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Q55786 (METH_SYNY3) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Methionine synthase

EC=2.1.1.13
Alternative name(s):
5-methyltetrahydrofolate--homocysteine methyltransferase
Methionine synthase, vitamin-B12 dependent
Short name=MS
Gene names
Name:metH
Ordered Locus Names:slr0212
OrganismSynechocystis sp. (strain PCC 6803 / Kazusa) [Reference proteome] [HAMAP]
Taxonomic identifier1111708 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechocystis

Protein attributes

Sequence length1195 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 activity

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

Cofactor

Methylcobalamin (MeCBL) By similarity.

Binds 1 zinc ion per subunit By similarity.

Pathway

Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetH route): step 1/1.

Domain

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.

Miscellaneous

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

Sequence similarities

Belongs to the vitamin-B12 dependent methionine synthase family.

Contains 1 AdoMet activation domain.

Contains 1 B12-binding domain.

Contains 1 B12-binding N-terminal domain.

Contains 1 Hcy-binding domain.

Contains 1 pterin-binding domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11951195Methionine synthase
PRO_0000204537

Regions

Domain1 – 309309Hcy-binding
Domain340 – 599260Pterin-binding
Domain629 – 72294B12-binding N-terminal
Domain724 – 859136B12-binding
Domain896 – 1195300AdoMet activation
Region812 – 8132Cobalamin-binding By similarity
Region1192 – 11932S-adenosyl-L-methionine binding By similarity

Sites

Metal binding2281Zinc By similarity
Metal binding2941Zinc By similarity
Metal binding2951Zinc By similarity
Metal binding7371Cobalt (cobalamin axial ligand) By similarity
Binding site7821Cobalamin By similarity
Binding site9451S-adenosyl-L-methionine By similarity
Binding site11381S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site11421Cobalamin; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q55786 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 1D9635B1B1DDB583

FASTA1,195132,540
        10         20         30         40         50         60 
MKSAFLDRIH SPDRPVLVFD GAMGTNLQVQ NLTAADFGGA EYEGCNEYLV HTKPEAVATV 

        70         80         90        100        110        120 
HRAFYEAGAD VVETDTFGGT PLVLAEYDLA DQSYYLNKAA AELAKAVAAE FSTPEKPRFV 

       130        140        150        160        170        180 
AGSMGPGTKL PTLGHVDYDS LKDAYVVQVR GLYDGGVDLL LVETCQDVLQ IKAALNAIEQ 

       190        200        210        220        230        240 
VFAEKGDRLP LMVSVTMETM GTMLVGTEMA AALAILEPYP IDILGLNCAT GPDLMKEHVK 

       250        260        270        280        290        300 
YLSEHSPFVV SCIPNAGLPE NVGGQAFYRL TPMELQMSLM HFIEDLGVQV IGGCCGTRPD 

       310        320        330        340        350        360 
HIKALADIAK DLQPKQRQPH YEPSAASIYS TQTYAQENSF LIIGERLNAS GSKKCRDLLN 

       370        380        390        400        410        420 
AEDWDSLVSL AKSQVKEGAQ ILDVNVDYVG RDGVRDMKEL ASRLVNNVTL PLMLDSTEWQ 

       430        440        450        460        470        480 
KMEAGLKVAG GKCILNSTNY EDGEERFYKV LEIAKEYGAG IVIGTIDEDG MGRTADKKFE 

       490        500        510        520        530        540 
IAKRAYEAAI AFGIPATEIF FDPLALPIST GIEEDRENGK ATVDAIRRIR QELPDCHILL 

       550        560        570        580        590        600 
GVSNVSFGLN PAARQVLNSI FLHECMQVGM DAAIVSANKI LPLAKIDPEQ QQVCLDLIYD 

       610        620        630        640        650        660 
RREFEGERCT YDPLTKLTTL FEGKTTKRDK SGDANLPVEE RLKRHIIDGE RLGLEEALNE 

       670        680        690        700        710        720 
ALKLYAPLDI INIYLLDGMK VVGELFGSGQ MQLPFVLQSA QTMKAAVAFL EPHMDKDDSA 

       730        740        750        760        770        780 
DNAKGTFLIA TVKGDVHDIG KNLVDIILSN NGYRVVNLGI KQPVENIIEA YKKHRPDCIA 

       790        800        810        820        830        840 
MSGLLVKSTA FMKENLEVFN QEGITVPVIL GGAALTPKFV HQDCQNTYKG QVIYGKDAFA 

       850        860        870        880        890        900 
DLHFMDKLMP AKNSHNWDDF QGFLGEYATE NGHNVTTDDG AKTNFGIEEE KLIDASEQSR 

       910        920        930        940        950        960 
EPEVIDTVRS EAVDPDLERP VPPFWGTKIL QSSDISLDEV FPLLDLQALF VGQWQFRKPR 

       970        980        990       1000       1010       1020 
EQSREEYEQF LAEKVHPILA EWKGKVMAEN LLHPTVVYGY FPCQSQGNTL LIYDPELVSQ 

      1030       1040       1050       1060       1070       1080 
NNGQIPPDAT AIAKFEFPRQ KSGRRLCIAD FFASKESGIT DVFPLQAVTV GEIATEYARK 

      1090       1100       1110       1120       1130       1140 
LFAGDNYTDY LYFHGMAVQM AEALAEWTHQ RIRQELGFGH LDPDNIRDLL QQRYQGSRYS 

      1150       1160       1170       1180       1190 
FGYPACPNMQ DQYTQLELLQ TERIGLYMDE SEQVYPEQST TAIISYHPAA KYFSA 

« Hide

References

[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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000022 Genomic DNA. Translation: BAA10438.1.
PIRS76592.
RefSeqNP_442368.1. NC_000911.1.
YP_005652428.1. NC_017277.1.
YP_007452244.1. NC_020286.1.

3D structure databases

ProteinModelPortalQ55786.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING1148.slr0212.

Proteomic databases

PaxDbQ55786.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAA10438; BAA10438; BAA10438.
GeneID952446.
KEGGsyn:slr0212.
syy:SYNGTS_2475.
syz:MYO_125000.
PATRIC23842418. VBISynSp132158_2749.

Phylogenomic databases

eggNOGCOG1410.
HOGENOMHOG000251408.
KOK00548.
OMAEEIHARY.
OrthoDBEOG6091CH.
PhylomeDBQ55786.

Enzyme and pathway databases

UniPathwayUPA00051; UER00081.

Family and domain databases

Gene3D1.10.1240.10. 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.
InterProIPR003759. 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]
PfamPF02310. 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]
PIRSFPIRSF000381. MetH. 1 hit.
SMARTSM01018. B12-binding_2. 1 hit.
[Graphical view]
SUPFAMSSF47644. SSF47644. 1 hit.
SSF51717. SSF51717. 1 hit.
SSF52242. SSF52242. 1 hit.
SSF56507. SSF56507. 1 hit.
SSF82282. SSF82282. 1 hit.
TIGRFAMsTIGR02082. metH. 1 hit.
PROSITEPS50974. 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]
ProtoNetSearch...

Entry information

Entry nameMETH_SYNY3
AccessionPrimary (citable) accession number: Q55786
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Synechocystis PCC 6803

Synechocystis (strain PCC 6803): entries and gene names

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways