ID D8U8B0_VOLCA Unreviewed; 429 AA.
AC D8U8B0;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=Arsenite methyltransferase {ECO:0000256|ARBA:ARBA00034545};
DE EC=2.1.1.137 {ECO:0000256|ARBA:ARBA00034521};
GN ORFNames=VOLCADRAFT_95757 {ECO:0000313|EMBL:EFJ44058.1};
OS Volvox carteri f. nagariensis.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Volvocaceae; Volvox.
OX NCBI_TaxID=3068 {ECO:0000313|Proteomes:UP000001058};
RN [1] {ECO:0000313|EMBL:EFJ44058.1, ECO:0000313|Proteomes:UP000001058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=f. Nagariensis / Eve {ECO:0000313|Proteomes:UP000001058};
RX PubMed=20616280; DOI=10.1126/science.1188800;
RA Prochnik S.E., Umen J., Nedelcu A.M., Hallmann A., Miller S.M., Nishii I.,
RA Ferris P., Kuo A., Mitros T., Fritz-Laylin L.K., Hellsten U., Chapman J.,
RA Simakov O., Rensing S.A., Terry A., Pangilinan J., Kapitonov V., Jurka J.,
RA Salamov A., Shapiro H., Schmutz J., Grimwood J., Lindquist E., Lucas S.,
RA Grigoriev I.V., Schmitt R., Kirk D., Rokhsar D.S.;
RT "Genomic analysis of organismal complexity in the multicellular green alga
RT Volvox carteri.";
RL Science 329:223-226(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 [thioredoxin]-dithiol + arsenic triglutathione + H2O + 2 S-
CC adenosyl-L-methionine = 2 [thioredoxin]-disulfide + dimethylarsinous
CC acid + 3 glutathione + 2 H(+) + 2 S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:69464, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:23808,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:59789, ChEBI:CHEBI:183640;
CC EC=2.1.1.137; Evidence={ECO:0000256|ARBA:ARBA00034402};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 [thioredoxin]-dithiol + arsenic triglutathione + 3 S-
CC adenosyl-L-methionine = 3 [thioredoxin]-disulfide + 3 glutathione + 3
CC H(+) + 3 S-adenosyl-L-homocysteine + trimethylarsine;
CC Xref=Rhea:RHEA:69432, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:27130, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:50058, ChEBI:CHEBI:57856, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:183640; EC=2.1.1.137;
CC Evidence={ECO:0000256|ARBA:ARBA00034419};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-dithiol + arsenic triglutathione + 2 H2O + S-
CC adenosyl-L-methionine = [thioredoxin]-disulfide + 3 glutathione +
CC H(+) + methylarsonous acid + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:69460, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17826,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:59789, ChEBI:CHEBI:183640;
CC EC=2.1.1.137; Evidence={ECO:0000256|ARBA:ARBA00034416};
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Arsenite
CC methyltransferase family. {ECO:0000256|ARBA:ARBA00034487}.
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DR EMBL; GL378367; EFJ44058.1; -; Genomic_DNA.
DR RefSeq; XP_002954859.1; XM_002954813.1.
DR AlphaFoldDB; D8U8B0; -.
DR STRING; 3068.D8U8B0; -.
DR GeneID; 9621586; -.
DR KEGG; vcn:VOLCADRAFT_95757; -.
DR eggNOG; ENOG502QQD6; Eukaryota.
DR InParanoid; D8U8B0; -.
DR OrthoDB; 101010at2759; -.
DR Proteomes; UP000001058; Unassembled WGS sequence.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.5.100; -; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR026669; Arsenite_MeTrfase-like.
DR InterPro; IPR025714; Methyltranfer_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR43675; ARSENITE METHYLTRANSFERASE; 1.
DR PANTHER; PTHR43675:SF8; ARSENITE METHYLTRANSFERASE; 1.
DR Pfam; PF13847; Methyltransf_31; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000001058};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 88..246
FT /note="Methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13847"
SQ SEQUENCE 429 AA; 46280 MW; 68FE1EA8FCC7EE68 CRC64;
MTATPVEPAA LAELTAAKQL GMDQAAVKET VKEYYGETLK GTGDLRTSAC TACKAPPPAV
RAALGAVPSE IKDKFYGCGN PIPTGIEGLR VLDLGCGSGR DCYVAAKLVG EKGTVTDMTI
HMSDSVDMTP PQLDVARAHC KSYCCETLGY GQPNMQFVQG EIEYLDRAGI EDESVDLIIS
NCVINLSPDK ARVLSESYRV LAPGGEMHFS DVYCDRRLPA AIRTHPVLLG ECLAGALYVN
DFIRLCRKVG FTDPRQLECE EITLHDPELR DLVGEARFYS ITYRKIFGEG PERLLRGFRT
RPKFLGTLVA VYKGTLPGCP HAYDLDDHHR PPGLRFKFVS FITVPSSLLP CPAPLLCRPP
PPSFVTNKPM LVCGNTASMV GETWLRPHFT VIGDRAVHFG QFDCSGPKVT AASPATSGLT
GACAGGACC
//