METE_MESCR
ID METE_MESCR Reviewed; 765 AA.
AC P93263;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase;
DE EC=2.1.1.14;
DE AltName: Full=Cobalamin-independent methionine synthase isozyme;
DE AltName: Full=Vitamin-B12-independent methionine synthase isozyme;
GN Name=METE;
OS Mesembryanthemum crystallinum (Common ice plant) (Cryophytum crystallinum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Aizoaceae; Mesembryanthemum;
OC Mesembryanthemum subgen. Cryophytum.
OX NCBI_TaxID=3544;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Michalowski C.B., Quigley-Landreau F., Bohnert H.J.;
RT "Mesembryanthemum crystallinum methionine synthase mRNA.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the transfer of a methyl group from 5-
CC methyltetrahydrofolate to homocysteine resulting in methionine
CC formation. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = L-
CC methionine + tetrahydropteroyltri-L-glutamate; Xref=Rhea:RHEA:21196,
CC ChEBI:CHEBI:57844, ChEBI:CHEBI:58140, ChEBI:CHEBI:58199,
CC ChEBI:CHEBI:58207; EC=2.1.1.14;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-methionine from L-homocysteine (MetE route): step 1/1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the vitamin-B12 independent methionine synthase
CC family. {ECO:0000305}.
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DR EMBL; U84889; AAB41896.1; -; mRNA.
DR PIR; T12575; T12575.
DR AlphaFoldDB; P93263; -.
DR SMR; P93263; -.
DR PRIDE; P93263; -.
DR UniPathway; UPA00051; UER00082.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003871; F:5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd03311; CIMS_C_terminal_like; 1.
DR Gene3D; 3.20.20.210; -; 2.
DR HAMAP; MF_00172; Meth_synth; 1.
DR InterPro; IPR013215; Cbl-indep_Met_Synth_N.
DR InterPro; IPR006276; Cobalamin-indep_Met_synthase.
DR InterPro; IPR002629; Met_Synth_C/arc.
DR InterPro; IPR038071; UROD/MetE-like_sf.
DR Pfam; PF08267; Meth_synt_1; 1.
DR Pfam; PF01717; Meth_synt_2; 1.
DR PIRSF; PIRSF000382; MeTrfase_B12_ind; 1.
DR SUPFAM; SSF51726; SSF51726; 2.
DR TIGRFAMs; TIGR01371; met_syn_B12ind; 1.
PE 2: Evidence at transcript level;
KW Amino-acid biosynthesis; Cytoplasm; Metal-binding; Methionine biosynthesis;
KW Methyltransferase; Transferase; Zinc.
FT CHAIN 1..765
FT /note="5-methyltetrahydropteroyltriglutamate--homocysteine
FT methyltransferase"
FT /id="PRO_0000098698"
FT ACT_SITE 701
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 18
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 116
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 437..439
FT /ligand="L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:58199"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 437..439
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 490
FT /ligand="L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:58199"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 490
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 495
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 518
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 521..522
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000250|UniProtKB:O50008"
FT BINDING 567
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 605
FT /ligand="L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:58199"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 605
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 647
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O50008"
FT BINDING 649
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O50008"
FT BINDING 658
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O50008"
FT BINDING 662
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O50008"
FT BINDING 671
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 733
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O50008"
SQ SEQUENCE 765 AA; 84822 MW; 8C510684202EA000 CRC64;
MASHIVGYPR MGPKRELKFA LESFWDGKST AEDLKKVSAD LRSSIWKQMA DAGIKYIPSN
TFSYYDQVLD TTAMLGAVPP RYGWTGGEIE FDVYFSMARG NASVPAMEMT KWFDTNYHFI
VPELGPEVNF SYASHKAVLE YKEAKALGVD TVPVLVGPVS YLLLSKQAKG VDKSFDLLSL
LPKILPIYKE VVAELKEAGA SWIQFDEPLL VMDLESHKLQ AFSAAYADLE STLSGLNVVV
ETYFADVTAE AYKTLISLKG VTGYGFDLVR GTKTLDLVKA EFPSGKYLFA GVVDGRNIWA
NDLAASLATL EALEGVVGKD KLVVSTSCSF LHTAVDLINE TKLDDEIKSW LAFAAQKVLE
VNALAKALSG QKDEAFFSAN AAALASRKSS PRVTNEAVQK AATALKGSDH RRATTVSSRL
DAQQKKLNLP ILPTTTIGSF PQTVELRRVR REYKAKKISE EEYVKAIKEE ISKVVKLQEE
LDIDVLVHGE PERNDMVEYF GEQLSGFAFS ANGWVQSYGS RCVKPPIIYG DVSRPNPMTV
FWSSMAQSMT ARPMKGMLTG PVTILNWSFV RNDQPRHETC YQIALAIKNE VEDLEKAGIN
VIQIDEAALR EGLPLRKSEH DFYLKWAVHS FRITNVGVQD TTQIHTHMCY SNFNDIIHSI
IDMDADVITI ENSRSDEKLL SVFREGVKYG AGIGPGVYDI HSPRIPPTEE LADRIRKMLA
VLESNVLWVN PDCGLKTRKY GEVNPALSNM VAAAKQLRQE LASAK
