ID J2SDX7_9PSED Unreviewed; 762 AA. AC J2SDX7; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 07-JUN-2017, entry version 26. DE RecName: Full=5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase {ECO:0000256|HAMAP-Rule:MF_00172, ECO:0000256|SAAS:SAAS00101669}; 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 ORFNames=PMI31_05817 {ECO:0000313|EMBL:EJM65141.1}; OS Pseudomonas sp. GM55. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1144333 {ECO:0000313|EMBL:EJM65141.1, ECO:0000313|Proteomes:UP000007268}; RN [1] {ECO:0000313|EMBL:EJM65141.1, ECO:0000313|Proteomes:UP000007268} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GM55 {ECO:0000313|EMBL:EJM65141.1, RC ECO:0000313|Proteomes:UP000007268}; RX PubMed=23045501; DOI=10.1128/JB.01243-12; RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L., RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.; RT "Twenty-one genome sequences from Pseudomonas species and 19 genome RT sequences from diverse bacteria isolated from the rhizosphere and RT endosphere of Populus deltoides."; RL J. Bacteriol. 194:5991-5993(2012). CC -!- FUNCTION: Catalyzes the transfer of a methyl group from 5- CC methyltetrahydrofolate to homocysteine resulting in methionine CC formation. {ECO:0000256|HAMAP-Rule:MF_00172, CC ECO:0000256|SAAS:SAAS00101695}. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydropteroyltri-L-glutamate + L- CC homocysteine = tetrahydropteroyltri-L-glutamate + L-methionine. CC {ECO:0000256|HAMAP-Rule:MF_00172, ECO:0000256|SAAS:SAAS00101678}. CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (MetE route): step CC 1/1. {ECO:0000256|SAAS:SAAS00363622}. CC -!- SIMILARITY: Belongs to the vitamin-B12 independent methionine CC synthase family. {ECO:0000256|HAMAP-Rule:MF_00172, CC ECO:0000256|SAAS:SAAS00577555}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EJM65141.1}. 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; AKJJ01000147; EJM65141.1; -; Genomic_DNA. DR RefSeq; WP_008023334.1; NZ_AKJJ01000147.1. DR EnsemblBacteria; EJM65141; EJM65141; PMI31_05817. DR PATRIC; fig|1144333.3.peg.5663; -. DR UniPathway; UPA00051; UER00082. DR Proteomes; UP000007268; Unassembled WGS sequence. DR GO; GO:0003871; F:5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-HAMAP. 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 Pfam; PF08267; Meth_synt_1; 1. DR Pfam; PF01717; Meth_synt_2; 1. DR PIRSF; PIRSF000382; MeTrfase_B12_ind; 1. DR TIGRFAMs; TIGR01371; met_syn_B12ind; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00172, KW ECO:0000256|SAAS:SAAS00050074}; KW Complete proteome {ECO:0000313|Proteomes:UP000007268}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00172, KW ECO:0000256|SAAS:SAAS00468534}; KW Methionine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00172, KW ECO:0000256|SAAS:SAAS00050076}; KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00172, KW ECO:0000256|SAAS:SAAS00050078, ECO:0000313|EMBL:EJM65141.1}; KW Repeat {ECO:0000256|HAMAP-Rule:MF_00172}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00172, KW ECO:0000256|SAAS:SAAS00050075, ECO:0000313|EMBL:EJM65141.1}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_00172, ECO:0000256|SAAS:SAAS00101720}. FT DOMAIN 4 315 Meth_synt_1. {ECO:0000259|Pfam:PF08267}. FT DOMAIN 433 755 Meth_synt_2. {ECO:0000259|Pfam:PF01717}. FT METAL 648 648 Zinc. {ECO:0000256|HAMAP-Rule:MF_00172}. FT METAL 650 650 Zinc. {ECO:0000256|HAMAP-Rule:MF_00172}. FT METAL 733 733 Zinc. {ECO:0000256|HAMAP-Rule:MF_00172}. SQ SEQUENCE 762 AA; 85937 MW; 50977FC3D366265D CRC64; MALAHSLGFP RIGRDRELKK AQEAFWKGEL DEAGLRAVGR DLRKTHWDLQ KKAGIELLPV GDFAWYDQVL THSLMFGVVP ERFRPHDGKA SLQTLFGMAR GVSDSCCGGA HAQEMTKWFD TNYHYLVPEF SADQQFQLGW EQLFEEVEEA RALGHDVKPV IIGPLTYLWL GKAKGVEFDK LELLDRLLPL YGQIFQRLAA QGVEWVQIDE PILVLDLPQA WKNAFERAYN LIQRDPLKKL VATYFGGLEE NLGLAANLPV DGLHIDLVRA PEQFPTILDR LPAYKVLSLG VVNGRNVWRC DLENALATLR YAQERLGDRL WVAPSCSLLH SPVDLGCEDQ LDSELKSWLA FAVQKCEEVA LLAQAVNEPE APKVLQALTQ SRAVQARRAA SPRIHKPAVQ ARVAAITARD SQRHSPFARR IEKQRAGLNL PLFPTTTIGS FPQTTSIRLA RQSFRQGKLT EAEYTEAMHS EIRHAVQVQE HLGLDVLVHG EAERNDMVEY FAEQLDGYVF TRFGWVQSYG SRCVKPAVIF GDLSRPKAMT VEWIRYAQGL TDKVMKGMLT GPVTMLMWSF PREDVSGEVQ ARQLALAIRD EVLDLEAAGI QIVQIDEAAF REGLPLRQAQ WQHYLDWATE VFRLCASGVR DETQIHTHMC YSEFNDVIES IAAMDADVIT IETSRSDMEL LDAFEAFAYP NEIGPGVYDI HSPRVPDASE MANLLRKAAK RIPADRLWVN PDCGLKTRGW AETEAALVHM VNAARQLRKE WA //