ID D0LDR3_GORB4 Unreviewed; 1199 AA.
AC D0LDR3;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 01-MAY-2013, entry version 30.
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; NGSKAFR; -.
DR BioCyc; GBRO526226:GHJF-2558-MONOMER; -.
DR GO; GO:0005622; C:intracellular; IEA:InterPro.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0008898; F:homocysteine S-methyltransferase activity; IEA:InterPro.
DR GO; GO:0008705; F:methionine synthase activity; IEA:EC.
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; SSF52242; Cbl-bd; 1.
DR SUPFAM; SSF51717; DHP_synth_like; 1.
DR SUPFAM; SSF56507; Met_synth_B12; 1.
DR SUPFAM; SSF47644; Met_synth_Cbl-bd; 1.
DR SUPFAM; SSF82282; S_methyl_trans; 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).
FT METAL 306 306 Zinc (By similarity).
FT METAL 307 307 Zinc (By similarity).
FT METAL 750 750 Cobalt (cobalamin axial ligand) (By
FT similarity).
FT BINDING 948 948 S-adenosyl-L-methionine (By similarity).
FT BINDING 1142 1142 S-adenosyl-L-methionine; via carbonyl
FT oxygen (By similarity).
FT BINDING 1146 1146 Cobalamin; via carbonyl oxygen (By
FT similarity).
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
//
