ID   METE_METTH              Reviewed;         308 AA.
AC   O26869;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Methionine synthase {ECO:0000255|HAMAP-Rule:MF_00288};
DE            EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_00288};
DE   AltName: Full=Homocysteine methyltransferase {ECO:0000255|HAMAP-Rule:MF_00288};
DE   AltName: Full=Methylcobalamin:homocysteine methyltransferase {ECO:0000255|HAMAP-Rule:MF_00288};
GN   Name=metE {ECO:0000255|HAMAP-Rule:MF_00288}; OrderedLocusNames=MTH_775;
OS   Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS   10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=187420;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA   Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA   Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA   Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA   Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA   Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA   Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA   Reeve J.N.;
RT   "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT   functional analysis and comparative genomics.";
RL   J. Bacteriol. 179:7135-7155(1997).
CC   -!- FUNCTION: Catalyzes the transfer of a methyl group to L-homocysteine
CC       resulting in methionine formation. Can use methylcobalamin and
CC       methylcobinamide as methyl donors, but methylcobalamin is not
CC       considered to be the physiological substrate. {ECO:0000255|HAMAP-
CC       Rule:MF_00288}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00288};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00288};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC       pathway. {ECO:0000255|HAMAP-Rule:MF_00288}.
CC   -!- SIMILARITY: Belongs to the archaeal MetE family. {ECO:0000255|HAMAP-
CC       Rule:MF_00288, ECO:0000305}.
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DR   EMBL; AE000666; AAB85278.1; -; Genomic_DNA.
DR   PIR; F69203; F69203.
DR   RefSeq; WP_010876413.1; NC_000916.1.
DR   AlphaFoldDB; O26869; -.
DR   SMR; O26869; -.
DR   STRING; 187420.MTH_775; -.
DR   EnsemblBacteria; AAB85278; AAB85278; MTH_775.
DR   GeneID; 1471183; -.
DR   KEGG; mth:MTH_775; -.
DR   PATRIC; fig|187420.15.peg.763; -.
DR   HOGENOM; CLU_040013_3_2_2; -.
DR   OMA; DPDCGMR; -.
DR   UniPathway; UPA00051; -.
DR   Proteomes; UP000005223; Chromosome.
DR   GO; GO:0003871; F:5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity; IEA:InterPro.
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; -; 1.
DR   HAMAP; MF_00288; MetE; 1.
DR   InterPro; IPR002629; Met_Synth_C/arc.
DR   InterPro; IPR022921; MetE_arc.
DR   InterPro; IPR038071; UROD/MetE-like_sf.
DR   Pfam; PF01717; Meth_synt_2; 1.
DR   SUPFAM; SSF51726; SSF51726; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Metal-binding; Methionine biosynthesis;
KW   Methyltransferase; Reference proteome; Transferase; Zinc.
FT   CHAIN           1..308
FT                   /note="Methionine synthase"
FT                   /id="PRO_0000098685"
FT   BINDING         201
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00288"
FT   BINDING         203
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00288"
FT   BINDING         224
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00288"
FT   BINDING         285
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00288"
SQ   SEQUENCE   308 AA;  33705 MW;  0157F63D21C80F4F CRC64;
     MITTVVGSYP TEPRGPETLG ERLLNFFGSY DRYRPAIEAA VRDQFRAGVD IISDGQVRGD
     MVGHFAAAIG GMKIEDGTSI IYSRITPPAG SIGAADLRYA YRILRGLTDD ESRGVKGIIT
     GPSTMIYASR IEGFYDPQKR DRAVMDMAGV LKIEAKHLQD AGAAMIQIDE PFLSTGIVDM
     KTAGRAIDHI AAGLDIEVSL HVCGDIRNVL SDLLRFKVDV LDLEFAGRPS NLEVLEEKWR
     GDKGVGFGCV DTTTERVESM EEIRNLIKRG ADIVGEENLY IDPDCGMRKL PRKAAFSKLR
     NMVMAAGN