METE_THEMA
ID METE_THEMA Reviewed; 734 AA.
AC Q9X112;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase {ECO:0000255|HAMAP-Rule:MF_00172};
DE EC=2.1.1.14 {ECO:0000255|HAMAP-Rule:MF_00172};
DE AltName: Full=Cobalamin-independent methionine synthase {ECO:0000255|HAMAP-Rule:MF_00172, ECO:0000303|PubMed:15630480, ECO:0000303|PubMed:18296644};
DE AltName: Full=Methionine synthase, vitamin-B12 independent isozyme {ECO:0000255|HAMAP-Rule:MF_00172};
GN Name=metE {ECO:0000255|HAMAP-Rule:MF_00172, ECO:0000303|PubMed:15630480,
GN ECO:0000303|PubMed:18296644}; OrderedLocusNames=TM_1286;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2] {ECO:0007744|PDB:1T7L, ECO:0007744|PDB:1XDJ, ECO:0007744|PDB:1XPG, ECO:0007744|PDB:1XR2}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-734 AND IN COMPLEXES WITH
RP 5-METHYLTETRAHYDROFOLATE; L-HOMOCYSTEINE AND ZINC, AND COFACTOR.
RX PubMed=15630480; DOI=10.1371/journal.pbio.0030031;
RA Pejchal R., Ludwig M.L.;
RT "Cobalamin-independent methionine synthase (MetE): a face-to-face double
RT barrel that evolved by gene duplication.";
RL PLoS Biol. 3:e31-e31(2005).
RN [3] {ECO:0007744|PDB:3BQ5, ECO:0007744|PDB:3BQ6}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-734 IN COMPLEXES WITH
RP L-HOMOCYSTEINE AND ZINC, COFACTOR, AND REACTION MECHANISM.
RX PubMed=18296644; DOI=10.1073/pnas.0709960105;
RA Koutmos M., Pejchal R., Bomer T.M., Matthews R.G., Smith J.L., Ludwig M.L.;
RT "Metal active site elasticity linked to activation of homocysteine in
RT methionine synthases.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:3286-3291(2008).
CC -!- FUNCTION: Catalyzes the transfer of a methyl group from 5-
CC methyltetrahydrofolate to homocysteine resulting in methionine
CC formation. {ECO:0000255|HAMAP-Rule:MF_00172}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = L-
CC methionine + tetrahydropteroyltri-L-glutamate; Xref=Rhea:RHEA:21196,
CC ChEBI:CHEBI:57844, ChEBI:CHEBI:58140, ChEBI:CHEBI:58199,
CC ChEBI:CHEBI:58207; EC=2.1.1.14; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00172};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00172,
CC ECO:0000269|PubMed:15630480, ECO:0000269|PubMed:18296644};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00172,
CC ECO:0000269|PubMed:15630480, ECO:0000269|PubMed:18296644};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-methionine from L-homocysteine (MetE route): step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_00172}.
CC -!- SIMILARITY: Belongs to the vitamin-B12 independent methionine synthase
CC family. {ECO:0000255|HAMAP-Rule:MF_00172, ECO:0000305}.
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DR EMBL; AE000512; AAD36360.1; -; Genomic_DNA.
DR PIR; E72271; E72271.
DR RefSeq; NP_229090.1; NC_000853.1.
DR RefSeq; WP_004079949.1; NZ_CP011107.1.
DR PDB; 1T7L; X-ray; 2.00 A; A/B=2-734.
DR PDB; 1XDJ; X-ray; 2.20 A; A/B=2-734.
DR PDB; 1XPG; X-ray; 2.59 A; A/B=2-732.
DR PDB; 1XR2; X-ray; 2.35 A; A/B=2-734.
DR PDB; 3BQ5; X-ray; 2.00 A; A/B=2-734.
DR PDB; 3BQ6; X-ray; 2.10 A; A/B=2-734.
DR PDBsum; 1T7L; -.
DR PDBsum; 1XDJ; -.
DR PDBsum; 1XPG; -.
DR PDBsum; 1XR2; -.
DR PDBsum; 3BQ5; -.
DR PDBsum; 3BQ6; -.
DR AlphaFoldDB; Q9X112; -.
DR SMR; Q9X112; -.
DR STRING; 243274.THEMA_07905; -.
DR DrugBank; DB04481; Erythritol.
DR DrugBank; DB04422; Homocysteine.
DR DNASU; 898197; -.
DR EnsemblBacteria; AAD36360; AAD36360; TM_1286.
DR KEGG; tma:TM1286; -.
DR eggNOG; COG0620; Bacteria.
DR InParanoid; Q9X112; -.
DR OMA; KVMKGML; -.
DR OrthoDB; 577156at2; -.
DR BRENDA; 2.1.1.14; 6331.
DR UniPathway; UPA00051; UER00082.
DR EvolutionaryTrace; Q9X112; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0003871; F:5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0071266; P:'de novo' L-methionine biosynthetic process; ISS:UniProtKB.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd03311; CIMS_C_terminal_like; 1.
DR Gene3D; 3.20.20.210; -; 2.
DR HAMAP; MF_00172; Meth_synth; 1.
DR InterPro; IPR013215; Cbl-indep_Met_Synth_N.
DR InterPro; IPR006276; Cobalamin-indep_Met_synthase.
DR InterPro; IPR002629; Met_Synth_C/arc.
DR InterPro; IPR038071; UROD/MetE-like_sf.
DR Pfam; PF08267; Meth_synt_1; 1.
DR Pfam; PF01717; Meth_synt_2; 1.
DR PIRSF; PIRSF000382; MeTrfase_B12_ind; 1.
DR SUPFAM; SSF51726; SSF51726; 2.
DR TIGRFAMs; TIGR01371; met_syn_B12ind; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Metal-binding;
KW Methionine biosynthesis; Methyltransferase; Reference proteome; Repeat;
KW Transferase; Zinc.
FT CHAIN 1..734
FT /note="5-methyltetrahydropteroyltriglutamate--homocysteine
FT methyltransferase"
FT /id="PRO_0000098674"
FT ACT_SITE 672
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 15..18
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000269|PubMed:15630480,
FT ECO:0007744|PDB:1XPG, ECO:0007744|PDB:1XR2"
FT BINDING 104
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000269|PubMed:15630480,
FT ECO:0007744|PDB:1XPG, ECO:0007744|PDB:1XR2"
FT BINDING 409..411
FT /ligand="L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:58199"
FT /evidence="ECO:0000269|PubMed:15630480,
FT ECO:0000269|PubMed:18296644, ECO:0007744|PDB:1XDJ,
FT ECO:0007744|PDB:3BQ6"
FT BINDING 409..411
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 462
FT /ligand="L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:58199"
FT /evidence="ECO:0000269|PubMed:15630480,
FT ECO:0000269|PubMed:18296644, ECO:0007744|PDB:1XDJ,
FT ECO:0007744|PDB:3BQ6"
FT BINDING 462
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 493..494
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000269|PubMed:15630480,
FT ECO:0007744|PDB:1XR2"
FT BINDING 539
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000269|PubMed:15630480,
FT ECO:0007744|PDB:1XPG, ECO:0007744|PDB:1XR2"
FT BINDING 577
FT /ligand="L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:58199"
FT /evidence="ECO:0000269|PubMed:15630480,
FT ECO:0000269|PubMed:18296644, ECO:0007744|PDB:1XDJ,
FT ECO:0007744|PDB:3BQ6"
FT BINDING 577
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 583
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000269|PubMed:15630480,
FT ECO:0007744|PDB:1XPG, ECO:0007744|PDB:1XR2"
FT BINDING 618
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:15630480,
FT ECO:0000269|PubMed:18296644, ECO:0007744|PDB:1XDJ,
FT ECO:0007744|PDB:1XPG, ECO:0007744|PDB:3BQ5,
FT ECO:0007744|PDB:3BQ6"
FT BINDING 620
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:15630480,
FT ECO:0000269|PubMed:18296644, ECO:0007744|PDB:1XDJ,
FT ECO:0007744|PDB:1XPG, ECO:0007744|PDB:3BQ5,
FT ECO:0007744|PDB:3BQ6"
FT BINDING 642
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:15630480,
FT ECO:0000269|PubMed:18296644, ECO:0007744|PDB:1XDJ,
FT ECO:0007744|PDB:1XPG, ECO:0007744|PDB:3BQ6"
FT BINDING 704
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:15630480,
FT ECO:0000269|PubMed:18296644, ECO:0007744|PDB:1XDJ,
FT ECO:0007744|PDB:1XPG, ECO:0007744|PDB:3BQ5,
FT ECO:0007744|PDB:3BQ6"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:3BQ5"
FT HELIX 16..25
FT /evidence="ECO:0007829|PDB:1T7L"
FT HELIX 31..52
FT /evidence="ECO:0007829|PDB:1T7L"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:1T7L"
FT HELIX 66..73
FT /evidence="ECO:0007829|PDB:1T7L"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:1T7L"
FT HELIX 87..94
FT /evidence="ECO:0007829|PDB:1T7L"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:1T7L"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:1T7L"
FT HELIX 128..137
FT /evidence="ECO:0007829|PDB:1T7L"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:1T7L"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:1T7L"
FT HELIX 150..155
FT /evidence="ECO:0007829|PDB:1T7L"
FT HELIX 167..190
FT /evidence="ECO:0007829|PDB:1T7L"
FT STRAND 196..199
FT /evidence="ECO:0007829|PDB:1T7L"
FT HELIX 201..204
FT /evidence="ECO:0007829|PDB:1T7L"
FT HELIX 209..220
FT /evidence="ECO:0007829|PDB:1T7L"
FT TURN 221..224
FT /evidence="ECO:0007829|PDB:1T7L"
FT STRAND 227..230
FT /evidence="ECO:0007829|PDB:1T7L"
FT HELIX 239..243
FT /evidence="ECO:0007829|PDB:1T7L"
FT STRAND 248..253
FT /evidence="ECO:0007829|PDB:1T7L"
FT HELIX 259..267
FT /evidence="ECO:0007829|PDB:1T7L"
FT STRAND 273..280
FT /evidence="ECO:0007829|PDB:1T7L"
FT HELIX 290..300
FT /evidence="ECO:0007829|PDB:1T7L"
FT STRAND 303..309
FT /evidence="ECO:0007829|PDB:1T7L"
FT HELIX 311..313
FT /evidence="ECO:0007829|PDB:1T7L"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:1T7L"
FT TURN 326..328
FT /evidence="ECO:0007829|PDB:1T7L"
FT HELIX 329..331
FT /evidence="ECO:0007829|PDB:1T7L"
FT HELIX 335..349
FT /evidence="ECO:0007829|PDB:1T7L"
FT TURN 362..365
FT /evidence="ECO:0007829|PDB:1T7L"
FT HELIX 368..375
FT /evidence="ECO:0007829|PDB:1T7L"
FT HELIX 379..381
FT /evidence="ECO:0007829|PDB:1T7L"
FT HELIX 388..399
FT /evidence="ECO:0007829|PDB:1T7L"
FT HELIX 416..426
FT /evidence="ECO:0007829|PDB:1T7L"
FT HELIX 432..453
FT /evidence="ECO:0007829|PDB:1T7L"
FT STRAND 456..458
FT /evidence="ECO:0007829|PDB:1T7L"
FT HELIX 468..473
FT /evidence="ECO:0007829|PDB:1T7L"
FT STRAND 476..480
FT /evidence="ECO:0007829|PDB:1T7L"
FT STRAND 487..490
FT /evidence="ECO:0007829|PDB:1T7L"
FT STRAND 493..495
FT /evidence="ECO:0007829|PDB:1T7L"
FT STRAND 499..505
FT /evidence="ECO:0007829|PDB:1T7L"
FT HELIX 512..520
FT /evidence="ECO:0007829|PDB:1T7L"
FT STRAND 526..531
FT /evidence="ECO:0007829|PDB:1T7L"
FT HELIX 533..538
FT /evidence="ECO:0007829|PDB:1T7L"
FT STRAND 540..542
FT /evidence="ECO:0007829|PDB:1T7L"
FT STRAND 544..546
FT /evidence="ECO:0007829|PDB:1T7L"
FT HELIX 548..568
FT /evidence="ECO:0007829|PDB:1T7L"
FT STRAND 573..577
FT /evidence="ECO:0007829|PDB:1T7L"
FT HELIX 580..583
FT /evidence="ECO:0007829|PDB:1T7L"
FT HELIX 589..591
FT /evidence="ECO:0007829|PDB:1T7L"
FT HELIX 592..606
FT /evidence="ECO:0007829|PDB:1T7L"
FT STRAND 613..618
FT /evidence="ECO:0007829|PDB:1T7L"
FT TURN 625..627
FT /evidence="ECO:0007829|PDB:1T7L"
FT HELIX 628..631
FT /evidence="ECO:0007829|PDB:1T7L"
FT STRAND 637..642
FT /evidence="ECO:0007829|PDB:1T7L"
FT TURN 644..648
FT /evidence="ECO:0007829|PDB:1T7L"
FT HELIX 649..651
FT /evidence="ECO:0007829|PDB:1T7L"
FT HELIX 652..655
FT /evidence="ECO:0007829|PDB:1T7L"
FT STRAND 662..667
FT /evidence="ECO:0007829|PDB:1T7L"
FT STRAND 673..675
FT /evidence="ECO:0007829|PDB:1XPG"
FT HELIX 679..689
FT /evidence="ECO:0007829|PDB:1T7L"
FT TURN 690..692
FT /evidence="ECO:0007829|PDB:1T7L"
FT HELIX 695..697
FT /evidence="ECO:0007829|PDB:1T7L"
FT STRAND 698..701
FT /evidence="ECO:0007829|PDB:1T7L"
FT HELIX 711..731
FT /evidence="ECO:0007829|PDB:1T7L"
SQ SEQUENCE 734 AA; 85571 MW; 34B19187480D443B CRC64;
MKAYAFGFPK IGEKREFKKA LEDFWKGKIT EEQFEEEMNK LRMYMVENYR KNVDVIPSNE
LSYYDFVLDT AVMVGAVPER FGEYRGLSTY FDMARGGKAL EMTKFFNTNY HYLVPEIETE
EFYLLENKPL EDYLFFKSKG IETAPWVIGP FTFLYLSKRN GEWIRRPNQM EKLLESLVSV
YKEVFEKLVE NGCKEILVNE PAFVCDLEKA HWDLILNVYR ELSEFPLTVF TYYDSVSDYE
ACVSLPVKRL HFDFVSNEEN LKNLEKHGFP EDKKLVAGVI NGRQPWKVDL RKVASLVEKL
GASAISNSCP LFHLPVTLEL ENNLPGGLKE KLAFAKEKLE ELKMLKDFLE GKTFDLPNVS
FEDFAVDLQA VERVRNLPED SFRREKEYTE RDRIQRERLN LPLFPTTTIG SFPQTPEVRK
MRSKYRKGEI SKEEYEAFIK EQIKKAIELQ EEIGLDVLVH GEFERTDMVE FFAEKLNGIA
TTQNGWVLSY GSRCYRPPII YGTVTRPEPM TLKEITYAQS LTEKPVKGML TGPVTIMSWS
YYREDIPERE IAYQIALAIN EEVKDLEEAG IKIVQIDEPA FREKAPIKKS KWPEYFEWAI
NAFNLAANAR PETQIHAHMC YSDFNEIIEY IHQLEFDVIS IEASRSKGEI ISAFENFKGW
IKQIGVGVWD IHSPAVPSIN EMREIVERVL RVLPKELIWI NPDCGLKTRN WDEVIPSLRN
MVALAKEMRE KFES
