ID B8LPY2_PICSI Unreviewed; 766 AA.
AC B8LPY2;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 08-NOV-2023, entry version 43.
DE RecName: Full=5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase {ECO:0000256|ARBA:ARBA00012034};
DE EC=2.1.1.14 {ECO:0000256|ARBA:ARBA00012034};
OS Picea sitchensis (Sitka spruce) (Pinus sitchensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Picea.
OX NCBI_TaxID=3332 {ECO:0000313|EMBL:ABR17712.1};
RN [1] {ECO:0000313|EMBL:ABR17712.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Green portion of the leader tissue
RC {ECO:0000313|EMBL:ABR17712.1};
RA Ralph S.G., Chun H.E., Liao N., Ali J., Reid K., Kolosova N., Cooper N.,
RA Cullis C., Jancsik S., Moore R., Mayo M., Wagner S., Holt R.A.,
RA Jones S.J.M., Marra M.A., Ritland C.E., Ritland K., Bohlmann J.;
RT "Full length cDNA sequences from Sitka Spruce (Picea sitchensis).";
RL Submitted (JUN-2007) 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:0000256|ARBA:ARBA00002777}.
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:0000256|ARBA:ARBA00001757};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR000382-2};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|PIRSR:PIRSR000382-
CC 2};
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:0000256|ARBA:ARBA00004681}.
CC -!- SIMILARITY: Belongs to the vitamin-B12 independent methionine synthase
CC family. {ECO:0000256|ARBA:ARBA00009553}.
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DR EMBL; EF677917; ABR17712.1; -; mRNA.
DR AlphaFoldDB; B8LPY2; -.
DR OMA; KVMKGML; -.
DR UniPathway; UPA00051; UER00082.
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 CDD; cd03312; CIMS_N_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 NCBIfam; TIGR01371; met_syn_B12ind; 1.
DR PANTHER; PTHR30519; 5-METHYLTETRAHYDROPTEROYLTRIGLUTAMATE--HOMOCYSTEINE METHYLTRANSFERASE; 1.
DR PANTHER; PTHR30519:SF0; 5-METHYLTETRAHYDROPTEROYLTRIGLUTAMATE--HOMOCYSTEINE METHYLTRANSFERASE; 1.
DR Pfam; PF08267; Meth_synt_1; 1.
DR Pfam; PF01717; Meth_synt_2; 1.
DR PIRSF; PIRSF000382; MeTrfase_B12_ind; 1.
DR SUPFAM; SSF51726; UROD/MetE-like; 2.
PE 2: Evidence at transcript level;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000382-2};
KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR000382-2}.
FT DOMAIN 3..317
FT /note="Cobalamin-independent methionine synthase MetE N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08267"
FT DOMAIN 433..756
FT /note="Cobalamin-independent methionine synthase MetE C-
FT terminal/archaeal"
FT /evidence="ECO:0000259|Pfam:PF01717"
FT ACT_SITE 702
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000382-3"
FT BINDING 18
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000256|PIRSR:PIRSR000382-1"
FT BINDING 116
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000256|PIRSR:PIRSR000382-1"
FT BINDING 438..440
FT /ligand="L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:58199"
FT /evidence="ECO:0000256|PIRSR:PIRSR000382-1"
FT BINDING 438..440
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000256|PIRSR:PIRSR000382-1"
FT BINDING 491
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000256|PIRSR:PIRSR000382-1"
FT BINDING 522..523
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000256|PIRSR:PIRSR000382-1"
FT BINDING 568
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000256|PIRSR:PIRSR000382-1"
FT BINDING 606
FT /ligand="L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:58199"
FT /evidence="ECO:0000256|PIRSR:PIRSR000382-1"
FT BINDING 606
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000256|PIRSR:PIRSR000382-1"
FT BINDING 648
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR000382-2"
FT BINDING 650
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR000382-2"
FT BINDING 659
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR000382-2"
FT BINDING 663
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR000382-2"
FT BINDING 672
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR000382-2"
FT BINDING 734
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR000382-2"
SQ SEQUENCE 766 AA; 84352 MW; B14DDFD1821B4277 CRC64;
MASHVVGYPR MGPKRELKFA LESFWDGKSS AADLEAVAKG LRASIWKQMV AAGVKLIPSN
TFSFYDQVLD TTAMLGAVPP RYSFAGGEIG FDTYFSMARG NATLPAMEMT KWFDTNYHYI
VPELGPEIKF AYSSHKAVAE YKEAKELGID TVPVIVGPVS YLLLSKPAKG VAKTFNLLSL
LDAILPIYKQ VVSELEAAGA TFVQFDEPSL VMDLEAHQLE AFSKAYSYLD AASLGVNLLV
ETYFADIPVE TYKTITGLKG ISAIGFDFIR GSKTLGLIKE AGFPADKVLF AGVVDGRNIW
ANDLADSLSV LESLENIVGK DKLVVSTSCS LLHTAVDLVN ETKLDSEIKS WLAFAAQKLI
EVDALAKALA GQKDEAFFAA NAAALASRRA SPRVTNEAVQ KAAAALKTSD HRRVTPVNVR
LEQQQKKLNL PILPTTTIGS FPQTVELRRV RREYKINKIS EDEYVSSIKE EIAKVVKLQE
DLDIDVLVHG EPERNDMVEY FGEQLQGFAF TVNGWVQSYG SRCVKPPVIY GDVSRPKPMT
VFWSKVAQSM TARPMKGMLT GPVTILNWSF VRNDQPRSET CMQIALAIKD EVEDLEAGGI
QVIQIDEAAL REGLPLRKAE HAYYLDWAVH GFRITNSGVQ DTTQIHTHMC YSNFNDIIHS
IIDMDADVIT IENSRSDEKL LSVFREGVKY GAGIGPGVYD IHSPRIPSTE EIADRISKML
AVLETNILWV NPDCGLKTRK YPEVVPALTN MVAAAKLLRA QLASAK
//
