METE_VIBHA
ID METE_VIBHA Reviewed; 760 AA.
AC Q8KRG6;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 75.
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};
OS Vibrio harveyi (Beneckea harveyi).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=669;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12366834; DOI=10.1046/j.1365-2958.2002.03128.x;
RA Chatterjee J., Miyamoto C.M., Zouzoulas A., Lang B.F., Skouris N.,
RA Meighen E.A.;
RT "MetR and CRP bind to the Vibrio harveyi lux promoters and regulate
RT luminescence.";
RL Mol. Microbiol. 46:101-111(2002).
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; AF535154; AAN04098.1; -; Genomic_DNA.
DR RefSeq; WP_038898631.1; NZ_UAVF01000033.1.
DR AlphaFoldDB; Q8KRG6; -.
DR SMR; Q8KRG6; -.
DR STRING; 669.AL538_03440; -.
DR GeneID; 57821789; -.
DR PATRIC; fig|669.65.peg.2305; -.
DR UniPathway; UPA00051; UER00082.
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..760
FT /note="5-methyltetrahydropteroyltriglutamate--homocysteine
FT methyltransferase"
FT /id="PRO_0000098676"
FT ACT_SITE 699
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 17..20
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 118
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 436..438
FT /ligand="L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:58199"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 436..438
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 489
FT /ligand="L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:58199"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 489
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 520..521
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 566
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 604
FT /ligand="L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:58199"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 604
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 610
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 646
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 648
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 670
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 731
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
SQ SEQUENCE 760 AA; 84974 MW; ACB41F667DBD8AC6 CRC64;
MTTTTHILGY PRIGEKRELK FAQEKYWRGE IEQTELKQVG ATLREKNWAT QAEAGLSFAT
AGDFAWYDHV LTTTLLLGHT PKRHANGFPD LDTLFKVGRG QSQAGCGCSG AAASDMTKWF
NTNYHYIVPE FSKDDSFEVS WPQLFEEVND AIKLGHNVKP VLLGPLSYLY LGKEIEEDFD
RLTLLPRLLT AYQAILSKLA NQGVEWVQID EPILSLELEE KWGDAFKLAY QVIRSDVKVL
LTTYFDSVSD TLDKIVELPV DGLHIDLSAS PEQLDEVVEK LPQGWVLSAG VVNGRNVWRS
DLSAQRERLQ PVKDKLGDNL WVASSCSLLH SPVDLDLEPA LSDEVKSWFA FAKQKVTEVA
LLGRALDGDH NAILVCDTYS QPIKDRKTAA HVNKPHVQAR LNSISASLTE RSAPYAERAA
HQAEVLGLPL LPTTTIGSFP QTSEIRVQRS AFRSGQLSTD DYHQALKGHI ADAVRRQEAL
DLDVLVHGEA ERNDMVEYFA ENLAGFQTTK FGWVQSYGSR CVKPAIVVAD IEREKPITVE
WSTYAQSLTN KQMKGMLTGP VTILCWTFPR EDITRKAIAD QLALALRDEV SDLQQAGINI
IQIDEPAIRE GLPLKKRDHK AYLQWAVDAF KIAAASAKPE TQIHTHMCYS EFNEIIDSVA
ALDADVITIE TSRSNMELLK AFEDFNYPNE IGPGVYDIHS PNIPSEEWIE ELIKKAAEKI
PAQRLWVNPD CGLKTRNWSE TEAALANLVS AAKKLRAELV
