ID G2FIT3_9GAMM Unreviewed; 1234 AA. AC G2FIT3; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 16-MAR-2016, entry version 26. DE SubName: Full=Methionine synthase {ECO:0000313|EMBL:EGW53268.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:EGW53268.1}; 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 -!- 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 -!- 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 Proteomes; UP000005167; Unassembled WGS sequence. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR003726; HCY_dom. DR InterPro; IPR011822; MetH. DR InterPro; IPR000489; Pterin-binding_dom. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. 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 Cobalt {ECO:0000256|PIRSR:PIRSR000381-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000005167}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1}; KW Methyltransferase {ECO:0000313|EMBL:EGW53268.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000005167}; KW Transferase {ECO:0000313|EMBL:EGW53268.1}; KW Zinc {ECO:0000256|PIRSR:PIRSR000381-1}. 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 METAL 245 245 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 308 308 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 309 309 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1}. FT METAL 758 758 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. 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 //