OMT12_DICDI
ID OMT12_DICDI Reviewed; 369 AA.
AC Q54B59;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=O-methyltransferase 12;
DE EC=2.1.1.-;
GN Name=omt12; ORFNames=DDB_G0293888;
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).
RN [2]
RP IDENTIFICATION.
RX PubMed=12796308; DOI=10.1128/ec.2.3.627-637.2003;
RA Maeda M., Sakamoto H., Iranfar N., Fuller D., Maruo T., Ogihara S.,
RA Morio T., Urushihara H., Tanaka Y., Loomis W.F.;
RT "Changing patterns of gene expression in Dictyostelium prestalk cell
RT subtypes recognized by in situ hybridization with genes from microarray
RT analyses.";
RL Eukaryot. Cell 2:627-637(2003).
RN [3]
RP IDENTIFICATION.
RX PubMed=15470253; DOI=10.1128/ec.3.5.1241-1248.2004;
RA Maruo T., Sakamoto H., Iranfar N., Fuller D., Morio T., Urushihara H.,
RA Tanaka Y., Maeda M., Loomis W.F.;
RT "Control of cell type proportioning in Dictyostelium discoideum by
RT differentiation-inducing factor as determined by in situ hybridization.";
RL Eukaryot. Cell 3:1241-1248(2004).
RN [4]
RP IDENTIFICATION.
RX PubMed=15470642; DOI=10.1387/ijdb.041862ns;
RA Shimada N., Maeda M., Urushihara H., Kawata T.;
RT "Identification of new modes of Dd-STATa regulation of gene expression in
RT Dictyostelium by in situ hybridisation.";
RL Int. J. Dev. Biol. 48:679-682(2004).
RN [5]
RP INDUCTION [LARGE SCALE ANALYSIS].
RX PubMed=18590548; DOI=10.1186/1471-2180-8-109;
RA Carilla-Latorre S., Calvo-Garrido J., Bloomfield G., Skelton J., Kay R.R.,
RA Ivens A., Martinez J.L., Escalante R.;
RT "Dictyostelium transcriptional responses to Pseudomonas aeruginosa: common
RT and specific effects from PAO1 and PA14 strains.";
RL BMC Microbiol. 8:109-109(2008).
RN [6]
RP IDENTIFICATION, FUNCTION, AND CHARACTERIZATION.
RX PubMed=18252726; DOI=10.1074/jbc.m709588200;
RA Ghosh R., Chhabra A., Phatale P.A., Samrat S.K., Sharma J., Gosain A.,
RA Mohanty D., Saran S., Gokhale R.S.;
RT "Dissecting the functional role of polyketide synthases in Dictyostelium
RT discoideum: biosynthesis of the differentiation regulating factor 4-methyl-
RT 5-pentylbenzene-1,3-diol.";
RL J. Biol. Chem. 283:11348-11354(2008).
CC -!- FUNCTION: S-adenosyl-L-methionine dependent O-methyltransferase that
CC may be involved in modifying resorcinol ring to synthesize a variant of
CC 4-methyl-5-pentylbenzene-1,3-diol. {ECO:0000269|PubMed:18252726}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=resorcinol + S-adenosyl-L-methionine = 3-methoxyphenol + H(+)
CC + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:26321, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:27810, ChEBI:CHEBI:52678, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789;
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; AAFI02000223; EAL60515.1; -; Genomic_DNA.
DR RefSeq; XP_628929.1; XM_628927.1.
DR AlphaFoldDB; Q54B59; -.
DR SMR; Q54B59; -.
DR STRING; 44689.DDB0229899; -.
DR PaxDb; Q54B59; -.
DR EnsemblProtists; EAL60515; EAL60515; DDB_G0293888.
DR GeneID; 8629471; -.
DR KEGG; ddi:DDB_G0293888; -.
DR dictyBase; DDB_G0293888; omt12.
DR eggNOG; KOG3178; Eukaryota.
DR HOGENOM; CLU_005533_12_0_1; -.
DR InParanoid; Q54B59; -.
DR PhylomeDB; Q54B59; -.
DR PRO; PR:Q54B59; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0008168; F:methyltransferase activity; IDA:dictyBase.
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; IDA:dictyBase.
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 1: Evidence at protein level;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..369
FT /note="O-methyltransferase 12"
FT /id="PRO_0000367480"
FT ACT_SITE 248
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 181
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 204
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 229..231
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 230
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 231
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 244
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ SEQUENCE 369 AA; 42586 MW; 593D2DB9D090152E CRC64;
MSDWDKTMDL LFGFVTGHIH SRMFETILKF SICDLLEDGP KHYSEISKII GFKNESYCYR
LMRYFVPYKL FNESVVQVGL FSKTPSSTQF SKNGTLKNLG RFHCQDHHYR IFESLPKTLE
MGKNQGPSSI GLSSFWEHFE TDESYKQLFH NAMKDYTSLI IDRLISKISL SPNFKTVVDI
GGSHGFLIGK LLESNPNIHG INFDLENIIN SSTSKNENFQ HPRLKHVSGD FFNSVPEADC
YILKYILHDW SDEKCITILN NIHKSLKPNG KLFINDLVLD PSNYTKEAVF KDILMMQYFD
AKERSINEWH QLFEKCGFKI DSVDTSISPQ LMIVSKINSS NINLNDCTNF NSEIVEEKLK
NSLPQFVNC
