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O33465

- METH_PSEPU

UniProt

O33465 - METH_PSEPU

Protein

Methionine synthase

Gene

metH

Organism
Pseudomonas putida (Arthrobacter siderocapsulatus)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 63 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    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.Curated

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi250 – 2501ZincPROSITE-ProRule annotation
    Metal bindingi313 – 3131ZincPROSITE-ProRule annotation

    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
    OrganismiPseudomonas putida (Arthrobacter siderocapsulatus)
    Taxonomic identifieri303 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – ›607›607Methionine synthasePRO_0000204535Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliO33465.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini8 – 328321Hcy-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini359 – ›607›249Pterin-bindingPROSITE-ProRule annotationAdd
    BLAST

    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 Hcy-binding domain.PROSITE-ProRule annotation
    Contains 1 pterin-binding domain.PROSITE-ProRule annotation

    Family and domain databases

    Gene3Di3.20.20.20. 1 hit.
    3.20.20.330. 1 hit.
    InterProiIPR011005. Dihydropteroate_synth-like.
    IPR011822. MetH.
    IPR000489. Pterin-binding.
    IPR003726. S_MeTrfase.
    [Graphical view]
    PfamiPF00809. Pterin_bind. 1 hit.
    PF02574. S-methyl_trans. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000381. MetH. 1 hit.
    SUPFAMiSSF51717. SSF51717. 1 hit.
    SSF82282. SSF82282. 1 hit.
    PROSITEiPS50970. HCY. 1 hit.
    PS50972. PTERIN_BINDING. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Fragment.

    O33465-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSDRSARLQA LQNALKERIL ILDGGMGTMI QSYRLEEHDY RGTRFADWPS    50
    DVKGNNDLLL LSRPDVIAAI EKAYLDAGAD ILETNTFNAT QISQADYGME 100
    SLVYELNVEG ARIARQVADA KTLETPDKPR FVAGVLGPTS RTCSISPDVN 150
    DPGYRNVTFD ELVENYIEAT RGLIEGGADL ILIETIFDTL NAKAAIFAVQ 200
    QVFEEDAVEL PIMISGTITD ASGRTLSGQT TEAFWNSVRH AKPISVGLNC 250
    ALGAKDLRPY LEELSTKADT HVSAHPNAGL PNAFGEYDET PAEMAAVVEE 300
    FAASGFLNII GGCSGTTPGH IQAIAEAVAK YKPREIPEIA KACRLSGLEP 350
    FTIDGQSLFV NVGERTNITG SAKFARLIRE ENYTEALEVA LQQVEAGAQV 400
    IDINMDEGML DSQAAMVRFL NMIAGEPDIS RVPIMIDSSK GEVIEAGLKC 450
    IQGKGIVNSI SMKEGVEQFK HHARLCKRYG AAVVVMAFDE VGQADTAARK 500
    KEICKRSYDI LVNEVGFPPE DIIFDPNIFA VATGIEEHNN YAVDFIEACA 550
    YIRDHLPHAL TSGGVSNVSF SFRGNNPVRE AIHSVFLFHA ISNGLTMGIV 600
    NAGLLEI 607
    Length:607
    Mass (Da):65,840
    Last modified:January 1, 1998 - v1
    Checksum:iBB7743CC28A922B3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei607 – 6071

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ000978 Genomic DNA. Translation: CAA04437.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ000978 Genomic DNA. Translation: CAA04437.1 .

    3D structure databases

    ProteinModelPortali O33465.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00051 ; UER00081 .

    Family and domain databases

    Gene3Di 3.20.20.20. 1 hit.
    3.20.20.330. 1 hit.
    InterProi IPR011005. Dihydropteroate_synth-like.
    IPR011822. MetH.
    IPR000489. Pterin-binding.
    IPR003726. S_MeTrfase.
    [Graphical view ]
    Pfami PF00809. Pterin_bind. 1 hit.
    PF02574. S-methyl_trans. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000381. MetH. 1 hit.
    SUPFAMi SSF51717. SSF51717. 1 hit.
    SSF82282. SSF82282. 1 hit.
    PROSITEi PS50970. HCY. 1 hit.
    PS50972. PTERIN_BINDING. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cis-trans isomerization of unsaturated fatty acids: cloning and sequencing of the cti gene from Pseudomonas putida P8."
      Holtwick R., Meinhardt F., Keweloh H.
      Appl. Environ. Microbiol. 63:4292-4297(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: P8.

    Entry informationi

    Entry nameiMETH_PSEPU
    AccessioniPrimary (citable) accession number: O33465
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 63 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

    Caution

    Ser-314 is present instead of the conserved Cys which is expected to be a zinc-binding residue.Curated

    Documents

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

    External Data

    Dasty 3