KEGG   ENZYME: 1.14.11.48
Entry
EC 1.14.11.48               Enzyme                                 
Name
xanthine dioxygenase;
XanA;
alpha-ketoglutarate-dependent xanthine hydroxylase
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor
Sysname
xanthine,2-oxoglutarate:oxygen oxidoreductase
Reaction(IUBMB)
xanthine + 2-oxoglutarate + O2 = urate + succinate + CO2 [RN:R10920]
Reaction(KEGG)
R10920
Substrate
xanthine [CPD:C00385];
2-oxoglutarate [CPD:C00026];
O2 [CPD:C00007]
Product
urate [CPD:C00366];
succinate [CPD:C00042];
CO2 [CPD:C00011]
Comment
Requires Fe2+ and L-ascorbate. The enzyme, which was characterized from fungi, is specific for xanthine.
History
EC 1.14.11.48 created 2015
Orthology
K23516  xanthine dioxygenase
Genes
APROF751_4638
KLAKLLA0_E04357g
KMXKLMA_20520
LTHKLTH0A03674g
ZROZYRO0D16324g
TGBHG536_0C04630
TDLTDEL_0H02320(TDEL0H02320)
ZMKHG535_0F03460
PPAPAS_chr3_0332
DHADEHA2A01518g
PICPICST_34838
PGUPGUG_04939
SPAASPAPADRAFT_60857
LELPVL30_001093
CALCAALFM_C201540WA(CaO19.1461)
CTPCTRG_01245
COTCORT_0A13470
CDUCD36_16390
CTENCANTEDRAFT_112698
YLIYALI0A06974g
CLUCLUG_03270
CLUSA9F13_01g09218
CAURCJI96_0002396
SLBAWJ20_5294
PKZC5L36_0E04300
BNNFOA43_002239
BBRXBRETT_005011
OPAHPODL_02648
SLUDSCDLUD_000378
NCRNCU09738
NTENEUTE1DRAFT78605(NEUTE1DRAFT_78605)
SMPSMAC_04772
PANPODANSg7245
PBELQC761_602860(XAN1)
PPSDQC762_602860(XAN1)
PPSPQC763_602860(XAN1)
PPSAQC764_602860(XAN1)
PGRIPgNI_08720 PgNI_11652
TMNUCRPA7_562 UCRPA7_8167 UCRPA7_8169
SSCKSPSK_05310 SPSK_05319 SPSK_07553
FGRFGSG_02692
FPUFPSE_00399
FPOAFPOAC1_002821(XAN1)
FVNFVRRES_03136
FVRFVEG_09012
FOXFOXG_10360
NHENECHADRAFT_94403
FFCNCS54_00820500
FKRNCS57_00863700
FMUJ7337_005382(XAN1)
TRETRIREDRAFT_77767
TRRM419DRAFT_35772
AMUSLMH87_008517
VALVDBG_04614
VDAVDAG_04163
CFJCFIO01_07110 CFIO01_12421 CFIO01_12422
CLUPCLUP02_14577 CLUP02_14578 CLUP02_15960
CHIGCH63R_11300 CH63R_12258 CH63R_12321
SAPOSAPIO_CDS0323
ELAUCREL1_10403 UCREL1_10408 UCREL1_2937
PFYPFICI_02622 PFICI_03917 PFICI_03927 PFICI_11089 PFICI_11090
SSLSS1G_04722
BFUBCIN_01g08370
PSCOLY89DRAFT_455914 LY89DRAFT_461846 LY89DRAFT_579972 LY89DRAFT_679151 LY89DRAFT_683826 LY89DRAFT_712245
GLZGLAREA_11001
ANIANIA_10081
ACTACLA_066400
AORAO090001000152
ANGAn01g14680
AFVAFLA_008496
ALUCAKAW2_20050A
ACHEACHE_70909A
APUUAPUU_11553A
PCSN7525_007948
PDPPDIP_55050
POUPOX_b01952
TMFEYB26_003731 EYB26_003733 EYB26_009981
TRGTRUGW13939_04711 TRUGW13939_11977 TRUGW13939_11979
PTEPTT_11857 PTT_11858
BZECOCCADRAFT_32934 COCCADRAFT_9324
BSCCOCSADRAFT_81895
BORCOCMIDRAFT_8838 COCMIDRAFT_90268
AALTCC77DRAFT_1029939 CC77DRAFT_1091742 CC77DRAFT_282647 CC77DRAFT_956058
ARABEKO05_0009821
PFJMYCFIDRAFT_132918 MYCFIDRAFT_191119 MYCFIDRAFT_204269 MYCFIDRAFT_210878 MYCFIDRAFT_4952
FFUCLAFUR5_06013
BCOMBAUCODRAFT_464815 BAUCODRAFT_70747
NPAUCRNP2_604 UCRNP2_605 UCRNP2_67 UCRNP2_9547
SPOSPCC576.01c
SOMSOMG_04881(xan1)
CNECNC06420
CNBCNBC0790
CNGCNAG_01542
CGICGB_C1100C
CDEUCNBG_3894
TMSTREMEDRAFT_26085
TASAA1Q1_00018
CCACCcaHIS019_0109030(CcaverHIS019_0109030)
TVSTRAVEDRAFT_67834
DSQDICSQDRAFT_96760
PCOPHACADRAFT_248632
SHSSTEHIDRAFT_101392 STEHIDRAFT_170594
PSQPUNSTDRAFT_117809
ADLAURDEDRAFT_79471
FMEFOMMEDRAFT_143156 FOMMEDRAFT_23586
GTRGLOTRDRAFT_102027 GLOTRDRAFT_134924
RSXRhiXN_09780
LBCLACBIDRAFT_181264 LACBIDRAFT_227808 LACBIDRAFT_242796 LACBIDRAFT_301478
CCICC1G_00598 CC1G_00658
ABPAGABI1DRAFT67631(AGABI1DRAFT_67631)
ABVAGABI2DRAFT196515(AGABI2DRAFT_196515)
PCUBJR316_0000256 JR316_0000260 JR316_0012159
MPRMPER_00967
MRRMoror_11000 Moror_1739
MOREE1B28_001800
SCMSCHCO_02505277(SCHCODRAFT_02505277)
CPUTCONPUDRAFT_79364 CONPUDRAFT_79365
SLASERLADRAFT_480389
WSEWALSEDRAFT_31174
UMAUMAG_03386
SGRAEX895_005468
MSYMMSY001_2908
PGRPGTG_00897
PTRCPtA15_17A261
PSTRPst134EA_030520
MLRMELLADRAFT_71644
PIFPITG_15878
PSOJPHYSODRAFT_491326
 » show all
Reference
1  [PMID:15948966]
  Authors
Cultrone A, Scazzocchio C, Rochet M, Montero-Moran G, Drevet C, Fernandez-Martin R
  Title
Convergent evolution of hydroxylation mechanisms in the fungal kingdom: molybdenum cofactor-independent hydroxylation of xanthine via alpha-ketoglutarate-dependent dioxygenases.
  Journal
Mol Microbiol 57:276-90 (2005)
DOI:10.1111/j.1365-2958.2005.04686.x
  Sequence
[ani:ANIA_10081] [ncr:NCU09738] [spo:SPCC576.01c]
Reference
2  [PMID:17429948]
  Authors
Montero-Moran GM, Li M, Rendon-Huerta E, Jourdan F, Lowe DJ, Stumpff-Kane AW, Feig M, Scazzocchio C, Hausinger RP
  Title
Purification and characterization of the FeII- and alpha-ketoglutarate-dependent  xanthine hydroxylase from Aspergillus nidulans.
  Journal
Biochemistry 46:5293-304 (2007)
DOI:10.1021/bi700065h
  Sequence
Reference
3  [PMID:18036331]
  Authors
Li M, Muller TA, Fraser BA, Hausinger RP
  Title
Characterization of active site variants of xanthine hydroxylase from Aspergillus nidulans.
  Journal
Arch Biochem Biophys 470:44-53 (2008)
DOI:10.1016/j.abb.2007.11.002
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 1.14.11.48
IUBMB Enzyme Nomenclature: 1.14.11.48
ExPASy - ENZYME nomenclature database: 1.14.11.48
BRENDA, the Enzyme Database: 1.14.11.48

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