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Database: UniProt
Entry: A0A0A2L647_PENIT
LinkDB: A0A0A2L647_PENIT
Original site: A0A0A2L647_PENIT 
ID   A0A0A2L647_PENIT        Unreviewed;       435 AA.
AC   A0A0A2L647;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=catechol O-methyltransferase {ECO:0000256|ARBA:ARBA00012880};
DE            EC=2.1.1.6 {ECO:0000256|ARBA:ARBA00012880};
GN   ORFNames=PITC_098650 {ECO:0000313|EMBL:KGO75582.1};
OS   Penicillium italicum (Blue mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO75582.1, ECO:0000313|Proteomes:UP000030104};
RN   [1] {ECO:0000313|EMBL:KGO75582.1, ECO:0000313|Proteomes:UP000030104}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHI-1 {ECO:0000313|EMBL:KGO75582.1,
RC   ECO:0000313|Proteomes:UP000030104};
RX   PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA   Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA   Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT   "Genome, transcriptome, and functional analyses of Penicillium expansum
RT   provide new insights into secondary metabolism and pathogenicity.";
RL   Mol. Plant Microbe Interact. 28:232-248(2015).
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Cation-dependent O-methyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00023453}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KGO75582.1}.
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DR   EMBL; JQGA01000456; KGO75582.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A2L647; -.
DR   STRING; 40296.A0A0A2L647; -.
DR   HOGENOM; CLU_630217_0_0_1; -.
DR   OrthoDB; 4040098at2759; -.
DR   PhylomeDB; A0A0A2L647; -.
DR   Proteomes; UP000030104; Unassembled WGS sequence.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0006584; P:catecholamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR002935; SAM_O-MeTrfase.
DR   PANTHER; PTHR43836; CATECHOL O-METHYLTRANSFERASE 1-RELATED; 1.
DR   PANTHER; PTHR43836:SF2; CATECHOL O-METHYLTRANSFERASE 1-RELATED; 1.
DR   Pfam; PF13578; Methyltransf_24; 1.
DR   SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51682; SAM_OMT_I; 1.
PE   3: Inferred from homology;
KW   Catecholamine metabolism {ECO:0000256|ARBA:ARBA00022939};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:KGO75582.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030104};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KGO75582.1}.
SQ   SEQUENCE   435 AA;  49100 MW;  28C5FA163FAFC342 CRC64;
     MAEPEIFTKY PSLKKMEGLN DEDIVESHDG REVTLLKYIY NHPDLDTKLR GSPSAILAAM
     DEFASQEDFL INIGSDKAQK LTDLVREYRP RVVVELGGYV GYSAILFGYI LKEIDEQHKP
     ELEEGEKSAS SKLKIYSVEI DPLIASVAMN LVSLAGLQDI VEVIVGASAH TLQRFHDEGI
     LAKTGIDLLF LDHDEALYEP DVKLAEKLGF LDKEDTVVIA DNVVRPGAPE YRSYMRQNPR
     LSQSWGLAGL IVPGDFECGW RAKKMGLKGI SKKLGQPVEE NRIGYAGMDA RMELIIGRHP
     IGTGKGFLLA GQLLLADCQE IRGIWEEVQM ARVYFVEVLH MHLRWYRRRA EENLVIFHCD
     DIDAVPVVNV SPKNIDTVIV DGKIVKQNDR LVGVDWEFLR DQMICRSQRL TEQAKVEMEK
     AESLFHSIFE KAVET
//
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