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Q9AJQ8

- METH_ALIFS

UniProt

Q9AJQ8 - METH_ALIFS

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Protein

Methionine synthase

Gene
metH
Organism
Aliivibrio fischeri (Vibrio fischeri)
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 bindingi249 – 2491Zinc By similarity
Metal bindingi312 – 3121Zinc By similarity
Metal bindingi313 – 3131Zinc By similarity
Metal bindingi761 – 7611Cobalt (cobalamin axial ligand) By similarity
Binding sitei806 – 8061Cobalamin By similarity
Binding sitei949 – 9491S-adenosyl-L-methionine By similarity
Binding sitei1137 – 11371S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding sitei1141 – 11411Cobalamin; via carbonyl oxygen By 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
OrganismiAliivibrio fischeri (Vibrio fischeri)
Taxonomic identifieri668 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeAliivibrio

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_0000204540Add
BLAST

Proteomic databases

PRIDEiQ9AJQ8.

Structurei

3D structure databases

ProteinModelPortaliQ9AJQ8.
SMRiQ9AJQ8. Positions 655-1225.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 327321Hcy-bindingAdd
BLAST
Domaini358 – 619262Pterin-bindingAdd
BLAST
Domaini652 – 74695B12-binding N-terminalAdd
BLAST
Domaini748 – 883136B12-bindingAdd
BLAST
Domaini899 – 1226328AdoMet activationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni836 – 8372Cobalamin-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

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.

Q9AJQ8-1 [UniParc]FASTAAdd to Basket

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MAGSNIKVQI EKQLSERILL IDGGMGTMIQ GYKFEEKDYR GGRFNQWHCD     50
LKGNNDLLVL SQPQIIRDIH EAYLEAGADI LETNTFNATT IAMADYDMES 100
LSEEINFEAA KLAREVADKW TEKTPNKPRY VAGVLGPTNR TCSISPDVND 150
PGFRNVSFDE LVEAYSESTR ALIRGGSDLI LIETIFDTLN AKACSFAVES 200
VFEELGITLP VMISGTITDA SGRTLSGQTT EAFYNALRHV KPISFGLNCA 250
LGPDELREYV SELSRISECY VSAHPNAGLP NAFGEYDLSP EDMAEHVAEW 300
ASSGFLNLIG GCCGTTPEHI RQMALVVEGV KPRQLPELPV ACRLSGLEPL 350
TIEKDSLFIN VGERTNVTGS ARFKRLIKEE LYDEALSVAQ EQVENGAQII 400
DINMDEGMLD AEACMVRFLN LCASEPEISK VPVMVDSSKW EVIEAGLKCI 450
QGKGIVNSIS LKEGKEKFVH QAKLIRRYGA AVIVMAFDEV GQADTRERKI 500
EICTNAYNIL VDEVGFPPED IIFDPNIFAV ATGIDEHNNY AVDFIEAVGD 550
IKRTLPHAMI SGGVSNVSFS FRGNNYVREA IHAVFLYHCF KNGMDMGIVN 600
AGQLEIYDNV PEDLREAVED VVLNRRDDST ERLLDIATEY LERAVGKVED 650
KSALEWRDWP VEKRLEHSLV KGITEFIVED TEEARINAER PIEVIEGPLM 700
DGMNVVGDLF GEGKMFLPQV VKSARVMKQA VAHLEPFINA SKEVGATNGK 750
ILLATVKGDV HDIGKNIVGV VLQCNNYEII DLGVMVSCET ILKVAKEENV 800
DIIGLSGLIT PSLDEMVHVA KEMERQGFDL PLLIGGATTS KAHTAVKIEQ 850
NYSQPVVYVN NASRAVGVCT SLLSNELKPS FVEKLDIDYE RVREQHSRKQ 900
PRTKPVTLEV ARANKVAIDW ASYTPPVPLK PGVHIFDNFD VSTLRNYIDW 950
TPFFMTWSLV GKYPKILEHE EVGEEAKRLF KDANDLLDRV EKEGLLKARG 1000
MCALFPASSV GDDIEVYTDE SRTTVAKVLH NLRQQTEKPK GFNYCLSDYI 1050
APKESGKNDW IGGFAVTGGI GERELADEYK ANGDDYNAIM IQAVADRLAE 1100
AFAEYLHEKV RKEIWGYSPN ETLSNDDLIR EKYQGIRPAP GYPACPEHTE 1150
KGALWELMNV EESIGMSLTS SYAMWPGASV SGMYFSHPDS RYFAIAQIQQ 1200
DQAESYADRK GWNMLEAEKW LGPNLN 1226
Length:1,226
Mass (Da):136,266
Last modified:June 1, 2001 - v1
Checksum:iAF210E43E119E50C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB039955 Genomic DNA. Translation: BAB39355.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB039955 Genomic DNA. Translation: BAB39355.1 .

3D structure databases

ProteinModelPortali Q9AJQ8.
SMRi Q9AJQ8. Positions 655-1225.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi Q9AJQ8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

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. "Identification of the cobalamin-dependent methionine synthase gene, metH, in Vibrio fischeri ATCC 7744 by sequencing using genomic DNA as a template."
    Kasai S., Yamazaki T.
    Gene 264:281-288(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 7744 / DSM 507 / NCIMB 1281 / 398.

Entry informationi

Entry nameiMETH_ALIFS
AccessioniPrimary (citable) accession number: Q9AJQ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 66 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.

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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