METE_KALTU
ID METE_KALTU Reviewed; 757 AA.
AC C1KEU0;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase {ECO:0000250|UniProtKB:O50008};
DE EC=2.1.1.14 {ECO:0000250|UniProtKB:O50008};
DE AltName: Full=Cobalamin-independent methionine synthase {ECO:0000303|PubMed:20238167};
DE AltName: Full=Pollen allergen Sal k 3 {ECO:0000303|PubMed:20238167};
DE AltName: Full=SkMetE {ECO:0000303|PubMed:20238167};
DE AltName: Full=Vitamin-B12-independent methionine synthase {ECO:0000305};
DE AltName: Allergen=Sal k 3.0101 {ECO:0000305};
DE Flags: Fragment;
OS Kali turgidum (Prickly saltwort) (Salsola kali).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Salsoloideae; Salsoleae; Kali.
OX NCBI_TaxID=151250 {ECO:0000312|EMBL:ACO34814.1};
RN [1] {ECO:0000312|EMBL:ACO34814.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, IDENTIFICATION BY MASS
RP SPECTROMETRY, ALLERGEN, AND 3D-STRUCTURE MODELING.
RC TISSUE=Pollen {ECO:0000303|PubMed:20238167};
RX PubMed=20238167; DOI=10.1007/s11033-010-0078-2;
RA Assarehzadegan M.A., Sankian M., Jabbari F., Tehrani M., Falak R.,
RA Varasteh A.;
RT "Identification of methionine synthase (Sal k 3), as a novel allergen of
RT Salsola kali pollen.";
RL Mol. Biol. Rep. 38:65-73(2011).
CC -!- FUNCTION: Catalyzes the transfer of a methyl group from 5-
CC methyltetrahydrofolate to homocysteine resulting in methionine
CC formation. {ECO:0000250|UniProtKB:O50008}.
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 Evidence={ECO:0000250|UniProtKB:O50008};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:O50008};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:O50008};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-methionine from L-homocysteine (MetE route): step 1/1.
CC {ECO:0000250|UniProtKB:O50008}.
CC -!- TISSUE SPECIFICITY: Expressed in pollen (at protein level).
CC {ECO:0000269|PubMed:20238167}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE in
CC patients allergic to the pollen of prickly saltwort. Both the
CC recombinant 45 kDa N-terminal fragment and the 39 kDa C-terminal
CC fragment of this protein bind to IgE in 67% of the 12 prickly saltwort
CC pollen-allergic patients tested. The same patients have also a positive
CC skin prick test (SPT) response toward these fragments.
CC {ECO:0000269|PubMed:20238167}.
CC -!- SIMILARITY: Belongs to the vitamin-B12 independent methionine synthase
CC family. {ECO:0000305}.
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DR EMBL; FJ821454; ACO34814.1; -; mRNA.
DR SMR; C1KEU0; -.
DR Allergome; 8167; Sal k 3.
DR Allergome; 8177; Sal k 3.0101.
DR UniPathway; UPA00051; UER00082.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0003871; F:5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008705; F:methionine synthase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0009086; P:methionine biosynthetic process; ISS:UniProtKB.
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 1: Evidence at protein level;
KW Allergen; Amino-acid biosynthesis; Metal-binding; Methionine biosynthesis;
KW Methyltransferase; Transferase; Zinc.
FT CHAIN 1..>757
FT /note="5-methyltetrahydropteroyltriglutamate--homocysteine
FT methyltransferase"
FT /id="PRO_0000455335"
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:O50008"
FT BINDING 116
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000250|UniProtKB:O50008"
FT BINDING 437..439
FT /ligand="L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:58199"
FT /evidence="ECO:0000250|UniProtKB:O50008"
FT BINDING 437..439
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000250|UniProtKB:O50008"
FT BINDING 490
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000250|UniProtKB:O50008"
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:O50008"
FT BINDING 605
FT /ligand="L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:58199"
FT /evidence="ECO:0000250|UniProtKB:O50008"
FT BINDING 605
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000250|UniProtKB:O50008"
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"
FT NON_TER 757
FT /evidence="ECO:0000312|EMBL:ACO34814.1"
SQ SEQUENCE 757 AA; 83563 MW; C4CB952950BBC2A1 CRC64;
MASHVVGYPR MGPKRELKFA LESFWDGKSS AEDLKKVAAD LRSSIWKQMA DAGIKYIPSN
TFAYYDQVLD TTAMLGAVPA RYGFNGGEIG FDLYFSMARG NASLPAMEMT KWFDTNYHYI
VPELGPEVKF AYSSHKAVDE YKEAKALGVD TVPVLVGPVS YLLLSKAAKG VEKSFPLLSL
LPKILPVYKE VIAELKAAGA STIQFDEPTL VMDLESHQLK AFTDAYADLE STLSGLNVLV
ETYFADLTPE AYKTLVSLNG VTAFGFDLVR GTKTLDLIKS GFPSGKYLFA GVVDGRNIWA
NDLAASLATL QSLESIVGKD KLVVSTSCSL LHTAVDLVNE TKLDDEIKSW LAFAAQKVLE
VNALAKALAG QKDEAFFSAN AAALASRKSS PRVTNEAVQK AAAGLKGSDH RRATTVSARL
DAQQKKLNLP VLPTTTIGSF PQTVELRRVR REYKAKKISE EEYVKAIKEE ISKVVKLQEE
LDIDVLVHGE PERNDMVEYF GEQLSGFAFT VNGWVQSYGS RCVKPPIIYG DVSRPKAMTV
FWSSLAQSMT SRPMKGMLTG PVTILNWSFV RNDQPRHETC YQIALAIEDE AEDLEKAGIN
VIQIDEAALR EGLPLRKSGH GFYLQWAVHS FRITNVGIQD TTQIHTHMCY SNFNDIIHSI
IDMDADVITI ENSRSDEKLL SVFREGVKYG AGIGPGVYDI HSPRIPPTEE LADRIRKMLA
VLESNVLWVN PDCGLKTRKY NEVNPALSNM VYAAKPI
