ID G2FIT3_9GAMM Unreviewed; 1234 AA. AC G2FIT3; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 23-MAY-2018, entry version 42. DE RecName: Full=Methionine synthase {ECO:0000256|PIRNR:PIRNR000381}; DE EC=2.1.1.13 {ECO:0000256|PIRNR:PIRNR000381}; DE AltName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000256|PIRNR:PIRNR000381}; GN Name=metH {ECO:0000313|EMBL:EGW53268.1}; GN ORFNames=TevJSym_bg00040 {ECO:0000313|EMBL:EGW53268.1}; OS endosymbiont of Tevnia jerichonana (vent Tica). OC Bacteria; Proteobacteria; Gammaproteobacteria; OC sulfur-oxidizing symbionts. OX NCBI_TaxID=1049564 {ECO:0000313|EMBL:EGW53268.1, ECO:0000313|Proteomes:UP000005167}; RN [1] {ECO:0000313|EMBL:EGW53268.1, ECO:0000313|Proteomes:UP000005167} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Gardebrecht A., Markert S., Felbeck H., Thuermer A., Albrecht D., RA Wollherr A., Kabisch J., Lehmann R., Daniel R., Liesegang H., RA Hecker M., Sievert S.M., Schweder T.; RT "The endosymbionts of the deep-sea tubeworms Riftia pachyptila and RT Tevnia jerichonana share an identical physiology as revealed by RT proteogenomic analyses."; RL ISME J. 0:0-0(2011). CC -!- FUNCTION: Catalyzes the transfer of a methyl group from methyl- CC cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and CC methionine. Subsequently, remethylates the cofactor using CC methyltetrahydrofolate. {ECO:0000256|PIRNR:PIRNR000381}. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + L-homocysteine = CC tetrahydrofolate + L-methionine. {ECO:0000256|PIRNR:PIRNR000381}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381- CC 1}; CC -!- COFACTOR: CC Name=methylcob(III)alamin; Xref=ChEBI:CHEBI:28115; CC Evidence={ECO:0000256|PIRNR:PIRNR000381, CC ECO:0000256|PIRSR:PIRSR000381-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (MetH route): step CC 1/1. {ECO:0000256|PIRNR:PIRNR000381}. 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:EGW53268.1}. 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; AFZB01000033; EGW53268.1; -; Genomic_DNA. DR EnsemblBacteria; EGW53268; EGW53268; TevJSym_bg00040. DR PATRIC; fig|1049564.3.peg.2817; -. DR OrthoDB; POG091H030I; -. DR UniPathway; UPA00051; UER00081. DR Proteomes; UP000005167; Unassembled WGS sequence. DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-UniRule. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR CDD; cd02069; methionine_synthase_B12_BD; 1. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 3. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR036724; Cobalamin-bd_sf. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR003726; HCY_dom. DR InterPro; IPR036589; HCY_dom_sf. DR InterPro; IPR033706; Met_synthase_B12-bd. DR InterPro; IPR011822; MetH. DR InterPro; IPR036594; Meth_synthase_dom. DR InterPro; IPR000489; Pterin-binding_dom. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR InterPro; IPR037010; VitB12-dep_Met_synth_activ_sf. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF000381; MetH; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR TIGRFAMs; TIGR02082; metH; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Amino-acid biosynthesis {ECO:0000256|PIRNR:PIRNR000381}; KW Cobalamin {ECO:0000256|PIRNR:PIRNR000381, KW ECO:0000256|PIRSR:PIRSR000381-2}; KW Cobalt {ECO:0000256|PIRNR:PIRNR000381, ECO:0000256|PIRSR:PIRSR000381- KW 1}; Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000005167}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR000381, KW ECO:0000256|PIRSR:PIRSR000381-1, ECO:0000256|PROSITE- KW ProRule:PRU00333}; KW Methionine biosynthesis {ECO:0000256|PIRNR:PIRNR000381}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR000381, ECO:0000256|PROSITE- KW ProRule:PRU00333, ECO:0000313|EMBL:EGW53268.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000005167}; KW S-adenosyl-L-methionine {ECO:0000256|PIRNR:PIRNR000381, KW ECO:0000256|PIRSR:PIRSR000381-2}; KW Transferase {ECO:0000256|PIRNR:PIRNR000381, ECO:0000256|PROSITE- KW ProRule:PRU00333, ECO:0000313|EMBL:EGW53268.1}; KW Zinc {ECO:0000256|PIRNR:PIRNR000381, ECO:0000256|PIRSR:PIRSR000381-1, KW ECO:0000256|PROSITE-ProRule:PRU00333}. FT DOMAIN 5 323 Hcy-binding. {ECO:0000259|PROSITE: FT PS50970}. FT DOMAIN 354 615 Pterin-binding. {ECO:0000259|PROSITE: FT PS50972}. FT DOMAIN 647 741 B12-binding N-terminal. FT {ECO:0000259|PROSITE:PS51337}. FT DOMAIN 745 880 B12-binding. {ECO:0000259|PROSITE: FT PS51332}. FT DOMAIN 896 1232 AdoMet activation. {ECO:0000259|PROSITE: FT PS50974}. FT REGION 833 834 Cobalamin-binding. {ECO:0000256|PIRSR: FT PIRSR000381-2}. FT REGION 1194 1195 S-adenosyl-L-methionine binding. FT {ECO:0000256|PIRSR:PIRSR000381-2}. FT COILED 879 899 {ECO:0000256|SAM:Coils}. FT METAL 245 245 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1, FT ECO:0000256|PROSITE-ProRule:PRU00333}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1, FT ECO:0000256|PROSITE-ProRule:PRU00333}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1, FT ECO:0000256|PROSITE-ProRule:PRU00333}. FT METAL 758 758 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. FT BINDING 803 803 Cobalamin. {ECO:0000256|PIRSR: FT PIRSR000381-2}. FT BINDING 946 946 S-adenosyl-L-methionine. FT {ECO:0000256|PIRSR:PIRSR000381-2}. FT BINDING 1139 1139 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000256|PIRSR:PIRSR000381- FT 2}. FT BINDING 1143 1143 Cobalamin; via carbonyl oxygen. FT {ECO:0000256|PIRSR:PIRSR000381-2}. SQ SEQUENCE 1234 AA; 136285 MW; D5F649C9B4E4EA60 CRC64; MDNITPELES ILCERILILD GAMGTMIQRH KLTEEDYRGE RFTDWPSDLK GNNDLLVLSQ PELIRNIHEE YMEAGADILE TNTFGANRIS MADYDMQELA YEMNVAGARL CREAADKYAT PEKPRYVAGV LGPTNRTASI SPDVNDPGAR NISFDELVEA YAEATRGLIE GGVDILLIET IFDTLNAKAA VAACEQVFDQ DQLRLPIMIS GTITDASGRT LSGQTTEAFY NSLRHARPIS IGLNCALGPE LMRQYVEEIS RVAECYVNVH PNAGLPNEFG EYDLGPEAMG QQIAEWAEAG FLNIIGGCCG TTPAHIKAIA EAVADQAPRK LPEIRPECRL SGLEPLNIGP DSLFVNVGER ANVTGSAKFK RLILNEEYEE ALDVCRAQVE NGAQVVDVNM DEAMLDGVAA MQRFLNLCAG EPDISKVPVM IDSSKWEIIE AGLKCVQGKP IVNSISMKEG IDKFKQQAKL CRRYGAAVIV MAFDEEGQAD TQARKVEICT RAYQILTEEV GFPAEDIIFD PNIFAVATGI PEHDNYGVDF IEATREIKAA CPHALISGGV SNVSFSFRGN NPVREAIHAV FLYHAIQAGM DMGIVNAAQL AVYDDLPAEL RDAVEDVVLN KDPEAGDRLV EIAPNYAGDV VGGNKVEDLE WRSWPVNKRL EHALVKGITE YIDTDTEEAR LAVDKSLEVI EGPLMDGMNV VGDLFGAGKM FLPQVVKSAR VMKKSVAYLE PFLEAEKAEC GVQAQGKILM ATVKGDVHDI GKNIVGVVLQ CNNYEVIDIG VMVPADTILK QAQEHQVDII GLSGLITPSL DEMVHVAKEM KRLRMSQPLM IGGATTSIAH TAVKIEPEYD HPVVYVPDAS RAVGVASNLL SKDLRDDYIA DLRRSYEDVR ERRASKNEAR NLVPIEAARA NPVAIDWDNF VACEPNKLGV NVMDDIQLEL LIDYIDWTFF FHAWQLKGRY PQILEDREKG EEAKKLLADA REMLHKIITE KWLTAKAVIG LFPANAVGDD VEVYGLQPAA GEQRRPISTL HFLRKQGKQP KGKANTCLAD FIAPKASGHS DYIGGFACTA GIGINDKIVE FEKDHDDYSA IMLKALADRL AEALAEWLHE RVRRHYWGYA ANEKLSNEER VAEKYTGIRP AMGYPASPDH TEKDMLWELL DVEKNTGIWL TEAKAMVPTA AVSGLYFSHP DSHYFAVGKI NRDQVVSYAA RIDMELQEVE RWLAPNLAYE PESN //