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Q55786

- METH_SYNY3

UniProt

Q55786 - METH_SYNY3

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Protein

Methionine synthase

Gene

metH

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).By similarity

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:

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
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 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.
InParanoidiQ55786.
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

        10         20         30         40         50
MKSAFLDRIH SPDRPVLVFD GAMGTNLQVQ NLTAADFGGA EYEGCNEYLV
60 70 80 90 100
HTKPEAVATV HRAFYEAGAD VVETDTFGGT PLVLAEYDLA DQSYYLNKAA
110 120 130 140 150
AELAKAVAAE FSTPEKPRFV AGSMGPGTKL PTLGHVDYDS LKDAYVVQVR
160 170 180 190 200
GLYDGGVDLL LVETCQDVLQ IKAALNAIEQ VFAEKGDRLP LMVSVTMETM
210 220 230 240 250
GTMLVGTEMA AALAILEPYP IDILGLNCAT GPDLMKEHVK YLSEHSPFVV
260 270 280 290 300
SCIPNAGLPE NVGGQAFYRL TPMELQMSLM HFIEDLGVQV IGGCCGTRPD
310 320 330 340 350
HIKALADIAK DLQPKQRQPH YEPSAASIYS TQTYAQENSF LIIGERLNAS
360 370 380 390 400
GSKKCRDLLN AEDWDSLVSL AKSQVKEGAQ ILDVNVDYVG RDGVRDMKEL
410 420 430 440 450
ASRLVNNVTL PLMLDSTEWQ KMEAGLKVAG GKCILNSTNY EDGEERFYKV
460 470 480 490 500
LEIAKEYGAG IVIGTIDEDG MGRTADKKFE IAKRAYEAAI AFGIPATEIF
510 520 530 540 550
FDPLALPIST GIEEDRENGK ATVDAIRRIR QELPDCHILL GVSNVSFGLN
560 570 580 590 600
PAARQVLNSI FLHECMQVGM DAAIVSANKI LPLAKIDPEQ QQVCLDLIYD
610 620 630 640 650
RREFEGERCT YDPLTKLTTL FEGKTTKRDK SGDANLPVEE RLKRHIIDGE
660 670 680 690 700
RLGLEEALNE ALKLYAPLDI INIYLLDGMK VVGELFGSGQ MQLPFVLQSA
710 720 730 740 750
QTMKAAVAFL EPHMDKDDSA DNAKGTFLIA TVKGDVHDIG KNLVDIILSN
760 770 780 790 800
NGYRVVNLGI KQPVENIIEA YKKHRPDCIA MSGLLVKSTA FMKENLEVFN
810 820 830 840 850
QEGITVPVIL GGAALTPKFV HQDCQNTYKG QVIYGKDAFA DLHFMDKLMP
860 870 880 890 900
AKNSHNWDDF QGFLGEYATE NGHNVTTDDG AKTNFGIEEE KLIDASEQSR
910 920 930 940 950
EPEVIDTVRS EAVDPDLERP VPPFWGTKIL QSSDISLDEV FPLLDLQALF
960 970 980 990 1000
VGQWQFRKPR EQSREEYEQF LAEKVHPILA EWKGKVMAEN LLHPTVVYGY
1010 1020 1030 1040 1050
FPCQSQGNTL LIYDPELVSQ NNGQIPPDAT AIAKFEFPRQ KSGRRLCIAD
1060 1070 1080 1090 1100
FFASKESGIT DVFPLQAVTV GEIATEYARK LFAGDNYTDY LYFHGMAVQM
1110 1120 1130 1140 1150
AEALAEWTHQ RIRQELGFGH LDPDNIRDLL QQRYQGSRYS FGYPACPNMQ
1160 1170 1180 1190
DQYTQLELLQ TERIGLYMDE SEQVYPEQST TAIISYHPAA KYFSA
Length:1,195
Mass (Da):132,540
Last modified:November 1, 1996 - v1
Checksum:i1D9635B1B1DDB583
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
PATRICi23842418. VBISynSp132158_2749.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
PATRICi 23842418. VBISynSp132158_2749.

Phylogenomic databases

eggNOGi COG1410.
HOGENOMi HOG000251408.
InParanoidi Q55786.
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: November 26, 2014
This is version 110 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