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METE_STRPN
ID   METE_STRPN              Reviewed;         749 AA.
AC   Q97S31;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 112.
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};
DE   AltName: Full=Methionine synthase, vitamin-B12 independent isozyme {ECO:0000255|HAMAP-Rule:MF_00172};
GN   Name=metE {ECO:0000255|HAMAP-Rule:MF_00172}; OrderedLocusNames=SP_0585;
OS   Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=170187;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-334 / TIGR4;
RX   PubMed=11463916; DOI=10.1126/science.1061217;
RA   Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA   Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA   Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA   Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA   Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA   McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA   Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA   Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT   "Complete genome sequence of a virulent isolate of Streptococcus
RT   pneumoniae.";
RL   Science 293:498-506(2001).
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       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00172};
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}.
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DR   EMBL; AE005672; AAK74738.1; -; Genomic_DNA.
DR   PIR; A95068; A95068.
DR   RefSeq; WP_000108201.1; NZ_AKVY01000001.1.
DR   AlphaFoldDB; Q97S31; -.
DR   SMR; Q97S31; -.
DR   STRING; 170187.SP_0585; -.
DR   EnsemblBacteria; AAK74738; AAK74738; SP_0585.
DR   KEGG; spn:SP_0585; -.
DR   eggNOG; COG0620; Bacteria.
DR   OMA; KVMKGML; -.
DR   PhylomeDB; Q97S31; -.
DR   BioCyc; SPNE170187:G1FZB-604-MON; -.
DR   UniPathway; UPA00051; UER00082.
DR   PHI-base; PHI:2733; -.
DR   Proteomes; UP000000585; Chromosome.
DR   GO; GO:0003871; F:5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity; IEA:UniProtKB-UniRule.
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; -; 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   3: Inferred from homology;
KW   Amino-acid biosynthesis; Metal-binding; Methionine biosynthesis;
KW   Methyltransferase; Repeat; Transferase; Zinc.
FT   CHAIN           1..749
FT                   /note="5-methyltetrahydropteroyltriglutamate--homocysteine
FT                   methyltransferase"
FT                   /id="PRO_0000098671"
FT   ACT_SITE        689
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         15..18
FT                   /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58207"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         114
FT                   /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58207"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         425..427
FT                   /ligand="L-homocysteine"
FT                   /ligand_id="ChEBI:CHEBI:58199"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         425..427
FT                   /ligand="L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:57844"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         478
FT                   /ligand="L-homocysteine"
FT                   /ligand_id="ChEBI:CHEBI:58199"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         478
FT                   /ligand="L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:57844"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         555
FT                   /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58207"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         593
FT                   /ligand="L-homocysteine"
FT                   /ligand_id="ChEBI:CHEBI:58199"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         593
FT                   /ligand="L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:57844"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         599
FT                   /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58207"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         636
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         638
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         660
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT   BINDING         721
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
SQ   SEQUENCE   749 AA;  84675 MW;  DDA22A3733576671 CRC64;
     MSTTIIGFPR LGEFRELKFT TEKYFRKEIS EEELLAAAKD LRAKHWNIVK EKGITEIPSN
     DFSHYDNFLD AAFLFNVVPA SVQNLDLSDL ERYFALGRGY QGEKGDVRAL PMKKWFNTNY
     HYIVPKFEKD TQVKLAGHKI FDEFQEAKEL GLNTRPVLVG PFTFLQLSDF EEGVKADDFV
     DSLVAAYQEV FAKLAELGAT RIQLDEAALV KDLTAEEKAL FLNLYNKLLA DKKGLEVLLQ
     TYFGDVRDVY ADLVNLPVDA IGLDFVEGKK TLELVKGGFP ADKTLYVGIV NGKNIWRNNY
     EKSLAVLEQI PAENIVLTSS CSLLHVPFTT ANEEFEPALL NHFAFAVEKL DEIRDLDAIR
     NGQGSEALAA NKELFATERV GENAELRARI AGLTDADYTR LPAFAEREAI QEEAFKLPAL
     PTTTIGSFPQ TKEVRAKRLA YRKGELSQKE YDAFLAETID EWIKWQEDID FDVLVHGEFE
     RNDMVEYFGQ NLSGYLFSKN GWVQSYGMRG VKPPIIWGDV TRLNPITVKW SSYAQSRTNK
     PVKGMLTGPV TILNWSFPRE DISIKDSTLQ IALAIKDEVL DLEAAGVKII QIDEAALREK
     LPLRRSDWYE DYLDWAIPAF RLVHSTVAPD TQIHTHMCYS EFTDIIPAID NMDADVISFE
     ANRSNLEILD ELKAKNFQTE VGPGVYDIHS PRVPNEGEID NTIEAILAKV PSKKVWINPD
     CGLKTRGIPE TKESLIRLVE AAKAAREKL
 
 
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