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Database: UniProt/TrEMBL
Entry: D0LDR3_GORB4
LinkDB: D0LDR3_GORB4
Original site: D0LDR3_GORB4 
ID   D0LDR3_GORB4            Unreviewed;      1199 AA.
AC   D0LDR3;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   09-JUL-2014, entry version 36.
DE   SubName: Full=Methionine synthase;
DE            EC=2.1.1.13;
GN   OrderedLocusNames=Gbro_2445;
OS   Gordonia bronchialis (strain ATCC 25592 / DSM 43247 / JCM 3198 / NCTC
OS   10667) (Rhodococcus bronchialis).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Gordoniaceae; Gordonia.
OX   NCBI_TaxID=526226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25592 / DSM 43247 / JCM 3198 / NCTC 10667;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
RA   Ivanova N., Ovchinnikova G., Saunders E., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA   Hugenholtz P., Woyke T., Wu D., Jando M., Schneider S., Goeker M.,
RA   Klenk H.-P., Eisen J.A.;
RT   "The complete chromosome of Gordonia bronchialis DSM 43247.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- COFACTOR: Cobalamin (By similarity).
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DR   EMBL; CP001802; ACY21686.1; -; Genomic_DNA.
DR   RefSeq; YP_003273579.1; NC_013441.1.
DR   STRING; 526226.Gbro_2445; -.
DR   EnsemblBacteria; ACY21686; ACY21686; Gbro_2445.
DR   GeneID; 8551809; -.
DR   KEGG; gbr:Gbro_2445; -.
DR   PATRIC; 32184503; VBIGorBro114338_2502.
DR   eggNOG; COG1410; -.
DR   HOGENOM; HOG000251408; -.
DR   KO; K00548; -.
DR   OMA; DAFMAVK; -.
DR   OrthoDB; EOG6091CH; -.
DR   BioCyc; GBRO526226:GHJF-2478-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      827    828       Cobalamin-binding (By similarity).
FT   REGION     1196   1197       S-adenosyl-L-methionine binding (By
FT                                similarity).
FT   METAL       240    240       Zinc (By similarity){EA5}.
FT   METAL       306    306       Zinc (By similarity){EA5}.
FT   METAL       307    307       Zinc (By similarity){EA5}.
FT   METAL       750    750       Cobalt (cobalamin axial ligand) (By
FT                                similarity){EA5}.
FT   BINDING     948    948       S-adenosyl-L-methionine (By
FT                                similarity){EA2}.
FT   BINDING    1142   1142       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen (By similarity){EA2}.
FT   BINDING    1146   1146       Cobalamin; via carbonyl oxygen (By
FT                                similarity){EA2}.
SQ   SEQUENCE   1199 AA;  130734 MW;  4F71BBF1480F805E CRC64;
     MSSVSRPDHS TDPADFDTTF MSAMSRRVLI GDGAMGTMLQ AADLTLDDFN GLEGCNEILN
     DARPDVLEGI HRAYFEAGAD AVETNTFGCN LSNLGDYDIA DRIRELAYKG TGIARGVADE
     MGPTANGTDR FVLGSIGPGT KLPSLGHTTF AVIRDAYFEC VAGMLDGGAD AILIETSQDL
     LQVKAAVVAA RRAMDKLGRR IPIISHVTVE TTGTMLLGSE IGAALTAIEP LGVDMIGLNC
     ATGPAEMSEH LRYLSRHARI PVSVMPNAGL PVLGPNGAEY PLSPEELAQA LHGFVAEFGL
     DFVGGCCGTT PEHIRQVAEA VHGATPAART PEHASETSSL YTAVPFDQDA SFLVIGERTN
     TNGSKAFREA MIAGDYQRCL DIAKDQTRDG AHMLDLNVDY VGRDGAVDMT ALASRFATSS
     TLPIMLDSTE PEVIRAGLET LGGRCAVNSV NYEDGDGPNS RFTRIMQLVV EHGAAVVALT
     IDEEGQARTA DWKVRIAERL IADITGNWGL AEEDIIIDAL TFPISTGQEE VRRDGIETIE
     AIRRIHEAHP EVHFTLGISN ISFGLNPAAR QVLNSVFLHE CVQAGLDTAI VHASKILPMA
     RIPEEHRKVA LDLVYDRRAP GYDPLQKLME LFEGVSAASA RESRAAELAK LPLFERLERR
     IVDGERNGLE DDLDEAMTTV PPLKIINETL LSGMKTVGEL FGSGQMQLPF VLQSAEVMKT
     AVAHLEPHME STGEDGKGRI VLATVKGDVH DIGKNLVDII LSNNGYEVVN IGIKQPITNI
     LDVAADKKVD VIGMSGLLVK STVVMKENLE EINARGLADE YPVLLGGAAL TRSYVENDLS
     ETYEGDVHYA RDAFEGLRLM DEIMATKRGE GPDPDSPEAI AAAEKAAERK ARHDRSKRIA
     AKRKAAEEPV EVPARSDVAA DNDIPAPPFW GTRIVKGVPV ADYLQLLDER ALFLGQWGLR
     GARGGDGPSY EDLVESEGRP RLRYWIDRLA TEGILQHAAV VYGYFPAVSD GDTVHVLTEP
     RPDAPVRYSF GFPRQQRSRF LCIADFIRSR EDAIRDGHVD VLPFQLVTMG QPIADFANEL
     FAADAYRDYL EVHGIGVQLT EALAEYWHQR VRSELRFGER TMDSEDPDEA QGFFDLEYRG
     ARFSFGYGAC PDLDDRAKMM ELLQPERIGV HLSEELQLHP EQSTDAFVLH HPEAKYFNT
//
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