ID A0A2X0MVY8_9BASI Unreviewed; 1460 AA.
AC A0A2X0MVY8;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=xanthine dehydrogenase {ECO:0000256|ARBA:ARBA00013123};
DE EC=1.17.1.4 {ECO:0000256|ARBA:ARBA00013123};
GN Name=BQ5605_C004g02802 {ECO:0000313|EMBL:SGY67730.1};
GN ORFNames=BQ5605_C004G02802 {ECO:0000313|EMBL:SGY67730.1};
OS Microbotryum silenes-dioicae.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Microbotryales; Microbotryaceae; Microbotryum.
OX NCBI_TaxID=796604 {ECO:0000313|EMBL:SGY67730.1, ECO:0000313|Proteomes:UP000249464};
RN [1] {ECO:0000313|EMBL:SGY67730.1, ECO:0000313|Proteomes:UP000249464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|ARBA:ARBA00000532};
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 Evidence={ECO:0000256|ARBA:ARBA00000239};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|PIRSR:PIRSR000127-2};
CC -!- COFACTOR:
CC Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
CC Evidence={ECO:0000256|PIRSR:PIRSR000127-3};
CC Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
CC {ECO:0000256|PIRSR:PIRSR000127-3};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|ARBA:ARBA00034078};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|PIRSR:PIRSR000127-3};
CC Note=Binds 2 [2Fe-2S] clusters. {ECO:0000256|PIRSR:PIRSR000127-3};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00006849}.
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DR EMBL; FQNC01000046; SGY67730.1; -; Genomic_DNA.
DR STRING; 796604.A0A2X0MVY8; -.
DR Proteomes; UP000249464; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 1.10.150.120; [2Fe-2S]-binding domain; 1.
DR Gene3D; 3.90.1170.50; Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead; 1.
DR Gene3D; 3.30.365.10; Aldehyde oxidase/xanthine dehydrogenase, molybdopterin binding domain; 4.
DR Gene3D; 3.30.390.50; CO dehydrogenase flavoprotein, C-terminal domain; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 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-like.
DR InterPro; IPR008274; AldOxase/xan_DH_MoCoBD1.
DR InterPro; IPR046867; AldOxase/xan_DH_MoCoBD2.
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 PANTHER; PTHR11908; XANTHINE DEHYDROGENASE; 1.
DR PANTHER; PTHR11908:SF100; XANTHINE DEHYDROGENASE; 1.
DR Pfam; PF01315; Ald_Xan_dh_C; 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 Pfam; PF02738; MoCoBD_1; 1.
DR Pfam; PF20256; MoCoBD_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; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF55447; CO dehydrogenase flavoprotein C-terminal domain-like; 1.
DR SUPFAM; SSF47741; CO dehydrogenase ISP C-domain like; 1.
DR SUPFAM; SSF54665; CO dehydrogenase molybdoprotein N-domain-like; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF56003; Molybdenum cofactor-binding domain; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714, ECO:0000256|PIRSR:PIRSR000127-3};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000127-2};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000127-3};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRSR:PIRSR000127-
KW 3};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000127-3};
KW Molybdenum {ECO:0000256|ARBA:ARBA00022505, ECO:0000256|PIRSR:PIRSR000127-
KW 3}; Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000249464}.
FT DOMAIN 17..106
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 339..529
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT REGION 240..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1392
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-1"
FT BINDING 58
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT BINDING 63
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT BINDING 66
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT BINDING 88
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT BINDING 125
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT BINDING 128
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT BINDING 165
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT BINDING 167
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT BINDING 367..374
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT BINDING 452
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT BINDING 462..466
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT BINDING 475
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT BINDING 539
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT BINDING 882
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT BINDING 913
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT BINDING 917
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT BINDING 995
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT BINDING 1027
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT BINDING 1029
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT BINDING 1205
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
SQ SEQUENCE 1460 AA; 157588 MW; FDF0CDC681FFB0DA CRC64;
MPDGSFVEPF ETQGWSSQLV FYLNGTSIAL DGSSIDPDTS LLSFIRSQPG LTGTKLGCGE
GGCGACTVVV QSKHPVQGHI QHLAVNACLA PLISVEGKHV ITVEGPSDNP HPLQERMWKL
SGSQCGFCTP GIVMSVYALL REAAYRGQLT VKDVELEGVL DGNLCRCTGY APILVAVKSF
VGGYLTKVNG NGAEASSGAK VDDSLVVPFN FDASGLDNED ATKKAKAGAC CGSNGCSKEA
STDVSMPVPS GKDTSEPPID ATAGAMGRTA PTGSSTDIKP TKPKGCGRAD CCQLDGGKGP
ASTAPTHSFP RFEFKPYRPG VELIFPPGLQ SHKLAPIKFG SKGRMWLRPT TLDQLLSLKA
QYPDAKVVGG SSEIAIEVGI LGRKYPVCLF VSDIPELYAI ELPDLKSNKP TFTFGANTPL
SEIEQVCKDL TKSLPKNQAG PFKAIKDQLR CFAGRQVRNT ASVAGNIATA SPISDLNPIW
LATGATLIAR NESQGEFELP LASFFTGYRK TALPADAIIV RIIVPVNTSS ETEVVRAYKQ
AKRRDDDISI VCACMAMRVD ADGTIKSAKL AYGGMAPFTI AATETQDYLV GKSITSDTLE
GALDVLAKEF DLAFDVPGGM AAYRRTLTLS FFFKFFVTVS IESGRPLDVA KELSSTEEIT
ESIHRSISSS TRDNSDPYAL EVVGKQEPHM SGLKHVTGEA IYCDDIPSIA NEAYVGLVLS
QRAHAKIVSV DASDALEQDG VVGFVDHNDL PNERANWWGS AAIDETFFAT DEVISHGQII
GAVVAKTKLI AAKAARLLKI EYEDLPVILT IEEAIAAGSF HPQYERRISR GDEISKAMSE
SECTLKGATR MGGQEHFYLE TMASLVVPKG EGGEVEVYSS TQALNDTQRW VAQIMGVPRN
RVVAKVKRLG GGFGGKETRS AMLTAVCALA AKKTKRPVRA MLDRDVDIRT TGQRHPCLGE
WKVGFTKEGK LTALDVQFYA NAGYSLDISG GVCDRALAHL ENSYWIPHVD FRARCCKTNT
VSNTAYRGFG GPQGMIVAEH YLEAIAEHLN LDIDHVRKIN LYKEAQKTPY HQKVLDWHVP
RLLEDCRKES DYDQRKQAVD KFNKEHKYRK RGIALVPTKF GLAFGVKAMN QGAALVHVRP
DHPQYMDGSV LVAHGGTEMG QGLYTKCCQV AAQELQVPLS SVFTSETATN TVPNAVPTAV
LDFIGSAGSD LQAHAVYNAC AELNKRLEPY RQKLGPDASF AALAGAAWGD RISLSATGHH
AMPDLGYVWN EQKETGNLFH YFTQGVAAAE VELDTLTGDH TVLRVDLKMD VGKSLNPAID
YGQIEGAFVQ GQGWCTIEES LWLKNGAIQT VGPGAYKIPG FADIPQVFNV ALLKDAEWPN
LGSIKASKGI GEPPFFLGCS VFLALRQAVK SARMDQGIQE SAEFRLPLTS ERLRLACGDR
LVQKAKVEQK EGQKGFFVYI
//
