ID   OMT10_DICDI             Reviewed;         437 AA.
AC   Q54FP4;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 2.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=O-methyltransferase 10;
DE            EC=2.1.1.-;
GN   Name=omt10; ORFNames=DDB_G0290719;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AAFI02000168; EAL62082.2; -; Genomic_DNA.
DR   RefSeq; XP_635585.3; XM_630493.2.
DR   AlphaFoldDB; Q54FP4; -.
DR   SMR; Q54FP4; -.
DR   STRING; 44689.DDB0266735; -.
DR   PaxDb; Q54FP4; -.
DR   GeneID; 8627793; -.
DR   KEGG; ddi:DDB_G0290719; -.
DR   dictyBase; DDB_G0290719; omt10.
DR   eggNOG; KOG3178; Eukaryota.
DR   HOGENOM; CLU_627671_0_0_1; -.
DR   InParanoid; Q54FP4; -.
DR   OMA; CELWDLA; -.
DR   PhylomeDB; Q54FP4; -.
DR   PRO; PR:Q54FP4; -.
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   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..437
FT                   /note="O-methyltransferase 10"
FT                   /id="PRO_0000371323"
FT   ACT_SITE        335
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         259
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         282
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         315
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         316
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ   SEQUENCE   437 AA;  49896 MW;  B06C97040C847113 CRC64;
     MEGVLSSLLA SSLIVGFPSL IFVCSILIYY YLCVMKKKIS SKDSLPPVIG VYIMRCIYSI
     TQYWEMIIPQ IKLYRISNDY IVFQCLSVVF TLKVMDYLKD GPKTIRELSQ LTKSSEKNLF
     RVMRALTQEH IFNYNQSNQT FSLNSCSKLL TSPPPPSSSP FEQNGILSTN DEELGCIFSM
     LSYPTFIDAW RSLKECIESG VSGFQAKHGM TFFQYIDEKD TYIKKIFDSA MRQSYATKIH
     TQIINGYDFS KYKKVCDIGG GIGFLGFEIV NHNANTCVCV LELEETVRNG LEQSKVDEKK
     QRIIEEQRLV FKTGNMFIPR SIPSANLYIM MQVIHDWNNN DAIKILSSVA STMRMERNHT
     GQSPKLLIID SILDDNINND TYKRSCIPDI IMMAIVGGEE RTLSQWGHII KESGLQVLTI
     KKFNRPPFLS LIELTIQ