YP54_SCHPO
ID YP54_SCHPO Reviewed; 391 AA.
AC B5BP48;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Putative alpha-ketoglutarate-dependent sulfonate dioxygenase;
DE EC=1.14.11.-;
GN ORFNames=SPBC460.04c;
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=18727152; DOI=10.1002/yea.1613;
RA Sasaki M., Idiris A., Tada A., Kumagai H., Giga-Hama Y., Tohda H.;
RT "The gap-filling sequence on the left arm of chromosome 2 in fission yeast
RT Schizosaccharomyces pombe.";
RL Yeast 25:673-679(2008).
CC -!- FUNCTION: Acts as an alpha-ketoglutarate-dependent dioxygenase active
CC on sulfonates. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Organosulfur degradation; alkanesulfonate degradation.
CC -!- SIMILARITY: Belongs to the TfdA dioxygenase family. {ECO:0000305}.
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DR EMBL; AB325691; BAG68904.1; -; Genomic_DNA.
DR AlphaFoldDB; B5BP48; -.
DR SMR; B5BP48; -.
DR STRING; 4896.SPBC460.04c.1; -.
DR PaxDb; B5BP48; -.
DR EnsemblFungi; SPBC460.04c.1; SPBC460.04c.1:pep; SPBC460.04c.
DR PomBase; SPBC460.04c; -.
DR VEuPathDB; FungiDB:SPBC460.04c; -.
DR eggNOG; ENOG502QT05; Eukaryota.
DR HOGENOM; CLU_036005_0_1_1; -.
DR InParanoid; B5BP48; -.
DR OMA; DANSHER; -.
DR UniPathway; UPA00338; -.
DR PRO; PR:B5BP48; -.
DR Proteomes; UP000002485; Chromosome II, gap-filling sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000907; F:sulfonate dioxygenase activity; ISO:PomBase.
DR GO; GO:0046306; P:alkanesulfonate catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0044273; P:sulfur compound catabolic process; ISO:PomBase.
DR Gene3D; 3.60.130.10; -; 1.
DR InterPro; IPR042098; TauD-like_sf.
DR InterPro; IPR003819; TauD/TfdA-like.
DR Pfam; PF02668; TauD; 1.
PE 3: Inferred from homology;
KW Dioxygenase; Iron; Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..391
FT /note="Putative alpha-ketoglutarate-dependent sulfonate
FT dioxygenase"
FT /id="PRO_0000415922"
FT REGION 262..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 204
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 206
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 231
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
FT BINDING 338
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
FT BINDING 353
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 364
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
FT BINDING 368
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
SQ SEQUENCE 391 AA; 44843 MW; 623285144518A6BE CRC64;
MATLTETISK ADKHDEKLTD FQYSKKIFNG VHEVEDDKQR TDFTTVRFGD VEKKFAVPKD
YKYKNVLPTF PNAVYNLTGE LAFEDKGLLA DPKFSNLLKD VTKVEHLARD LGTVLYGIQL
SKLNDAQKNE LARYIAERGV VYFPDQEQTL EEFQELGQYY GHSHKHGSNS RPFEDKFAEF
QVVYSDRFSP YDQHAKNNSL RYWHSDVSFE KQPSAQTFFK ALTVPEQGGD TLFISGYAAY
EALSTPLKKY LEGLTVVHSG KEQSEYHRRS GQHVRLDGDT NAHPIVRTHP VTGWKSLFIS
PGFTRYIPGI PRGESDAILD YLYQHIANLS QSTVRIKWTS NGVAAWDNRI VIHRATYDHL
PQTRHLVRIA AQGEVPFFDA NSHERSEDLR E