ID A5WD09_PSYWF Unreviewed; 1272 AA. AC A5WD09; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 03-JUL-2019, entry version 97. 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 OrderedLocusNames=PsycPRwf_0595 {ECO:0000313|EMBL:ABQ93550.1}; OS Psychrobacter sp. (strain PRwf-1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Psychrobacter. OX NCBI_TaxID=349106 {ECO:0000313|EMBL:ABQ93550.1, ECO:0000313|Proteomes:UP000001993}; RN [1] {ECO:0000313|EMBL:ABQ93550.1, ECO:0000313|Proteomes:UP000001993} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PRwf-1 {ECO:0000313|EMBL:ABQ93550.1, RC ECO:0000313|Proteomes:UP000001993}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Tiedje J., RA Richardson P.; RT "Complete sequence of chromosome of Psychrobacter sp. PRwf-1."; RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases. 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: CC Reaction=(6S)-5-methyl-5,6,7,8-tetrahydrofolate + L-homocysteine = CC (6S)-5,6,7,8-tetrahydrofolate + L-methionine; CC Xref=Rhea:RHEA:11172, ChEBI:CHEBI:18608, ChEBI:CHEBI:57453, CC ChEBI:CHEBI:57844, ChEBI:CHEBI:58199; EC=2.1.1.13; CC Evidence={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 --------------------------------------------------------------------------- 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; CP000713; ABQ93550.1; -; Genomic_DNA. DR STRING; 349106.PsycPRwf_0595; -. DR EnsemblBacteria; ABQ93550; ABQ93550; PsycPRwf_0595. DR KEGG; prw:PsycPRwf_0595; -. DR eggNOG; ENOG4105C3R; Bacteria. DR eggNOG; COG0646; LUCA. DR eggNOG; COG1410; LUCA. DR HOGENOM; HOG000251409; -. DR KO; K00548; -. DR OMA; ADCIAMS; -. DR BioCyc; PSP349106:G12XP-603-MONOMER; -. DR UniPathway; UPA00051; UER00081. DR Proteomes; UP000001993; Chromosome. 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; -; 1. 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:UP000001993}; 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:PRU00346, ECO:0000313|EMBL:ABQ93550.1}; 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:PRU00346, ECO:0000313|EMBL:ABQ93550.1}; KW Zinc {ECO:0000256|PIRNR:PIRNR000381, ECO:0000256|PIRSR:PIRSR000381-1, KW ECO:0000256|PROSITE-ProRule:PRU00333}. FT DOMAIN 47 367 Hcy-binding. {ECO:0000259|PROSITE: FT PS50970}. FT DOMAIN 398 658 Pterin-binding. {ECO:0000259|PROSITE: FT PS50972}. FT DOMAIN 695 789 B12-binding N-terminal. FT {ECO:0000259|PROSITE:PS51337}. FT DOMAIN 791 927 B12-binding. {ECO:0000259|PROSITE: FT PS51332}. FT DOMAIN 943 1272 AdoMet activation. {ECO:0000259|PROSITE: FT PS50974}. FT REGION 1 29 Disordered. {ECO:0000256|MobiDB-lite: FT A5WD09}. FT REGION 879 880 Cobalamin-binding. {ECO:0000256|PIRSR: FT PIRSR000381-2}. FT REGION 1238 1239 S-adenosyl-L-methionine binding. FT {ECO:0000256|PIRSR:PIRSR000381-2}. FT COILED 923 943 {ECO:0000256|SAM:Coils}. FT COMPBIAS 7 21 Polyampholyte. {ECO:0000256|MobiDB-lite: FT A5WD09}. FT METAL 289 289 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1, FT ECO:0000256|PROSITE-ProRule:PRU00333}. FT METAL 352 352 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1, FT ECO:0000256|PROSITE-ProRule:PRU00333}. FT METAL 353 353 Zinc. {ECO:0000256|PIRSR:PIRSR000381-1, FT ECO:0000256|PROSITE-ProRule:PRU00333}. FT METAL 804 804 Cobalt (cobalamin axial ligand). FT {ECO:0000256|PIRSR:PIRSR000381-1}. FT BINDING 849 849 Cobalamin. {ECO:0000256|PIRSR: FT PIRSR000381-2}. FT BINDING 993 993 S-adenosyl-L-methionine. FT {ECO:0000256|PIRSR:PIRSR000381-2}. FT BINDING 1183 1183 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000256|PIRSR:PIRSR000381- FT 2}. FT BINDING 1187 1187 Cobalamin; via carbonyl oxygen. FT {ECO:0000256|PIRSR:PIRSR000381-2}. SQ SEQUENCE 1272 AA; 140989 MW; EF63F634CBFEEDAB CRC64; MANCSHPEHN TKKDLPETAI KKGHNPDNFN LVPPAKFPFK EQQLTARQRI VEQLNQRILM LDGAMGTQIQ TFKLGESDYR GERFADFTQD VQGNNDLLVL TQPELIKSIH RDHLTAGADI IETNSFNGTQ ISMADYAMEH LVPEINKEAA RLAREVADEF TAQNPDKPRF VAGVIGPTSR TCSLSPDVND PAYRNVTFDE LVDNYTEALF ALIEGGIDLV LIETIFDTLN AKAAIFAVTG VFETIGFELP IMISGTITDA SGRTLSGQTA EAFYNSIRHA KPLSVGFNCA LGADALKPHI QTLSDIADTY ISAHPNAGLP NEFGEYDETP EQTAALLDGF GKSGLLNIVG GCCGTRPEHI KAIHDVMQKY PPRQIPTIAP ACRLSGLEPF TITKDSLFVN VGERTNVTGS KKFLRLIKTG EFTEALDVAR NQVDGGAQIV DINMDEGMLD SKGAMIHFLN LVAGEPDISR VPLMIDSSKW DIIEEGLKRT QGKSVVNSIS LKEGYDEFVK HAKLCMRYGA AVIVMAFDED GQADSYERKI QICQRSYDIL VNEVGFPSED IIFDPNIFAV ATGITEHNNY GADFINATRW ITDNLPNAMV SGGVSNVSFS FRGNPIREAI NAVFLYHAIQ AGLTMGIVNP AMLEVYDEIP KEARDAIEDV MLNRNQGESG QEATERLMTI AEAYVAGGKK NDGTIDLSWR EQSVEKRIEH ALVKGITTYI DEDTEEARLK YPKPLHVIEG PLMDGMNVVG DLFGAGKMFL PQVVKSARVM KRAVAVLNPY IEAEKVEGEV KGKVVMATVK GDVHDIGKNI VGVVLGCNGY DVVDLGVMVP CDKILDTAIA EKADIIGLSG LITPSLDEMV YVAKQMQERG MTLPLMIGGA TTSKAHTAVK IEPNYQNDAV IYVSDASRSV GVVTKLLSQE HRVELLRETR EEYQKVRERL ANRKPKAAKL SYQESIEQGF KFDWDNYTPP VPNEQGQIIF DNYPIENLLP YIDWTPFFVS WGLVGKYPKI FDDEVVGAEA KDLFANAKAL MQTFIDEQLV TPKGVFKIMP ARRTDHDTVT VYDKEPSAGG QPTHVFEHLR QQSDKASGKP NYSLADFISP SEDYDDYLGG FTVSIVGAQE LSDSYKEAGD DYNAIMVQAL CDRLAEAFAE HLHELIRTKY WGYQPTEQLT NEELIKEKYV GIRPAPGYPA CPEHTEKGKL FDWLDTTNAI GTYLTESFAM WPASSVSGFY YSHPESTYFN VGKIDRDQLE DYAKRKDWDI KTAEKWLNPN LT //