OMT1_PHACR
ID OMT1_PHACR Reviewed; 470 AA.
AC P0CT89;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2016, sequence version 1.
DT 03-AUG-2022, entry version 17.
DE RecName: Full=4-O-methyltransferase 1 {ECO:0000303|PubMed:26672450};
DE Short=Mtrase 1 {ECO:0000303|PubMed:26672450};
DE EC=2.1.1.- {ECO:0000269|PubMed:26672450};
GN ORFNames=fgenesh1_kg.2_#_1379_#_Locus12621v1rpkm4.09;
OS Phanerochaete chrysosporium (strain RP-78 / ATCC MYA-4764 / FGSC 9002)
OS (White-rot fungus) (Sporotrichum pruinosum).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Phanerochaetaceae; Phanerodontia; Phanerodontia chrysosporium.
OX NCBI_TaxID=273507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RP-78 / ATCC MYA-4764 / FGSC 9002;
RX PubMed=15122302; DOI=10.1038/nbt967;
RA Martinez D., Larrondo L.F., Putnam N., Gelpke M.D.S., Huang K., Chapman J.,
RA Helfenbein K.G., Ramaiya P., Detter J.C., Larimer F., Coutinho P.M.,
RA Henrissat B., Berka R., Cullen D., Rokhsar D.;
RT "Genome sequence of the lignocellulose degrading fungus Phanerochaete
RT chrysosporium strain RP78.";
RL Nat. Biotechnol. 22:695-700(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=RP-78 / ATCC MYA-4764 / FGSC 9002;
RX PubMed=16524749; DOI=10.1016/j.fgb.2006.01.003;
RA Vanden Wymelenberg A., Minges P., Sabat G., Martinez D., Aerts A.,
RA Salamov A., Grigoriev I., Shapiro H., Putnam N., Belinky P., Dosoretz C.,
RA Gaskell J., Kersten P., Cullen D.;
RT "Computational analysis of the Phanerochaete chrysosporium v2.0 genome
RT database and mass spectrometry identification of peptides in ligninolytic
RT cultures reveal complex mixtures of secreted proteins.";
RL Fungal Genet. Biol. 43:343-356(2006).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=RP-78 / ATCC MYA-4764 / FGSC 9002;
RX PubMed=24853079; DOI=10.1016/j.fgb.2014.05.001;
RA Ohm R.A., Riley R., Salamov A., Min B., Choi I.-G., Grigoriev I.V.;
RT "Genomics of wood-degrading fungi.";
RL Fungal Genet. Biol. 72:82-90(2014).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=26672450; DOI=10.1016/j.enzmictec.2015.08.016;
RA Pham L.T.M., Kim Y.H.;
RT "Discovery and characterization of new O-methyltransferase from the genome
RT of the lignin-degrading fungus Phanerochaete chrysosporium for enhanced
RT lignin degradation.";
RL Enzyme Microb. Technol. 82:66-73(2016).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that
CC preferentially catalyzes the methylation of 4-OH phenolic compounds
CC like coniferyl alcohol, vanillyl alcohol and ferrulic acid. May play a
CC role in promoting lignin degradation by methylating and inactivating
CC free-hydroxyl phenolic compounds, products of lignin cleavage which are
CC known inhibitors of lignin peroxidases. {ECO:0000269|PubMed:26672450}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:26672450};
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Cation-independent O-methyltransferase family. COMT
CC subfamily. {ECO:0000305}.
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DR EMBL; AADS01000380; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P0CT89; -.
DR SMR; P0CT89; -.
DR PRIDE; P0CT89; -.
DR VEuPathDB; FungiDB:AGR57_2642; -.
DR GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR GO; GO:0046274; P:lignin catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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 Pfam; PF00891; Methyltransf_2; 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 Lignin degradation; Methyltransferase; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..470
FT /note="4-O-methyltransferase 1"
FT /id="PRO_0000435966"
FT ACT_SITE 348
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 274..275
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O04385"
FT BINDING 297
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O04385"
FT BINDING 328..329
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O04385"
FT BINDING 344
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O04385"
SQ SEQUENCE 470 AA; 51784 MW; 4471BE4883C37449 CRC64;
MPSPLRQLLE LMIQAVETLE SVCEEKGISL PDLHAPYTPA SEAFLRIPAA IEAANVITAA
ADHMSAIVSP PTSYLYKFLG GPCRAVAIRA CLESNVSEII REAGPSGIHV DDIAKKNGHD
AQKLARFLRY LATHHIYREV SPDVFTHSRL SCFFDTYKPS AEVIANPKQK YDNTRGFAAP
ASHHLDITFK AAALAWETMD DPKTGHSDEL TDAPFARAFP EDKTLWNLLE RDAFARNRFD
LTMVAVAQRQ SPDSIFRAFD WERLPAGALV VEVGGGMGTS AFPLATKYPE MRLVVQDLPD
VIAKAEKLWT EKMPDALSSG RVVLQGHDCF APQPQTDAAV FLLKMILHDW SDEYCVKILR
QLRAAARPDT ALVIVDCLVP LACRLDDAAE AALPGAVGPQ APPPLLPNYG TVNEYVYNMD
VMMHLLFNAQ ERTVAQFTRV LLRAGWRVCA VHRTQEGNGV FLQSVEAVPA
