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Q55786

- METH_SYNY3

UniProt

Q55786 - METH_SYNY3

Protein

Methionine synthase

Gene

metH

Organism
Synechocystis sp. (strain PCC 6803 / Kazusa)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Catalyzes the transfer of a methyl group from methyl-cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate By similarity.By similarity

    Catalytic activityi

    5-methyltetrahydrofolate + L-homocysteine = tetrahydrofolate + L-methionine.

    Cofactori

    Methylcobalamin (MeCBL).By similarity
    Binds 1 zinc ion per subunit.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi228 – 2281ZincPROSITE-ProRule annotation
    Metal bindingi294 – 2941ZincPROSITE-ProRule annotation
    Metal bindingi295 – 2951ZincPROSITE-ProRule annotation
    Metal bindingi737 – 7371Cobalt (cobalamin axial ligand)By similarity
    Binding sitei782 – 7821CobalaminBy similarity
    Binding sitei945 – 9451S-adenosyl-L-methionineBy similarity
    Binding sitei1138 – 11381S-adenosyl-L-methionine; via carbonyl oxygenBy similarity
    Binding sitei1142 – 11421Cobalamin; via carbonyl oxygenBy similarity

    GO - Molecular functioni

    1. cobalamin binding Source: UniProtKB-KW
    2. methionine synthase activity Source: UniProtKB-EC
    3. S-adenosylmethionine-homocysteine S-methyltransferase activity Source: InterPro
    4. zinc ion binding Source: InterPro

    GO - Biological processi

    1. pteridine-containing compound metabolic process Source: InterPro

    Keywords - Molecular functioni

    Methyltransferase, Transferase

    Keywords - Biological processi

    Amino-acid biosynthesis, Methionine biosynthesis

    Keywords - Ligandi

    Cobalamin, Cobalt, Metal-binding, S-adenosyl-L-methionine, Zinc

    Enzyme and pathway databases

    UniPathwayiUPA00051; UER00081.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methionine synthase (EC:2.1.1.13)
    Alternative name(s):
    5-methyltetrahydrofolate--homocysteine methyltransferase
    Methionine synthase, vitamin-B12 dependent
    Short name:
    MS
    Gene namesi
    Name:metH
    Ordered Locus Names:slr0212
    OrganismiSynechocystis sp. (strain PCC 6803 / Kazusa)
    Taxonomic identifieri1111708 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechocystis
    ProteomesiUP000001425: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    1. intracellular Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11951195Methionine synthasePRO_0000204537Add
    BLAST

    Proteomic databases

    PaxDbiQ55786.

    Interactioni

    Protein-protein interaction databases

    STRINGi1148.slr0212.

    Structurei

    3D structure databases

    ProteinModelPortaliQ55786.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 309309Hcy-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini340 – 599260Pterin-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini629 – 72294B12-binding N-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini724 – 859136B12-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini896 – 1195300AdoMet activationPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni812 – 8132Cobalamin-bindingBy similarity
    Regioni1192 – 11932S-adenosyl-L-methionine bindingBy similarity

    Domaini

    Modular enzyme with four functionally distinct domains. The isolated Hcy-binding domain catalyzes methyl transfer from free methylcobalamin to homocysteine. The Hcy-binding domain in association with the pterin-binding domain catalyzes the methylation of cob(I)alamin by methyltetrahydrofolate and the methylation of homocysteine. The B12-binding domain binds the cofactor. The AdoMet activation domain binds S-adenosyl-L-methionine. Under aerobic conditions cob(I)alamin can be converted to inactive cob(II)alamin. Reductive methylation by S-adenosyl-L-methionine and flavodoxin regenerates methylcobalamin By similarity.By similarity

    Sequence similaritiesi

    Contains 1 AdoMet activation domain.PROSITE-ProRule annotation
    Contains 1 B12-binding domain.PROSITE-ProRule annotation
    Contains 1 Hcy-binding domain.PROSITE-ProRule annotation
    Contains 1 pterin-binding domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG1410.
    HOGENOMiHOG000251408.
    KOiK00548.
    OMAiEEIHARY.
    OrthoDBiEOG6091CH.
    PhylomeDBiQ55786.

    Family and domain databases

    Gene3Di1.10.1240.10. 1 hit.
    3.10.196.10. 1 hit.
    3.20.20.20. 1 hit.
    3.20.20.330. 1 hit.
    3.40.50.280. 1 hit.
    InterProiIPR003759. Cbl-bd_cap.
    IPR006158. Cobalamin-bd.
    IPR011005. Dihydropteroate_synth-like.
    IPR011822. MetH.
    IPR000489. Pterin-binding.
    IPR003726. S_MeTrfase.
    IPR004223. VitB12-dep_Met_synth_activ_dom.
    [Graphical view]
    PfamiPF02310. B12-binding. 1 hit.
    PF02607. B12-binding_2. 1 hit.
    PF02965. Met_synt_B12. 1 hit.
    PF00809. Pterin_bind. 1 hit.
    PF02574. S-methyl_trans. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000381. MetH. 1 hit.
    SMARTiSM01018. B12-binding_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF47644. SSF47644. 1 hit.
    SSF51717. SSF51717. 1 hit.
    SSF52242. SSF52242. 1 hit.
    SSF56507. SSF56507. 1 hit.
    SSF82282. SSF82282. 1 hit.
    TIGRFAMsiTIGR02082. metH. 1 hit.
    PROSITEiPS50974. ADOMET_ACTIVATION. 1 hit.
    PS51332. B12_BINDING. 1 hit.
    PS51337. B12_BINDING_NTER. 1 hit.
    PS50970. HCY. 1 hit.
    PS50972. PTERIN_BINDING. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q55786-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKSAFLDRIH SPDRPVLVFD GAMGTNLQVQ NLTAADFGGA EYEGCNEYLV     50
    HTKPEAVATV HRAFYEAGAD VVETDTFGGT PLVLAEYDLA DQSYYLNKAA 100
    AELAKAVAAE FSTPEKPRFV AGSMGPGTKL PTLGHVDYDS LKDAYVVQVR 150
    GLYDGGVDLL LVETCQDVLQ IKAALNAIEQ VFAEKGDRLP LMVSVTMETM 200
    GTMLVGTEMA AALAILEPYP IDILGLNCAT GPDLMKEHVK YLSEHSPFVV 250
    SCIPNAGLPE NVGGQAFYRL TPMELQMSLM HFIEDLGVQV IGGCCGTRPD 300
    HIKALADIAK DLQPKQRQPH YEPSAASIYS TQTYAQENSF LIIGERLNAS 350
    GSKKCRDLLN AEDWDSLVSL AKSQVKEGAQ ILDVNVDYVG RDGVRDMKEL 400
    ASRLVNNVTL PLMLDSTEWQ KMEAGLKVAG GKCILNSTNY EDGEERFYKV 450
    LEIAKEYGAG IVIGTIDEDG MGRTADKKFE IAKRAYEAAI AFGIPATEIF 500
    FDPLALPIST GIEEDRENGK ATVDAIRRIR QELPDCHILL GVSNVSFGLN 550
    PAARQVLNSI FLHECMQVGM DAAIVSANKI LPLAKIDPEQ QQVCLDLIYD 600
    RREFEGERCT YDPLTKLTTL FEGKTTKRDK SGDANLPVEE RLKRHIIDGE 650
    RLGLEEALNE ALKLYAPLDI INIYLLDGMK VVGELFGSGQ MQLPFVLQSA 700
    QTMKAAVAFL EPHMDKDDSA DNAKGTFLIA TVKGDVHDIG KNLVDIILSN 750
    NGYRVVNLGI KQPVENIIEA YKKHRPDCIA MSGLLVKSTA FMKENLEVFN 800
    QEGITVPVIL GGAALTPKFV HQDCQNTYKG QVIYGKDAFA DLHFMDKLMP 850
    AKNSHNWDDF QGFLGEYATE NGHNVTTDDG AKTNFGIEEE KLIDASEQSR 900
    EPEVIDTVRS EAVDPDLERP VPPFWGTKIL QSSDISLDEV FPLLDLQALF 950
    VGQWQFRKPR EQSREEYEQF LAEKVHPILA EWKGKVMAEN LLHPTVVYGY 1000
    FPCQSQGNTL LIYDPELVSQ NNGQIPPDAT AIAKFEFPRQ KSGRRLCIAD 1050
    FFASKESGIT DVFPLQAVTV GEIATEYARK LFAGDNYTDY LYFHGMAVQM 1100
    AEALAEWTHQ RIRQELGFGH LDPDNIRDLL QQRYQGSRYS FGYPACPNMQ 1150
    DQYTQLELLQ TERIGLYMDE SEQVYPEQST TAIISYHPAA KYFSA 1195
    Length:1,195
    Mass (Da):132,540
    Last modified:November 1, 1996 - v1
    Checksum:i1D9635B1B1DDB583
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000022 Genomic DNA. Translation: BAA10438.1.
    PIRiS76592.
    RefSeqiNP_442368.1. NC_000911.1.
    YP_005652428.1. NC_017277.1.
    YP_007452244.1. NC_020286.1.

    Genome annotation databases

    EnsemblBacteriaiBAA10438; BAA10438; BAA10438.
    GeneIDi952446.
    KEGGisyn:slr0212.
    syy:SYNGTS_2475.
    syz:MYO_125000.
    PATRICi23842418. VBISynSp132158_2749.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000022 Genomic DNA. Translation: BAA10438.1 .
    PIRi S76592.
    RefSeqi NP_442368.1. NC_000911.1.
    YP_005652428.1. NC_017277.1.
    YP_007452244.1. NC_020286.1.

    3D structure databases

    ProteinModelPortali Q55786.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 1148.slr0212.

    Proteomic databases

    PaxDbi Q55786.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAA10438 ; BAA10438 ; BAA10438 .
    GeneIDi 952446.
    KEGGi syn:slr0212.
    syy:SYNGTS_2475.
    syz:MYO_125000.
    PATRICi 23842418. VBISynSp132158_2749.

    Phylogenomic databases

    eggNOGi COG1410.
    HOGENOMi HOG000251408.
    KOi K00548.
    OMAi EEIHARY.
    OrthoDBi EOG6091CH.
    PhylomeDBi Q55786.

    Enzyme and pathway databases

    UniPathwayi UPA00051 ; UER00081 .

    Family and domain databases

    Gene3Di 1.10.1240.10. 1 hit.
    3.10.196.10. 1 hit.
    3.20.20.20. 1 hit.
    3.20.20.330. 1 hit.
    3.40.50.280. 1 hit.
    InterProi IPR003759. Cbl-bd_cap.
    IPR006158. Cobalamin-bd.
    IPR011005. Dihydropteroate_synth-like.
    IPR011822. MetH.
    IPR000489. Pterin-binding.
    IPR003726. S_MeTrfase.
    IPR004223. VitB12-dep_Met_synth_activ_dom.
    [Graphical view ]
    Pfami PF02310. B12-binding. 1 hit.
    PF02607. B12-binding_2. 1 hit.
    PF02965. Met_synt_B12. 1 hit.
    PF00809. Pterin_bind. 1 hit.
    PF02574. S-methyl_trans. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000381. MetH. 1 hit.
    SMARTi SM01018. B12-binding_2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47644. SSF47644. 1 hit.
    SSF51717. SSF51717. 1 hit.
    SSF52242. SSF52242. 1 hit.
    SSF56507. SSF56507. 1 hit.
    SSF82282. SSF82282. 1 hit.
    TIGRFAMsi TIGR02082. metH. 1 hit.
    PROSITEi PS50974. ADOMET_ACTIVATION. 1 hit.
    PS51332. B12_BINDING. 1 hit.
    PS51337. B12_BINDING_NTER. 1 hit.
    PS50970. HCY. 1 hit.
    PS50972. PTERIN_BINDING. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region from map positions 64% to 92% of the genome."
      Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N., Sugiura M., Tabata S.
      DNA Res. 2:153-166(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 27184 / PCC 6803 / N-1.
    2. "Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions."
      Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.
      , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
      DNA Res. 3:109-136(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: PCC 6803 / Kazusa.

    Entry informationi

    Entry nameiMETH_SYNY3
    AccessioniPrimary (citable) accession number: Q55786
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 108 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    L-homocysteine is bound via the zinc atom.By similarity

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families
    3. Synechocystis PCC 6803
      Synechocystis (strain PCC 6803): entries and gene names

    External Data

    Dasty 3