METE_PYRFU
ID METE_PYRFU Reviewed; 338 AA.
AC Q8TH63;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=PF1269;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE009950; AAL81393.1; -; Genomic_DNA.
DR RefSeq; WP_011012413.1; NZ_CP023154.1.
DR AlphaFoldDB; Q8TH63; -.
DR SMR; Q8TH63; -.
DR STRING; 186497.PF1269; -.
DR EnsemblBacteria; AAL81393; AAL81393; PF1269.
DR GeneID; 41713072; -.
DR KEGG; pfu:PF1269; -.
DR PATRIC; fig|186497.12.peg.1331; -.
DR eggNOG; arCOG01876; Archaea.
DR HOGENOM; CLU_040013_3_2_2; -.
DR OMA; DPDCGMR; -.
DR OrthoDB; 21172at2157; -.
DR PhylomeDB; Q8TH63; -.
DR UniPathway; UPA00051; -.
DR Proteomes; UP000001013; 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..338
FT /note="Methionine synthase"
FT /id="PRO_0000098688"
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; 39315 MW; 91B297C589A0507E CRC64;
MELPILPTSV IGSYPKPRWL LRMYKLRELG KIPEEDFKEA VRDASISVLR EHERAGIDIP
WDGEMGRSEM TEYFTSKIKG FKFYGPVRVW GNAYFNKAAA VDKLEYEEPL VLDEFLWVKE
NTTREIVKIP ITGPYTIAEW SFNEYYPDKE SFVMDLAEII NKELKVLEKH GAKFVQLDEP
AMLNHPSEVP LAVDAINRAV KGIKMKVGLH VCYSNYNLLA DYFDEIKVTQ FALEFANRNF
RDMDFLKKLS NKELGFGVVD VHNPRVESVE EIRQAIKKVF TYLEPEWVYI NPDCGLKLLD
RKIAYQKLVN MVQAVRGVRK ELEKEGKTTI EFRTLKDI
