Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9AJQ8

- METH_ALIFS

UniProt

Q9AJQ8 - METH_ALIFS

Protein

Methionine synthase

Gene

metH

Organism
Aliivibrio fischeri (Vibrio fischeri)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 67 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    Methylcobalamin (MeCBL).By similarity
    Binds 1 zinc ion per subunit.By similarity

    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

    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

    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.
    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

    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

    « Hide

    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: October 1, 2014
    This is version 67 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