XDH_CALVI
ID XDH_CALVI Reviewed; 1353 AA.
AC P08793;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Xanthine dehydrogenase;
DE Short=XD;
DE EC=1.17.1.4;
GN Name=XDH;
OS Calliphora vicina (Blue blowfly) (Calliphora erythrocephala).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC Calliphoridae; Calliphorinae; Calliphora.
OX NCBI_TaxID=7373;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=2516831; DOI=10.1016/0378-1119(89)90432-0;
RA Houde M., Tiveron M.C., Bregegere F.;
RT "Divergence of the nucleotide sequences encoding xanthine dehydrogenase in
RT Calliphora vicina and Drosophila melanogaster.";
RL Gene 85:391-402(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 208-367.
RX PubMed=2830167; DOI=10.1016/0378-1119(87)90328-3;
RA Rocher-Chambonnet C., Berreur P., Houde M., Tiveron M.C., Lepesant J.-A.,
RA Bregegere F.;
RT "Cloning and partial characterization of the xanthine dehydrogenase gene of
RT Calliphora vicina, a distant relative of Drosophila melanogaster.";
RL Gene 59:201-212(1987).
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 -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; X07229; CAA30189.1; -; mRNA.
DR EMBL; X07323; CAA30281.1; -; Genomic_DNA.
DR EMBL; X07324; CAA30281.1; JOINED; Genomic_DNA.
DR EMBL; X07325; CAA30281.1; JOINED; Genomic_DNA.
DR EMBL; M18423; AAA27879.1; -; Genomic_DNA.
DR PIR; JQ0407; JQ0407.
DR AlphaFoldDB; P08793; -.
DR SMR; P08793; -.
DR PRIDE; P08793; -.
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:0004854; F:xanthine dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0004855; F:xanthine oxidase activity; IEA:InterPro.
DR GO; GO:0009115; P:xanthine catabolic process; ISS:UniProtKB.
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; IPR022407; OxRdtase_Mopterin_BS.
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.
DR PROSITE; PS00559; MOLYBDOPTERIN_EUK; 1.
PE 2: Evidence at transcript level;
KW 2Fe-2S; FAD; Flavoprotein; Iron; Iron-sulfur; Metal-binding; Molybdenum;
KW NAD; Oxidoreductase; Peroxisome.
FT CHAIN 1..1353
FT /note="Xanthine dehydrogenase"
FT /id="PRO_0000166078"
FT DOMAIN 17..104
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 245..434
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT ACT_SITE 1285
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 56
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22985"
FT BINDING 61
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22985"
FT BINDING 64
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22985"
FT BINDING 86
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22985"
FT BINDING 126
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22985"
FT BINDING 129
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22985"
FT BINDING 161
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22985"
FT BINDING 163
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22985"
FT BINDING 273..280
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 353
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 363..367
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 376
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 424
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 442
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 790
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 821
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 825
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 903
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 935
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 937
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1102
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"
SQ SEQUENCE 1353 AA; 150209 MW; 7120361C57C3E297 CRC64;
MTQEHNAAVL DLNPTFSTLI FFVNGKKVID TNPDPECTLL TYLREKLRLC GTKLGCGEGG
CGACTVMISR IDTLTNRIKH IAVNACLTPV CAMHGSAVTT VEGIGSTRTR LHPVQERLAK
AHGSQCGFCT PGIVMSMYAL LRNLSQPSMK DLEIAFQGNL CRCTGYRPIL EGYKTFTKEF
GCAMGDKCCK VNGNKCGEGM ENGGDMVDDK LFEKSEFVPF DPSQEPIFPP ELQLNKDWDS
QTLVYKGERA TWYRPGNLED LLKIKAQFPE AKLVVGNTEI GVEVKFKHFL YPVLVNPTKV
KEMIDVQELE DSIYFGASVS LMDIDRILRS SIEKLPEHQT RFFQCAVNML HYFAGKQIRN
VASLGGNIMT GSPISDMNPV LMAGAVKFKV AKYVEGQIKY REVCMASGFF TGYRKNVIEP
TEILVGLYFP KTLEHQYVVA FKQAKRRDDD IAIVNAAINV FIDPRSITVD KVYMAFGGMA
PTTVLATRTA DIMVKQQWNK VLMERVVENL CAELPLAPSA PGGMIAYRRS LVVSLFFKAY
LTITQQLIKS GILPQDSLPQ EELSGSDVFH TPALKSAQLF EKVSNKQSEC DPIGRPKIHA
SALKQATGEA IYCDDMPRME NELYLALVLS TKAHAKILSI DASEALAMPG VHAFFSSKDI
TQHENEVGPV FHDEEVFASD MVYCQGQVIG AIAADNPNFS SKTARKVTIE YEDIKPVIIT
IEQAIEHKSY FPDYPRFTEI GDVEKAFSEA DHVYEGSCRM GGQEHFYLET HASLAVPRDS
DEIEIFCSTQ HPSEVQKLVA HVLSTSAHRV VCRAKRLGGG FGGKESRAIA VALPVALACH
RLRRPIRCML DRDEDMMITG TRHPFLFKYK IAFTSEGRLT GCYIECYNNA GWSMDLSFSV
LERAMFHFEN CYKIPNIKVG GWVCKTNLPS NTAFRGFGGP QGMFAGEHII RDVARILGKD
YLEIMKQNFY KEGDITHYQQ KLDNFPIEKC FYDCLQQSNY YQKRKEIEEF NRNHRWRKRG
ISLVPTKYGI AFGVSHLNQA GALINIYADG SVLLSHGGVE IGQGLHTKMI QCCARALQIP
IEFIHISETA TDKVPNTSPT AASSGSDLNG MAVLDACEKL NKRLAPIKEA NPNGSWTEWI
NKAYFERVSL SATGFYRMPD IGYDPVQNPN ALMYNYFTNG VGSSIVEIDC LTGDHQVLST
DIVMDIGSSL NPAIDIGQIE GAFMQGYGLF TLEEMIYSPQ GVLYSRGPGM YKLPGFADIP
GEFNVTILTG AANPRAVYSS KAVGEPPLFI GCSVFFAIKE AITSARLMNG LSEDFKLESP
ATSARIRMAC QDEFTNLIEQ PPAGSYVPWN IVP
