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METE_VIBVU
ID   METE_VIBVU              Reviewed;         778 AA.
AC   Q8CWK1;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 106.
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=VV1_2219;
OS   Vibrio vulnificus (strain CMCP6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=216895;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CMCP6;
RA   Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT   "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL   Submitted (DEC-2002) 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: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; AE016795; AAO10600.1; -; Genomic_DNA.
DR   RefSeq; WP_011080092.1; NC_004459.3.
DR   AlphaFoldDB; Q8CWK1; -.
DR   SMR; Q8CWK1; -.
DR   EnsemblBacteria; AAO10600; AAO10600; VV1_2219.
DR   KEGG; vvu:VV1_2219; -.
DR   HOGENOM; CLU_013175_0_0_6; -.
DR   OMA; KVMKGML; -.
DR   UniPathway; UPA00051; UER00082.
DR   Proteomes; UP000002275; Chromosome 1.
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; Repeat; Transferase; Zinc.
FT   CHAIN           1..778
FT                   /note="5-methyltetrahydropteroyltriglutamate--homocysteine
FT                   methyltransferase"
FT                   /id="PRO_0000098678"
FT   ACT_SITE        699
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         118
FT                   /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58207"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         436..438
FT                   /ligand="L-homocysteine"
FT                   /ligand_id="ChEBI:CHEBI:58199"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         436..438
FT                   /ligand="L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:57844"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         489
FT                   /ligand="L-homocysteine"
FT                   /ligand_id="ChEBI:CHEBI:58199"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         489
FT                   /ligand="L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:57844"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         520..521
FT                   /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58207"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         566
FT                   /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58207"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         604
FT                   /ligand="L-homocysteine"
FT                   /ligand_id="ChEBI:CHEBI:58199"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         604
FT                   /ligand="L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:57844"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         610
FT                   /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58207"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         646
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         648
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         670
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         731
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
SQ   SEQUENCE   778 AA;  86854 MW;  CE93F61CBF8E1505 CRC64;
     MTTTTHILGY PRIGEKRELK FAQEKYWRGE IDQAELKKVG AELRHKNWQT QASAGLSFAV
     AGDFAWYDHV LTTTLLLGHV PKRHRHGFPD LDTLFRVGRG QSQSSCACHG AAASDMTKWF
     NTNYHYIVPE FSKEDTFEVS WPQLFEEVNE AVQAGHNVKP VLLGPLSYLY LGKEIEDGFD
     RLTLLPRLLT AYQAILAKLA KQGVEWVQID EPILALELEK PWLDAFKLAY QVIRSDVKVL
     LTTYFDSVVD SLDRIVELSV DGLHVDLSAA PEQLDAVLAK LPQNWVLSLG VVNGRNVWRS
     DVKAQLERLQ PVKAALGERL WVASSCSLLH SPVDLELEAG LSAEVRSWFA FAKQKVSEVV
     LLGKALDGDA AAIAQCEAYS QPIQARKSAA HVHKATVQSR VNAITAELAQ RSVPYAERAR
     HQAEVLQLPL LPTTTIGSFP QTSEIRVQRS AYRSGQLSSA EYEQALKGHI ADAVKRQEAL
     DLDVLVHGEA ERNDMVEYFA ENLAGFQTTQ FGWVQSYGSR CVKPAIVVAD IEREQPITVG
     WSTYAQSLTS KQMKGMLTGP VTILCWTFPR EDISRKAIAQ QLALALRDEV SDLQDAGINI
     IQIDEPAIRE GLPLKKRDHQ NYLDWAVEAF RISAASARPE TQIHTHMCYS EFNEIIESVA
     ALDADVITIE TSRSNMELLK AFEEFNYPNE IGPGVYDIHS PNIPSEEWIV DLVKKAAQKI
     PVERLWVNPD CGLKTRNWPE TEAALANLVS AAKRLRKEFA KETTAVNSEA VADVETEA
 
 
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