OMT9_DICDI
ID OMT9_DICDI Reviewed; 357 AA.
AC Q54GZ0;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=O-methyltransferase 9;
DE EC=2.1.1.-;
GN Name=omt9; ORFNames=DDB_G0289823;
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; AAFI02000149; EAL62512.1; -; Genomic_DNA.
DR RefSeq; XP_636017.1; XM_630925.1.
DR AlphaFoldDB; Q54GZ0; -.
DR SMR; Q54GZ0; -.
DR PaxDb; Q54GZ0; -.
DR EnsemblProtists; EAL62512; EAL62512; DDB_G0289823.
DR GeneID; 8627343; -.
DR KEGG; ddi:DDB_G0289823; -.
DR dictyBase; DDB_G0289823; omt9.
DR eggNOG; KOG3178; Eukaryota.
DR HOGENOM; CLU_005533_12_0_1; -.
DR InParanoid; Q54GZ0; -.
DR OMA; EYMEGFL; -.
DR PhylomeDB; Q54GZ0; -.
DR PRO; PR:Q54GZ0; -.
DR Proteomes; UP000002195; Chromosome 5.
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..357
FT /note="O-methyltransferase 9"
FT /id="PRO_0000367479"
FT ACT_SITE 267
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 200
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 224
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 249
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 250
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 263
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ SEQUENCE 357 AA; 41073 MW; E47308D2DB744BFF CRC64;
MDSGLSTPQL PITNMNNEIT TDWDKAMNLI MTCVSGHIHS RMFNIVMKLN ICDILEDGPK
SIKQVSDTIG MDENSCFRLL RYFVAHELFS EDKSNIGTFE KTSISTMFSS KGKLRPMGER
YTHDLHYKMF ESLPETFANG HSNATKSVGV NHFWELFDLH PQYKDLFNQT MKVYTEAAIS
NITQSKGIDF SQYDTVVDIG GNHGLLIGNL LEIYPTIKHG INFDLDVVIN SSDQTLRYSH
PRLTHIPGNF FESVPESDCY IMKFILHDWP TQDCVKILKT ISKSMKPNAK IHLFEIIIDP
RKGYSKYETY IDILMFQMVN AKERTLDEWK ELFELADFKL ERVVDDIKTG CMVVSKK
