A0A2K3CUX5 · A0A2K3CUX5_CHLRE

Function

Cofactor

Protein has several cofactor binding sites:
FAD (UniProtKB | Rhea| CHEBI:57692 )

FMN (UniProtKB | Rhea| CHEBI:58210 )

GO annotations

all annotationsall molecular functionnucleotide bindingmolecular_functionnucleic acid bindingdna bindingchromatin bindingdna-binding transcription factor activityrna bindingcytoskeletal motor activitycatalytic activitynuclease activitysignaling receptor bindingstructural molecule activitytransporter activitybindingprotein bindingtranslation factor activity, rna bindinglipid bindingkinase activitytransferase activityhydrolase activityoxygen bindingenzyme regulator activitycarbohydrate bindingsignaling receptor activitytranslation regulator activitytranscription regulator activityother molecular functionall biological processcarbohydrate metabolic processgeneration of precursor metabolites and energynucleobase-containing compound metabolic processdna metabolic processtranslationlipid metabolic processtransportresponse to stresscell cyclecell communicationsignal transductioncell-cell signalingmulticellular organism developmentcircadian rhythmbiological_processmetabolic processcatabolic processbiosynthetic processresponse to light stimulusresponse to external stimulustropismresponse to biotic stimulusresponse to abiotic stimulusresponse to endogenous stimulusembryo developmentpost-embryonic developmentfruit ripeningabscissionpollinationflower developmentcellular processprogrammed cell deathphotosynthesiscellular component organizationcell growthprotein metabolic processcellular homeostasissecondary metabolic processreproductive processcell differentiationprotein modification processgrowthepigenetic regulation of gene expressionresponse to chemicalanatomical structure developmentregulation of molecular functionother biological processall cellular componentcellular_componentextracellular regioncell wallintracellular anatomical structurenucleusnuclear envelopenucleoplasmnucleoluscytoplasmmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuscytosolribosomecytoskeletonplasma membranechloroplastplastidthylakoidmembraneexternal encapsulating structureother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytosol
Molecular Function[methionine synthase] reductase activity
Molecular Functionflavin adenine dinucleotide binding
Molecular FunctionFMN binding
Biological Processhomocysteine metabolic process
Biological Processmethionine biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Methionine synthase reductase
  • EC number

Gene names

    • ORF names
      CHLRE_16g683550v5

Organism names

Accessions

  • Primary accession
    A0A2K3CUX5

Proteomes

Genome annotation databases

Subcellular Location

PTM/Processing

Features

Showing features for signal, chain.

TypeIDPosition(s)Description
Signal1-29
ChainPRO_501444673430-1772Methionine synthase reductase

Expression

Gene expression databases

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region29-63Disordered
Compositional bias34-52Basic and acidic residues
Domain112-255Flavodoxin-like
Domain418-561Flavodoxin-like
Region572-631Disordered
Region704-724Disordered
Domain725-869Flavodoxin-like
Compositional bias933-1047Basic and acidic residues
Region933-1234Disordered
Compositional bias1101-1116Polar residues
Compositional bias1137-1158Basic and acidic residues
Compositional bias1174-1195Basic and acidic residues
Compositional bias1214-1232Polar residues
Domain1345-1614FAD-binding FR-type
Region1424-1443Disordered

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,772
  • Mass (Da)
    182,052
  • Last updated
    2018-03-28 v1
  • Checksum
    D9FCCFA024F26FDC
MKIGVAVAGGFGALLLLTPLATFLLAASAQKRKTSPKGGDKAARKSETKESNDKAVPMNAGNAAPPSARAVAAAPAAAAATGGNAILARLKQQRAAPPPPAVAATAGAKPPLTFAFASQTGTGAEIARNLAAEAVEKGYKAQCMSLTELGYAALTSGRTPYLVIVASSTGDGDPPDNSGAFFVALRKKQEGKPLVGVKFTLLGLGDSNYTRFMYVSRAIKGRLLDLGAAEFYPCAEADEVDGIESVVDPWSEGLWTALAAETPAAAEQQPPAEVAAAAPAAAPVAAVSVAAPSASVPAPSTGATSSAATGGNAILARLRQQRAAPMEGGAATAAIEPSTTAAAASSAPAAAVAEAGVVVHVATAAAPPGKQDAATAAAPAPAAAAATGGNAILARLKQQRAAPPPPAVAATAGTKPPLTFAFASQTGTGAEIARNLAAEAVEKGYKAQCMSLTELGYAALTSGRTPYLVIVASSTGDGDPPDNSGAFFVALRKKQEGKPLVGVKFTLLGLGDSNYTRFMYVSRAIKGRLLDLGAAEFYPCAEADEVDGIESVVDPWSEGLWTALDADIAPQKDQAADQPPVAVTAGPSGPSRRSVEMMTGMSRTPAASAMPSKPSTPGPQTPTTPGTPSAVAATAPALVDAPSRSLVPETSAKSAVPKVEEAAVPVAATGGAAVLAKLRSGQPNADSAESLTVAAAAAAPEAAAKQENTAAKSAQPPAEPAKPPVTFAYASQTGTGEEIARNLAAEAIQRGYKAICAPLNELGFAAITPSRTPVLVVIASSTGDGDPPENATNFFVALRKKQDKPAPLAGVRYTLLGLGDSNYTRFMGAPRAIKSRLAELGAAEFYPCAEADEVDGIESVVDRWTAGIWAAIAAATAAGQDAMAAVSIDAPSATAAVKPAAVKVGPSESEIAAAAAAAAVAAEAAAKAAAEKEAAEKAAKEPAEKAATEAAEKEAAETAAKEAAEAAEKAAKEAAEKEAAEQAAKDAAEKEAAEKETAEKAAKEAAEKEAAEKEAAEQEAAEKAAKEAAEKEAAEKAAAEKAAKEAADMVAAEAATRAGAEATTAEEAATAATVSAAADAEELAEAEASAAALAAAAQHPERPSSTATSDDGGSLLPSSLLSVMEAGAAPGAHDHGLPTIKESRVFEEEPEPEAAAEAGAKEGKPSGLKVLPEAATEDGDDPLLSPRETEDGGDDMLLTPRGSVRGGGGRPDSRGSVASSTATGTTGTWRRSVDLKSKSHMVAEAARRRSLEKPARLQAKPLNVNFPKREENVVKRKDEKAYGLLLGLAPVGVDTKGAPALLPCRLRLLWEKDEKRTDGVLTREMLRPSREERHKLDPGGMYSPQQPFWAHISDARYETAFWSDRKVLHLELSIRGSNIAYSPGDAIGVLPANHPDLVANLCKRLNLNADRVFYISAPKDTSQAGDAASEAGEAAPATPAGRPATHIPSPCSIGYAFANCVDLTSPARKSLLRLLAEHAHDASEKRTLLFLSAKGGKDAYAHEIAEHQPSLLDLLVRFPSVTPPLDALLDALPPLAPRMYSITSSRRDSAKGPNRLSVALSVVRFKTRYGTRLGVASAWLDRLASPWTTEGISNPANPVWVPIYLRRSADFKPPADLSSPLIMVGPGTGVAPFRGFLQERRALIRENKPESVGEAVLFFGCRREDEDYIFKEELELMKAEGTLSALHVAFSRAQETKVYVQDLIKAQGEKVWGLLQAGGYLYVCGDGAAMAKDVHAALIAVAGTHGGLSEADATAFLQNLTRERRYVRDVWS

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias34-52Basic and acidic residues
Compositional bias933-1047Basic and acidic residues
Compositional bias1101-1116Polar residues
Compositional bias1137-1158Basic and acidic residues
Compositional bias1174-1195Basic and acidic residues
Compositional bias1214-1232Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CM008977
EMBL· GenBank· DDBJ
PNW72074.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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