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Database: UniProt/TrEMBL
Entry: B7M7S5_ECO8A
LinkDB: B7M7S5_ECO8A
Original site: B7M7S5_ECO8A 
ID   B7M7S5_ECO8A            Unreviewed;      1227 AA.
AC   B7M7S5;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   09-JUL-2014, entry version 37.
DE   SubName: Full=Homocysteine-N5-methyltetrahydrofolate transmethylase, B12-dependent;
DE            EC=2.1.1.13;
GN   Name=metH; OrderedLocusNames=ECIAI1_4241;
OS   Escherichia coli O8 (strain IAI1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585034;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IAI1;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A.,
RA   Chiapello H., Clermont O., Cruveiller S., Danchin A., Diard M.,
RA   Dossat C., Karoui M.E., Frapy E., Garry L., Ghigo J.M., Gilles A.M.,
RA   Johnson J., Le Bouguenec C., Lescat M., Mangenot S.,
RA   Martinez-Jehanne V., Matic I., Nassif X., Oztas S., Petit M.A.,
RA   Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J., Vacherie B.,
RA   Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- COFACTOR: Cobalamin (By similarity).
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DR   EMBL; CU928160; CAR00991.1; -; Genomic_DNA.
DR   RefSeq; YP_002389483.1; NC_011741.1.
DR   ProteinModelPortal; B7M7S5; -.
DR   SMR; B7M7S5; 651-1227.
DR   STRING; 585034.ECIAI1_4241; -.
DR   EnsemblBacteria; CAR00991; CAR00991; ECIAI1_4241.
DR   GeneID; 7126044; -.
DR   KEGG; ecr:ECIAI1_4241; -.
DR   PATRIC; 18327701; VBIEscCol26572_4114.
DR   eggNOG; COG1410; -.
DR   HOGENOM; HOG000251409; -.
DR   KO; K00548; -.
DR   OMA; LTEHYAM; -.
DR   OrthoDB; EOG6091CH; -.
DR   BioCyc; ECOL585034:GJ84-4251-MONOMER; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
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; IPR011822; MetH.
DR   InterPro; IPR000489; Pterin-binding.
DR   InterPro; IPR003726; S_MeTrfase.
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   3: Inferred from homology;
KW   Cobalamin; Cobalt; Complete proteome; Metal-binding;
KW   Methyltransferase; S-adenosyl-L-methionine; Transferase; Zinc.
FT   REGION      834    835       Cobalamin-binding (By similarity).
FT   REGION     1189   1190       S-adenosyl-L-methionine binding (By
FT                                similarity).
FT   METAL       247    247       Zinc (By similarity).
FT   METAL       310    310       Zinc (By similarity).
FT   METAL       311    311       Zinc (By similarity).
FT   METAL       759    759       Cobalt (cobalamin axial ligand) (By
FT                                similarity).
FT   BINDING     946    946       S-adenosyl-L-methionine (By
FT                                similarity){EA8}.
FT   BINDING    1134   1134       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen (By similarity){EA8}.
FT   BINDING    1138   1138       Cobalamin; via carbonyl oxygen (By
FT                                similarity){EA8}.
SQ   SEQUENCE   1227 AA;  135969 MW;  31A0CAA1E9127CD9 CRC64;
     MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK
     PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA
     RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDGLV AAYRESTKAL VEGGADLILI
     ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA
     LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ
     AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG
     ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI
     AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV
     VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ
     DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG
     QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN
     KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK
     SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL
     GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA
     HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR
     TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY
     PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT
     HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH
     DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP
     ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV
     EDYARRKGMS VSDVERWLAP NLGYDAD
//
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