METE_BACSU
ID METE_BACSU Reviewed; 762 AA.
AC P80877; O34386;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 4.
DT 03-AUG-2022, entry version 145.
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};
DE AltName: Full=Superoxide-inducible protein 9;
DE Short=SOI9;
GN Name=metE {ECO:0000255|HAMAP-Rule:MF_00172}; Synonyms=metC;
GN OrderedLocusNames=BSU13180;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Devine K.M.;
RT "Sequence of the Bacillus subtilis genome between xlyA and ykoR.";
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP SEQUENCE REVISION TO 15; 302; 309; 328 AND 446.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [4]
RP PROTEIN SEQUENCE OF 2-24.
RC STRAIN=168 / IS58;
RX PubMed=9298659; DOI=10.1002/elps.1150180820;
RA Antelmann H., Bernhardt J., Schmid R., Mach H., Voelker U., Hecker M.;
RT "First steps from a two-dimensional protein index towards a response-
RT regulation map for Bacillus subtilis.";
RL Electrophoresis 18:1451-1463(1997).
RN [5]
RP PTM, AND POST-TRANSLATIONAL MODIFICATION AT CYS-719.
RX PubMed=24313874; DOI=10.1089/ars.2013.5327;
RA Gaballa A., Chi B.K., Roberts A.A., Becher D., Hamilton C.J., Antelmann H.,
RA Helmann J.D.;
RT "Redox regulation in Bacillus subtilis: The bacilliredoxins BrxA(YphP) and
RT BrxB(YqiW) function in de-bacillithiolation of S-bacillithiolated OhrR and
RT MetE.";
RL Antioxid. Redox Signal. 21:357-367(2014).
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 -!- INDUCTION: By superoxide.
CC -!- PTM: In response to oxidative stress, Cys-719 can react with
CC bacillithiol (BSH) to form mixed disulfides. S-bacillithiolation leads
CC to loss of catalytic activity and methionine auxotrophy.
CC {ECO:0000305|PubMed:24313874}.
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; AJ002571; CAA05597.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13175.2; -; Genomic_DNA.
DR PIR; C69657; C69657.
DR RefSeq; NP_389201.2; NC_000964.3.
DR RefSeq; WP_003232565.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; P80877; -.
DR SMR; P80877; -.
DR IntAct; P80877; 2.
DR MINT; P80877; -.
DR STRING; 224308.BSU13180; -.
DR PaxDb; P80877; -.
DR PRIDE; P80877; -.
DR EnsemblBacteria; CAB13175; CAB13175; BSU_13180.
DR GeneID; 936480; -.
DR KEGG; bsu:BSU13180; -.
DR PATRIC; fig|224308.179.peg.1431; -.
DR eggNOG; COG0620; Bacteria.
DR InParanoid; P80877; -.
DR OMA; KVMKGML; -.
DR PhylomeDB; P80877; -.
DR BioCyc; BSUB:BSU13180-MON; -.
DR BioCyc; MetaCyc:MON-14559; -.
DR UniPathway; UPA00051; UER00082.
DR Proteomes; UP000001570; 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 1: Evidence at protein level;
KW Amino-acid biosynthesis; Direct protein sequencing; Metal-binding;
KW Methionine biosynthesis; Methyltransferase; Reference proteome; Repeat;
KW Transferase; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298659"
FT CHAIN 2..762
FT /note="5-methyltetrahydropteroyltriglutamate--homocysteine
FT methyltransferase"
FT /id="PRO_0000098613"
FT ACT_SITE 698
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 18..21
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 112
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 435..437
FT /ligand="L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:58199"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 435..437
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 488
FT /ligand="L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:58199"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 488
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 519..520
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 565
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 603
FT /ligand="L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:58199"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 603
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 609
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 645
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 647
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 669
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 730
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT MOD_RES 719
FT /note="S-bacillithiol cysteine disulfide"
FT /evidence="ECO:0000269|PubMed:24313874"
FT CONFLICT 15
FT /note="G -> D (in Ref. 1; CAA05597)"
FT /evidence="ECO:0000305"
FT CONFLICT 20
FT /note="W -> Q (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 302
FT /note="R -> S (in Ref. 1; CAA05597)"
FT /evidence="ECO:0000305"
FT CONFLICT 309
FT /note="I -> V (in Ref. 1; CAA05597)"
FT /evidence="ECO:0000305"
FT CONFLICT 328
FT /note="H -> D (in Ref. 1; CAA05597)"
FT /evidence="ECO:0000305"
FT CONFLICT 446
FT /note="S -> R (in Ref. 1; CAA05597)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 762 AA; 86806 MW; BB85B09E6C1179EF CRC64;
MTTIKTSNLG FPRIGLNREW KKALEAYWKG STDKDTFLKQ IDELFLSAVK TQIDQQIDVV
PVSDFTQYDH VLDTAVSFNW IPKRFRHLTD ATDTYFAIAR GIKDAVSSEM TKWFNTNYHY
IVPEYDESIE FRLTRNKQLE DYRRIKQEYG VETKPVIVGP YTFVTLAKGY EPSEAKAIQK
RLVPLYVQLL KELEEEGVKW VQIDEPALVT ASSEDVRGAK ELFESITSEL SSLNVLLQTY
FDSVDAYEEL ISYPVQGIGL DFVHDKGRNL EQLKTHGFPT DKVLAAGVID GRNIWKADLE
ERLDAVLDIL SIAKVDELWI QPSSSLLHVP VAKHPDEHLE KDLLNGLSYA KEKLAELTAL
KEGLVSGKAA ISEEIQQAKA DIQALKQFAT GANSEQKKEL EQLTDKDFKR PIPFEERLAL
QNESLGLPLL PTTTIGSFPQ SAEVRSARQK WRKAEWSDEQ YQNFINAETK RWIDIQEELE
LDVLVHGEFE RTDMVEYFGE KLAGFAFTKY AWVQSYGSRC VRPPVIYGDV EFIEPMTVKD
TVYAQSLTSK HVKGMLTGPV TILNWSFPRN DISRKEIAFQ IGLALRKEVK ALEDAGIQII
QVDEPALREG LPLKTRDWDE YLTWAAEAFR LTTSSVKNET QIHTHMCYSN FEDIVDTIND
LDADVITIEH SRSHGGFLDY LKNHPYLKGL GLGVYDIHSP RVPSTEEMYN IIVDALAVCP
TDRFWVNPDC GLKTRQQEET VAALKNMVEA AKQARAQQTQ LV
