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 01-MAY-2013, entry version 100.
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: Cobalamin (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 PATRIC; 23842418; VBISynSp132158_2749.
DR eggNOG; COG1410; -.
DR HOGENOM; HOG000251408; -.
DR KO; K00548; -.
DR OMA; NGSKAFR; -.
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: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; 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 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
//
