XDH_EMENI
ID XDH_EMENI Reviewed; 1363 AA.
AC Q12553; C8VFY5; Q5B1G7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Xanthine dehydrogenase;
DE EC=1.17.1.4;
DE AltName: Full=Purine hydroxylase I;
GN Name=hxA; ORFNames=AN5613;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=biA1;
RX PubMed=7876088; DOI=10.1074/jbc.270.8.3534;
RA Glatigny A., Scazzocchio C.;
RT "Cloning and molecular characterization of hxA, the gene coding for the
RT xanthine dehydrogenase (purine hydroxylase I) of Aspergillus nidulans.";
RL J. Biol. Chem. 270:3534-3550(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
CC -!- FUNCTION: Key enzyme in purine degradation. Catalyzes the oxidation of
CC hypoxanthine to xanthine. Catalyzes the oxidation of xanthine to uric
CC acid (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) + xanthine = H(+) + NADH + urate;
CC Xref=Rhea:RHEA:16669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17712, ChEBI:CHEBI:17775, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.17.1.4;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hypoxanthine + NAD(+) = H(+) + NADH + xanthine;
CC Xref=Rhea:RHEA:24670, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17368, ChEBI:CHEBI:17712, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.17.1.4;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302; Evidence={ECO:0000250};
CC Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
CC {ECO:0000250};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000250|UniProtKB:P22985};
CC Note=Binds 2 [2Fe-2S] clusters per subunit.
CC {ECO:0000250|UniProtKB:P22985};
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}.
CC -!- INDUCTION: By 2-thiouric acid. Repressed by ammonium.
CC {ECO:0000269|PubMed:7876088}.
CC -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; X82827; CAA58034.1; -; Genomic_DNA.
DR EMBL; AACD01000098; EAA62706.1; -; Genomic_DNA.
DR EMBL; BN001305; CBF81549.1; -; Genomic_DNA.
DR PIR; A55875; A55875.
DR RefSeq; XP_663217.1; XM_658125.1.
DR AlphaFoldDB; Q12553; -.
DR SMR; Q12553; -.
DR STRING; 162425.CADANIAP00003457; -.
DR EnsemblFungi; CBF81549; CBF81549; ANIA_05613.
DR EnsemblFungi; EAA62706; EAA62706; AN5613.2.
DR GeneID; 2871900; -.
DR KEGG; ani:AN5613.2; -.
DR VEuPathDB; FungiDB:AN5613; -.
DR eggNOG; KOG0430; Eukaryota.
DR HOGENOM; CLU_001681_1_2_1; -.
DR InParanoid; Q12553; -.
DR OMA; DIGYVWG; -.
DR OrthoDB; 48717at2759; -.
DR Proteomes; UP000000560; Chromosome V.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; ISS:UniProtKB.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; ISS:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0043546; F:molybdopterin cofactor binding; ISS:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0004854; F:xanthine dehydrogenase activity; IDA:AspGD.
DR GO; GO:0004855; F:xanthine oxidase activity; IEA:InterPro.
DR GO; GO:0006145; P:purine nucleobase catabolic process; IDA:AspGD.
DR GO; GO:0009115; P:xanthine catabolic process; ISS:UniProtKB.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.30.43.10; -; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR InterPro; IPR002888; 2Fe-2S-bd.
DR InterPro; IPR036884; 2Fe-2S-bd_dom_sf.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR000674; Ald_Oxase/Xan_DH_a/b.
DR InterPro; IPR036856; Ald_Oxase/Xan_DH_a/b_sf.
DR InterPro; IPR016208; Ald_Oxase/xanthine_DH.
DR InterPro; IPR008274; AldOxase/xan_DH_Mopterin-bd.
DR InterPro; IPR037165; AldOxase/xan_DH_Mopterin-bd_sf.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR005107; CO_DH_flav_C.
DR InterPro; IPR036683; CO_DH_flav_C_dom_sf.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR002346; Mopterin_DH_FAD-bd.
DR InterPro; IPR014307; Xanthine_DH_ssu.
DR PANTHER; PTHR11908; PTHR11908; 1.
DR Pfam; PF01315; Ald_Xan_dh_C; 1.
DR Pfam; PF02738; Ald_Xan_dh_C2; 1.
DR Pfam; PF03450; CO_deh_flav_C; 1.
DR Pfam; PF00941; FAD_binding_5; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF01799; Fer2_2; 1.
DR PIRSF; PIRSF000127; Xanthine_DH; 1.
DR SMART; SM01008; Ald_Xan_dh_C; 1.
DR SMART; SM01092; CO_deh_flav_C; 1.
DR SUPFAM; SSF47741; SSF47741; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR SUPFAM; SSF54665; SSF54665; 1.
DR SUPFAM; SSF55447; SSF55447; 1.
DR SUPFAM; SSF56003; SSF56003; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR TIGRFAMs; TIGR02963; xanthine_xdhA; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 2: Evidence at transcript level;
KW 2Fe-2S; FAD; Flavoprotein; Iron; Iron-sulfur; Metal-binding; Molybdenum;
KW NAD; Oxidoreductase; Peroxisome; Reference proteome.
FT CHAIN 1..1363
FT /note="Xanthine dehydrogenase"
FT /id="PRO_0000166087"
FT DOMAIN 35..121
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 266..450
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT ACT_SITE 1295
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 73
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22985"
FT BINDING 78
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22985"
FT BINDING 81
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22985"
FT BINDING 103
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22985"
FT BINDING 142
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22985"
FT BINDING 145
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22985"
FT BINDING 177
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22985"
FT BINDING 179
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22985"
FT BINDING 294..301
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 374
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 384..388
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 397
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 459
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 798
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000250"
FT BINDING 829
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000250"
FT BINDING 833
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 911
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 943
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000250"
FT BINDING 945
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1041
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1110
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000250"
FT CONFLICT 741
FT /note="R -> H (in Ref. 1; CAA58034)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1363 AA; 149523 MW; 18D8F50B731EDE4B CRC64;
MAPGVLLQPS QSELEAASPP KAAASLLQLT EEWDDTIRFY LNGTKVILDS VDPEITLLEY
LRGIGLTGTK LGCAEGGCGA CTVVVSQINP TTKKLYHASI NACIAPLVAV DGKHVITVEG
IGNVKNPHAI QQRLAIGNGS QCGFCTPGIV MSLYALLRND PKPSEHAVEE AFDGNLCRCT
GYRPILDAAQ SFTSPIGCGK ARANGGSGCC MEEQKGTNGC CKGSSEETTE DVKHKFASPD
FIEYKPDTEL IFPPSLWKHE LRPLAFGNKR KKWYRPVTVQ QLLEIKSIHP DAKLIGGSTE
TQIEIKFKQM RYGASVYLGD LAELRQFAFH DNYLEIGANI SLTDLESVCD QAIERYGSAR
GQPFAAIKKQ LRYFAGRQIR NVASPAGNLA TASPISDLNP VFVATNTTLV ARSLDKETEI
PMTQFFRGYR STALPPDAII SSLRIPTASE KGEYLRAYKQ SKRKDDDIAI VNAALRVSLS
SSNDVTSVSL VFGGMAPLTV SARNAEAFLT GKKFTDPATL EGTMGALEQD FNLKFGVPGG
MATYRKSLAL GFFYRFYHDV LSQIEARSSD LDNSVVAEIE RAISTGEKDN EASAAYQQRV
LGRAGPHLSA LKQATGEAQY TDDIPAQKNE LYGCMVLSTK AHAKLLSVNT EAALEIPGVI
DYVDHKDLPS PRANWWGAPN CDEVFFAVDK VTTAGQPIGM ILANTAKAAE EGARAVKVEY
EELPVILSIE EAIEAQSFFE RFRYIKNGDP ESAFRDADHV FEGVSRMGGQ EHFYLETQAC
VAIPKAEDGE MEIWSSTQNP TETQSYVAQV TGVAANKIVS RVKRLGGGFG GKETRSVQLA
GICATAAAKV RRPVRCMLNR DEDIATSGQR HPFYCKWKVG VTREGKLLAL DADVYANGGH
TQDLSGAVVE RSLSHIDNVY RFPNIYVRGR ICKTNTVSNT AFRGFGGPQG LFFAESIISE
VADHLDLQVE QLRILNMYEP GDMTHFNQEL KDWHVPLMYD QVLQESEYFE RRKAVEEYNR
THKWSKRGMA IIPTKFGISF TALFLNQAGA LVHIYHDGSV LVAHGGVEMG QGLHTKMTMI
AAEALGVPLS DVFISETATN TVANTSSTAA SASSDLNGYA IYNACTQLNE RLKPYREKMP
NATLKDLAHA AYFDRVNLSA QGYYRTPDIG YTWGENKGQM FFYFTQGVTA AEVEIDTLTG
DWTPLRADIK MDVGRTINPS IDYGQIEGAY IQGQGLFTTE ESLWHRTTGQ IFTKGPGNYK
IPGFRDIPQI FNVSLLKDVE WENLRTIQRS RGVGEPPLFM GSAAFFAIRD ALKAARKEWG
VTDVLSLVSP ATPERIRVSC ADPIIERARV KAEEGEKSFF VAI
