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Q55786

- METH_SYNY3

UniProt

Q55786 - METH_SYNY3

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Protein
Methionine synthase
Gene
metH, slr0212
Organism
Synechocystis sp. (strain PCC 6803 / Kazusa)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

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.

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 – 2281Zinc By similarity
Metal bindingi294 – 2941Zinc By similarity
Metal bindingi295 – 2951Zinc By similarity
Metal bindingi737 – 7371Cobalt (cobalamin axial ligand) By similarity
Binding sitei782 – 7821Cobalamin By similarity
Binding sitei945 – 9451S-adenosyl-L-methionine By similarity
Binding sitei1138 – 11381S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding sitei1142 – 11421Cobalamin; via carbonyl oxygen By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. pteridine-containing compound metabolic process Source: InterPro
Complete GO annotation...

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
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11951195Methionine synthase
PRO_0000204537Add
BLAST

Proteomic databases

PaxDbiQ55786.

Interactioni

Protein-protein interaction databases

STRINGi1148.slr0212.

Structurei

3D structure databases

ProteinModelPortaliQ55786.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 309309Hcy-binding
Add
BLAST
Domaini340 – 599260Pterin-binding
Add
BLAST
Domaini629 – 72294B12-binding N-terminal
Add
BLAST
Domaini724 – 859136B12-binding
Add
BLAST
Domaini896 – 1195300AdoMet activation
Add
BLAST

Region

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

Sequence similaritiesi

Contains 1 B12-binding domain.
Contains 1 Hcy-binding domain.

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

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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...

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: July 9, 2014
This is version 107 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

Similar proteinsi