XANA_SCHPO
ID XANA_SCHPO Reviewed; 413 AA.
AC O74885; Q9C0U8;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Alpha-ketoglutarate-dependent xanthine dioxygenase xan1 {ECO:0000303|PubMed:15948966};
DE EC=1.14.11.48 {ECO:0000269|PubMed:15948966};
GN Name=xan1; ORFNames=SPCC576.01c, SPCPB1C11.04c;
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=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 FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=15948966; DOI=10.1111/j.1365-2958.2005.04686.x;
RA Cultrone A., Scazzocchio C., Rochet M., Montero-Moran G., Drevet C.,
RA Fernandez-Martin R.;
RT "Convergent evolution of hydroxylation mechanisms in the fungal kingdom:
RT molybdenum cofactor-independent hydroxylation of xanthine via alpha-
RT ketoglutarate-dependent dioxygenases.";
RL Mol. Microbiol. 57:276-290(2005).
CC -!- FUNCTION: Alpha-ketoglutarate-dependent xanthine dioxygenase is a non-
CC heme mononuclear Fe(2+) enzyme that decarboxylates alpha-ketoglutarate
CC to succinate and CO(2) while hydroxylating xanthine to generate uric
CC acid (PubMed:15948966). Allows xanthine utilization as a nitrogen
CC source (PubMed:15948966). {ECO:0000269|PubMed:15948966}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + O2 + xanthine = CO2 + succinate + urate;
CC Xref=Rhea:RHEA:43120, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:17712, ChEBI:CHEBI:17775,
CC ChEBI:CHEBI:30031; EC=1.14.11.48;
CC Evidence={ECO:0000269|PubMed:15948966};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43121;
CC Evidence={ECO:0000269|PubMed:15948966};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:P37610};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:P37610};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:C8VSZ2}.
CC -!- DISRUPTION PHENOTYPE: Leads to cells defective for the utilization of
CC hypoxanthine or xanthine as nitrogen sources, while being still able to
CC utilize uric acid or allantoic acid. {ECO:0000269|PubMed:15948966}.
CC -!- SIMILARITY: Belongs to the TfdA dioxygenase family. {ECO:0000305}.
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DR EMBL; CU329672; CAC36937.1; -; Genomic_DNA.
DR PIR; T41411; T41411.
DR RefSeq; NP_588427.2; NM_001023418.1.
DR AlphaFoldDB; O74885; -.
DR SMR; O74885; -.
DR BioGRID; 276110; 10.
DR STRING; 4896.SPCC576.01c.1; -.
DR MaxQB; O74885; -.
DR PaxDb; O74885; -.
DR EnsemblFungi; SPCC576.01c.1; SPCC576.01c.1:pep; SPCC576.01c.
DR GeneID; 2539549; -.
DR KEGG; spo:SPCC576.01c; -.
DR PomBase; SPCC576.01c; xan1.
DR VEuPathDB; FungiDB:SPCC576.01c; -.
DR eggNOG; ENOG502QS34; Eukaryota.
DR HOGENOM; CLU_046574_1_0_1; -.
DR InParanoid; O74885; -.
DR OMA; MVWKNPV; -.
DR PhylomeDB; O74885; -.
DR PRO; PR:O74885; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0097641; F:alpha-ketoglutarate-dependent xanthine dioxygenase activity; IDA:PomBase.
DR GO; GO:0005506; F:iron ion binding; TAS:PomBase.
DR GO; GO:0009115; P:xanthine catabolic process; IMP: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 1: Evidence at protein level;
KW Cytoplasm; Dioxygenase; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..413
FT /note="Alpha-ketoglutarate-dependent xanthine dioxygenase
FT xan1"
FT /id="PRO_0000194021"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 183
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P37610"
FT BINDING 185
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P37610"
FT BINDING 228
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:P37610"
FT BINDING 362
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:P37610"
FT BINDING 377
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P37610"
FT BINDING 389
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:P37610"
SQ SEQUENCE 413 AA; 46604 MW; E313B5A751B58531 CRC64;
MSATATTTVV EPPTTTLTGA TEPPFTAYTT SQGLRVSPVP LPEHNTDVGF GALIENVDLN
NLSDEQFEDI RKALFEHQVV CFPNQHNLPP ETQYAITHRF DPESSTYGHG NRTNQQNNSI
LHPDLHTLPG VPQVQLIGHG VVKDHYGLEE VRLKHPHHRT FHRDPISEEE EKEKQVTRFY
RWHIDAALYD YNPPVVTTLL AVNAPQGTQT LRYDDKSGHE MPVPLGSTAF ASGYRMYELL
TDEEKKVAAR TRVQYFPHAY VTINKARALP NGLGMYSEGL ELDKSELPPW EESRVKTFPL
LWKNPVTGKL ALQTHGCCAE KILIDNEDGT TTVIDDLPKV REILYNYQRP GINPERVYCH
DWKNGDFVIF HNRGVTHCIT GAYRDDQTRI FHQCNLAASH PPAGPSEEDI AAM
