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SMTA_BRAOT
ID   SMTA_BRAOT              Reviewed;         346 AA.
AC   Q4VNK0;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=Selenocysteine Se-methyltransferase;
DE            Short=BoSMT;
DE            EC=2.1.1.280;
GN   Name=SMT;
OS   Brassica oleracea var. italica (Broccoli).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=36774;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION BY SELENATE AND SULFATE, ACTIVITY
RP   REGULATION, AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Green comet;
RX   PubMed=15863700; DOI=10.1104/pp.104.056549;
RA   Lyi S.M., Heller L.I., Rutzke M., Welch R.M., Kochian L.V., Li L.;
RT   "Molecular and biochemical characterization of the selenocysteine Se-
RT   methyltransferase gene and Se-methylselenocysteine synthesis in broccoli.";
RL   Plant Physiol. 138:409-420(2005).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=cv. Green comet;
RX   PubMed=17391716; DOI=10.1016/j.phytochem.2007.02.007;
RA   Lyi S.M., Zhou X., Kochian L.V., Li L.;
RT   "Biochemical and molecular characterization of the homocysteine S-
RT   methyltransferase from broccoli (Brassica oleracea var. italica).";
RL   Phytochemistry 68:1112-1119(2007).
CC   -!- FUNCTION: Catalyzes the methylation of DL- and L-selenocysteine with S-
CC       methylmethionine as donor. Methylates also DL-homocysteine, DL- and L-
CC       cysteine in vitro. May be involved in selenium detoxification.
CC       {ECO:0000269|PubMed:15863700, ECO:0000269|PubMed:17391716}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-selenocysteine + S-methyl-L-methionine = H(+) + L-methionine
CC         + Se-methyl-L-selenocysteine; Xref=Rhea:RHEA:26341,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57843, ChEBI:CHEBI:57844,
CC         ChEBI:CHEBI:58252, ChEBI:CHEBI:58531; EC=2.1.1.280;
CC         Evidence={ECO:0000269|PubMed:15863700, ECO:0000269|PubMed:17391716};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00333};
CC   -!- ACTIVITY REGULATION: Inhibited by L-methionine.
CC       {ECO:0000269|PubMed:15863700}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.0. {ECO:0000269|PubMed:15863700};
CC   -!- TISSUE SPECIFICITY: Expressed in roots, young leaves and florets, but
CC       not detected in plants not exposed to selenium.
CC       {ECO:0000269|PubMed:15863700}.
CC   -!- INDUCTION: Up-regulated by selenate, but not by selenite. Down-
CC       regulated by sulfate. {ECO:0000269|PubMed:15863700}.
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DR   EMBL; AY817737; AAX20123.1; -; mRNA.
DR   AlphaFoldDB; Q4VNK0; -.
DR   SMR; Q4VNK0; -.
DR   KEGG; ag:AAX20123; -.
DR   BioCyc; MetaCyc:MON-15249; -.
DR   BRENDA; 2.1.1.280; 947.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016205; F:selenocysteine methyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0032259; P:methylation; IDA:UniProtKB.
DR   GO; GO:0010269; P:response to selenium ion; IDA:UniProtKB.
DR   Gene3D; 3.20.20.330; -; 1.
DR   InterPro; IPR003726; HCY_dom.
DR   InterPro; IPR036589; HCY_dom_sf.
DR   Pfam; PF02574; S-methyl_trans; 1.
DR   SUPFAM; SSF82282; SSF82282; 1.
DR   PROSITE; PS50970; HCY; 1.
PE   1: Evidence at protein level;
KW   Metal-binding; Methyltransferase; Transferase; Zinc.
FT   CHAIN           1..346
FT                   /note="Selenocysteine Se-methyltransferase"
FT                   /id="PRO_0000409375"
FT   DOMAIN          13..330
FT                   /note="Hcy-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00333"
FT   BINDING         248
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00333"
FT   BINDING         315
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00333"
FT   BINDING         316
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00333"
SQ   SEQUENCE   346 AA;  37863 MW;  50E11284D078FC8D CRC64;
     MVTGNTKAET FYSMKELLKE TGGYAIIDGG LATELERHGA DLNDPLWSAK CLLTSPHLIH
     TVHLDYLEAG ADIISSASYQ ATIQGFEAKG YSIEKSESLL RKSVEIACEA RSTYYDKCKD
     DDDKKILKKR PILVAASVGS YGAFLADGSE YSGIYGDLIT LETLKDFHRR RVQVLAESGA
     DIIAFETIPN KLEAQAFAEL LDEGVAKIPG WFSFNSKDGV NVVSGDSIKE CIAIAEACEK
     VVAVGINCTP PRFIEGLVLE IAKVTSKPIL VYPNSGERYD PERKEWVENT GVGNEDFVSY
     VEKWMDAGVS LLGGCCRTTP TTIRAIHKRL VSRRSLFSSS SSSSHH
 
 
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