ID Q664W6_YERPS Unreviewed; 1230 AA.
AC Q664W6;
DT 11-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 11-OCT-2004, sequence version 1.
DT 01-MAY-2013, entry version 65.
DE SubName: Full=5-Methyltetrahydrofolate--homocysteine methyltransferase;
DE EC=2.1.1.13;
GN Name=metH; OrderedLocusNames=YPTB3653;
OS Yersinia pseudotuberculosis serotype I (strain IP32953).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Yersinia.
OX NCBI_TaxID=273123;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP32953;
RX PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin L.V.,
RA Brubaker R.R., Fowler J., Hinnebusch B.J., Marceau M., Medigue C.,
RA Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA Derbise A., Hauser L.J., Garcia E.;
RT "Insights into the evolution of Yersinia pestis through whole-genome
RT comparison with Yersinia pseudotuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC -!- COFACTOR: Cobalamin (By similarity).
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DR EMBL; BX936398; CAH22891.1; -; Genomic_DNA.
DR RefSeq; YP_072134.1; NC_006155.1.
DR ProteinModelPortal; Q664W6; -.
DR SMR; Q664W6; 654-1230.
DR STRING; 273123.YPTB3653; -.
DR EnsemblBacteria; CAH22891; CAH22891; YPTB3653.
DR GeneID; 2956026; -.
DR KEGG; yps:YPTB3653; -.
DR PATRIC; 18646693; VBIYerPse22266_4386.
DR HOGENOM; HOG000251409; -.
DR KO; K00548; -.
DR OMA; VRKEFWG; -.
DR ProtClustDB; PRK09490; -.
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 PANTHER; PTHR21091:SF9; PTHR21091:SF9; 1.
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 837 838 Cobalamin-binding (By similarity).
FT REGION 1192 1193 S-adenosyl-L-methionine binding (By
FT similarity).
FT METAL 251 251 Zinc (By similarity).
FT METAL 314 314 Zinc (By similarity).
FT METAL 315 315 Zinc (By similarity).
FT METAL 762 762 Cobalt (cobalamin axial ligand) (By
FT similarity).
FT BINDING 949 949 S-adenosyl-L-methionine (By similarity).
FT BINDING 1137 1137 S-adenosyl-L-methionine; via carbonyl
FT oxygen (By similarity).
FT BINDING 1141 1141 Cobalamin; via carbonyl oxygen (By
FT similarity).
SQ SEQUENCE 1230 AA; 136022 MW; 58D685B9AB3A452A CRC64;
MDTVIDNKVK ELHQQLAQRI LVLDGGMGTM IQSYRLEEAD YRGARFADWA SDLKGNNDLL
VLSKPEVITA IHNAYLEAGA DILETNTFNS TSIAMADYQM ASLSAEINYE AARLARICAD
EWSARTPEKP RYVAGVLGPT NRTASISPKV NDPAFRNVSF DQLVEAYRES TRALIEGGVD
LIMIETVFDT LNAKAATFAV ESEFEAMGVL LPVMISGTIT DASGRTLSGQ TTEAFYNSLR
HVKPLSFGLN CALGPDELRQ YVAELSRISE YYVSAHPNAG LPNAFGEYDL EAKEMAEQIG
EWARAGFLNI VGGCCGTTPR HIAAMVNAVA GVPPRPLPDI PVACRLAGLE PLTIDANTLF
VNVGERTNVT GSARFKRLIK EEKYGEALDV ARQQVESGAQ IIDINMDEGM LDAEAAMVRF
LNLIAGEPDI ARVPIMIDSS RWDVIEKGLK CIQGKGIVNS ISMKEGVDAF IHHAKLVRRY
GAAMVVMAFD ETGQADTRAR KIEICRRAYK ILTETVGFPP EDIIFDPNIF AVATGIEEHN
NYAVDFIEAC ADIKAELPHA LISGGVSNVS FSFRGNDPVR EAIHAVFLYY AIRNGMDMGI
VNAGQLAIYD DLSDELRDAV EDVILNRRDD STERLLDLAE KYRDSKSGEV AIQQAEWRGW
PVVKRLEYSL VKGITEFIEL DTEEARQQAD RPIEVIEGPL MSGMNVVGDL FGEGKMFLPQ
VVKSARVMKQ AVAYLEPYIE ASKQKGTTAG KILLATVKGD VHDIGKNIVG VVLQCNNYEI
IDLGVMVPTE KILRTAREEK VDIIGLSGLI TPSLDEMVNV AKEMERQGFT LPLLIGGATT
SKAHTAVKIE QNYSGSTTYV SNASRSVGVV SALLSDTQRE AFVAKTRKEY ETVRIQHARK
KPRTPPVSLQ AARNNPTVID WENYTPPVAH KLGVQVVEAS IETLRNYIDW TPFFMTWSLA
GKYPRILEDE VVGEEAKRLL ADANALLDKL SAEDLLHPKG VVGLFPANSV GDDIEIYRDE
RRDEVLAISY HLRQQTEKTD FPNYCLADYV APKSSGKADY FGAFAVTGGL EEDALADAYD
AQHDDYNKIM IKALSDRLAE AFAEYLHERV RKVYWGFAPN ENLSNEELVR ENYQGIRPAP
GYPACPEHTE KGQIWQLLDV ETHTGMKLTE SYAMWPGASV SGWYFSHPDS KYFAVAQIQR
DQVEDYAARK GMPTAEVERW LAPNLGYDAD
//
