OMT2_PHACR
ID OMT2_PHACR Reviewed; 447 AA.
AC P0CT90;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2016, sequence version 1.
DT 03-AUG-2022, entry version 15.
DE RecName: Full=3-O-methyltransferase 2 {ECO:0000303|PubMed:26672450};
DE Short=Mtrase 2 {ECO:0000303|PubMed:26672450};
DE EC=2.1.1.- {ECO:0000269|PubMed:26672450};
GN ORFNames=e_gw1.4.1014.1;
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 3-OH phenolic compounds
CC like isovanillic acid and 3-OH-4-Met cinnamic acid. May play a role in
CC promoting lignin degradation by methylating and inactivating free-
CC 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 8.0. {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; AADS01000354; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P0CT90; -.
DR SMR; P0CT90; -.
DR VEuPathDB; FungiDB:AGR57_4912; -.
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..447
FT /note="3-O-methyltransferase 2"
FT /id="PRO_0000435967"
FT ACT_SITE 338
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 264..265
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O04385"
FT BINDING 287
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O04385"
FT BINDING 318..319
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O04385"
FT BINDING 334
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O04385"
SQ SEQUENCE 447 AA; 49734 MW; EC5E8926B8577A7C CRC64;
MSDYPKTPQA AHLTALVELI SSSVNEVISV YSAAGRDIPS LDSLEEGFLE TPATTPPGLR
HARQIIEAAC AQLCVTIAQP GDCIVNKAFA YTESACLQVA ANAKISDFLA DKPDGLHTEE
LAKLSGVDAG KLGQVLRFLA TKHVYREVRP NVYANNRLSV KLMSSDPVSC NVGVCTGELF
QAATAAWDTL SDKEYGPSYL PTKTAFRKVH GATFFEYYET HVRLNLPRFS GAMVGWGNIT
DRGLLPQMYE WQRLEPGATI CDVGGNNGHA TLDLVKEYPM ISVIVQDLES LRPRWSDLWA
RELPDAIQDG RTSFVPIDFF RDIPVRNCDV YYIRHILHDW PDASCVQILR NVKEAMQPSS
RVLIHEYVLQ QTTRDDVTVE NDSAPEPLLP NYGNGRIRRY YQDITMLLGL NSKERTLQEF
IDIGAQAGLK FVKLWDGGQT ALVEFSC
