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Database: UniProt
Entry: Q55786
LinkDB: Q55786
Original site: Q55786 
ID   METH_SYNY3              Reviewed;        1195 AA.
AC   Q55786;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-APR-2014, entry version 105.
DE   RecName: Full=Methionine synthase;
DE            EC=2.1.1.13;
DE   AltName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase;
DE   AltName: Full=Methionine synthase, vitamin-B12 dependent;
DE            Short=MS;
GN   Name=metH; OrderedLocusNames=slr0212;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC   Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX   PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA   Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA   Sugiura M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb
RT   region from map positions 64% to 92% of the genome.";
RL   DNA Res. 2:153-166(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T.,
RA   Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S.,
RA   Shimpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M.,
RA   Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the
RT   entire genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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 (By similarity).
CC   -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + L-homocysteine =
CC       tetrahydrofolate + L-methionine.
CC   -!- COFACTOR: Methylcobalamin (MeCBL) (By similarity).
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de
CC       novo pathway; L-methionine from L-homocysteine (MetH route): step
CC       1/1.
CC   -!- DOMAIN: Modular enzyme with four functionally distinct domains.
CC       The isolated Hcy-binding domain catalyzes methyl transfer from
CC       free methylcobalamin to homocysteine. The Hcy-binding domain in
CC       association with the pterin-binding domain catalyzes the
CC       methylation of cob(I)alamin by methyltetrahydrofolate and the
CC       methylation of homocysteine. The B12-binding domain binds the
CC       cofactor. The AdoMet activation domain binds S-adenosyl-L-
CC       methionine. Under aerobic conditions cob(I)alamin can be converted
CC       to inactive cob(II)alamin. Reductive methylation by S-adenosyl-L-
CC       methionine and flavodoxin regenerates methylcobalamin (By
CC       similarity).
CC   -!- MISCELLANEOUS: L-homocysteine is bound via the zinc atom (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the vitamin-B12 dependent methionine
CC       synthase family.
CC   -!- SIMILARITY: Contains 1 AdoMet activation domain.
CC   -!- SIMILARITY: Contains 1 B12-binding domain.
CC   -!- SIMILARITY: Contains 1 B12-binding N-terminal domain.
CC   -!- SIMILARITY: Contains 1 Hcy-binding domain.
CC   -!- SIMILARITY: Contains 1 pterin-binding domain.
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DR   EMBL; BA000022; BAA10438.1; -; Genomic_DNA.
DR   PIR; S76592; S76592.
DR   RefSeq; NP_442368.1; NC_000911.1.
DR   RefSeq; YP_005652428.1; NC_017277.1.
DR   RefSeq; YP_007452244.1; NC_020286.1.
DR   ProteinModelPortal; Q55786; -.
DR   STRING; 1148.slr0212; -.
DR   PaxDb; Q55786; -.
DR   EnsemblBacteria; BAA10438; BAA10438; BAA10438.
DR   GeneID; 12253657; -.
DR   GeneID; 14617922; -.
DR   GeneID; 952446; -.
DR   KEGG; syn:slr0212; -.
DR   KEGG; syy:SYNGTS_2475; -.
DR   KEGG; syz:MYO_125000; -.
DR   PATRIC; 23842418; VBISynSp132158_2749.
DR   eggNOG; COG1410; -.
DR   HOGENOM; HOG000251408; -.
DR   KO; K00548; -.
DR   OMA; SMKEGEA; -.
DR   OrthoDB; EOG6091CH; -.
DR   PhylomeDB; Q55786; -.
DR   ProtClustDB; CLSK893539; -.
DR   UniPathway; UPA00051; UER00081.
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:UniProtKB-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   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   Amino-acid biosynthesis; Cobalamin; Cobalt; Complete proteome;
KW   Metal-binding; Methionine biosynthesis; Methyltransferase;
KW   Reference proteome; Repeat; S-adenosyl-L-methionine; Transferase;
KW   Zinc.
FT   CHAIN         1   1195       Methionine synthase.
FT                                /FTId=PRO_0000204537.
FT   DOMAIN        1    309       Hcy-binding.
FT   DOMAIN      340    599       Pterin-binding.
FT   DOMAIN      629    722       B12-binding N-terminal.
FT   DOMAIN      724    859       B12-binding.
FT   DOMAIN      896   1195       AdoMet activation.
FT   REGION      812    813       Cobalamin-binding (By similarity).
FT   REGION     1192   1193       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       737    737       Cobalt (cobalamin axial ligand) (By
FT                                similarity).
FT   BINDING     782    782       Cobalamin (By similarity).
FT   BINDING     945    945       S-adenosyl-L-methionine (By similarity).
FT   BINDING    1138   1138       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen (By similarity).
FT   BINDING    1142   1142       Cobalamin; via carbonyl oxygen (By
FT                                similarity).
SQ   SEQUENCE   1195 AA;  132540 MW;  1D9635B1B1DDB583 CRC64;
     MKSAFLDRIH SPDRPVLVFD GAMGTNLQVQ NLTAADFGGA EYEGCNEYLV HTKPEAVATV
     HRAFYEAGAD VVETDTFGGT PLVLAEYDLA DQSYYLNKAA AELAKAVAAE FSTPEKPRFV
     AGSMGPGTKL PTLGHVDYDS LKDAYVVQVR GLYDGGVDLL LVETCQDVLQ IKAALNAIEQ
     VFAEKGDRLP LMVSVTMETM GTMLVGTEMA AALAILEPYP IDILGLNCAT GPDLMKEHVK
     YLSEHSPFVV SCIPNAGLPE NVGGQAFYRL TPMELQMSLM HFIEDLGVQV IGGCCGTRPD
     HIKALADIAK DLQPKQRQPH YEPSAASIYS TQTYAQENSF LIIGERLNAS GSKKCRDLLN
     AEDWDSLVSL AKSQVKEGAQ ILDVNVDYVG RDGVRDMKEL ASRLVNNVTL PLMLDSTEWQ
     KMEAGLKVAG GKCILNSTNY EDGEERFYKV LEIAKEYGAG IVIGTIDEDG MGRTADKKFE
     IAKRAYEAAI AFGIPATEIF FDPLALPIST GIEEDRENGK ATVDAIRRIR QELPDCHILL
     GVSNVSFGLN PAARQVLNSI FLHECMQVGM DAAIVSANKI LPLAKIDPEQ QQVCLDLIYD
     RREFEGERCT YDPLTKLTTL FEGKTTKRDK SGDANLPVEE RLKRHIIDGE RLGLEEALNE
     ALKLYAPLDI INIYLLDGMK VVGELFGSGQ MQLPFVLQSA QTMKAAVAFL EPHMDKDDSA
     DNAKGTFLIA TVKGDVHDIG KNLVDIILSN NGYRVVNLGI KQPVENIIEA YKKHRPDCIA
     MSGLLVKSTA FMKENLEVFN QEGITVPVIL GGAALTPKFV HQDCQNTYKG QVIYGKDAFA
     DLHFMDKLMP AKNSHNWDDF QGFLGEYATE NGHNVTTDDG AKTNFGIEEE KLIDASEQSR
     EPEVIDTVRS EAVDPDLERP VPPFWGTKIL QSSDISLDEV FPLLDLQALF VGQWQFRKPR
     EQSREEYEQF LAEKVHPILA EWKGKVMAEN LLHPTVVYGY FPCQSQGNTL LIYDPELVSQ
     NNGQIPPDAT AIAKFEFPRQ KSGRRLCIAD FFASKESGIT DVFPLQAVTV GEIATEYARK
     LFAGDNYTDY LYFHGMAVQM AEALAEWTHQ RIRQELGFGH LDPDNIRDLL QQRYQGSRYS
     FGYPACPNMQ DQYTQLELLQ TERIGLYMDE SEQVYPEQST TAIISYHPAA KYFSA
//
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