METE_BURCJ
ID METE_BURCJ Reviewed; 764 AA.
AC B4EJ37;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 68.
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};
GN OrderedLocusNames=BceJ2315_59240; ORFNames=BCAM2484;
OS Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 /
OS NCTC 13227 / J2315 / CF5610) (Burkholderia cepacia (strain J2315)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=216591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610;
RX PubMed=18931103; DOI=10.1128/jb.01230-08;
RA Holden M.T., Seth-Smith H.M., Crossman L.C., Sebaihia M., Bentley S.D.,
RA Cerdeno-Tarraga A.M., Thomson N.R., Bason N., Quail M.A., Sharp S.,
RA Cherevach I., Churcher C., Goodhead I., Hauser H., Holroyd N., Mungall K.,
RA Scott P., Walker D., White B., Rose H., Iversen P., Mil-Homens D.,
RA Rocha E.P., Fialho A.M., Baldwin A., Dowson C., Barrell B.G., Govan J.R.,
RA Vandamme P., Hart C.A., Mahenthiralingam E., Parkhill J.;
RT "The genome of Burkholderia cenocepacia J2315, an epidemic pathogen of
RT cystic fibrosis patients.";
RL J. Bacteriol. 191:261-277(2009).
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; AM747721; CAR56349.1; -; Genomic_DNA.
DR RefSeq; WP_006488503.1; NC_011001.1.
DR AlphaFoldDB; B4EJ37; -.
DR SMR; B4EJ37; -.
DR STRING; 216591.BCAM2484; -.
DR PRIDE; B4EJ37; -.
DR EnsemblBacteria; CAR56349; CAR56349; BCAM2484.
DR KEGG; bcj:BCAM2484; -.
DR eggNOG; COG0620; Bacteria.
DR HOGENOM; CLU_013175_0_0_4; -.
DR OMA; KVMKGML; -.
DR OrthoDB; 577156at2; -.
DR BioCyc; BCEN216591:G1G1V-6588-MON; -.
DR UniPathway; UPA00051; UER00082.
DR Proteomes; UP000001035; Chromosome 2.
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..764
FT /note="5-methyltetrahydropteroyltriglutamate--homocysteine
FT methyltransferase"
FT /id="PRO_1000097819"
FT ACT_SITE 703
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 16..19
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 121
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 440..442
FT /ligand="L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:58199"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 440..442
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 493
FT /ligand="L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:58199"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 493
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 524..525
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 570
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 608
FT /ligand="L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:58199"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 608
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 614
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 650
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 652
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 674
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 735
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
SQ SEQUENCE 764 AA; 85411 MW; 82D5EC9375D19CD8 CRC64;
MVTTHNLGFP RIGAKRELKF GLERYWKGES SRDELKALGA ELRRRHWHDQ RDLDLAPIGD
FAFYDQVLDM SFTLGNLPKR VQDFHGDALD NAFRVARGRS AQSAEAHAAC CGGVAAGEMT
KWFDTNYHYI VPEFHADTNF SLDPSRLLQQ LAEANAQGVN AKPVILGPVT YLWLGKAKDD
SDRLALLPKL LPVYGALLDT LTAQGVEWVQ IDEPILVTEL DAEWRQAFRT AYAALETRRI
NLLLATYFGQ LQDNLTLAAS LPVDGLHIDA INARDEVDAL VRELPPERVL SIGAINGRNI
WKTDLNATLD WLEPLAKQLG DRLWLAPSCS LLHVPVDLAN EAKLDAEIRS WLAFALQKLD
ELKVLATALN EGRDTVADAL AANAAAIESR RRSPRVNNPA VKAAIARIDA RLGNRASPYA
QRASKQSARL NLPAFPTTTI GSFPQTAEIR QARSRFKAGT LDEAGYRTAM QAEIERSVRE
QESLELDVLV HGEAERNDMV EYFGEQLDGY AFSQFGWVQS YGSRCVKPPI LFGDISRPKA
MTVEWITYAQ SLTNKPMKGM LTGPVTILNW SFVRDDQPRS VSCYQLALAI RDEVLDLEQA
GVRVIQIDEA ALREGLPLRR AQWSEYLKWA VESFRITANG VQDDTQIHTH MCYSEFNDII
ASIADMDADV ITIETSRSDM ELLDAFDDFK YPNEIGPGVY DIHSPNIPTQ DHIVGLMRKA
AERIPAERLW VNPDCGLKTR QWGEVIPALT NMVAAAKTLR NQVR
