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Q5E814

- METH_VIBF1

UniProt

Q5E814 - METH_VIBF1

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Protein

Methionine synthase

Gene

metH

Organism
Vibrio fischeri (strain ATCC 700601 / ES114)
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 bindingi249 – 2491ZincPROSITE-ProRule annotation
Metal bindingi312 – 3121ZincPROSITE-ProRule annotation
Metal bindingi313 – 3131ZincPROSITE-ProRule annotation
Metal bindingi761 – 7611Cobalt (cobalamin axial ligand)By similarity
Binding sitei806 – 8061CobalaminBy similarity
Binding sitei949 – 9491S-adenosyl-L-methionineBy similarity
Binding sitei1137 – 11371S-adenosyl-L-methionine; via carbonyl oxygenBy similarity
Binding sitei1141 – 11411Cobalamin; 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

BioCyciAFIS312309:GIWP-343-MONOMER.
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:VF_0337
OrganismiVibrio fischeri (strain ATCC 700601 / ES114)
Taxonomic identifieri312309 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeAliivibrio
ProteomesiUP000000537: Chromosome I

Subcellular locationi

GO - Cellular componenti

  1. intracellular Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12261226Methionine synthasePRO_0000204539Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi312309.VF_0337.

Structurei

3D structure databases

ProteinModelPortaliQ5E814.
SMRiQ5E814. Positions 655-1225.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 327321Hcy-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini358 – 619262Pterin-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini652 – 74695B12-binding N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini748 – 883136B12-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini899 – 1226328AdoMet activationPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni836 – 8372Cobalamin-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.
HOGENOMiHOG000251409.
KOiK00548.
OMAiLTEHYAM.
OrthoDBiEOG6091CH.

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.

Q5E814-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAGSNIKVQI EKQLSERILL IDGGMGTMIQ GYKFEEEDYR GERFNKWHCD
60 70 80 90 100
LKGNNDLLVL SQPQIIRDIH EAYLEAGADI LETNTFNATT IAMADYDMES
110 120 130 140 150
LSEEINFEAA KLAREVADKW TEKTPNKPRY VAGVLGPTNR TCSISPDVND
160 170 180 190 200
PGFRNVSFDE LVEAYSESTR ALIRGGSDLI LIETIFDTLN AKACSFAVES
210 220 230 240 250
VFEELDITLP VMISGTITDA SGRTLSGQTT EAFYNALRHV KPISFGLNCA
260 270 280 290 300
LGPDELREYV SDLSRISECY VSAHPNAGLP NAFGEYDLSP EDMAEHVAEW
310 320 330 340 350
ASSGFLNLIG GCCGTTPEHI RQMALVVEGV KPRQLPELPV ACRLSGLEPL
360 370 380 390 400
TIEKDSLFIN VGERTNVTGS ARFKRLIKEE LYDEALSVAQ EQVENGAQII
410 420 430 440 450
DINMDEGMLD AEACMVRFLN LCASEPEISK VPVMVDSSKW EVIEAGLKCI
460 470 480 490 500
QGKGIVNSIS LKEGKEKFVH QAKLIRRYGA AVIVMAFDEV GQADTRERKI
510 520 530 540 550
EICTNAYNIL VDEVGFPPED IIFDPNIFAV ATGIDEHNNY AVDFIEAVGD
560 570 580 590 600
IKRTLPHAMI SGGVSNVSFS FRGNNYVREA IHAVFLYHCF KNGMDMGIVN
610 620 630 640 650
AGQLEIYDNV PEDLREAVED VVLNRRDDST ERLLDIATEY LERAVGKVED
660 670 680 690 700
KSALEWRDWP VEKRLEHSLV KGITEFIVED TEEARINAEK PIEVIEGPLM
710 720 730 740 750
DGMNVVGDLF GEGKMFLPQV VKSARVMKQA VAHLEPFINA SKEVGATNGK
760 770 780 790 800
ILLATVKGDV HDIGKNIVGV VLQCNNYEII DLGVMVSCET ILKVAKEENV
810 820 830 840 850
DIIGLSGLIT PSLDEMVHVA KEMERQGFDL PLLIGGATTS KAHTAVKIEQ
860 870 880 890 900
NYSQPVVYVN NASRAVGVCT SLLSDELKPS FVEKLDIDYE RVREQHSRKQ
910 920 930 940 950
PRTKPVTLEV ARANKVAIDW ASYTPPVPLK PGVHIFDNFD VSTLRNYIDW
960 970 980 990 1000
TPFFMTWSLV GKYPKILDHE EVGEEAKRLF KDANDLLDRV EKEGLLKARG
1010 1020 1030 1040 1050
MCALFPASSV GDDIEVYTDE SRTKVAKVLH NLRQQTEKPK GFNYCLSDYI
1060 1070 1080 1090 1100
APKESGKNDW IGGFAVTGGI GERELADEYK ANGDDYNAIM IQAVADRLAE
1110 1120 1130 1140 1150
AFAEYLHEKV RKEIWGYSPN ETLSNDDLIR EKYQGIRPAP GYPACPEHTE
1160 1170 1180 1190 1200
KGALWELMNV EESIGMSLTS SYAMWPGASV SGMYFSHPDS RYFAIAQIQQ
1210 1220
DQAESYADRK GWNMLEAEKW LGPNLN
Length:1,226
Mass (Da):136,369
Last modified:March 15, 2005 - v1
Checksum:iA1464CA5E141F3BD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000020 Genomic DNA. Translation: AAW84832.1.
RefSeqiWP_011261140.1. NC_006840.2.
YP_203720.1. NC_006840.2.

Genome annotation databases

EnsemblBacteriaiAAW84832; AAW84832; VF_0337.
GeneIDi3277291.
KEGGivfi:VF_0337.
PATRICi20111162. VBIVibFis127983_0328.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000020 Genomic DNA. Translation: AAW84832.1 .
RefSeqi WP_011261140.1. NC_006840.2.
YP_203720.1. NC_006840.2.

3D structure databases

ProteinModelPortali Q5E814.
SMRi Q5E814. Positions 655-1225.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 312309.VF_0337.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAW84832 ; AAW84832 ; VF_0337 .
GeneIDi 3277291.
KEGGi vfi:VF_0337.
PATRICi 20111162. VBIVibFis127983_0328.

Phylogenomic databases

eggNOGi COG1410.
HOGENOMi HOG000251409.
KOi K00548.
OMAi LTEHYAM.
OrthoDBi EOG6091CH.

Enzyme and pathway databases

UniPathwayi UPA00051 ; UER00081 .
BioCyci AFIS312309:GIWP-343-MONOMER.

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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700601 / ES114.

Entry informationi

Entry nameiMETH_VIBF1
AccessioniPrimary (citable) accession number: Q5E814
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: March 15, 2005
Last modified: November 26, 2014
This is version 73 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

External Data

Dasty 3