ID A0A0A1TJE6_9HYPO Unreviewed; 1419 AA.
AC A0A0A1TJE6;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=xanthine dehydrogenase {ECO:0000256|ARBA:ARBA00013123};
DE EC=1.17.1.4 {ECO:0000256|ARBA:ARBA00013123};
GN ORFNames=VHEMI05726 {ECO:0000313|EMBL:CEJ89912.1};
OS [Torrubiella] hemipterigena.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae;
OC Clavicipitaceae incertae sedis; 'Torrubiella' clade.
OX NCBI_TaxID=1531966 {ECO:0000313|EMBL:CEJ89912.1, ECO:0000313|Proteomes:UP000039046};
RN [1] {ECO:0000313|EMBL:CEJ89912.1, ECO:0000313|Proteomes:UP000039046}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Horn F., Habel A., Scharf D.H., Dworschak J., Brakhage A.A., Guthke R.,
RA Hertweck C., Linde J.;
RT "Draft Genome Sequence and Gene Annotation of the Entomopathogenic Fungus
RT Verticillium hemipterigenum.";
RL Genome Announc. 3:e01439-e01414(2015).
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 -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
CC -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00006849}.
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DR EMBL; CDHN01000003; CEJ89912.1; -; Genomic_DNA.
DR STRING; 1531966.A0A0A1TJE6; -.
DR HOGENOM; CLU_001681_1_2_1; -.
DR OrthoDB; 5485853at2759; -.
DR Proteomes; UP000039046; Unassembled WGS sequence.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
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:0004854; F:xanthine dehydrogenase activity; IEA:UniProtKB-EC.
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 InterPro; IPR014307; Xanthine_DH_ssu.
DR NCBIfam; TIGR02963; xanthine_xdhA; 1.
DR PANTHER; PTHR11908; XANTHINE DEHYDROGENASE; 1.
DR PANTHER; PTHR11908:SF130; 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 Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Reference proteome {ECO:0000313|Proteomes:UP000039046}.
FT DOMAIN 26..112
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 309..493
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT ACT_SITE 1342
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-1"
FT BINDING 64
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT BINDING 69
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT BINDING 72
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT BINDING 94
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT BINDING 133
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT BINDING 136
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT BINDING 168
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT BINDING 170
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT BINDING 417
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT BINDING 440
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT BINDING 502
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT BINDING 841
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 872
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 876
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT BINDING 954
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT BINDING 986
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 988
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT BINDING 1084
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT BINDING 1153
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 1419 AA; 154932 MW; 15415E3A4F37ADC2 CRC64;
MAPAPTMIQE KSASAELAAL AASFDDTLRF YLNGTKIVLE NIDPEVTVLE YLRGIGLTGT
KLGCGEGGCG ACTIVVSQFN PTTKEIYHAS VNACLAPLVS LDGKHVITIE GIGNTKGPHP
TQERVAKSHG SQCGFCTPGI VMSLYALLRN NSEPSEHDME EAFDGNLCRC TGYRPILDAA
HTFSAKPACG MSKANGGGGC CMDEKKTNGT TNGTTNGVGN GPTNGVGHEV TNGTTNRTTN
GTTNGTTNGG GCCMDKGNGK PSGGCCMDKK TDDQPIKRFT PPGFIEYNPD TELIFPPQLK
KQELRPLSFG NKRKTWLRPV TLDQLLQIKS VYPDAKIIGG STETQIEIKF KQIKYPISVY
VGDIAELRQY KFYDDHIEIG GNVVLTDVEG ICEKAMGHYG PVRGQVFEGI LKQLKYFAGR
QIRNVGTPAG NLVTASPISD LNPALWGANA VLIAKSASKE TELPMNQFFI GYRKTALPQD
AIISSIRIPV TAAKGECYRT YKQAKRKDDD IAIVTSSLRV KVDEEGIVES CNLIYGGMGP
FTLAAKQAQE YLIGKRFAEL ETLEGTMSAL ERDFDMKYDV PGGMPSYRKA LAFGFFYRFY
HDALSHMSEA DGKADLQAVG EIERALSKGA IDEHSAAKYE KEVTGKSNPH VAALKQTTGE
AQYTDDIPAM KNELHASWVL STKPHAKIKS IDYGPALDMP GVVDYVDHTD MPSPEANKFG
TPFFDDTIFA VDKVYTAGQP IALILATSAS RAHEAARAVK IEYEVLPAVL SIEDAIEADS
YLDFSKQIVK GDTEKAFANS DYVFTGTVRM GGQEHFYLET NACLVVPKPE DGEMEIFAST
QNTTETQTFA ARACDVAFNK VVVRVKRLGG GFGGKESRPA VLSSAVALAA KKTKKPVRCM
LTREDDMLTS GQRHPFLGKY KLGINKDGKI QALDCDIYNN AGYSYDLSCA VCERAMTHVD
GCYSIPNVNI RGHLCKTNTM SNTAFRGFGG PQGIFIAESF MEEAADRLGM SVELLREINF
YKHHEETHFN QMLQDWHVPL MYKQVYDGFD YAERRKAITQ FNLDNKWRKR GLSIIPTKFG
ISFTALFLNQ AGALVHIYHD GSVLVAHGGT EMGQGLHTKM TQIAAQALGV PLDNVFISET
ATNTVPNTSP TAASASSDLN GFAIFNACQQ INERLAPYRE KLGKDATMKQ LAHAAYFDRV
NLSAQGFYKT PEIGYNWDTN KGKMFFYFTQ GVAAAEVEID TLTGAWTCLR SDIKMDVGQS
INPAIDYGQI QGAFIQGMGL FTMEESLWLS SGPGAGNLFT RGPGAYKIPG FRDIPQEFNV
SLLKDVEWKE LRTIQRSRGV GEPPLFLGSV VFFGIRDALK AARRSVGVEA TIGQDDSPGL
LRLTSPATSE RIRLACEDDI MKRARVEPKE GQKGFFVFI
//
