METE_METJA
ID METE_METJA Reviewed; 308 AA.
AC Q58868;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
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=MJ1473;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB99479.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L77117; AAB99479.1; ALT_INIT; Genomic_DNA.
DR PIR; H64483; H64483.
DR RefSeq; WP_064496838.1; NC_000909.1.
DR AlphaFoldDB; Q58868; -.
DR SMR; Q58868; -.
DR STRING; 243232.MJ_1473; -.
DR EnsemblBacteria; AAB99479; AAB99479; MJ_1473.
DR GeneID; 1452378; -.
DR KEGG; mja:MJ_1473; -.
DR eggNOG; arCOG01876; Archaea.
DR HOGENOM; CLU_040013_3_2_2; -.
DR InParanoid; Q58868; -.
DR OMA; DPDCGMR; -.
DR OrthoDB; 21172at2157; -.
DR PhylomeDB; Q58868; -.
DR UniPathway; UPA00051; -.
DR Proteomes; UP000000805; 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_0000098684"
FT BINDING 192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00288"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00288"
FT BINDING 215
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00288"
FT BINDING 282
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; 34724 MW; 6032FD5C97E2565D CRC64;
MITTVVGSYP VVKKEETFLD KVKKVFGLYD EYKYAIERAV KDQVKAGVNI ISDGQVRGDM
VEIFTNNMYG FDGKRVVGRV EFIKPITLKD ILYAKSIAKK LNPNVEIKGI ITGPCTIASS
VRVESCYSDN RDENLIYDIA KALRKEVEAL KKHVPIIQID EPILSTGMYD FDVARKAIDI
IVDGLNIKFA MHVCGNVYNI IDELNKFNVD ILDHEFASNK KNLVILESME KKVGFGCVNT
KVKKVESVEE IKSLIEEGIE ILKNNEKLNK NLSDNILIDP DCGMRLLPID VAFNKLKNMV
EATKLIKI
