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Database: UniProt
Entry: A0A0B2SP06_GLYSO
LinkDB: A0A0B2SP06_GLYSO
Original site: A0A0B2SP06_GLYSO 
ID   A0A0B2SP06_GLYSO        Unreviewed;       803 AA.
AC   A0A0B2SP06;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase {ECO:0000256|ARBA:ARBA00012034};
DE            EC=2.1.1.14 {ECO:0000256|ARBA:ARBA00012034};
GN   ORFNames=D0Y65_035534 {ECO:0000313|EMBL:RZB70595.1}, glysoja_045875
GN   {ECO:0000313|EMBL:KHN46660.1};
OS   Glycine soja (Wild soybean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3848 {ECO:0000313|EMBL:KHN46660.1};
RN   [1] {ECO:0000313|EMBL:KHN46660.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Root {ECO:0000313|EMBL:KHN46660.1};
RA   Lam H.-M., Qi X., Li M.-W., Liu X., Xie M., Ni M., Xu X.;
RT   "Identification of a novel salt tolerance gene in wild soybean by whole-
RT   genome sequencing.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:RZB70595.1, ECO:0000313|Proteomes:UP000289340}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. W05 {ECO:0000313|Proteomes:UP000289340};
RC   TISSUE=Hypocotyl of etiolated seedlings {ECO:0000313|EMBL:RZB70595.1};
RA   Xie M., Chung C.Y.L., Li M.-W., Wong F.-L., Chan T.-F., Lam H.-M.;
RT   "A high-quality reference genome of wild soybean provides a powerful tool
RT   to mine soybean genomes.";
RL   Submitted (SEP-2018) 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; KN640992; KHN46660.1; -; Genomic_DNA.
DR   EMBL; QZWG01000013; RZB70595.1; -; Genomic_DNA.
DR   OrthoDB; 1326895at2759; -.
DR   UniPathway; UPA00051; UER00082.
DR   Proteomes; UP000289340; Chromosome 13.
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:SF25; 5-METHYLTETRAHYDROPTEROYLTRIGLUTAMATE--HOMOCYSTEINE METHYLTRANSFERASE 3, CHLOROPLASTIC; 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   3: Inferred from homology;
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   ECO:0000313|EMBL:KHN46660.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000289340};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KHN46660.1};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR000382-2}.
FT   DOMAIN          41..353
FT                   /note="Cobalamin-independent methionine synthase MetE N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08267"
FT   DOMAIN          470..793
FT                   /note="Cobalamin-independent methionine synthase MetE C-
FT                   terminal/archaeal"
FT                   /evidence="ECO:0000259|Pfam:PF01717"
FT   ACT_SITE        739
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000382-3"
FT   BINDING         56
FT                   /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58207"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000382-1"
FT   BINDING         154
FT                   /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58207"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000382-1"
FT   BINDING         475..477
FT                   /ligand="L-homocysteine"
FT                   /ligand_id="ChEBI:CHEBI:58199"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000382-1"
FT   BINDING         475..477
FT                   /ligand="L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:57844"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000382-1"
FT   BINDING         528
FT                   /ligand="L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:57844"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000382-1"
FT   BINDING         559..560
FT                   /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58207"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000382-1"
FT   BINDING         605
FT                   /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58207"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000382-1"
FT   BINDING         643
FT                   /ligand="L-homocysteine"
FT                   /ligand_id="ChEBI:CHEBI:58199"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000382-1"
FT   BINDING         643
FT                   /ligand="L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:57844"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000382-1"
FT   BINDING         685
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         687
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         696
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         700
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         709
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         771
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   803 AA;  89070 MW;  68CA74EB29C87727 CRC64;
     MYKLSSIQCV APFTFSLCTL SFSSYSLRFS VRATSSRAMA SHIVGYPRMG PKRELKFALE
     SFWDGKSSAE ELQKVAADLR SAIWKQMADA GIKYIPSNTF SLYDQVLDTT AMLGAVPSRY
     NWNGGEIGFD VYFSMARGNA SVPAMEMTKW FDTNYHYIVP ELGPDVKFSY ASHKAVDEFK
     EAKVLGVNTV PVLVGPVSYL LLSKPAKGVE KSFSLLSLID KILPVYREVV AELKAAGATW
     IQFDEPTLVK DLNTHQLQAF THAYAELESS LSGFNVLIET YFADVPAEAY KTLTSLKAVT
     AYGFDIVRGT KTLDLIKQGF PSGKFLFAGV VDGRNIWANS LASSLNTLQA LGDIVGNDKV
     VVSTSCSLLH TAVDLVNETK LDQEIKSWLA FAAQKVVEVN ALAKALSGQK DEVFFSANAA
     ALDSRKSSPR VTNEAVQKAA AALKGSDHRR ATNVSARLDS QQKKLNLPVL PTTTIGSFPQ
     TADLRRVRRE FKANKISEED YIHFIKEEIN NVVKLQEELD IDVLVHGEPE RNDMVEYFGE
     QLSGFAFTAN GWVQSYGSRC VKPPIIYGDV SRPKPMTVFW SSTAQSLTKR PMKGMLTGPV
     TILNWSFVRD DQPRFETCYQ IALAIKDEVE DLEKAGITVI QIDEAALREG LPLRKSEEAF
     YLNWAVHSFR ITNCGVEDTT QIHTHMCYSN FNDIIHSIID MDADVITIEN SRSDEKLLSV
     FREGVKYGAG IGPGIYDIHS PRIPPTEEIA DRINKMLAVL ESNILWVNPD CGLKTRKYTE
     VKPALTNMVA AAKLIRNQLA SAK
//
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