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METE_SYNJB
ID   METE_SYNJB              Reviewed;         754 AA.
AC   Q2JKE8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase {ECO:0000255|HAMAP-Rule:MF_00172};
DE            EC=2.1.1.14 {ECO:0000255|HAMAP-Rule:MF_00172};
DE   AltName: Full=Cobalamin-independent methionine synthase {ECO:0000255|HAMAP-Rule:MF_00172};
DE   AltName: Full=Methionine synthase, vitamin-B12 independent isozyme {ECO:0000255|HAMAP-Rule:MF_00172};
GN   Name=metE {ECO:0000255|HAMAP-Rule:MF_00172}; OrderedLocusNames=CYB_1886;
OS   Synechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium
OS   Yellowstone B-Prime).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=321332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JA-2-3B'a(2-13);
RX   PubMed=18059494; DOI=10.1038/ismej.2007.46;
RA   Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M., Hamamura N.,
RA   Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.;
RT   "Population level functional diversity in a microbial community revealed by
RT   comparative genomic and metagenomic analyses.";
RL   ISME J. 1:703-713(2007).
CC   -!- FUNCTION: Catalyzes the transfer of a methyl group from 5-
CC       methyltetrahydrofolate to homocysteine resulting in methionine
CC       formation. {ECO:0000255|HAMAP-Rule:MF_00172}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00172};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00172};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00172};
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:0000255|HAMAP-Rule:MF_00172}.
CC   -!- SIMILARITY: Belongs to the vitamin-B12 independent methionine synthase
CC       family. {ECO:0000255|HAMAP-Rule:MF_00172}.
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DR   EMBL; CP000240; ABD02841.1; -; Genomic_DNA.
DR   RefSeq; WP_011433481.1; NC_007776.1.
DR   AlphaFoldDB; Q2JKE8; -.
DR   SMR; Q2JKE8; -.
DR   STRING; 321332.CYB_1886; -.
DR   PRIDE; Q2JKE8; -.
DR   KEGG; cyb:CYB_1886; -.
DR   eggNOG; COG0620; Bacteria.
DR   HOGENOM; CLU_013175_0_0_3; -.
DR   OMA; KVMKGML; -.
DR   OrthoDB; 577156at2; -.
DR   UniPathway; UPA00051; UER00082.
DR   Proteomes; UP000001938; Chromosome.
DR   GO; GO:0003871; F:5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   Amino-acid biosynthesis; Metal-binding; Methionine biosynthesis;
KW   Methyltransferase; Reference proteome; Repeat; Transferase; Zinc.
FT   CHAIN           1..754
FT                   /note="5-methyltetrahydropteroyltriglutamate--homocysteine
FT                   methyltransferase"
FT                   /id="PRO_1000017287"
FT   ACT_SITE        684
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         17..20
FT                   /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58207"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         110
FT                   /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58207"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         421..423
FT                   /ligand="L-homocysteine"
FT                   /ligand_id="ChEBI:CHEBI:58199"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         421..423
FT                   /ligand="L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:57844"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         474
FT                   /ligand="L-homocysteine"
FT                   /ligand_id="ChEBI:CHEBI:58199"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         474
FT                   /ligand="L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:57844"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         505..506
FT                   /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58207"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         551
FT                   /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58207"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         589
FT                   /ligand="L-homocysteine"
FT                   /ligand_id="ChEBI:CHEBI:58199"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         589
FT                   /ligand="L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:57844"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         595
FT                   /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58207"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         631
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         633
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         655
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         716
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
SQ   SEQUENCE   754 AA;  84676 MW;  EAD695787C51316B CRC64;
     MTAQTMTLGY ARMGKRRELK KALEGFWSGA LGSEALLATF WDLETQAWQT QLQAGIDHIA
     VGDQTLYDHV LDWATWLGLI PSRFRGLSGL DRYFAMARGR EGLPALEMTK WFDTNYHYLV
     PEIEPEADPS PNFGDFLERV RRAQGILGER TSPVVLSPVT LLCLSQRSGD LRADLEKLLP
     LYRDLLQELK QLGIPEVQIH DPILVTSQGS GLREAVEMSY RQLATAGIPV HLVTYFDDLG
     ETYPWVVQLP VAGISLDFTR GHTLDLVRTY GFPADQILGA GVVDARNVWK VQPETVLASL
     RELQGVAPNL RVQPSASLQF VPHDAALEAQ LPEPLRNVLS FAEQKLAEVA LLARALNGED
     TAAQQAEIQQ QWQSFAQFSP PNPQVRQALA NLKLQDFERF LPYEQRLSRQ VQLPPLPTTT
     IGSFPQTPEV RQWRAKYKRG EVSQAEYEAA IDAEIAKCIR IQEEIGLDVL VHGEFERTDM
     VEYFAQKLEG FAFTEHGWVQ SYGSRCVRPP ILYGDVVRPQ PMTVREFQVA QSHTQKPVKG
     MLTGPVTMLN WSFPRVDIPR REQALQIALA LRAEVADLEA AGAVMVQVDE PALREGLPLK
     KERWPEYLSW AVDAFRLATG GAKPETQIHT HMCYSEFGDI IEHIERLDAD VLSIENSRSN
     NKTLLQIAQA GYRHQVGNGV YDVHSPAVPS VEQILQQLRT GLAHLPVEQT WVNPDCGLKT
     RRWEEVIPAL KNMVAAAHQL GEELLETQPE GLRE
 
 
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