MULTISPECIES: methionine synthase [Escherichia].

LOCUS       WP_000096047            1227 aa            linear   BCT 27-MAR-2023
ACCESSION   WP_000096047
VERSION     WP_000096047.1
KEYWORDS    RefSeq.
SOURCE      Escherichia
  ORGANISM  Escherichia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 1227)
  AUTHORS   Dixon,M.M., Huang,S., Matthews,R.G. and Ludwig,M.
  TITLE     The structure of the C-terminal domain of methionine synthase:
            presenting S-adenosylmethionine for reductive methylation of B12
  JOURNAL   Structure 4 (11), 1263-1275 (1996)
   PUBMED   8939751
REFERENCE   2  (residues 1 to 1227)
  AUTHORS   Drummond,J.T., Loo,R.R. and Matthews,R.G.
  TITLE     Electrospray mass spectrometric analysis of the domains of a large
            enzyme: observation of the occupied cobalamin-binding domain and
            redefinition of the carboxyl terminus of methionine synthase
  JOURNAL   Biochemistry 32 (36), 9282-9289 (1993)
   PUBMED   8369296
REFERENCE   3  (residues 1 to 1227)
  AUTHORS   Luschinsky,C.L., Drummond,J.T., Matthews,R.G. and Ludwig,M.L.
  TITLE     Crystallization and preliminary X-ray diffraction studies of the
            cobalamin-binding domain of methionine synthase from Escherichia
            coli
  JOURNAL   J Mol Biol 225 (2), 557-560 (1992)
   PUBMED   1593636
REFERENCE   4  (residues 1 to 1227)
  AUTHORS   Banerjee,R.V., Johnston,N.L., Sobeski,J.K., Datta,P. and
            Matthews,R.G.
  TITLE     Cloning and sequence analysis of the Escherichia coli metH gene
            encoding cobalamin-dependent methionine synthase and isolation of a
            tryptic fragment containing the cobalamin-binding domain
  JOURNAL   J Biol Chem 264 (23), 13888-13895 (1989)
   PUBMED   2668277
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF007024.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09490
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1227
                     /organism="Escherichia"
                     /db_xref="taxon:561"
     gene            1..1227
                     /gene="metH"
     Protein         1..1227
                     /product="methionine synthase"
                     /EC_number="2.1.1.13"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0008705 - methionine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0031419 - cobalamin binding [Evidence
                     IEA]"
                     /GO_process="GO:0009086 - methionine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=135910
     Region          1..1223
                     /region_name="metH"
                     /note="B12-dependent methionine synthase; Provisional;
                     PRK09490"
                     /db_xref="CDD:236539"
ORIGIN      
        1 msskveqlra qlnerilvld ggmgtmiqsy rlneadfrge rfadwpcdlk gnndllvlsk
       61 peviaaihna yfeagadiie tntfnsttia madyqmesls aeinfaaakl aracadewta
      121 rtpekpryva gvlgptnrta sispdvndpa frnitfdqlv aayrestkal veggadlili
      181 etvfdtlnak aavfavktef ealgvelpim isgtitdasg rtlsgqttea fynslrhaea
      241 ltfglncalg pdelrqyvqe lsriaecyvt ahpnaglpna fgeydldadt makqirewaq
      301 agflnivggc cgttpqhiaa msraveglap rklpeipvac rlsgleplni gddslfvnvg
      361 ertnvtgsak fkrlikeeky sealdvarqq vengaqiidi nmdegmldae aamvrflnli
      421 agepdiarvp imidsskwev iekglkciqg kgivnsismk egvdafihha kllrrygaav
      481 vvmafdeqgq adtrarkiei crraykilte evgfppedii fdpnifavat gieehnnyaq
      541 dfigacedik relphalisg gvsnvsfsfr gndpvreaih avflyyairn gmdmgivnag
      601 qlaiyddlpa elrdavedvi lnrrddgter llelaekyrg sktddtanaq qaewrswevn
      661 krleyslvkg itefieqdte earqqatrpi eviegplmdg mnvvgdlfge gkmflpqvvk
      721 sarvmkqava ylepfieask eqgktngkmv iatvkgdvhd igknivgvvl qcnnyeivdl
      781 gvmvpaekil rtakevnadl iglsglitps ldemvnvake merqgftipl liggattska
      841 htavkieqny sgptvyvqna srtvgvvaal lsdtqrddfv artrkeyetv riqhgrkkpr
      901 tppvtleaar dndfafdwqa ytppvahrlg vqeveasiet lrnyidwtpf fmtwslagky
      961 priledevvg veaqrlfkda ndmldklsae ktlnprgvvg lfpanrvgdd ieiyrdetrt
     1021 hvinvshhlr qqtektgfan ycladfvapk lsgkadyiga favtggleed aladafeaqh
     1081 ddynkimvka ladrlaeafa eylhervrkv ywgyapnenl sneelireny qgirpapgyp
     1141 acpehtekat iwellevekh tgmkltesfa mwpgasvsgw yfshpdskyy avaqiqrdqv
     1201 edyarrkgms vsdverwlap nlgydad