HMT4_MAIZE
ID HMT4_MAIZE Reviewed; 342 AA.
AC Q9FUM7;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Homocysteine S-methyltransferase 4;
DE EC=2.1.1.10;
DE AltName: Full=S-methylmethionine:homocysteine methyltransferase 4;
DE Short=SMM:Hcy S-methyltransferase 4;
DE AltName: Full=ZmHMT-4;
GN Name=HMT-4;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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).
CC -!- FUNCTION: Catalyzes methyl transfer from S-methylmethionine (SMM) to
CC adenosyl-L-homocysteine (AdoMet). SMM degradation (by HMT-1, HMT-2,
CC HMT-3 and HMT-4) and biosynthesis (by MMT1) constitute the SMM cycle in
CC plants, which is probably required to achieve short term control of
CC AdoMet level (By similarity). {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00333};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
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DR EMBL; AF297047; AAG22540.1; -; mRNA.
DR RefSeq; NP_001105014.1; NM_001111544.1.
DR AlphaFoldDB; Q9FUM7; -.
DR SMR; Q9FUM7; -.
DR STRING; 4577.GRMZM2G039166_P01; -.
DR PaxDb; Q9FUM7; -.
DR PRIDE; Q9FUM7; -.
DR GeneID; 541876; -.
DR KEGG; zma:541876; -.
DR eggNOG; KOG1579; Eukaryota.
DR OrthoDB; 731388at2759; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; Q9FUM7; baseline and differential.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061627; F:S-methylmethionine-homocysteine S-methyltransferase activity; IEA:RHEA.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Amino-acid biosynthesis; Metal-binding; Methionine biosynthesis;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase; Zinc.
FT CHAIN 1..342
FT /note="Homocysteine S-methyltransferase 4"
FT /id="PRO_0000114617"
FT DOMAIN 13..328
FT /note="Hcy-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00333"
FT BINDING 245
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00333"
FT BINDING 313
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00333"
FT BINDING 314
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00333"
SQ SEQUENCE 342 AA; 36460 MW; 922EE23117D10FBB CRC64;
MWFGGGPIDA AGALRGFVRE AGGCAVVDGG LGTELEAHGA DLHDALWSAK CLASAPHLIR
KVHLDYLEAG ADVIISASYQ ATIEGFQSRG FSRDESEELL RRSVHVAQEA RRVFAAEGDR
SSRRGRPPAL VAASVGSYGA YRADGSEYSG DYGKSMTKED LKNFHRRRLQ VLAGAGPDLI
AFETIPNKLE AQVYAELLEE NGIRIPAWFS FTSKDGVNAA SGDPINECAA VADSCPRVDA
VGVNCTAPRF IHGLILSIKK VTSKPIVVYP NSGETYVAET NEWVDSDGAT GTDDFVSRVG
EWRRAGAALI GGCCRTSPAT VRAIARAVRE AEYDDIPAVA VL
