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METE_PYRHO
ID   METE_PYRHO              Reviewed;         338 AA.
AC   O58816;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 116.
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=PH1089;
OS   Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS   100139 / OT-3).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=70601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX   PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA   Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA   Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA   Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA   Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA   Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT   "Complete sequence and gene organization of the genome of a hyper-
RT   thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL   DNA Res. 5:55-76(1998).
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; BA000001; BAA30188.1; -; Genomic_DNA.
DR   PIR; F71103; F71103.
DR   RefSeq; WP_010885175.1; NC_000961.1.
DR   AlphaFoldDB; O58816; -.
DR   SMR; O58816; -.
DR   STRING; 70601.3257505; -.
DR   DNASU; 1443410; -.
DR   EnsemblBacteria; BAA30188; BAA30188; BAA30188.
DR   GeneID; 1443410; -.
DR   KEGG; pho:PH1089; -.
DR   eggNOG; arCOG01876; Archaea.
DR   OMA; DPDCGMR; -.
DR   OrthoDB; 21172at2157; -.
DR   UniPathway; UPA00051; -.
DR   Proteomes; UP000000752; 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; Transferase; Zinc.
FT   CHAIN           1..338
FT                   /note="Methionine synthase"
FT                   /id="PRO_0000098689"
FT   BINDING         210
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00288"
FT   BINDING         212
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00288"
FT   BINDING         234
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00288"
FT   BINDING         294
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00288"
SQ   SEQUENCE   338 AA;  39411 MW;  9CDBC9BC74DC281E CRC64;
     MELPILPTSV IGSYPKPRWL LRMYRLRDLG KIPEEDFKEA VKDASVSVLR EHERAGVDIP
     WDGEMWRTEM TEHFTAKIGG FKFYGPVRVW GNAYFNKAAA VDKLEYKEPL VLEEFLWVKK
     NTTREVVKIP ITGPYTIAEW SFNEYYPDKE SFIMDLAKII NKELKMLENH GALYIQLDEP
     AMLNHPDEVP LAVEAINKAV KGIKIKVGLH VCYSNYYLLA DYFDEIRVTQ FALEFANRQF
     RDMDFLKKLS NKELGFGVVD VHNPRIESVE EIVKAIKKVF EYVEPELLYI NPDCGMKLLD
     RNIAYNKLVN MVKATELVRK ELEREGKKTT EFRTLKDI
 
 
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