(data stored in SCRATCH zone)

SWISSPROT: C1ASR2_RHOOB

ID   C1ASR2_RHOOB            Unreviewed;      1189 AA.
AC   C1ASR2;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   30-AUG-2017, entry version 66.
DE   SubName: Full=Methionine synthase {ECO:0000313|EMBL:BAH48844.1};
DE            EC=2.1.1.13 {ECO:0000313|EMBL:BAH48844.1};
GN   Name=metH {ECO:0000313|EMBL:BAH48844.1};
GN   OrderedLocusNames=ROP_05970 {ECO:0000313|EMBL:BAH48844.1};
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH48844.1, ECO:0000313|Proteomes:UP000002212};
RN   [1] {ECO:0000313|EMBL:BAH48844.1, ECO:0000313|Proteomes:UP000002212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:BAH48844.1,
RC   ECO:0000313|Proteomes:UP000002212};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus
RT   erythropolis PR4 and Rhodococcus opacus B4.";
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; AP011115; BAH48844.1; -; Genomic_DNA.
DR   RefSeq; WP_012687849.1; NC_012522.1.
DR   STRING; 632772.ROP_05970; -.
DR   EnsemblBacteria; BAH48844; BAH48844; ROP_05970.
DR   KEGG; rop:ROP_05970; -.
DR   PATRIC; fig|632772.20.peg.655; -.
DR   eggNOG; ENOG4105C3R; Bacteria.
DR   eggNOG; COG0646; LUCA.
DR   eggNOG; COG1410; LUCA.
DR   HOGENOM; HOG000251408; -.
DR   KO; K00548; -.
DR   OMA; KYPRPLN; -.
DR   OrthoDB; POG091H030I; -.
DR   Proteomes; UP000002212; 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; -; 1.
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; C1ASR2.
DR   SWISS-2DPAGE; C1ASR2.
KW   Cobalamin {ECO:0000256|PIRSR:PIRSR000381-2};
KW   Cobalt {ECO:0000256|PIRSR:PIRSR000381-1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002212};
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:BAH48844.1};
KW   S-adenosyl-L-methionine {ECO:0000256|PIRSR:PIRSR000381-2};
KW   Transferase {ECO:0000256|PROSITE-ProRule:PRU00346,
KW   ECO:0000313|EMBL:BAH48844.1};
KW   Zinc {ECO:0000256|PIRSR:PIRSR000381-1, ECO:0000256|PROSITE-
KW   ProRule:PRU00333}.
FT   DOMAIN        6    310       Hcy-binding. {ECO:0000259|PROSITE:
FT                                PS50970}.
FT   DOMAIN      341    604       Pterin-binding. {ECO:0000259|PROSITE:
FT                                PS50972}.
FT   DOMAIN      633    726       B12-binding N-terminal.
FT                                {ECO:0000259|PROSITE:PS51337}.
FT   DOMAIN      726    863       B12-binding. {ECO:0000259|PROSITE:
FT                                PS51332}.
FT   DOMAIN      890   1189       AdoMet activation. {ECO:0000259|PROSITE:
FT                                PS50974}.
FT   REGION      816    817       Cobalamin-binding. {ECO:0000256|PIRSR:
FT                                PIRSR000381-2}.
FT   REGION     1186   1187       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|PIRSR:PIRSR000381-2}.
FT   METAL       229    229       Zinc. {ECO:0000256|PIRSR:PIRSR000381-1,
FT                                ECO:0000256|PROSITE-ProRule:PRU00333}.
FT   METAL       295    295       Zinc. {ECO:0000256|PIRSR:PIRSR000381-1,
FT                                ECO:0000256|PROSITE-ProRule:PRU00333}.
FT   METAL       296    296       Zinc. {ECO:0000256|PIRSR:PIRSR000381-1,
FT                                ECO:0000256|PROSITE-ProRule:PRU00333}.
FT   METAL       739    739       Cobalt (cobalamin axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR000381-1}.
FT   BINDING     784    784       Cobalamin. {ECO:0000256|PIRSR:
FT                                PIRSR000381-2}.
FT   BINDING     937    937       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PIRSR:PIRSR000381-2}.
FT   BINDING    1132   1132       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|PIRSR:PIRSR000381-
FT                                2}.
FT   BINDING    1136   1136       Cobalamin; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR000381-2}.
SQ   SEQUENCE   1189 AA;  129561 MW;  EFEBD199B456CE68 CRC64;
     MSAPFHSALL DALNQRVVIG DGAMGTMLQA ADLTLDDFLG LEGCNEILND TRPDVLKEIH
     RAYFEAGADA VETNTFGCNL PNLADYDISD RIRELAEKGT RLAREVADEM GPGRDGMGRF
     VLGSMGPGTK LPTLGHAPFA ILRDAYAEAA MGMIDGGADA ILVETCQDLL QVKAAILGSQ
     RAMETLGSRL PIITHVTVET TGTMLLGSEI GAALTALEPL GIDMIGLNCA TGPAEMSEHL
     RHLSKYSSLP VSVMPNAGLP QLGPNGAEYP LTAEELAEAL SGFVTEFGLG LVGGCCGTTP
     EHIRQVADAV RLVEKAARNP VHESGTSSLY TAVPFEQDAS ILMIGERTNS NGSKAFREAM
     IAEDYQKCLD IAKDQTRDGA HMLDLNVDYV GRDGAADMAA LASRFATSST LPIMLDSTEP
     AVLQAGLEHL GGRCAVNSVN YEDGDGPDSR FQKIMRLVKE HGAAVVALTI DEEGQARTAE
     HKVRIAERLL EDITVNWGLD ESDIIIDALT FPISTGQEEV RRDGIETIEA IRELKKRHPR
     VHFTLGVSNI SFGLNPAARQ VLNSVFLHEC TEAGLDTAIV HASKILPMAR IPDEQRETAL
     DLVYDRRREG YDPLQKLMEL FEGVSAASAR ESRAQELAAL PLFERLERRI VDGERNGLDD
     DLTAAMEEKP PLAIINETLL SGMKTVGELF GSGQMQLPFV LQSAEVMKAA VAYLEPHMEA
     TDEDGKGRIV IATVKGDVHD IGKNLVDIIL SNNGYDVVNL GIKQPIATIL DAAIEQKADV
     IGMSGLLVKS TVVMKDNLQE LNAKGVAEKF PVLLGGAALT RSYVENDLAE VYEGDVSYAR
     DAFEGLHKMD EIMAVKRGGA PDPDSPEAIA AREKAAERKA RHERSKRIAE KRKAAEVPVE
     LPERSDVATD IAVPSPPFWG NRIVKGVSLS DYSGLLDERA LFLGQWGLRG QRSGDGPTYE
     ELVETEGRPR LRYWLDRLST EGILAHAAVV YGYFPAVSEG DDVVVLTDPT PDAEERFRFT
     FPRQHRDRFL CVADFVRSRT EAKETGQVDV FPMQLVTMGQ PIADFANELF AANAYRDYLE
     VHGIGVQLTE SLAEYWHQRV REELVLPGGH NVGEQDPSEV SGFFDLAYRG ARYSFGYGAC
     PNLEDRAKMV ALLEPERIGV KLSEELQLHP EQSTDAFVLH HPEAKYFNV
//

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