COMT1_SCHPO
ID COMT1_SCHPO Reviewed; 266 AA.
AC O42898;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Probable catechol O-methyltransferase 1;
DE EC=2.1.1.6;
GN ORFNames=SPBC119.03;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a catechol + S-adenosyl-L-methionine = a guaiacol + H(+) + S-
CC adenosyl-L-homocysteine; Xref=Rhea:RHEA:17877, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33566, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:134251; EC=2.1.1.6;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Cation-dependent O-methyltransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01019}.
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DR EMBL; CU329671; CAA17918.1; -; Genomic_DNA.
DR PIR; T39301; T39301.
DR RefSeq; NP_595284.1; NM_001021191.2.
DR PDB; 5ZY5; X-ray; 2.29 A; A/B=1-266.
DR PDB; 5ZY6; X-ray; 2.10 A; A/B=1-266.
DR PDBsum; 5ZY5; -.
DR PDBsum; 5ZY6; -.
DR AlphaFoldDB; O42898; -.
DR SMR; O42898; -.
DR BioGRID; 276612; 1.
DR STRING; 4896.SPBC119.03.1; -.
DR iPTMnet; O42898; -.
DR MaxQB; O42898; -.
DR PaxDb; O42898; -.
DR EnsemblFungi; SPBC119.03.1; SPBC119.03.1:pep; SPBC119.03.
DR GeneID; 2540074; -.
DR KEGG; spo:SPBC119.03; -.
DR PomBase; SPBC119.03; -.
DR VEuPathDB; FungiDB:SPBC119.03; -.
DR eggNOG; KOG1663; Eukaryota.
DR HOGENOM; CLU_050461_0_0_1; -.
DR InParanoid; O42898; -.
DR OMA; HEYSDLK; -.
DR PhylomeDB; O42898; -.
DR BRENDA; 2.1.1.6; 5613.
DR Reactome; R-SPO-156581; Methylation.
DR Reactome; R-SPO-379397; Enzymatic degradation of dopamine by COMT.
DR Reactome; R-SPO-379398; Enzymatic degradation of Dopamine by monoamine oxidase.
DR PRO; PR:O42898; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008171; F:O-methyltransferase activity; EXP:PomBase.
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; -; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR002935; SAM_O-MeTrfase.
DR Pfam; PF01596; Methyltransf_3; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51682; SAM_OMT_I; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Catecholamine metabolism; Cytoplasm; Magnesium;
KW Metal-binding; Methyltransferase; Nucleus; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..266
FT /note="Probable catechol O-methyltransferase 1"
FT /id="PRO_0000318148"
FT BINDING 56
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 78
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 86
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 106
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 107
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 135
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 162
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 162
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 165
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 190
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT HELIX 11..20
FT /evidence="ECO:0007829|PDB:5ZY6"
FT HELIX 24..30
FT /evidence="ECO:0007829|PDB:5ZY6"
FT HELIX 34..43
FT /evidence="ECO:0007829|PDB:5ZY6"
FT HELIX 58..71
FT /evidence="ECO:0007829|PDB:5ZY6"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:5ZY6"
FT HELIX 85..95
FT /evidence="ECO:0007829|PDB:5ZY6"
FT STRAND 101..107
FT /evidence="ECO:0007829|PDB:5ZY6"
FT HELIX 109..121
FT /evidence="ECO:0007829|PDB:5ZY6"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:5ZY6"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:5ZY6"
FT HELIX 135..147
FT /evidence="ECO:0007829|PDB:5ZY6"
FT STRAND 157..161
FT /evidence="ECO:0007829|PDB:5ZY6"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:5ZY6"
FT HELIX 168..177
FT /evidence="ECO:0007829|PDB:5ZY6"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:5ZY6"
FT HELIX 192..196
FT /evidence="ECO:0007829|PDB:5ZY6"
FT HELIX 198..203
FT /evidence="ECO:0007829|PDB:5ZY6"
FT HELIX 208..217
FT /evidence="ECO:0007829|PDB:5ZY6"
FT STRAND 232..240
FT /evidence="ECO:0007829|PDB:5ZY6"
FT STRAND 253..262
FT /evidence="ECO:0007829|PDB:5ZY6"
SQ SEQUENCE 266 AA; 30267 MW; 99316BCF4FAED5EA CRC64;
MPHMEDNGSE KEQLFLQHIQ NLPQERLDAI RGHPELVLKE IDEFTYPDGS GVRMCIGDVK
GGFIVGKIRE RKPKIMVELG GYLGYSAILF GNEISKIPGG RYYSLEVNED YAKIAYELVK
LAGLDEIVTI MIGKACDSLV ELQQKLLHKD LGFQALDMVF IDHWKDLYVP DLRVIESLNM
IAPGTLLVAD NIITPGAPEY HKYVNMSPEE RRGYQAKVRN VNGFDFIGRW DLIYKTETKE
FEGVIRNKHR KDAVDVTECV GYAKKD
