(data stored in SCRATCH zone)

SWISSPROT: C5B6Y7_EDWI9

ID   C5B6Y7_EDWI9            Unreviewed;      1227 AA.
AC   C5B6Y7;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   30-AUG-2017, entry version 59.
DE   SubName: Full=Methionine synthase, putative {ECO:0000313|EMBL:ACR67449.1};
DE            EC=2.1.1.13 {ECO:0000313|EMBL:ACR67449.1};
GN   OrderedLocusNames=NT01EI_0206 {ECO:0000313|EMBL:ACR67449.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67449.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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=methyl(III)cobalamin; Xref=ChEBI:CHEBI:28115;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000381-2};
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DR   EMBL; CP001600; ACR67449.1; -; Genomic_DNA.
DR   STRING; 634503.NT01EI_0206; -.
DR   EnsemblBacteria; ACR67449; ACR67449; NT01EI_0206.
DR   KEGG; eic:NT01EI_0206; -.
DR   eggNOG; ENOG4105C3R; Bacteria.
DR   eggNOG; COG0646; LUCA.
DR   eggNOG; COG1410; LUCA.
DR   HOGENOM; HOG000251409; -.
DR   KO; K00548; -.
DR   OMA; KYPRPLN; -.
DR   OrthoDB; POG091H030I; -.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR   GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; -; 2.
DR   Gene3D; 3.20.20.330; -; 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; IPR033706; Met_synthase_B12-bd.
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;
DR   PRODOM; C5B6Y7.
DR   SWISS-2DPAGE; C5B6Y7.
KW   Cobalamin {ECO:0000256|PIRSR:PIRSR000381-2};
KW   Cobalt {ECO:0000256|PIRSR:PIRSR000381-1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000381-1, ECO:0000256|PROSITE-
KW   ProRule:PRU00333};
KW   Methyltransferase {ECO:0000256|PROSITE-ProRule:PRU00346,
KW   ECO:0000313|EMBL:ACR67449.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485};
KW   S-adenosyl-L-methionine {ECO:0000256|PIRSR:PIRSR000381-2};
KW   Transferase {ECO:0000256|PROSITE-ProRule:PRU00346,
KW   ECO:0000313|EMBL:ACR67449.1};
KW   Zinc {ECO:0000256|PIRSR:PIRSR000381-1, ECO:0000256|PROSITE-
KW   ProRule:PRU00333}.
FT   DOMAIN        5    325       Hcy-binding. {ECO:0000259|PROSITE:
FT                                PS50970}.
FT   DOMAIN      356    620       Pterin-binding. {ECO:0000259|PROSITE:
FT                                PS50972}.
FT   DOMAIN      650    744       B12-binding N-terminal.
FT                                {ECO:0000259|PROSITE:PS51337}.
FT   DOMAIN      746    881       B12-binding. {ECO:0000259|PROSITE:
FT                                PS51332}.
FT   DOMAIN      897   1227       AdoMet activation. {ECO:0000259|PROSITE:
FT                                PS50974}.
FT   REGION      834    835       Cobalamin-binding. {ECO:0000256|PIRSR:
FT                                PIRSR000381-2}.
FT   REGION     1189   1190       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|PIRSR:PIRSR000381-2}.
FT   METAL       247    247       Zinc. {ECO:0000256|PIRSR:PIRSR000381-1,
FT                                ECO:0000256|PROSITE-ProRule:PRU00333}.
FT   METAL       310    310       Zinc. {ECO:0000256|PIRSR:PIRSR000381-1,
FT                                ECO:0000256|PROSITE-ProRule:PRU00333}.
FT   METAL       311    311       Zinc. {ECO:0000256|PIRSR:PIRSR000381-1,
FT                                ECO:0000256|PROSITE-ProRule:PRU00333}.
FT   METAL       759    759       Cobalt (cobalamin axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR000381-1}.
FT   BINDING     804    804       Cobalamin. {ECO:0000256|PIRSR:
FT                                PIRSR000381-2}.
FT   BINDING     946    946       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PIRSR:PIRSR000381-2}.
FT   BINDING    1134   1134       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|PIRSR:PIRSR000381-
FT                                2}.
FT   BINDING    1138   1138       Cobalamin; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR000381-2}.
SQ   SEQUENCE   1227 AA;  134310 MW;  BD89282560F6C723 CRC64;
     MNTTCERLRR RLDKRILVLD GGMGTMIQRY GLSEQDFRAE RFVDWPCDLK GNNDLLALTR
     PDIISAIHYA YLEAGADILE TNTFNATRIA MADYRMEALA PEINYRAASL ARACADEWTA
     RTPHQPRFVA GVLGPTNRTA SISPEVNDPA CRNITFDQLV AAYRESARAL IEGGVDLLMI
     ETVFDTLNAK AAVYALECEF AALGVTLPVM ISGTITDASG RTLSGQTTEA FYNALRHARP
     LSFGLNCALG PEDLRQYVAE LSRVAECHVS AHPNAGLPNA FGEYDLSPQA MAQQIAEWAR
     AGYLNIVGGC CGTTPEHIAA ISRAVQGIAP RALPALPVAC RLSGLEPLTI DETSLFVNVG
     ERTNVTGSAK FKRLIKENKY DDALDVARQQ VASGAQIIDI NMDEGMLDAE AAMVRFLNLI
     AGEPDIARVP LMIDSSRWSV IEAGLKCIQG KGVVNSLSLK EGEANFLQHA RQVRRFGAAL
     VVMAFDEQGQ ADTLARKVAI CRRAYQLLTE RIGFPPEDII FDPNIFAVAT GIEEHSNYAV
     DFIAACAEIK AQLPHALISG GVSNVSFSFR GNEAVREAIH AVFLYHAIRH GMDMGIVNAG
     QLAIYDDLPD DLRTAAEAVI LNQGSDATDR LLALAERYRD SQGSTQAEGQ QAEWRSWPVA
     QRLEYALVKG IGEFIAQDTE AARLEADRPI AVIEGPLMAG MNRVGDLFGD GKMFLPQVVK
     SARVMKQAVA YLSPFIEASK QRGSSAGKVL LATVKGDVHD IGKNIVGVVL QCNNYEIIDL
     GVMVPAERIL RVAREERVDI IGLSGLITPS LDEMVNVASE MERQGFTLPL LIGGATTSKA
     HTAVKIAPAY GGPTVYVQNA SRTVGVVAAL LSEAQRGPFI ERTRREYEAA RAQHGRQTPR
     TPPVTLAQAR ANGVVTDWSA CPPPVPQRLG VQTMQPGIAR LRDYIDWTPF FLTWSLAGKY
     PRILQDKVVG EEARRLLADA NGLLDRLEAS GSLTPRGVFG LFAANRRGDD VLIYRDESRR
     EVLAVSHHLR QQSDKSAGPN YCLADFIAAA DEGIADYIGA FAVTGGLEEE ALAQAFDAQH
     DDYHKIMVKA LADRLAEAFA EYLHQQVRKV HWGYAADEAL DNEQLIRENY RGIRPAPGYP
     ACPEHSEKAT LWRLLDVERH TGMRLTESYA MWPGASVSGW YFSHPHSKYF TVARVQRDQV
     ADYAARKGIP LAEAERWLAP NLGYEVE
//

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