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Database: UniProt/TrEMBL
Entry: B1WZ63_CYAA5
LinkDB: B1WZ63_CYAA5
Original site: B1WZ63_CYAA5 
ID   B1WZ63_CYAA5            Unreviewed;      1193 AA.
AC   B1WZ63;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   09-JUL-2014, entry version 48.
DE   SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase;
GN   Name=metH; OrderedLocusNames=cce_0077;
OS   Cyanothece sp. (strain ATCC 51142).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC   Cyanothece.
OX   NCBI_TaxID=43989;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51142;
RX   PubMed=18812508; DOI=10.1073/pnas.0805418105;
RA   Welsh E.A., Liberton M., Stockel J., Loh T., Elvitigala T., Wang C.,
RA   Wollam A., Fulton R.S., Clifton S.W., Jacobs J.M., Aurora R.,
RA   Ghosh B.K., Sherman L.A., Smith R.D., Wilson R.K., Pakrasi H.B.;
RT   "The genome of Cyanothece 51142, a unicellular diazotrophic
RT   cyanobacterium important in the marine nitrogen cycle.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:15094-15099(2008).
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- COFACTOR: Cobalamin (By similarity).
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DR   EMBL; CP000806; ACB49429.1; -; Genomic_DNA.
DR   RefSeq; YP_001801495.1; NC_010546.1.
DR   ProteinModelPortal; B1WZ63; -.
DR   STRING; 43989.cce_0077; -.
DR   EnsemblBacteria; ACB49429; ACB49429; cce_0077.
DR   GeneID; 6167043; -.
DR   KEGG; cyt:cce_0077; -.
DR   PATRIC; 21538622; VBICyaSp130209_0162.
DR   eggNOG; COG1410; -.
DR   HOGENOM; HOG000251408; -.
DR   KO; K00548; -.
DR   OMA; LTEHYAM; -.
DR   OrthoDB; EOG6091CH; -.
DR   BioCyc; CSP43989:GKC8-80-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:InterPro.
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      814    815       Cobalamin-binding (By similarity).
FT   REGION     1190   1191       S-adenosyl-L-methionine binding (By
FT                                similarity).
FT   METAL       228    228       Zinc (By similarity){EA8}.
FT   METAL       294    294       Zinc (By similarity){EA8}.
FT   METAL       295    295       Zinc (By similarity){EA8}.
FT   METAL       739    739       Cobalt (cobalamin axial ligand) (By
FT                                similarity){EA8}.
FT   BINDING     943    943       S-adenosyl-L-methionine (By
FT                                similarity){EA2}.
FT   BINDING    1136   1136       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen (By similarity){EA2}.
FT   BINDING    1140   1140       Cobalamin; via carbonyl oxygen (By
FT                                similarity){EA2}.
SQ   SEQUENCE   1193 AA;  133169 MW;  97F5FBE651A345B6 CRC64;
     MNSTFLNHLN SPKRPVLVFD GATGTSLQSQ NLTADDFGGP EYEGCNEYLV HTKPEAVEKV
     HRGFLEVGAD VIETDTFGGT SIVLAEYDLA DKAYYLNKKA AEIAKKMAAE YSTPEKPRFV
     AGSMGPGTKL PTLGHIDFDT LRDAYIEQAE GLYDGGADLL IIETCQDVLQ IKAALNAVEA
     VFEKKRNRLP IMVSITMETM GTMLVGTEIS AALAILEPYK IDILGLNCAT GPEQMKEHIK
     YLSEHSPFIV SCIPNAGLPE NVGGQAHYRL TPIELKMALM HFIEDLGVQI IGGCCGTRPD
     HIKALSELSQ DLTPKERHPD YEPSAASIYS TQPYIQDNSF LIVGERLNAS GSKKCRQLLD
     AEDWDSLVSL AKSQVKEGAH VLDVNVDYVG RDGVRDMHEL ASRLVNNITL PLMLDSTEWQ
     KMESGLKVAG GKCILNSTNY EDGEERFLKV LELAKKYGAG VVVGTIDEEG MGRTADKKFE
     IAKRAYNAAI DYGIPAHEIF FDPLALPIST GIEEDRENGK ATVEAIKRIR EELPGCHIIL
     GISNISFGLN PAARQVLNSV FLYESMQVGL DGAIVSASKI LPLVKIEEDH QKVCRDLIYD
     RREFDGDICT YDPLTKLTEL FAGKTTKKDP SKTASLPIEE RLKQHIIDGE RLGLEDALSE
     ALKQYPPLDI INVFLLDGMK TVGELFGSGQ MQLPFVLQSA QTMKAAVAYL EPFMDKEEGE
     ENDSGKGKFL IATVKGDVHD IGKNLVDIIL SNNGYKVINL GIKQPVENII QAYEEHQPDC
     IAMSGLLVKS TAFMKDNLEV FNERGIDVPV ILGGAALTPK FVYEDCQNTY KGKVVYGKDA
     FSDLHFMDKL MPAKSAENWD NLQGFLGEFT DNNSLFQEER GEKAAEKATE KNGKSSTQET
     PTVIDTKRSE AVEILEPATP PFWGTKILKS NEFDLNEIFW YLDLQALIAG QWQFRKPKDQ
     SREEYEAFLA EKVYPILEEW KQKVVTENLL HPTVIYGYFP CQSQDNSLLV YDPETIRNAN
     NKIPEDLDPI WKIDFPRQKS GRRLCIADFF SPKESGKIDV FPMQAVTVGD IATEYAQKLF
     AANDYTNYLY YHGMAVQTAE ALAEWTHAKI RRELGFADKE PDNIREMLQQ HYQGSRYSFG
     YPACPNIQDQ YKQLEVMGCD RINMYMDESE QIYPEQSTTA IIAYHPVAKY FSA
//
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