ID B1WZ63_CYAA5 Unreviewed; 1193 AA.
AC B1WZ63;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 01-MAY-2013, entry version 40.
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; NGSKAFR; -.
DR ProtClustDB; CLSK893539; -.
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: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; 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 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).
FT METAL 294 294 Zinc (By similarity).
FT METAL 295 295 Zinc (By similarity).
FT METAL 739 739 Cobalt (cobalamin axial ligand) (By
FT similarity).
FT BINDING 943 943 S-adenosyl-L-methionine (By similarity).
FT BINDING 1136 1136 S-adenosyl-L-methionine; via carbonyl
FT oxygen (By similarity).
FT BINDING 1140 1140 Cobalamin; via carbonyl oxygen (By
FT similarity).
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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