DMTA_DICDI
ID DMTA_DICDI Reviewed; 363 AA.
AC Q8T638; Q54HL9;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Des-methyl DIF-1 methyltransferase A {ECO:0000303|PubMed:11163223};
DE EC=2.1.1.- {ECO:0000269|PubMed:9446571};
DE AltName: Full=O-methyltransferase 8;
GN Name=dmtA {ECO:0000303|PubMed:11163223}; Synonyms=omt8;
GN ORFNames=DDB_G0289329;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RC STRAIN=AX2;
RX PubMed=11163223; DOI=10.1016/s1097-2765(00)00147-7;
RA Thompson C.R., Kay R.R.;
RT "The role of DIF-1 signaling in Dictyostelium development.";
RL Mol. Cell 6:1509-1514(2000).
RN [2]
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 [3]
RP CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9446571; DOI=10.1074/jbc.273.5.2669;
RA Kay R.R.;
RT "The biosynthesis of differentiation-inducing factor, a chlorinated signal
RT molecule regulating Dictyostelium development.";
RL J. Biol. Chem. 273:2669-2675(1998).
RN [4]
RP INDUCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=11748133; DOI=10.1242/dev.128.24.4959;
RA Kay R.R., Thompson C.R.;
RT "Cross-induction of cell types in Dictyostelium: evidence that DIF-1 is
RT made by prespore cells.";
RL Development 128:4959-4966(2001).
RN [5]
RP FUNCTION.
RX PubMed=16906151; DOI=10.1038/nchembio811;
RA Austin M.B., Saito T., Bowman M.E., Haydock S., Kato A., Moore B.S.,
RA Kay R.R., Noel J.P.;
RT "Biosynthesis of Dictyostelium discoideum differentiation-inducing factor
RT by a hybrid type I fatty acid-type III polyketide synthase.";
RL Nat. Chem. Biol. 2:494-502(2006).
RN [6]
RP FUNCTION.
RX PubMed=20231486; DOI=10.1073/pnas.1001681107;
RA Neumann C.S., Walsh C.T., Kay R.R.;
RT "A flavin-dependent halogenase catalyzes the chlorination step in the
RT biosynthesis of Dictyostelium differentiation-inducing factor 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:5798-5803(2010).
CC -!- FUNCTION: O-methyltransferase; part of the gene cluster that mediates
CC the biosynthesis of DIF-1 (Differentiation Inducing Factor-1), a signal
CC molecule involved in the differentiation of pstO (prestalk-O) cells
CC (PubMed:9446571). The three-step process begins with the formation of
CC (2,4,6-trihydroxyphenyl)-1-hexan-1-one (THPH) by the polyketide
CC synthase StlB (PubMed:16906151). THPH is then dichlorinated by the
CC flavin-dependent halogenase ChlA (PubMed:20231486). The last step of
CC DIF-1 biosynthesis is the O-methylation of dichloro-THPH (or des-
CC methyl-DIF-1) by the methyltransferase DmtA to yield DIF-1
CC (PubMed:9446571). {ECO:0000269|PubMed:16906151,
CC ECO:0000269|PubMed:20231486, ECO:0000269|PubMed:9446571}.
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 Evidence={ECO:0000269|PubMed:9446571};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.1 uM for chloro-THPH {ECO:0000269|PubMed:9446571};
CC KM=14.6 uM for dichloro-THPH {ECO:0000269|PubMed:9446571};
CC KM=17.7 uM for 2-methoxydichloro-THPH {ECO:0000269|PubMed:9446571};
CC pH dependence:
CC Optimum pH is 6.5-7.5. {ECO:0000269|PubMed:9446571};
CC -!- DEVELOPMENTAL STAGE: Maximally expressed in prespore cells. Detectable
CC expression levels during aggregation stage. Maximum expression at the
CC first-finger/slug stage. {ECO:0000269|PubMed:11163223,
CC ECO:0000269|PubMed:11748133}.
CC -!- INDUCTION: By cyclic-AMP; this induction is inhibited by DIF-1.
CC {ECO:0000269|PubMed:11748133}.
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; AF487404; AAL93252.1; -; mRNA.
DR EMBL; AAFI02000139; EAL62751.1; -; Genomic_DNA.
DR RefSeq; XP_636282.1; XM_631190.1.
DR AlphaFoldDB; Q8T638; -.
DR SMR; Q8T638; -.
DR STRING; 44689.DDB0219945; -.
DR PaxDb; Q8T638; -.
DR EnsemblProtists; EAL62751; EAL62751; DDB_G0289329.
DR GeneID; 8627100; -.
DR KEGG; ddi:DDB_G0289329; -.
DR dictyBase; DDB_G0289329; dmtA.
DR eggNOG; KOG3178; Eukaryota.
DR HOGENOM; CLU_005533_12_0_1; -.
DR InParanoid; Q8T638; -.
DR OMA; IYIDYFY; -.
DR PhylomeDB; Q8T638; -.
DR Reactome; R-DDI-209931; Serotonin and melatonin biosynthesis.
DR SABIO-RK; Q8T638; -.
DR PRO; PR:Q8T638; -.
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; IDA:dictyBase.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IDA:dictyBase.
DR GO; GO:0019438; P:aromatic compound biosynthetic process; IBA:GO_Central.
DR GO; GO:0031154; P:culmination involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0031148; P:DIF-1 biosynthetic process; IDA:dictyBase.
DR GO; GO:0032259; P:methylation; IBA:GO_Central.
DR GO; GO:0010942; P:positive regulation of cell death; IMP:dictyBase.
DR GO; GO:0045595; P:regulation of cell differentiation; IMP:dictyBase.
DR GO; GO:0031288; P:sorocarp morphogenesis; IMP:dictyBase.
DR GO; GO:0031149; P:sorocarp stalk cell differentiation; IMP:dictyBase.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IMP:dictyBase.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR031725; ASMT_dimerisation.
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; PF16864; Dimerisation2; 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 Differentiation; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Sporulation; Transferase.
FT CHAIN 1..363
FT /note="Des-methyl DIF-1 methyltransferase A"
FT /id="PRO_0000328624"
FT ACT_SITE 270
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 195
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 221
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 251
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 266
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ SEQUENCE 363 AA; 41619 MW; 91B1472F1CFACA41 CRC64;
MISNSDCDEN LIKQQQQEIQ DKNFLIDVAI GYTKSNALSC ALKYKIPQLL EDKSKSCKEL
SEILKVNCDN LYRLLRTLST IGIFIEDEVE DGVFRNSRLS NLLRNSNSDS WVNNVYLQSH
PNVIQSFMYL DKTIECGTSQ GMTSQGFSSA WELFEKDKSL NAHFHNTMTS FTSDEIKTIL
EYIDFNQYKS IVDLGGSSGE LLKSIAKSSR GQLVESFINF DLPLVINQNK VNNENGAAEF
DKRYSEVASD LFVDSDYPSA DCYTLKFIFH MFNDDKVLTI LDKISKSIKP NGKVYVFDHI
VQPKNQPYAP FYFDLQMIVN FNGKERSQNE WKTIFEKSPF KIDTILILPD SKRMSVIELS
LKQ
