ID   METE_AERPE              Reviewed;         332 AA.
AC   Q9YA91;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 105.
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};
GN   Name=metE {ECO:0000255|HAMAP-Rule:MF_00288}; OrderedLocusNames=APE_2048;
OS   Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS   K1).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Aeropyrum.
OX   NCBI_TaxID=272557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX   PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA   Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA   Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA   Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT   "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT   Aeropyrum pernix K1.";
RL   DNA Res. 6:83-101(1999).
CC   -!- FUNCTION: Catalyzes the transfer of a methyl group to L-homocysteine
CC       resulting in methionine formation. The physiological methyl donor is
CC       unknown. {ECO:0000255|HAMAP-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; BA000002; BAA81058.1; -; Genomic_DNA.
DR   PIR; B72509; B72509.
DR   AlphaFoldDB; Q9YA91; -.
DR   SMR; Q9YA91; -.
DR   STRING; 272557.APE_2048; -.
DR   EnsemblBacteria; BAA81058; BAA81058; APE_2048.
DR   KEGG; ape:APE_2048; -.
DR   PATRIC; fig|272557.25.peg.1360; -.
DR   eggNOG; arCOG01876; Archaea.
DR   OMA; DPDCGMR; -.
DR   UniPathway; UPA00051; -.
DR   Proteomes; UP000002518; 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..332
FT                   /note="Methionine synthase"
FT                   /id="PRO_0000098683"
FT   BINDING         217
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00288"
FT   BINDING         219
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00288"
FT   BINDING         241
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00288"
FT   BINDING         304
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00288"
SQ   SEQUENCE   332 AA;  38631 MW;  C5F75DEC444F7859 CRC64;
     MSHSYSVPKK FPTTVVGSYP KIGPASEAIK KRRAGEISEE EFHRIARESI RMVVEDYIWA
     GVDIISDGEQ TREDMVVYFA ERLEGYREGD WVRVFDNVYF RKPIVAGRVR WVRPMIIEDW
     EYARSISAGR PVKFIITGPY TMLEWSFDLH YGDRRELIFD LARAIRREID EALARGAEYI
     QVDEPALSTR PFKEEAELLK EALDIIFKGV GAKRIVHICY GELERILPYI LDYPVDQFDL
     EMKNSNFRLL PYLKEYGYDK EIGYGVIDVH SFQVESVGEV KEAIDRLMKM DIVGPEKVYV
     DPDCGLKRLP RDVARAKLKN MVEAARLARE EW