; AT4G13940.1; AT4G13940. [O23255-1]
DR GeneID; 827028; -.
DR Gramene; AT4G13940.1; AT4G13940.1; AT4G13940. [O23255-1]
DR KEGG; ath:AT4G13940; -.
DR Araport; AT4G13940; -.
DR TAIR; locus:2129256; AT4G13940.
DR eggNOG; KOG1370; Eukaryota.
DR InParanoid; O23255; -.
DR PhylomeDB; O23255; -.
DR BioCyc; ARA:AT4G13940-MON; -.
DR UniPathway; UPA00314; UER00076.
DR PRO; PR:O23255; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O23255; baseline and differential.
DR Genevisible; O23255; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0004013; F:adenosylhomocysteinase activity; IMP:TAIR.
DR GO; GO:0005507; F:copper ion binding; HDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0006346; P:DNA methylation-dependent heterochromatin assembly; IMP:TAIR.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0016441; P:post-transcriptional gene silencing; IMP:TAIR.
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 1: Evidence at protein level;
KW Alternative splicing; Hydrolase; NAD; One-carbon metabolism;
KW Reference proteome.
FT CHAIN 1..485
FT /note="Adenosylhomocysteinase 1"
FT /id="PRO_0000116920"
FT BINDING 64
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P10760"
FT BINDING 139
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P10760"
FT BINDING 205
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P10760"
FT BINDING 206..208
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P23526"
FT BINDING 235
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P10760"
FT BINDING 239
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P10760"
FT BINDING 271..276
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P23526"
FT BINDING 292
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P23526"
FT BINDING 348..350
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P23526"
FT BINDING 397
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P23526"
FT BINDING 404
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P23526"
FT BINDING 479..483
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P10760"
FT BINDING 479
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P10760"
FT BINDING 483
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P10760"
FT MUTAGEN 386
FT /note="G->E: In hog1-2; genome-wide demethylation and loss
FT of transcriptional gene silencing."
FT /evidence="ECO:0000269|PubMed:15659630"
FT MUTAGEN 414
FT /note="T->I: In hog1-1; genome-wide demethylation and loss
FT of transcriptional gene silencing."
FT /evidence="ECO:0000269|PubMed:15659630"
FT MUTAGEN 444
FT /note="D->N: In hog1-3; genome-wide demethylation and loss
FT of transcriptional gene silencing."
FT /evidence="ECO:0000269|PubMed:15659630"
FT CONFLICT 80
FT /note="E -> Q (in Ref. 8; CAB09795)"
FT /evidence="ECO:0000305"
FT CONFLICT 96
FT /note="A -> R (in Ref. 8; CAB09795)"
FT /evidence="ECO:0000305"
FT CONFLICT 392
FT /note="E -> Q (in Ref. 8; CAB09795)"
FT /evidence="ECO:0000305"
FT CONFLICT 460
FT /note="T -> R (in Ref. 8; CAB09795)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 485 AA; 53379 MW; 1113270A0F46C86C CRC64;
MALLVEKTSS GREYKVKDMS QADFGRLELE LAEVEMPGLM ACRTEFGPSQ PFKGARITGS
LHMTIQTAVL IETLTALGAE VRWCSCNIFS TQDHAAAAIA RDSAAVFAWK GETLQEYWWC
TERALDWGPG GGPDLIVDDG GDATLLIHEG VKAEEIFEKT GQVPDPTSTD NPEFQIVLSI
IKEGLQVDPK KYHKMKERLV GVSEETTTGV KRLYQMQQNG TLLFPAINVN DSVTKSKFDN
LYGCRHSLPD GLMRATDVMI AGKVAVICGY GDVGKGCAAA MKTAGARVIV TEIDPICALQ
ALMEGLQVLT LEDVVSEADI FVTTTGNKDI IMVDHMRKMK NNAIVCNIGH FDNEIDMLGL
ETYPGVKRIT IKPQTDRWVF PETKAGIIVL AEGRLMNLGC ATGHPSFVMS CSFTNQVIAQ
LELWNEKASG KYEKKVYVLP KHLDEKVALL HLGKLGARLT KLSKDQSDYV SIPIEGPYKP
PHYRY
