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Database: UniProt
Entry: D8U8B0_VOLCA
LinkDB: D8U8B0_VOLCA
Original site: D8U8B0_VOLCA 
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
//
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