(data stored in SCRATCH zone)

SWISSPROT: Q2IM33_ANADE

ID   Q2IM33_ANADE            Unreviewed;      1150 AA.
AC   Q2IM33;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   08-MAY-2019, entry version 106.
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=Adeh_0085 {ECO:0000313|EMBL:ABC79862.1};
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397 {ECO:0000313|EMBL:ABC79862.1, ECO:0000313|Proteomes:UP000001935};
RN   [1] {ECO:0000313|EMBL:ABC79862.1, ECO:0000313|Proteomes:UP000001935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C {ECO:0000313|EMBL:ABC79862.1,
RC   ECO:0000313|Proteomes:UP000001935};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000001935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C {ECO:0000313|Proteomes:UP000001935};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000251; ABC79862.1; -; Genomic_DNA.
DR   RefSeq; WP_011419145.1; NC_007760.1.
DR   STRING; 290397.Adeh_0085; -.
DR   EnsemblBacteria; ABC79862; ABC79862; Adeh_0085.
DR   KEGG; ade:Adeh_0085; -.
DR   eggNOG; ENOG4105C3R; Bacteria.
DR   eggNOG; COG0646; LUCA.
DR   eggNOG; COG1410; LUCA.
DR   HOGENOM; HOG000251408; -.
DR   KO; K00548; -.
DR   OMA; ADCIAMS; -.
DR   BioCyc; ADEH290397:G1G5W-89-MONOMER; -.
DR   UniPathway; UPA00051; UER00081.
DR   Proteomes; UP000001935; 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   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; 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; Q2IM33.
DR   SWISS-2DPAGE; Q2IM33.
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:UP000001935};
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:ABC79862.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001935};
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:ABC79862.1};
KW   Zinc {ECO:0000256|PIRNR:PIRNR000381, ECO:0000256|PIRSR:PIRSR000381-1,
KW   ECO:0000256|PROSITE-ProRule:PRU00333}.
FT   DOMAIN        1    308       Hcy-binding. {ECO:0000259|PROSITE:
FT                                PS50970}.
FT   DOMAIN      340    595       Pterin-binding. {ECO:0000259|PROSITE:
FT                                PS50972}.
FT   DOMAIN      627    720       B12-binding N-terminal.
FT                                {ECO:0000259|PROSITE:PS51337}.
FT   DOMAIN      720    859       B12-binding. {ECO:0000259|PROSITE:
FT                                PS51332}.
FT   DOMAIN      871   1150       AdoMet activation. {ECO:0000259|PROSITE:
FT                                PS50974}.
FT   REGION      808    809       Cobalamin-binding. {ECO:0000256|PIRSR:
FT                                PIRSR000381-2}.
FT   REGION     1139   1140       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|PIRSR:PIRSR000381-2}.
FT   METAL       227    227       Zinc. {ECO:0000256|PIRSR:PIRSR000381-1,
FT                                ECO:0000256|PROSITE-ProRule:PRU00333}.
FT   METAL       293    293       Zinc. {ECO:0000256|PIRSR:PIRSR000381-1,
FT                                ECO:0000256|PROSITE-ProRule:PRU00333}.
FT   METAL       294    294       Zinc. {ECO:0000256|PIRSR:PIRSR000381-1,
FT                                ECO:0000256|PROSITE-ProRule:PRU00333}.
FT   METAL       733    733       Cobalt (cobalamin axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR000381-1}.
FT   BINDING     778    778       Cobalamin. {ECO:0000256|PIRSR:
FT                                PIRSR000381-2}.
FT   BINDING     920    920       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PIRSR:PIRSR000381-2}.
FT   BINDING    1084   1084       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|PIRSR:PIRSR000381-
FT                                2}.
FT   BINDING    1088   1088       Cobalamin; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR000381-2}.
SQ   SEQUENCE   1150 AA;  124694 MW;  12AFF759931FB023 CRC64;
     MTFREALERR PLVFDGAMGT QIQRHQLTAA EFGGKEGAND LLTLTRPDLI EEIHARYFAV
     GCDVVETNTF GSSRLKLDEY GLGHRTYEVN CRAAILARRA AERFSTPDHP RFVAGSIGPT
     GMLPSSSDPA LGNITSDALE RIFFEQAKGL VEGGVDALII ETQQDMLELR AAVLACDAVR
     REALRDVFVI AQPTLIDANG RMLLGTDVGS AVATLERLPV DAVGLNCSTG PDEMRASVKA
     LAERCSHWVS VLPNAGMPEN EDGRAVYKLS PDDLARALAG FVAEYGVDIV GGCCGTTPEH
     LRKVVEALRG LSAPRRRRPA PAAELSSAMK AVPLAMEPRP LVVGERLNSQ GSRKVKELLL
     ADDYAGLVQI ARGQVEAGAH VLDVCVALNE RDDEAAQMRT LAKLLAQSVD APLMIDSTEP
     DVIEGALKVY PGRCIVNSVN LEKSGERVRR VLPLVRRYGA AVVAMTIDEK GMAQTAERKA
     EVARRIVAVA KDHGIPPDSL VFDALTFTLA TGGEEYRRSA VETLEGIRRI KAENPGVLTT
     LGVSNVSFGL AKSAREVVNS VFLYHAVQAG LDLAIVNPKD ILPYPAIDAA ERALAEDLVF
     DRRPDALARL IAHFGAKGAP EKAAVDPLAG AAGKGAEERI HLQILHRRPE GIEALIDEAL
     TRRSAVDVLN QVLLPAMKDV GDRFGAGELI LPFVLQSAEV MKKAVAHLEQ FLEKKAGATK
     GNVVLATVYG DVHDIGKNLV KTILSNNGFT VHDLGKQVPV TTVLDKALQV NADAIGLSAL
     LVSTSKQMPF CVEELHRRNL SFPVIIGGAA INRRFGYRTH FAQDGTPYAG GVFYAKDAFE
     GLEVVEALVD PARREALKRE VLQKAVAEKE RPADKPMAPA PARRTGAVAP AARIPTPPFW
     GPRVVPSGSV ALADVWPHLD LAELFKLQWG VKAKGAEYER LVREEFGPKL EELKAEAQAQ
     GWLVPKVVYG YFPCHAEGND LVVLDPTHRK AEVARLALPR QPDDRNLCLA DYFREERGAD
     VCALQVVTVG DQATHLAEQA QERGDYTRAL FLHGLAVETA EALAEYWHRQ VRAELGLADG
     QGKRYSPGYP SWPELSDQRQ VWKLLDPVRT IGVSLTDACQ MVPEQSTSAI VLHHPDAIYF
     LVRGLERAAG
//

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