ID F4GUQ7_PUSST Unreviewed; 764 AA. AC F4GUQ7; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAR-2024, entry version 65. DE RecName: Full=5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase {ECO:0000256|HAMAP-Rule:MF_00172}; DE EC=2.1.1.14 {ECO:0000256|HAMAP-Rule:MF_00172}; DE AltName: Full=Cobalamin-independent methionine synthase {ECO:0000256|HAMAP-Rule:MF_00172}; DE AltName: Full=Methionine synthase, vitamin-B12 independent isozyme {ECO:0000256|HAMAP-Rule:MF_00172}; GN Name=metE {ECO:0000256|HAMAP-Rule:MF_00172}; GN OrderedLocusNames=PT7_1349 {ECO:0000313|EMBL:AEC19889.1}; OS Pusillimonas sp. (strain T7-7). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Pusillimonas. OX NCBI_TaxID=1007105 {ECO:0000313|EMBL:AEC19889.1, ECO:0000313|Proteomes:UP000008737}; RN [1] {ECO:0000313|EMBL:AEC19889.1, ECO:0000313|Proteomes:UP000008737} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=T7-7 {ECO:0000313|EMBL:AEC19889.1, RC ECO:0000313|Proteomes:UP000008737}; RX PubMed=21622753; DOI=10.1128/JB.05242-11; RA Cao B., Ma T., Ren Y., Ren Y., Li G., Li P., Guo X., Ding P., Feng L.; RT "Complete genome sequence of Pusillimonas sp. T7-7, a cold-tolerant diesel RT oil-degrading bacterium isolated from the Bohai Sea in China."; RL J. Bacteriol. 193:4021-4022(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=T7-7; RA Cao B., Ma T., Li P., Jiang L., Li Y., Guo X., Feng L.; RT "Genome Announcement Complete Genome Sequence of Pusillimonas sp. T7-7, a RT novel species isolated from the Bohai Sea, China."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the transfer of a methyl group from 5- CC methyltetrahydrofolate to homocysteine resulting in methionine CC formation. {ECO:0000256|ARBA:ARBA00002777, ECO:0000256|HAMAP- CC 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:0000256|HAMAP- CC Rule:MF_00172}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00172}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00172}; 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, ECO:0000256|HAMAP-Rule:MF_00172}. CC -!- SIMILARITY: Belongs to the vitamin-B12 independent methionine synthase CC family. {ECO:0000256|ARBA:ARBA00009553, ECO:0000256|HAMAP- CC 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; CP002663; AEC19889.1; -; Genomic_DNA. DR RefSeq; WP_013742425.1; NC_015458.1. DR AlphaFoldDB; F4GUQ7; -. DR STRING; 1007105.PT7_1349; -. DR KEGG; put:PT7_1349; -. DR eggNOG; COG0620; Bacteria. DR HOGENOM; CLU_013175_0_0_4; -. DR OrthoDB; 244285at2; -. DR UniPathway; UPA00051; UER00082. DR Proteomes; UP000008737; 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 CDD; cd03312; CIMS_N_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 NCBIfam; TIGR01371; met_syn_B12ind; 1. 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, ECO:0000256|HAMAP- KW Rule:MF_00172}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00172}; KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167, ECO:0000256|HAMAP- KW Rule:MF_00172}; KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP- KW Rule:MF_00172}; Repeat {ECO:0000256|HAMAP-Rule:MF_00172}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00172}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00172}. FT DOMAIN 4..320 FT /note="Cobalamin-independent methionine synthase MetE N- FT terminal" FT /evidence="ECO:0000259|Pfam:PF08267" FT DOMAIN 438..759 FT /note="Cobalamin-independent methionine synthase MetE C- FT terminal/archaeal" FT /evidence="ECO:0000259|Pfam:PF01717" FT ACT_SITE 705 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172, FT ECO:0000256|PIRSR:PIRSR000382-3" FT BINDING 16..19 FT /ligand="5-methyltetrahydropteroyltri-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58207" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172" FT BINDING 19 FT /ligand="5-methyltetrahydropteroyltri-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58207" FT /evidence="ECO:0000256|PIRSR:PIRSR000382-1" FT BINDING 117 FT /ligand="5-methyltetrahydropteroyltri-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58207" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172" FT BINDING 122 FT /ligand="5-methyltetrahydropteroyltri-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58207" FT /evidence="ECO:0000256|PIRSR:PIRSR000382-1" FT BINDING 442..444 FT /ligand="L-homocysteine" FT /ligand_id="ChEBI:CHEBI:58199" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172, FT ECO:0000256|PIRSR:PIRSR000382-1" FT BINDING 442..444 FT /ligand="L-methionine" FT /ligand_id="ChEBI:CHEBI:57844" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172, FT ECO:0000256|PIRSR:PIRSR000382-1" FT BINDING 495 FT /ligand="L-homocysteine" FT /ligand_id="ChEBI:CHEBI:58199" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172" FT BINDING 495 FT /ligand="L-methionine" FT /ligand_id="ChEBI:CHEBI:57844" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172, FT ECO:0000256|PIRSR:PIRSR000382-1" FT BINDING 526..527 FT /ligand="5-methyltetrahydropteroyltri-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58207" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172, FT ECO:0000256|PIRSR:PIRSR000382-1" FT BINDING 572 FT /ligand="5-methyltetrahydropteroyltri-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58207" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172, FT ECO:0000256|PIRSR:PIRSR000382-1" FT BINDING 610 FT /ligand="L-homocysteine" FT /ligand_id="ChEBI:CHEBI:58199" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172, FT ECO:0000256|PIRSR:PIRSR000382-1" FT BINDING 610 FT /ligand="L-methionine" FT /ligand_id="ChEBI:CHEBI:57844" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172, FT ECO:0000256|PIRSR:PIRSR000382-1" FT BINDING 616 FT /ligand="5-methyltetrahydropteroyltri-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58207" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172" FT BINDING 652 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" FT BINDING 652 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172" FT BINDING 654 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172" FT BINDING 654 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" FT BINDING 676 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" FT BINDING 676 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172" FT BINDING 737 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" FT BINDING 737 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00172" SQ SEQUENCE 764 AA; 85584 MW; 3F43BC18C6AFB4E1 CRC64; MTITHNLGFP RIGVRRELKS SLEAYWAGKQ TLPELEATGR ELRARHWRLQ AKSGLQFVPV GDFAWYDHIL EWTTLLGAVP ARFGQPSDED VGLDTLFRMA RGRAPSGSPA AACEMTKWFD TNYHYIVPEL VPEQSYRIAR SYLFDQIREA QSLGHKAKPV IPGPLTWLWL GKGDAFAQGA SDTAKLTLLD NLVPVYVQAL EQIQNLGVEW VQIDEPILGL DLPDAWQQAF QPVYETLAKG GPRVLLATYF EDLKENVQVL KGLPVDGVHV DLVRAPDQLA RVAAVLDDRQ VLSAGLIDGR NVWRSDLDKA GDQIRQVAQQ RGDRLWLAPS CSLLHVPVDL DAERDLDAEL RSWLSFATQK LDELNVLASS LANTVDADTQ EALVQQRVAL INRKNSSRIH NPAVQQRLKA SVSVTRDRAP FQQRIASQQK KLGLPSYPTT TIGSFPQTSE IRLARRDWKQ GALSDTAYEK AMRAEIEHVI RFQEKIGLDV LVHGEPERND MVEYFGELLG GFAFTQNGWV QSYGSRCVKP PIIFGDVVRP AAMTVAWSAY AQSLTEKPVK GMLTGPVTIL QWSFVRDDQP RATTCQQLAL ALRDEVTDLE AAGITVIQID EPAFREGLPL RRADWRVYLD WAVDCFRLST GGVQDDTQIH THMCYSEFND IIESIAAMDA DVITIETSRS NMELLGAFED FHYPNDIGPG VYDIHSPNVP QLEWMVDLMK KASGRLPAER LWVNPDCGLK TRGWPETEAA LLAMVKAAET LRYT //