OMT7_DICDI
ID OMT7_DICDI Reviewed; 339 AA.
AC Q54S95;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=O-methyltransferase 7;
DE EC=2.1.1.-;
GN Name=omt7; ORFNames=DDB_G0282591;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3,5-dichloro-2,4,6-trihydroxyphenyl)hexan-1-one + S-adenosyl-
CC L-methionine = 1-(3,5-dichloro-2,6-dihydroxy-4-methoxyphenyl)hexan-1-
CC one + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:48396,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:90397, ChEBI:CHEBI:90398;
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Cation-independent O-methyltransferase family. COMT
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01020}.
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DR EMBL; AAFI02000047; EAL66155.1; -; Genomic_DNA.
DR RefSeq; XP_640144.1; XM_635052.1.
DR AlphaFoldDB; Q54S95; -.
DR SMR; Q54S95; -.
DR STRING; 44689.DDB0266733; -.
DR PaxDb; Q54S95; -.
DR EnsemblProtists; EAL66155; EAL66155; DDB_G0282591.
DR GeneID; 8623681; -.
DR KEGG; ddi:DDB_G0282591; -.
DR dictyBase; DDB_G0282591; omt7.
DR eggNOG; KOG3178; Eukaryota.
DR HOGENOM; CLU_005533_12_0_1; -.
DR InParanoid; Q54S95; -.
DR OMA; MMMTANG; -.
DR PhylomeDB; Q54S95; -.
DR PRO; PR:Q54S95; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0106268; F:3,5-dichloro-THPH methyl transferase activity; IEA:RHEA.
DR GO; GO:0008171; F:O-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IBA:GO_Central.
DR GO; GO:0019438; P:aromatic compound biosynthetic process; IBA:GO_Central.
DR GO; GO:0032259; P:methylation; IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR016461; COMT-like.
DR InterPro; IPR001077; O_MeTrfase_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11746; PTHR11746; 1.
DR Pfam; PF00891; Methyltransf_2; 1.
DR PIRSF; PIRSF005739; O-mtase; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51683; SAM_OMT_II; 1.
PE 3: Inferred from homology;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..339
FT /note="O-methyltransferase 7"
FT /id="PRO_0000367585"
FT ACT_SITE 250
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 186
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 209
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 232
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 233
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 246
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ SEQUENCE 339 AA; 39662 MW; 0A374B5C6889B863 CRC64;
MESNDLNKES LENWNESWDL VMTFGMGHLT SKLFNILMNN SIFDMINESP KHYKEIAKII
NFNEFSCYRL LRYFVPYGLF EENNEIFSIT NKSKKLIKSG GIYNLCTFFS SNDYFKLYST
IPESFEQNKN LGPSSFGFDD FWDIVKTNEH FKYSFNQEMR EFSNLSIPTI IKNTDFSSFN
TVVDVGGSHG RIVGELVKKY ENLNGIVFDL ETVINSSIEK IKHPRIEYVS GSFFESVPSA
DCYVLKNILH DWDDEKCLEI LKTISKSMKE NSKIFIFDEI IDPNDYRKLS LFLDVTVFHF
FNSRERSLND WKQLCDKSDF KIDSINNVTQ PQLLILSKK
