ID   A0A4P6PH65_9BACT        Unreviewed;       755 AA.
AC   A0A4P6PH65;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   29-MAY-2024, entry version 22.
DE   RecName: Full=5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase {ECO:0000256|HAMAP-Rule:MF_00172};
DE            EC=2.1.1.14 {ECO:0000256|HAMAP-Rule:MF_00172};
DE   AltName: Full=Cobalamin-independent methionine synthase {ECO:0000256|HAMAP-Rule:MF_00172};
DE   AltName: Full=Methionine synthase, vitamin-B12 independent isozyme {ECO:0000256|HAMAP-Rule:MF_00172};
GN   Name=metE {ECO:0000256|HAMAP-Rule:MF_00172,
GN   ECO:0000313|EMBL:QBG49077.1};
GN   ORFNames=EGM51_17350 {ECO:0000313|EMBL:QBG49077.1};
OS   Verrucomicrobia bacterium S94.
OC   Bacteria; Verrucomicrobiota.
OX   NCBI_TaxID=2488809 {ECO:0000313|EMBL:QBG49077.1, ECO:0000313|Proteomes:UP000289135};
RN   [1] {ECO:0000313|EMBL:QBG49077.1, ECO:0000313|Proteomes:UP000289135}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S94 {ECO:0000313|EMBL:QBG49077.1,
RC   ECO:0000313|Proteomes:UP000289135};
RA   Baek K.;
RT   "Verrucomicrobia bacterium S94.";
RL   Submitted (NOV-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, ECO:0000256|HAMAP-
CC       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:0000256|HAMAP-
CC         Rule:MF_00172};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00172};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00172};
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, ECO:0000256|HAMAP-Rule:MF_00172}.
CC   -!- SIMILARITY: Belongs to the vitamin-B12 independent methionine synthase
CC       family. {ECO:0000256|ARBA:ARBA00009553, ECO:0000256|HAMAP-
CC       Rule:MF_00172}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP036201; QBG49077.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4P6PH65; -.
DR   KEGG; vbs:EGM51_17350; -.
DR   OrthoDB; 244285at2; -.
DR   UniPathway; UPA00051; UER00082.
DR   Proteomes; UP000289135; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0005576; C:extracellular region; IEA:TreeGrafter.
DR   GO; GO:0003871; F:5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008705; F:methionine synthase activity; IEA:TreeGrafter.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_00172};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00172};
KW   Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167, ECO:0000256|HAMAP-
KW   Rule:MF_00172};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW   Rule:MF_00172}; Reference proteome {ECO:0000313|Proteomes:UP000289135};
KW   Repeat {ECO:0000256|HAMAP-Rule:MF_00172};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00172};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00172}.
FT   DOMAIN          3..307
FT                   /note="Cobalamin-independent methionine synthase MetE N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08267"
FT   DOMAIN          426..747
FT                   /note="Cobalamin-independent methionine synthase MetE C-
FT                   terminal/archaeal"
FT                   /evidence="ECO:0000259|Pfam:PF01717"
FT   ACT_SITE        694
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00172,
FT                   ECO:0000256|PIRSR:PIRSR000382-3"
FT   BINDING         15..18
FT                   /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58207"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00172"
FT   BINDING         18
FT                   /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58207"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000382-1"
FT   BINDING         112
FT                   /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58207"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00172"
FT   BINDING         117
FT                   /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58207"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000382-1"
FT   BINDING         431..433
FT                   /ligand="L-homocysteine"
FT                   /ligand_id="ChEBI:CHEBI:58199"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00172,
FT                   ECO:0000256|PIRSR:PIRSR000382-1"
FT   BINDING         431..433
FT                   /ligand="L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:57844"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00172,
FT                   ECO:0000256|PIRSR:PIRSR000382-1"
FT   BINDING         484
FT                   /ligand="L-homocysteine"
FT                   /ligand_id="ChEBI:CHEBI:58199"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00172"
FT   BINDING         484
FT                   /ligand="L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:57844"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00172,
FT                   ECO:0000256|PIRSR:PIRSR000382-1"
FT   BINDING         515..516
FT                   /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58207"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00172,
FT                   ECO:0000256|PIRSR:PIRSR000382-1"
FT   BINDING         561
FT                   /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58207"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00172,
FT                   ECO:0000256|PIRSR:PIRSR000382-1"
FT   BINDING         599
FT                   /ligand="L-homocysteine"
FT                   /ligand_id="ChEBI:CHEBI:58199"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00172,
FT                   ECO:0000256|PIRSR:PIRSR000382-1"
FT   BINDING         599
FT                   /ligand="L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:57844"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00172,
FT                   ECO:0000256|PIRSR:PIRSR000382-1"
FT   BINDING         605
FT                   /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58207"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00172"
FT   BINDING         641
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00172"
FT   BINDING         641
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         643
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         643
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00172"
FT   BINDING         665
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00172"
FT   BINDING         665
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         726
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00172"
FT   BINDING         726
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   755 AA;  85517 MW;  C853B36E6449CCDA CRC64;
     MKSHILGFPR IGSQRELKFA IEAYWRRACS ESELLLRTEQ IKLQNWTVQQ KAGLDYVCTG
     DFSLYDHVLD VSRMIGAVPA RFQTPGLSEL DIYFNMARGN AEAGIAPMEM TKWFDTNYHY
     IVPEIEADMQ LAYSSDTLVR ETEAALKQGF RPKPVVVGPL TYLALAKAAE GVNKWDALDA
     ITGVYSTLLE KLSGLTDCIQ LDEPILCTDL PTEIRERAEQ TYAVLRSHAR HTRLLLGTYF
     GGLNENLDLT ARLPVDVLHI DLVRAPGQLD DVLTKWPEHK DLSLGLIDGR NIWKADLAEL
     LKQIVKAKPT RHTDQLWIGS SCSLLHTPVS LEPETDLLPE LKAWMAFAVE KCSEVKTLTL
     AAQGCNVNEE LLENKKIISS RKNSPLSLDF EVRKRVEQVD ARMCRRARPF AERKKCQQAR
     LNLPLLPTTT IGSFPQTKEI RNIRKAFRNG DCDQSAYTQA MQQEICSVIQ EQELAGLDVL
     VHGEPERNDM VEYFGQQMNG FCFSQYGWVQ SYGSRCVKPP IIYGDVSRPA PMTLDWIQYA
     QSQTEKPLKG MLTGPVTMLC WSFVRDDLPR AAVCRQIALA IRDEVLDLEK AGIGMIQIDE
     AAFREGLPIR KDEQEEYLNW AVENFRLATS GVRDETQIHT HMCYSEFNTI LQEIAAMDAD
     VISIEASRSD MELLQAFETF HYPNDIGPGV WDIHSPRVPS VTEIRTLIEN ALKVIPKEQL
     WINPDCGLKT RGWPETRQAL RNMVEATTAV RKILQ
//