METE_METTM
ID METE_METTM Reviewed; 309 AA.
AC P55299; D9PX16;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 102.
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;
DE AltName: Full=Methylcobalamin:homocysteine methyltransferase;
GN Name=metE {ECO:0000255|HAMAP-Rule:MF_00288};
GN OrderedLocusNames=MTBMA_c11710;
OS Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM
OS 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium
OS thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=79929;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=8617278; DOI=10.1111/j.1432-1033.1996.00294.x;
RA Vaupel M., Dietz H., Linder D., Thauer R.K.;
RT "Primary structure of cyclohydrolase (Mch) from Methanobacterium
RT thermoautotrophicum (strain Marburg) and functional expression of the mch
RT gene in Escherichia coli.";
RL Eur. J. Biochem. 236:294-300(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=20802048; DOI=10.1128/jb.00844-10;
RA Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A., Seedorf H.,
RA Gottschalk G., Thauer R.K.;
RT "Complete genome sequence of Methanothermobacter marburgensis, a
RT methanoarchaeon model organism.";
RL J. Bacteriol. 192:5850-5851(2010).
RN [3]
RP PROTEIN SEQUENCE OF 3-24, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=10469143; DOI=10.1046/j.1432-1327.1999.00559.x;
RA Schroeder I., Thauer R.K.;
RT "Methylcobalamin:homocysteine methyltransferase from Methanobacterium
RT thermoautotrophicum. Identification as the metE gene product.";
RL Eur. J. Biochem. 263:789-796(1999).
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. It was proposed that, in
CC vivo, a so-far-unidentified enzyme catalyzes methyltransfer from 5-
CC methyltetrahydromethanopterin (5-CH3-H4MPT) to a corrinoid protein, and
CC that the MetE gene product catalyzes the further transfer to L-
CC homocysteine. Is not active with L-cysteine, coenzyme M, coenzyme B,
CC glutathione or dithiothreitol as substrate.
CC {ECO:0000269|PubMed:10469143}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q9X112,
CC ECO:0000255|HAMAP-Rule:MF_00288};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9X112,
CC ECO:0000255|HAMAP-Rule:MF_00288};
CC -!- ACTIVITY REGULATION: Is activated by phosphates.
CC {ECO:0000269|PubMed:10469143}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.1 mM for L-homocysteine {ECO:0000269|PubMed:10469143};
CC pH dependence:
CC Optimum pH is 7.0-8.0. {ECO:0000269|PubMed:10469143};
CC Temperature dependence:
CC Optimum temperature is 65 degrees Celsius. At this temperature, the
CC enzyme is rapidly inactivated. {ECO:0000269|PubMed:10469143};
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=CAA63062.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X92082; CAA63062.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP001710; ADL58764.1; -; Genomic_DNA.
DR PIR; S62191; S62191.
DR RefSeq; WP_013295986.1; NC_014408.1.
DR AlphaFoldDB; P55299; -.
DR SMR; P55299; -.
DR STRING; 79929.MTBMA_c11710; -.
DR EnsemblBacteria; ADL58764; ADL58764; MTBMA_c11710.
DR GeneID; 9704879; -.
DR KEGG; mmg:MTBMA_c11710; -.
DR PATRIC; fig|79929.8.peg.1140; -.
DR HOGENOM; CLU_040013_3_2_2; -.
DR OMA; DPDCGMR; -.
DR OrthoDB; 21172at2157; -.
DR BioCyc; MetaCyc:MON-20454; -.
DR UniPathway; UPA00051; -.
DR Proteomes; UP000000345; 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 1: Evidence at protein level;
KW Amino-acid biosynthesis; Direct protein sequencing; Metal-binding;
KW Methionine biosynthesis; Methyltransferase; Transferase; Zinc.
FT CHAIN 1..309
FT /note="Methionine synthase"
FT /id="PRO_0000098686"
FT BINDING 201
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9X112, ECO:0000255|HAMAP-
FT Rule:MF_00288"
FT BINDING 203
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9X112, ECO:0000255|HAMAP-
FT Rule:MF_00288"
FT BINDING 224
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9X112, ECO:0000255|HAMAP-
FT Rule:MF_00288"
FT BINDING 285
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9X112, ECO:0000255|HAMAP-
FT Rule:MF_00288"
FT CONFLICT 100
FT /note="A -> R (in Ref. 1; CAA63062)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 309 AA; 33447 MW; 831541C7F47E3473 CRC64;
MITTVVGSYP ATPREPETLR ERISSFIGSY DACRPAIETA VRDQVRAGVD IISDGQVRGD
MVGHFAEAMG GMMVKDGVSI IFSRITPPAG SIGSDDLIYA IKILRKLTDD ESKGVKGIIT
GPSTMAHASK IEGFYSPQKR ERAIMDMADA LRVEAEHLQD AGALMIQIDE PFLSTGMVDM
GTARRAVKRI SGALDVDVSL HVCGDISGVI GELLTFPVDM LDLEFAGRPS NLEVLAEKWR
GDKKLGFGCV DTSTEVVEST DTIKNLIERG ADIAGEDNLY IDPDCGMRKL PREAAFSKLR
NMVKAASEF
