XANA_NEUCR
ID XANA_NEUCR Reviewed; 420 AA.
AC Q7SEI7;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Alpha-ketoglutarate-dependent xanthine dioxygenase xan-1 {ECO:0000303|PubMed:15948966};
DE EC=1.14.11.48 {ECO:0000269|PubMed:15948966};
GN Name=xan-1 {ECO:0000303|PubMed:15948966}; ORFNames=NCU09738;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
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 -!- SIMILARITY: Belongs to the TfdA dioxygenase family. {ECO:0000305}.
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DR EMBL; CM002239; EAA35204.1; -; Genomic_DNA.
DR RefSeq; XP_964440.1; XM_959347.3.
DR AlphaFoldDB; Q7SEI7; -.
DR SMR; Q7SEI7; -.
DR STRING; 5141.EFNCRP00000009473; -.
DR EnsemblFungi; EAA35204; EAA35204; NCU09738.
DR GeneID; 3880580; -.
DR KEGG; ncr:NCU09738; -.
DR VEuPathDB; FungiDB:NCU09738; -.
DR HOGENOM; CLU_046574_1_0_1; -.
DR InParanoid; Q7SEI7; -.
DR OMA; MVWKNPV; -.
DR Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0097641; F:alpha-ketoglutarate-dependent xanthine dioxygenase activity; IEA:RHEA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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..420
FT /note="Alpha-ketoglutarate-dependent xanthine dioxygenase
FT xan-1"
FT /id="PRO_0000446006"
FT BINDING 157
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P37610"
FT BINDING 159
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P37610"
FT BINDING 206
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:P37610"
FT BINDING 336
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:P37610"
FT BINDING 351
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P37610"
FT BINDING 366
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:P37610"
FT BINDING 366
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P37610"
SQ SEQUENCE 420 AA; 46410 MW; 763C53B811D3ECF6 CRC64;
MASNTTVPVI TPLAHPEGSK LDFGATVSGV DIENLTDRDF AILRTALFTH QVLVIKSQSH
VSPRAQYELT QRFDPLAAPL YGHGNTDSGS VGSKSILHPD LKTIPHQPQV QVIGNGFVPT
YEGLSNIQLR HPHHRTFHST SIPASHDLTH TRFYRWHIDA ALYGGVARAP PVVTTLLAVK
VPQGRRQTCV YDDGTGDELD VPLGTTAFVS GYKMYDILSE TQKAFARSTR VEYAPHPYVW
MSSAKSRSTG LGLVSEGKEM PMEELPEIEE DRIQILPMCW RNPVTGKLAL QVHPSAVRRL
HLEDGTVVED LKEVREIVYG LQRPGIAPGL VYAHDWEEGD LVIFHNRGTL HSVVGAFAES
EVRLFRQCNI AGSEFPMGPE EEEKEEELVH AEQEEGVVEV TKQESLPELR MGAVEVGVAA
