ID A5WD09_PSYWF Unreviewed; 1272 AA. AC A5WD09; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 07-OCT-2020, entry version 104. 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., Pitluck S., RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Kim E., Tiedje J., 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; Xref=Rhea:RHEA:11172, CC ChEBI:CHEBI:18608, ChEBI:CHEBI:57453, ChEBI:CHEBI:57844, CC ChEBI:CHEBI:58199; EC=2.1.1.13; CC Evidence={ECO:0000256|ARBA:ARBA00001700, CC ECO:0000256|PIRNR:PIRNR000381}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|ARBA:ARBA00001947, CC ECO:0000256|PIRNR:PIRNR000381, ECO:0000256|PROSITE-ProRule:PRU00333}; CC -!- COFACTOR: CC Name=methylcob(III)alamin; Xref=ChEBI:CHEBI:28115; CC Evidence={ECO:0000256|ARBA:ARBA00001956, CC ECO:0000256|PIRNR:PIRNR000381, ECO:0000256|PIRSR:PIRSR000381-2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo CC pathway; L-methionine from L-homocysteine (MetH route): step 1/1. CC {ECO:0000256|ARBA:ARBA00005178, ECO:0000256|PIRNR:PIRNR000381}. CC -!- DOMAIN: Modular enzyme with four functionally distinct domains. The CC isolated Hcy-binding domain catalyzes methyl transfer from free CC methylcobalamin to homocysteine. The Hcy-binding domain in association CC with the pterin-binding domain catalyzes the methylation of CC cob(I)alamin by methyltetrahydrofolate and the methylation of CC homocysteine. The B12-binding domain binds the cofactor. The AdoMet CC activation domain binds S-adenosyl-L-methionine. Under aerobic CC conditions cob(I)alamin can be converted to inactive cob(II)alamin. CC Reductive methylation by S-adenosyl-L-methionine and flavodoxin CC regenerates methylcobalamin. {ECO:0000256|PIRNR:PIRNR000381}. CC -!- SIMILARITY: Belongs to the vitamin-B12 dependent methionine synthase CC family. {ECO:0000256|ARBA:ARBA00010398}. 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; COG0646; Bacteria. DR eggNOG; COG1410; Bacteria. DR HOGENOM; CLU_004914_4_0_6; -. DR KO; K00548; -. DR OMA; ADCIAMS; -. 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:0032259; P:methylation; IEA:UniProtKB-KW. 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 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, KW ECO:0000256|PIRNR:PIRNR000381}; KW Cobalamin {ECO:0000256|ARBA:ARBA00022628, ECO:0000256|PIRNR:PIRNR000381, KW ECO:0000256|PIRSR:PIRSR000381-2}; KW Cobalt {ECO:0000256|ARBA:ARBA00023285, ECO:0000256|PIRNR:PIRNR000381, KW ECO:0000256|PIRSR:PIRSR000381-1}; Coiled coil {ECO:0000256|SAM:Coils}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRNR:PIRNR000381, ECO:0000256|PIRSR:PIRSR000381-1, KW ECO:0000256|PROSITE-ProRule:PRU00333}; KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167, KW ECO:0000256|PIRNR:PIRNR000381}; KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, KW ECO:0000256|PIRNR:PIRNR000381, ECO:0000256|PROSITE-ProRule:PRU00346, KW ECO:0000313|EMBL:ABQ93550.1}; Repeat {ECO:0000256|ARBA:ARBA00022737}; KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, KW ECO:0000256|PIRNR:PIRNR000381, ECO:0000256|PIRSR:PIRSR000381-2}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000381, KW ECO:0000256|PROSITE-ProRule:PRU00346, ECO:0000313|EMBL:ABQ93550.1}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR000381, KW ECO:0000256|PIRSR:PIRSR000381-1, ECO:0000256|PROSITE-ProRule:PRU00333}. FT DOMAIN 47..367 FT /note="Hcy-binding" FT /evidence="ECO:0000259|PROSITE:PS50970" FT DOMAIN 398..658 FT /note="Pterin-binding" FT /evidence="ECO:0000259|PROSITE:PS50972" FT DOMAIN 695..789 FT /note="B12-binding N-terminal" FT /evidence="ECO:0000259|PROSITE:PS51337" FT DOMAIN 791..927 FT /note="B12-binding" FT /evidence="ECO:0000259|PROSITE:PS51332" FT DOMAIN 943..1272 FT /note="AdoMet activation" FT /evidence="ECO:0000259|PROSITE:PS50974" FT REGION 1..29 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 879..880 FT /note="Cobalamin-binding" FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2" FT REGION 1238..1239 FT /note="S-adenosyl-L-methionine binding" FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2" FT COILED 923..943 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 7..21 FT /note="Polyampholyte" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT METAL 289 FT /note="Zinc" FT /evidence="ECO:0000256|PIRSR:PIRSR000381-1, FT ECO:0000256|PROSITE-ProRule:PRU00333" FT METAL 352 FT /note="Zinc" FT /evidence="ECO:0000256|PIRSR:PIRSR000381-1, FT ECO:0000256|PROSITE-ProRule:PRU00333" FT METAL 353 FT /note="Zinc" FT /evidence="ECO:0000256|PIRSR:PIRSR000381-1, FT ECO:0000256|PROSITE-ProRule:PRU00333" FT METAL 804 FT /note="Cobalt (cobalamin axial ligand)" FT /evidence="ECO:0000256|PIRSR:PIRSR000381-1" FT BINDING 849 FT /note="Cobalamin" FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2" FT BINDING 993 FT /note="S-adenosyl-L-methionine" FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2" FT BINDING 1183 FT /note="S-adenosyl-L-methionine; via carbonyl oxygen" FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2" FT BINDING 1187 FT /note="Cobalamin; via carbonyl oxygen" FT /evidence="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 //