ID C0ZUN9_RHOE4 Unreviewed; 768 AA. AC C0ZUN9; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 27-MAR-2024, entry version 76. DE RecName: Full=5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase {ECO:0000256|ARBA:ARBA00012034}; DE EC=2.1.1.14 {ECO:0000256|ARBA:ARBA00012034}; GN OrderedLocusNames=RER_15760 {ECO:0000313|EMBL:BAH32284.1}; OS Rhodococcus erythropolis (strain PR4 / NBRC 100887). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae; OC Rhodococcus; Rhodococcus erythropolis group. OX NCBI_TaxID=234621 {ECO:0000313|EMBL:BAH32284.1, ECO:0000313|Proteomes:UP000002204}; RN [1] {ECO:0000313|Proteomes:UP000002204} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204}; RA Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S., RA Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.; RT "Comparison of the complete genome sequences of Rhodococcus erythropolis RT PR4 and Rhodococcus opacus B4."; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:BAH32284.1, ECO:0000313|Proteomes:UP000002204} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204}; RX PubMed=16423019; DOI=10.1111/j.1462-2920.2005.00899.x; RA Sekine M., Tanikawa S., Omata S., Saito M., Fujisawa T., Tsukatani N., RA Tajima T., Sekigawa T., Kosugi H., Matsuo Y., Nishiko R., Imamura K., RA Ito M., Narita H., Tago S., Fujita N., Harayama S.; RT "Sequence analysis of three plasmids harboured in Rhodococcus erythropolis RT strain PR4."; RL Environ. Microbiol. 8:334-346(2006). CC -!- FUNCTION: Catalyzes the transfer of a methyl group from 5- CC methyltetrahydrofolate to homocysteine resulting in methionine CC formation. {ECO:0000256|ARBA:ARBA00002777}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000382-2}; CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|PIRSR:PIRSR000382- CC 2}; 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:0000256|ARBA:ARBA00004681}. CC -!- SIMILARITY: Belongs to the vitamin-B12 independent methionine synthase CC family. {ECO:0000256|ARBA:ARBA00009553}. 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; AP008957; BAH32284.1; -; Genomic_DNA. DR RefSeq; WP_019744430.1; NC_012490.1. DR AlphaFoldDB; C0ZUN9; -. DR GeneID; 57488289; -. DR KEGG; rer:RER_15760; -. DR PATRIC; fig|234621.6.peg.2061; -. DR eggNOG; COG0620; Bacteria. DR HOGENOM; CLU_013175_0_0_11; -. DR UniPathway; UPA00051; UER00082. DR Proteomes; UP000002204; Chromosome. DR GO; GO:0003871; F:5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW. DR CDD; cd03311; CIMS_C_terminal_like; 1. DR CDD; cd03312; CIMS_N_terminal_like; 1. DR Gene3D; 3.20.20.210; -; 2. 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 PANTHER; PTHR30519; 5-METHYLTETRAHYDROPTEROYLTRIGLUTAMATE--HOMOCYSTEINE METHYLTRANSFERASE; 1. DR PANTHER; PTHR30519:SF0; 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 {ECO:0000256|ARBA:ARBA00022605}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR000382-2}; KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167}; KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, KW ECO:0000313|EMBL:BAH32284.1}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:BAH32284.1}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR000382-2}. FT DOMAIN 10..326 FT /note="Cobalamin-independent methionine synthase MetE N- FT terminal" FT /evidence="ECO:0000259|Pfam:PF08267" FT DOMAIN 433..754 FT /note="Cobalamin-independent methionine synthase MetE C- FT terminal/archaeal" FT /evidence="ECO:0000259|Pfam:PF01717" FT BINDING 25 FT /ligand="5-methyltetrahydropteroyltri-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58207" FT /evidence="ECO:0000256|PIRSR:PIRSR000382-1" FT BINDING 124 FT /ligand="5-methyltetrahydropteroyltri-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58207" FT /evidence="ECO:0000256|PIRSR:PIRSR000382-1" FT BINDING 490 FT /ligand="L-methionine" FT /ligand_id="ChEBI:CHEBI:57844" FT /evidence="ECO:0000256|PIRSR:PIRSR000382-1" FT BINDING 521..522 FT /ligand="5-methyltetrahydropteroyltri-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58207" FT /evidence="ECO:0000256|PIRSR:PIRSR000382-1" FT BINDING 605 FT /ligand="L-homocysteine" FT /ligand_id="ChEBI:CHEBI:58199" FT /evidence="ECO:0000256|PIRSR:PIRSR000382-1" FT BINDING 605 FT /ligand="L-methionine" FT /ligand_id="ChEBI:CHEBI:57844" FT /evidence="ECO:0000256|PIRSR:PIRSR000382-1" FT BINDING 647 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR000382-2" SQ SEQUENCE 768 AA; 86009 MW; C532D284222D733B CRC64; MSSSTAAFGS SVLGYPRIGP RRELKRALES YWHGTSDKDA LLAVAKELQE STWSELAATG LSQVPGNTFS FYDHVLDNAL LFGAVPERFK PLEGALDPLD FYFTMARGRP DFPPLELVRF FGTNYYYRQP EIDANTVFSL NSEALLDEFE RAKARGIELR PVIMGPVSLL LLSKVGPATE KSDPNFTPLD LLDALLPEYE KLFEQLAKAG ATCVQLDEPS VTEDRTPEEL AALGRAYEKL STAPLRPRLL VTGPYGKFGE ALNILAPTKI EAFGLDLVHG KITAEELAAV PNIKRKRIYA GVVDGRNVWR VDRFNTLTYL NELKDVVPDL VVSTSSSLLH VPYDVLSEYD IPGDVADRLA FAKQKVGEVV SLAKALTEGP SDKWRKRPTK VHFKLKHAVR ARVNAIKPED RVRAPYEERR KAQQERLNLP LVPAQTLGSF PQTDAIRQAR YELGQGRLEW DDYYKRIQEE IERTIRLQED IGLDVFVHGE HERNDMVQYF AELLEGYAFT HNGWVQAYGS RCTRPPILYG DIARPKPMTV EWIAYAQSLT DKPVKGMLTG PVTMIARSFV RQDQPLYETA EQLALVIRDE IADLEAAGIA IIQVDEPAIR ELLPLREDGR EAYLEWAVDA FRLATGGAKP ETQIHTHLTY SARSSVVDAI ERLDADVTAI VATRSITWVL EALKEGALTH GVGPGVYESR SARIPDIDEL DELLTEASES ISLDRLWANP DGGLKTRHPW QLEPSLRNMV AAARRLRRRA EQAERDAG //