(data stored in ACNUC9543 zone)

SWISSPROT: A0A0E1NU22_YERPA

ID   A0A0E1NU22_YERPA        Unreviewed;      1231 AA.
AC   A0A0E1NU22;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   10-APR-2019, entry version 33.
DE   RecName: Full=Methionine synthase {ECO:0000256|PIRNR:PIRNR000381};
DE            EC=2.1.1.13 {ECO:0000256|PIRNR:PIRNR000381};
DE   AltName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000256|PIRNR:PIRNR000381};
GN   OrderedLocusNames=YPA_0021 {ECO:0000313|EMBL:ABG11990.1};
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102 {ECO:0000313|EMBL:ABG11990.1, ECO:0000313|Proteomes:UP000001971};
RN   [1] {ECO:0000313|EMBL:ABG11990.1, ECO:0000313|Proteomes:UP000001971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua {ECO:0000313|EMBL:ABG11990.1,
RC   ECO:0000313|Proteomes:UP000001971};
RX   PubMed=16740952; DOI=10.1128/JB.00124-06;
RA   Chain P.S., Hu P., Malfatti S.A., Radnedge L., Larimer F.,
RA   Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and
RT   Nepal516: evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
CC   -!- FUNCTION: Catalyzes the transfer of a methyl group from methyl-
CC       cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and
CC       methionine. Subsequently, remethylates the cofactor using
CC       methyltetrahydrofolate. {ECO:0000256|PIRNR:PIRNR000381}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-5-methyl-5,6,7,8-tetrahydrofolate + L-homocysteine =
CC         (6S)-5,6,7,8-tetrahydrofolate + L-methionine;
CC         Xref=Rhea:RHEA:11172, ChEBI:CHEBI:18608, ChEBI:CHEBI:57453,
CC         ChEBI:CHEBI:57844, ChEBI:CHEBI:58199; EC=2.1.1.13;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000381};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000381-1};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000381-
CC       1};
CC   -!- COFACTOR:
CC       Name=methylcob(III)alamin; Xref=ChEBI:CHEBI:28115;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000381,
CC         ECO:0000256|PIRSR:PIRSR000381-2};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de
CC       novo pathway; L-methionine from L-homocysteine (MetH route): step
CC       1/1. {ECO:0000256|PIRNR:PIRNR000381}.
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DR   EMBL; CP000308; ABG11990.1; -; Genomic_DNA.
DR   RefSeq; WP_002212080.1; NZ_CP009906.1.
DR   EnsemblBacteria; ABG11990; ABG11990; YPA_0021.
DR   EnsemblBacteria; AJJ80410; AJJ80410; CH58_2855.
DR   KEGG; ypa:YPA_0021; -.
DR   PATRIC; fig|360102.15.peg.3010; -.
DR   KO; K00548; -.
DR   OMA; ADCIAMS; -.
DR   UniPathway; UPA00051; UER00081.
DR   Proteomes; UP000001971; Chromosome.
DR   GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro.
DR   CDD; cd02069; methionine_synthase_B12_BD; 1.
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   InterPro; IPR003759; Cbl-bd_cap.
DR   InterPro; IPR006158; Cobalamin-bd.
DR   InterPro; IPR036724; Cobalamin-bd_sf.
DR   InterPro; IPR011005; Dihydropteroate_synth-like.
DR   InterPro; IPR003726; HCY_dom.
DR   InterPro; IPR036589; HCY_dom_sf.
DR   InterPro; IPR033706; Met_synthase_B12-bd.
DR   InterPro; IPR011822; MetH.
DR   InterPro; IPR036594; Meth_synthase_dom.
DR   InterPro; IPR000489; Pterin-binding_dom.
DR   InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom.
DR   InterPro; IPR037010; VitB12-dep_Met_synth_activ_sf.
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   4: Predicted;
DR   PRODOM; A0A0E1NU22.
DR   SWISS-2DPAGE; A0A0E1NU22.
KW   Amino-acid biosynthesis {ECO:0000256|PIRNR:PIRNR000381};
KW   Cobalamin {ECO:0000256|PIRNR:PIRNR000381,
KW   ECO:0000256|PIRSR:PIRSR000381-2};
KW   Cobalt {ECO:0000256|PIRNR:PIRNR000381, ECO:0000256|PIRSR:PIRSR000381-
KW   1}; Complete proteome {ECO:0000313|Proteomes:UP000001971};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR000381,
KW   ECO:0000256|PIRSR:PIRSR000381-1, ECO:0000256|PROSITE-
KW   ProRule:PRU00333};
KW   Methionine biosynthesis {ECO:0000256|PIRNR:PIRNR000381};
KW   Methyltransferase {ECO:0000256|PIRNR:PIRNR000381, ECO:0000256|PROSITE-
KW   ProRule:PRU00333, ECO:0000313|EMBL:ABG11990.1};
KW   S-adenosyl-L-methionine {ECO:0000256|PIRNR:PIRNR000381,
KW   ECO:0000256|PIRSR:PIRSR000381-2};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000381, ECO:0000256|PROSITE-
KW   ProRule:PRU00333, ECO:0000313|EMBL:ABG11990.1};
KW   Zinc {ECO:0000256|PIRNR:PIRNR000381, ECO:0000256|PIRSR:PIRSR000381-1,
KW   ECO:0000256|PROSITE-ProRule:PRU00333}.
FT   REGION      838    839       Cobalamin-binding. {ECO:0000256|PIRSR:
FT                                PIRSR000381-2}.
FT   REGION     1193   1194       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|PIRSR:PIRSR000381-2}.
FT   METAL       252    252       Zinc. {ECO:0000256|PIRSR:PIRSR000381-1,
FT                                ECO:0000256|PROSITE-ProRule:PRU00333}.
FT   METAL       315    315       Zinc. {ECO:0000256|PIRSR:PIRSR000381-1,
FT                                ECO:0000256|PROSITE-ProRule:PRU00333}.
FT   METAL       316    316       Zinc. {ECO:0000256|PIRSR:PIRSR000381-1,
FT                                ECO:0000256|PROSITE-ProRule:PRU00333}.
FT   METAL       763    763       Cobalt (cobalamin axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR000381-1}.
FT   BINDING     808    808       Cobalamin. {ECO:0000256|PIRSR:
FT                                PIRSR000381-2}.
FT   BINDING     950    950       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PIRSR:PIRSR000381-2}.
FT   BINDING    1138   1138       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|PIRSR:PIRSR000381-
FT                                2}.
FT   BINDING    1142   1142       Cobalamin; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR000381-2}.
SQ   SEQUENCE   1231 AA;  136149 MW;  ED23132892137500 CRC64;
     MVDTVIDNKV KELHQQLAQR ILVLDGGMGT MIQSYRLEEA DYRGARFADW ASDLKGNNDL
     LVLSKPEVIT AIHNAYLEAG ADILETNTFN STSIAMADYQ MASLSAEINY EAARLARICA
     DEWSARTPEK PRYVAGVLGP TNRTASISPK VNDPAFRNVS FDQLVEAYRE STRALIEGGV
     DLIMIETVFD TLNAKAATFA VESEFEVMGV LLPVMISGTI TDASGRTLSG QTTEAFYNSL
     RHVKPLSFGL NCALGPDELR QYVAELSRIS EYYVSAHPNA GLPNAFGEYD LEAKEMAEQI
     GEWARAGFLN IVGGCCGTTP RHIAAMVNAV AGVPPRPLPD IPVACRLAGL EPLTIDANTL
     FVNVGERTNV TGSARFKRLI KEEKYGEALD VARQQVESGA QIIDINMDEG MLDAEAAMVR
     FLNLIAGEPD IARVPIMIDS SRWDVIEKGL KCIQGKGIVN SISMKEGVDA FIHHAKLVRR
     YGAAMVVMAF DETGQADTRA RKIEICRRAY KILTETVGFP PEDIIFDPNI FAVATGIEEH
     NNYAVDFIEA CADIKAELPH ALISGGVSNV SFSFRGNDPV REAIHAVFLY YAIRNGMDMG
     IVNAGQLAIY DDLSDELRDA VEDVILNRRD DSTERLLDLA EKYRDSKSGE VAIQQAEWRG
     WPVVKRLEYS LVKGITEFIE LDTEEARQQA DRPIEVIEGP LMSGMNVVGD LFGEGKMFLP
     QVVKSARVMK QAVAYLEPYI EASKQKGTTA GKILLATVKG DVHDIGKNIV GVVLQCNNYE
     IIDLGVMVPT EKILRTAREE KVDIIGLSGL ITPSLDEMVN VAKEMERQGF TLPLLIGGAT
     TSKAHTAVKI EQNYSGSTTY VSNASRSVGV VSALLSDTQR EAFVAKTRKE YETVRIQHAR
     KKPRTPPVSL QAARNNPTVI DWENYTPPVA HKLGVQVVEA SIETLRNYID WTPFFMTWSL
     AGKYPRILED EVVGEEAKRL LADANALLDK LSAEDLLHPK GVVGLFPANS VGDDIEIYRD
     ERRDEVLAIS YHLRQQTEKT DFPNYCLADY VAPKSSGKAD YFGAFAVTGG LEEDALADAY
     DAQHDDYNKI MIKALSDRLA EAFAEYLHER VRKVYWGFAP NENLSNEELV RENYQGIRPA
     PGYPACPEHT EKGQIWQLLD VETHTGMKLT ESYAMWPGAS VSGWYFSHPD SKYFAVAQIQ
     RDQVEDYAAR KGMPTAEVER WLAPNLGYDA D
//

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