ID METE_HAEIG Reviewed; 756 AA. AC A5UFD9; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 10-JUL-2007, sequence version 1. DT 02-SEP-2026, entry version 95. 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=CGSHiGG_02260; OS Haemophilus influenzae (strain PittGG). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Pasteurellales; Pasteurellaceae; Haemophilus. OX NCBI_TaxID=374931; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PittGG; RX PubMed=17550610; DOI=10.1186/gb-2007-8-6-r103; RA Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C., RA Ehrlich G.D.; RT "Characterization and modeling of the Haemophilus influenzae core and RT supragenomes based on the complete genomic sequences of Rd and 12 clinical RT nontypeable strains."; RL Genome Biol. 8:R103.1-R103.18(2007). 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 = CC tetrahydropteroyltri-L-glutamate + L-methionine; CC Xref=Rhea:RHEA:21196, ChEBI:CHEBI:57844, ChEBI:CHEBI:58140, CC ChEBI:CHEBI:58199, ChEBI:CHEBI:58207; EC=2.1.1.14; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00172}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP- CC 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000672; ABQ99494.1; -; Genomic_DNA. DR AlphaFoldDB; A5UFD9; -. DR SMR; A5UFD9; -. DR KEGG; hiq:CGSHiGG_02260; -. DR HOGENOM; CLU_013175_0_0_6; -. 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:0008652; P:amino acid biosynthetic process; IEA:InterPro. DR CDD; cd03311; CIMS_C_terminal_like; 1. DR CDD; cd03312; CIMS_N_terminal_like; 1. DR FunFam; 3.20.20.210:FF:000002; 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase; 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 NCBIfam; TIGR01371; met_syn_B12ind; 1. DR NCBIfam; NF003556; PRK05222.1; 1. DR PANTHER; PTHR30519; 5-METHYLTETRAHYDROPTEROYLTRIGLUTAMATE--HOMOCYSTEINE METHYLTRANSFERASE; 1. DR Pfam; PF08267; Meth_synt_1; 1. DR Pfam; PF01717; Meth_synt_2; 1. DR PIRSF; PIRSF000382; MeTrfase_B12_ind; 1. DR SUPFAM; SSF51726; UROD/MetE-like; 2. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Metal-binding; Methionine biosynthesis; KW Methyltransferase; Repeat; Transferase; Zinc. FT CHAIN 1..756 FT /note="5-methyltetrahydropteroyltriglutamate--homocysteine FT methyltransferase" FT /id="PRO_1000017246" FT ACT_SITE 695 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 112 FT /ligand="5-methyltetrahydropteroyltri-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58207" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" FT BINDING 432..434 FT /ligand="L-homocysteine" FT /ligand_id="ChEBI:CHEBI:58199" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" FT BINDING 432..434 FT /ligand="L-methionine" FT /ligand_id="ChEBI:CHEBI:57844" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" FT BINDING 485 FT /ligand="L-homocysteine" FT /ligand_id="ChEBI:CHEBI:58199" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" FT BINDING 485 FT /ligand="L-methionine" FT /ligand_id="ChEBI:CHEBI:57844" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" FT BINDING 516..517 FT /ligand="5-methyltetrahydropteroyltri-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58207" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" FT BINDING 562 FT /ligand="5-methyltetrahydropteroyltri-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58207" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" FT BINDING 600 FT /ligand="L-homocysteine" FT /ligand_id="ChEBI:CHEBI:58199" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" FT BINDING 600 FT /ligand="L-methionine" FT /ligand_id="ChEBI:CHEBI:57844" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" FT BINDING 606 FT /ligand="5-methyltetrahydropteroyltri-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58207" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" FT BINDING 642 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" FT BINDING 644 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" FT BINDING 666 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" FT BINDING 727 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172" SQ SEQUENCE 756 AA; 85193 MW; 591EC596FAA0DC65 CRC64; MTTSHILGFP RVGAKRELKF AQERYWRKEL AEQDLLDLAK ALREKNWKHQ AAANADFVAV GDFTFYDHIL DLQVATGAIP ARFGFDSQNL TLDQYFQLAR GNKDQFAIEM TKWFDTNYHY LVPEFQKSTA FKANPAHYVN QIREAKALGL NFKPVIVGPL TFLWLGKEKG EAFNRFDLLN QLVPVYVEIL NALVAEGAEW IQIDEPALAL DLPAEWVEAY KSVYAELSKV NAKLLLATYF GSVAEHAELL KALPVAGLHL DLVRAPEQLA AFEDYSKVLS AGVIEGRNIW RANLNKVLDV LEPLKAKLGE RLWIAPSCSL LHTPFDLEVE VQLKEKNTAL YSWLSFTLQK VEELNVLKQA LNNGRASVQA ALDASQAAAD ARATSKEIHR PEVAERLANL PKGADQRKSP FAERIVKQNA WLNLPLLPTT NIGSFPQTTE IRHARASFKK GELSLADYEA AMKKEIEYVV RRQEELDLDV LVHGEAERND MVEYFGELLD GFAFTKFGWV QSYGSRCVKP PVIYGDVIRP EPMTVRWSQY AQSLTNRVMK GMLTGPVTIL QWSFVRNDIP RSTVCKQIGV ALSDEVLDLE AAGIKVIQID EPAIREGLPL KRADWDAYLQ WAGEAFRLSS MGVQDDTQIH THMCYSEFND ILPAIAALDA DVITIETSRS DMELLTAFAD FKYPNDIGPG VYDIHSPRVP TATEVEHLLR KALNVIPKER LWVNPDCGLK TRGWTETIDQ LKVMVDVTKK LRAELA //