位置:首页 > 蛋白库 > HMT3_ARATH
HMT3_ARATH
ID   HMT3_ARATH              Reviewed;         347 AA.
AC   Q8LAX0; Q9LUI7;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 2.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Homocysteine S-methyltransferase 3;
DE            EC=2.1.1.10;
DE   AltName: Full=S-methylmethionine:homocysteine methyltransferase 3;
DE            Short=AtHMT-3;
DE            Short=SMM:Hcy S-methyltransferase 3;
GN   Name=HMT3; OrderedLocusNames=At3g22740; ORFNames=MWI23.11;
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], ENZYME ACTIVITY, PROBABLE FUNCTION OF SMM
RP   CYCLE, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Columbia; TISSUE=Leaf;
RX   PubMed=11309147; DOI=10.1046/j.1365-313x.2001.00988.x;
RA   Ranocha P., McNeil S.D., Ziemak M.J., Li C., Tarczynski M.C., Hanson A.D.;
RT   "The S-methylmethionine cycle in angiosperms: ubiquity, antiquity and
RT   activity.";
RL   Plant J. 25:575-584(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT   features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:131-135(2000).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
RN   [5]
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   [6]
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.
CC   -!- FUNCTION: Catalyzes methyl transfer from S-methylmethionine (SMM) to
CC       adenosyl-L-homocysteine (AdoMet). SMM degradation (by HMT-1, HMT-2 and
CC       HMT-3) and biosynthesis (by MMT1) constitute the SMM cycle in plants,
CC       which is probably required to achieve short term control of AdoMet
CC       level.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-homocysteine + S-methyl-L-methionine = H(+) + 2 L-
CC         methionine; Xref=Rhea:RHEA:26337, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57844, ChEBI:CHEBI:58199, ChEBI:CHEBI:58252; EC=2.1.1.10;
CC         Evidence={ECO:0000269|PubMed:11309147};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00333};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=335 uM for S-methylmethionine {ECO:0000269|PubMed:11309147};
CC         KM=1760 uM for (S,S)-AdoMet {ECO:0000269|PubMed:11309147};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed predominantly in rosette leaves.
CC       Expressed in roots, cauline leaves and developing seeds.
CC       {ECO:0000269|PubMed:11309147}.
CC   -!- MISCELLANEOUS: In contrast to HMT-1, it is not inhibited by methionine.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF297394; AAG10301.1; -; mRNA.
DR   EMBL; AB022223; BAB01249.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE76672.1; -; Genomic_DNA.
DR   EMBL; AK118021; BAC42654.1; -; mRNA.
DR   EMBL; BT005318; AAO63382.1; -; mRNA.
DR   EMBL; AY087554; AAM65096.1; -; mRNA.
DR   RefSeq; NP_566715.1; NM_113173.3.
DR   AlphaFoldDB; Q8LAX0; -.
DR   SMR; Q8LAX0; -.
DR   STRING; 3702.AT3G22740.1; -.
DR   PaxDb; Q8LAX0; -.
DR   PRIDE; Q8LAX0; -.
DR   ProteomicsDB; 230213; -.
DR   EnsemblPlants; AT3G22740.1; AT3G22740.1; AT3G22740.
DR   GeneID; 821845; -.
DR   Gramene; AT3G22740.1; AT3G22740.1; AT3G22740.
DR   KEGG; ath:AT3G22740; -.
DR   Araport; AT3G22740; -.
DR   TAIR; locus:2094419; AT3G22740.
DR   eggNOG; KOG1579; Eukaryota.
DR   HOGENOM; CLU_004914_3_2_1; -.
DR   InParanoid; Q8LAX0; -.
DR   OMA; YIGGCCK; -.
DR   OrthoDB; 731388at2759; -.
DR   PhylomeDB; Q8LAX0; -.
DR   BioCyc; ARA:AT3G22740-MON; -.
DR   BioCyc; MetaCyc:AT3G22740-MON; -.
DR   BRENDA; 2.1.1.10; 399.
DR   SABIO-RK; Q8LAX0; -.
DR   PRO; PR:Q8LAX0; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q8LAX0; baseline and differential.
DR   Genevisible; Q8LAX0; AT.
DR   GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0061627; F:S-methylmethionine-homocysteine S-methyltransferase activity; IEA:RHEA.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0009086; P:methionine biosynthetic process; IBA:GO_Central.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0033528; P:S-methylmethionine cycle; IBA:GO_Central.
DR   Gene3D; 3.20.20.330; -; 1.
DR   InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT.
DR   InterPro; IPR003726; HCY_dom.
DR   InterPro; IPR036589; HCY_dom_sf.
DR   Pfam; PF02574; S-methyl_trans; 1.
DR   PIRSF; PIRSF037505; Betaine_HMT; 1.
DR   SUPFAM; SSF82282; SSF82282; 1.
DR   PROSITE; PS50970; HCY; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Metal-binding; Methionine biosynthesis;
KW   Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase; Zinc.
FT   CHAIN           1..347
FT                   /note="Homocysteine S-methyltransferase 3"
FT                   /id="PRO_0000114613"
FT   DOMAIN          12..333
FT                   /note="Hcy-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00333"
FT   BINDING         251
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00333"
FT   BINDING         318
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00333"
FT   BINDING         319
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00333"
FT   CONFLICT        24
FT                   /note="A -> E (in Ref. 6; AAM65096)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        45
FT                   /note="L -> I (in Ref. 6; AAM65096)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        117
FT                   /note="C -> W (in Ref. 6; AAM65096)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   347 AA;  37882 MW;  45CDC34973F820CC CRC64;
     MGSFVKEETS SLMTDFLEKC GGYAVVDGGF ATELQRHGAD INDPLWSAKC LITSPHLVTK
     VHLDYLESGA NIIITASYQA TIQGFVAKGL SVGEAENLLR RSVEITYEAR EIFYNRCTKG
     SWDFAYAGKA SRRPILVAAS VGSYGAYLAD GSEYSGIYGD SVSKETLKDF HRRRVQILAK
     SGADLIAFET IPNKLEAEAY ADLLEEEDID IPAWFSFTSK DGVSVPRGDS VVECAKVADS
     CKNVVAIGIN CTAPRYIHAL IISLRQMTRK PIVVYPNSGE VYDGLNKKWI KSEGESEEDF
     VSYVSKWRDA GASLFGGCCR TTPNTIRAIA KVLSDEPSAA SKPKFGQ
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024