ID   XDH_BOVIN               Reviewed;        1332 AA.
AC   P80457; Q95325;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   27-MAR-2024, entry version 185.
DE   RecName: Full=Xanthine dehydrogenase/oxidase;
DE   Includes:
DE     RecName: Full=Xanthine dehydrogenase;
DE              Short=XD;
DE              EC=1.17.1.4 {ECO:0000269|PubMed:11005854, ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401, ECO:0000269|PubMed:4352904};
DE   Includes:
DE     RecName: Full=Xanthine oxidase;
DE              Short=XO;
DE              EC=1.17.3.2 {ECO:0000269|PubMed:11005854, ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401, ECO:0000269|PubMed:4352904};
DE     AltName: Full=Xanthine oxidoreductase;
DE              Short=XOR;
GN   Name=XDH;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Mammary gland;
RX   PubMed=8708081; DOI=10.3168/jds.s0022-0302(96)76351-8;
RA   Berglund L., Rasmussen J.T., Andersen M.D., Rasmussen M.S., Petersen T.E.;
RT   "Purification of the bovine xanthine oxidoreductase from milk fat globule
RT   membranes and cloning of complementary deoxyribonucleic acid.";
RL   J. Dairy Sci. 79:198-204(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=9388547; DOI=10.1042/bst0250791;
RA   Terao M., Kurosaki M., Zanotta S., Garattini E.;
RT   "The xanthine oxidoreductase gene: structure and regulation.";
RL   Biochem. Soc. Trans. 25:791-796(1997).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-23; 186-205 AND 552-562.
RC   TISSUE=Milk;
RX   PubMed=7556219; DOI=10.1111/j.1432-1033.1995.tb20856.x;
RA   Turner N.A., Doyle W.A., Ventom A.M., Bray R.C.;
RT   "Properties of rabbit liver aldehyde oxidase and the relationship of the
RT   enzyme to xanthine oxidase and dehydrogenase.";
RL   Eur. J. Biochem. 232:646-657(1995).
RN   [4]
RP   CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   CONVERSION BY PARTIAL PROTEOLYSIS AND BY REDUCING AGENTS.
RX   PubMed=4352904; DOI=10.1042/bj1310191;
RA   Battelli M.G., Lorenzoni E., Stripe F.;
RT   "Milk xanthine oxidase type D (dehydrogenase) and type O (oxidase).
RT   Purification, interconversion and some properties.";
RL   Biochem. J. 131:191-198(1973).
RN   [5]
RP   ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF
RP   ARG-335; TRP-336 AND ARG-427.
RX   PubMed=12817083; DOI=10.1073/pnas.1431485100;
RA   Kuwabara Y., Nishino T., Okamoto K., Matsumura T., Eger B.T., Pai E.F.,
RA   Nishino T.;
RT   "Unique amino acids cluster for switching from the dehydrogenase to oxidase
RT   form of xanthine oxidoreductase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:8170-8175(2003).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEXES WITH FAD; IRON-SULFUR
RP   CENTERS; SALICYLATE, SUBUNIT, COFACTOR, CATALYTIC ACTIVITY, ACTIVITY
RP   REGULATION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=11005854; DOI=10.1073/pnas.97.20.10723;
RA   Enroth C., Eger B.T., Okamoto K., Nishino T., Nishino T., Pai E.F.;
RT   "Crystal structures of bovine milk xanthine dehydrogenase and xanthine
RT   oxidase: structure-based mechanism of conversion.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:10723-10728(2000).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH FAD; MOLYBDOPTERIN;
RP   IRON-SULFUR CENTERS AND SYNTHETIC INHIBITOR TEI-6720, COFACTOR, CATALYTIC
RP   ACTIVITY, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=12421831; DOI=10.1074/jbc.m208307200;
RA   Okamoto K., Eger B.T., Nishino T., Kondo S., Pai E.F., Nishino T.;
RT   "An extremely potent inhibitor of xanthine oxidoreductase. Crystal
RT   structure of the enzyme-inhibitor complex and mechanism of inhibition.";
RL   J. Biol. Chem. 278:1848-1855(2003).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) IN COMPLEX WITH FAD; MOLYBDOPTERIN;
RP   IRON-SULFUR CENTERS AND INHIBITOR FYX-051, ACTIVE SITE, COFACTOR, CATALYTIC
RP   ACTIVITY, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=15148401; DOI=10.1073/pnas.0400973101;
RA   Okamoto K., Matsumoto K., Hille R., Eger B.T., Pai E.F., Nishino T.;
RT   "The crystal structure of xanthine oxidoreductase during catalysis:
RT   implications for reaction mechanism and enzyme inhibition.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7931-7936(2004).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEXES WITH FAD; MOLYBDOPTERIN;
RP   IRON-SULFUR CENTERS; CALCIUM IONS; XANTHINE AND LUMAZINE, COFACTOR, AND
RP   SUBUNIT.
RX   PubMed=19109252; DOI=10.1074/jbc.m804517200;
RA   Pauff J.M., Cao H., Hille R.;
RT   "Substrate orientation and catalysis at the molybdenum site in xanthine
RT   oxidase: crystal structures in complex with xanthine and lumazine.";
RL   J. Biol. Chem. 284:8760-8767(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. Contributes to the generation of reactive oxygen species.
CC       {ECO:0000250|UniProtKB:P22985}.
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:0000269|PubMed:11005854, ECO:0000269|PubMed:12421831,
CC         ECO:0000269|PubMed:15148401, ECO:0000269|PubMed:4352904};
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:0000269|PubMed:11005854, ECO:0000269|PubMed:12421831,
CC         ECO:0000269|PubMed:15148401, ECO:0000269|PubMed:4352904};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O2 + xanthine = H2O2 + urate; Xref=Rhea:RHEA:21132,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:17712, ChEBI:CHEBI:17775; EC=1.17.3.2;
CC         Evidence={ECO:0000269|PubMed:11005854, ECO:0000269|PubMed:12421831,
CC         ECO:0000269|PubMed:15148401, ECO:0000269|PubMed:4352904};
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401,
CC         ECO:0000269|PubMed:19109252};
CC       Note=Binds 2 [2Fe-2S] clusters per subunit.
CC       {ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401,
CC       ECO:0000269|PubMed:19109252};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401,
CC         ECO:0000269|PubMed:19109252};
CC   -!- COFACTOR:
CC       Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
CC         Evidence={ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401,
CC         ECO:0000269|PubMed:19109252};
CC       Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
CC       {ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401,
CC       ECO:0000269|PubMed:19109252};
CC   -!- ACTIVITY REGULATION: Can be converted from the dehydrogenase form (D)
CC       to the oxidase form (O) irreversibly by proteolysis or reversibly
CC       through the oxidation of sulfhydryl groups.
CC       {ECO:0000269|PubMed:11005854, ECO:0000269|PubMed:12817083,
CC       ECO:0000269|PubMed:4352904}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=111 uM for molecular oxygen in dehydrogenase form
CC         {ECO:0000269|PubMed:12817083, ECO:0000269|PubMed:4352904};
CC         KM=37.7 uM for molecular oxygen in oxygenase form
CC         {ECO:0000269|PubMed:12817083, ECO:0000269|PubMed:4352904};
CC         KM=20.8 uM for NAD {ECO:0000269|PubMed:12817083,
CC         ECO:0000269|PubMed:4352904};
CC         KM=5 uM for xanthine {ECO:0000269|PubMed:12817083,
CC         ECO:0000269|PubMed:4352904};
CC   -!- SUBUNIT: Homodimer. Interacts with BTN1A1 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Peroxisome. Secreted.
CC   -!- TISSUE SPECIFICITY: Detected in milk (at protein level).
CC       {ECO:0000269|PubMed:11005854, ECO:0000269|PubMed:12421831,
CC       ECO:0000269|PubMed:15148401}.
CC   -!- PTM: Subject to partial proteolysis; this alters the enzyme from the
CC       dehydrogenase form (D) to the oxidase form (O).
CC   -!- PTM: Contains sulfhydryl groups that are easily oxidized (in vitro);
CC       this alters the enzyme from the dehydrogenase form (D) to the oxidase
CC       form (O).
CC   -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Worthington enzyme manual;
CC       URL="https://www.worthington-biochem.com/XO/";
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DR   EMBL; X83508; CAA58497.1; -; mRNA.
DR   EMBL; X98491; CAA67117.1; -; mRNA.
DR   PIR; S65135; S65135.
DR   RefSeq; NP_776397.1; NM_173972.2.
DR   PDB; 1FIQ; X-ray; 2.50 A; A=1-219, B=220-569, C=570-1332.
DR   PDB; 1FO4; X-ray; 2.10 A; A/B=1-1332.
DR   PDB; 1N5X; X-ray; 2.80 A; A/B=2-1332.
DR   PDB; 1V97; X-ray; 1.94 A; A/B=1-1332.
DR   PDB; 1VDV; X-ray; 1.98 A; A/B=1-1332.
DR   PDB; 3AM9; X-ray; 2.17 A; A/B=1-1332.
DR   PDB; 3AMZ; X-ray; 2.10 A; A/B=1-1332.
DR   PDB; 3AX7; X-ray; 2.34 A; A/B=1-1332.
DR   PDB; 3AX9; X-ray; 2.30 A; A/B=1-1332.
DR   PDB; 3B9J; X-ray; 2.30 A; A/I=1-219, B/J=220-569, C/K=570-1332.
DR   PDB; 3BDJ; X-ray; 2.00 A; A/B=1-1332.
DR   PDB; 3ETR; X-ray; 2.20 A; A/L=2-165, B/M=224-528, C/N=571-1325.
DR   PDB; 3EUB; X-ray; 2.60 A; 2/A/J/S=1-165, 3/B/K/T=224-528, 4/C/L/U=571-1332.
DR   PDB; 3NRZ; X-ray; 1.80 A; A/J=2-165, B/K=224-528, C/L=571-1326.
DR   PDB; 3NS1; X-ray; 2.60 A; A/J=2-165, B/K=224-528, C/L=571-1325.
DR   PDB; 3NVV; X-ray; 1.82 A; A/J=2-165, B/K=195-528, C/L=571-1325.
DR   PDB; 3NVW; X-ray; 1.60 A; A/J=2-165, B/K=195-528, C/L=571-1326.
DR   PDB; 3NVY; X-ray; 2.00 A; A/J=2-165, B/K=195-528, C/L=571-1326.
DR   PDB; 3NVZ; X-ray; 1.60 A; A/J=2-165, B/K=224-528, C/L=571-1325.
DR   PDB; 3SR6; X-ray; 2.10 A; A/J=2-165, B/K=224-528, C/L=571-1315.
DR   PDB; 3UNA; X-ray; 1.90 A; A/B=1-1332.
DR   PDB; 3UNC; X-ray; 1.65 A; A/B=1-1332.
DR   PDB; 3UNI; X-ray; 2.20 A; A/B=1-1332.
DR   PDB; 8J79; X-ray; 1.99 A; A/B=1-1332.
DR   PDBsum; 1FIQ; -.
DR   PDBsum; 1FO4; -.
DR   PDBsum; 1N5X; -.
DR   PDBsum; 1V97; -.
DR   PDBsum; 1VDV; -.
DR   PDBsum; 3AM9; -.
DR   PDBsum; 3AMZ; -.
DR   PDBsum; 3AX7; -.
DR   PDBsum; 3AX9; -.
DR   PDBsum; 3B9J; -.
DR   PDBsum; 3BDJ; -.
DR   PDBsum; 3ETR; -.
DR   PDBsum; 3EUB; -.
DR   PDBsum; 3NRZ; -.
DR   PDBsum; 3NS1; -.
DR   PDBsum; 3NVV; -.
DR   PDBsum; 3NVW; -.
DR   PDBsum; 3NVY; -.
DR   PDBsum; 3NVZ; -.
DR   PDBsum; 3SR6; -.
DR   PDBsum; 3UNA; -.
DR   PDBsum; 3UNC; -.
DR   PDBsum; 3UNI; -.
DR   PDBsum; 8J79; -.
DR   AlphaFoldDB; P80457; -.
DR   SMR; P80457; -.
DR   IntAct; P80457; 1.
DR   STRING; 9913.ENSBTAP00000061483; -.
DR   BindingDB; P80457; -.
DR   ChEMBL; CHEMBL3649; -.
DR   DrugCentral; P80457; -.
DR   PaxDb; 9913-ENSBTAP00000016620; -.
DR   PeptideAtlas; P80457; -.
DR   GeneID; 280960; -.
DR   KEGG; bta:280960; -.
DR   CTD; 7498; -.
DR   eggNOG; KOG0430; Eukaryota.
DR   InParanoid; P80457; -.
DR   OrthoDB; 5485853at2759; -.
DR   BRENDA; 1.17.1.4; 908.
DR   BRENDA; 1.17.3.2; 908.
DR   SABIO-RK; P80457; -.
DR   EvolutionaryTrace; P80457; -.
DR   PRO; PR:P80457; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IDA:CAFA.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0002197; C:xanthine dehydrogenase complex; IDA:CAFA.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:CAFA.
DR   GO; GO:0071949; F:FAD binding; IDA:CAFA.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; ISS:UniProtKB.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0030151; F:molybdenum ion binding; IDA:CAFA.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; IDA:CAFA.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:CAFA.
DR   GO; GO:0004854; F:xanthine dehydrogenase activity; ISS:UniProtKB.
DR   GO; GO:0004855; F:xanthine oxidase activity; ISS:UniProtKB.
DR   GO; GO:0009115; P:xanthine catabolic process; ISS:UniProtKB.
DR   DisProt; DP00450; -.
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; 5.
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; IPR022407; OxRdtase_Mopterin_BS.
DR   InterPro; IPR014307; Xanthine_DH_ssu.
DR   NCBIfam; TIGR02963; xanthine_xdhA; 1.
DR   PANTHER; PTHR11908; XANTHINE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11908:SF80; XANTHINE DEHYDROGENASE_OXIDASE; 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.
DR   PROSITE; PS00559; MOLYBDOPTERIN_EUK; 1.
PE   1: Evidence at protein level;
KW   2Fe-2S; 3D-structure; Cytoplasm; Direct protein sequencing; Disulfide bond;
KW   FAD; Flavoprotein; Iron; Iron-sulfur; Metal-binding; Molybdenum; NAD;
KW   Oxidoreductase; Peroxisome; Reference proteome; Secreted.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:7556219"
FT   CHAIN           2..1332
FT                   /note="Xanthine dehydrogenase/oxidase"
FT                   /id="PRO_0000166082"
FT   DOMAIN          4..91
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   DOMAIN          229..414
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT   ACT_SITE        1261
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000269|PubMed:15148401"
FT   BINDING         43
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:12421831,
FT                   ECO:0000269|PubMed:15148401, ECO:0000269|PubMed:19109252"
FT   BINDING         48
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:12421831,
FT                   ECO:0000269|PubMed:15148401, ECO:0000269|PubMed:19109252"
FT   BINDING         51
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:12421831,
FT                   ECO:0000269|PubMed:15148401, ECO:0000269|PubMed:19109252"
FT   BINDING         73
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:12421831,
FT                   ECO:0000269|PubMed:15148401, ECO:0000269|PubMed:19109252"
FT   BINDING         113
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:12421831,
FT                   ECO:0000269|PubMed:15148401, ECO:0000269|PubMed:19109252"
FT   BINDING         116
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:12421831,
FT                   ECO:0000269|PubMed:15148401, ECO:0000269|PubMed:19109252"
FT   BINDING         148
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:12421831,
FT                   ECO:0000269|PubMed:15148401, ECO:0000269|PubMed:19109252"
FT   BINDING         150
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:12421831,
FT                   ECO:0000269|PubMed:15148401, ECO:0000269|PubMed:19109252"
FT   BINDING         257..264
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000269|PubMed:12421831,
FT                   ECO:0000269|PubMed:15148401"
FT   BINDING         337
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000269|PubMed:12421831,
FT                   ECO:0000269|PubMed:15148401"
FT   BINDING         347..351
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000269|PubMed:12421831,
FT                   ECO:0000269|PubMed:15148401"
FT   BINDING         360
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000269|PubMed:12421831,
FT                   ECO:0000269|PubMed:15148401"
FT   BINDING         404
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000269|PubMed:12421831,
FT                   ECO:0000269|PubMed:15148401"
FT   BINDING         422
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000269|PubMed:12421831,
FT                   ECO:0000269|PubMed:15148401"
FT   BINDING         767
FT                   /ligand="Mo-molybdopterin"
FT                   /ligand_id="ChEBI:CHEBI:71302"
FT                   /ligand_part="Mo"
FT                   /ligand_part_id="ChEBI:CHEBI:28685"
FT                   /evidence="ECO:0000269|PubMed:12421831,
FT                   ECO:0000269|PubMed:15148401, ECO:0000269|PubMed:19109252"
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:0000269|PubMed:12421831,
FT                   ECO:0000269|PubMed:15148401, ECO:0000269|PubMed:19109252"
FT   BINDING         802
FT                   /ligand="substrate"
FT   BINDING         880
FT                   /ligand="substrate"
FT   BINDING         912
FT                   /ligand="Mo-molybdopterin"
FT                   /ligand_id="ChEBI:CHEBI:71302"
FT                   /ligand_part="Mo"
FT                   /ligand_part_id="ChEBI:CHEBI:28685"
FT                   /evidence="ECO:0000269|PubMed:12421831,
FT                   ECO:0000269|PubMed:15148401, ECO:0000269|PubMed:19109252"
FT   BINDING         914
FT                   /ligand="substrate"
FT   BINDING         1010
FT                   /ligand="substrate"
FT   BINDING         1079
FT                   /ligand="Mo-molybdopterin"
FT                   /ligand_id="ChEBI:CHEBI:71302"
FT                   /ligand_part="Mo"
FT                   /ligand_part_id="ChEBI:CHEBI:28685"
FT                   /evidence="ECO:0000269|PubMed:12421831,
FT                   ECO:0000269|PubMed:15148401, ECO:0000269|PubMed:19109252"
FT   DISULFID        535..992
FT                   /note="In oxidase form"
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         335
FT                   /note="R->A: Promotes conversion to the oxidase form that
FT                   utilizes molecular oxygen as electron acceptor. Interferes
FT                   with normal conversion to the dehydrogenase form by
FT                   reducing agents."
FT                   /evidence="ECO:0000269|PubMed:12817083"
FT   MUTAGEN         336
FT                   /note="W->A: Promotes conversion to the oxidase form that
FT                   utilizes molecular oxygen as electron acceptor. Interferes
FT                   with normal conversion to the dehydrogenase form by
FT                   reducing agents."
FT                   /evidence="ECO:0000269|PubMed:12817083"
FT   MUTAGEN         427
FT                   /note="R->Q: Promotes conversion to the oxidase form that
FT                   utilizes molecular oxygen as electron acceptor. Interferes
FT                   with normal conversion to the dehydrogenase form by
FT                   reducing agents."
FT                   /evidence="ECO:0000269|PubMed:12817083"
FT   CONFLICT        188
FT                   /note="T -> TQ (in Ref. 2; CAA67117)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        199
FT                   /note="E -> K (in Ref. 2; CAA67117)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        366
FT                   /note="M -> V (in Ref. 2; CAA67117)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        552
FT                   /note="D -> H (in Ref. 1; CAA58497)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        958
FT                   /note="R -> K (in Ref. 2; CAA67117)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        976
FT                   /note="Q -> E (in Ref. 2; CAA67117)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1039..1040
FT                   /note="GQ -> E (in Ref. 2; CAA67117)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1244
FT                   /note="L -> V (in Ref. 2; CAA67117)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1268
FT                   /note="A -> P (in Ref. 2; CAA67117)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1279..1281
FT                   /note="RAA -> ARG (in Ref. 2; CAA67117)"
FT                   /evidence="ECO:0000305"
FT   STRAND          6..10
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   STRAND          13..17
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   HELIX           26..32
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   STRAND          44..48
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   STRAND          52..59
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   TURN            60..63
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   STRAND          64..71
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   TURN            72..74
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   HELIX           77..79
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   STRAND          84..86
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   HELIX           88..90
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   STRAND          94..96
FT                   /evidence="ECO:0007829|PDB:1V97"
FT   HELIX           100..107
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   HELIX           117..130
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   HELIX           136..140
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   TURN            142..145
FT                   /evidence="ECO:0007829|PDB:3NVZ"
FT   STRAND          149..151
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   HELIX           154..161
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   HELIX           198..200
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   HELIX           206..208
FT                   /evidence="ECO:0007829|PDB:3UNC"
FT   HELIX           214..218
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   HELIX           219..221
FT                   /evidence="ECO:0007829|PDB:1FO4"
FT   STRAND          227..230
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   STRAND          235..238
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   HELIX           242..251
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   HELIX           264..270
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   STRAND          276..280
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   HELIX           285..287
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   STRAND          290..292
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   STRAND          294..300
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   HELIX           305..318
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   HELIX           321..323
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   HELIX           325..334
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   STRAND          336..338
FT                   /evidence="ECO:0007829|PDB:3EUB"
FT   HELIX           340..343
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   HELIX           348..354
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   HELIX           362..367
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   STRAND          371..376
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   STRAND          379..384
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   HELIX           387..389
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   STRAND          403..410
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   STRAND          416..422
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   STRAND          428..431
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   STRAND          435..443
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   STRAND          446..462
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   HELIX           467..471
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   TURN            472..475
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   STRAND          477..479
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   HELIX           480..493
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   HELIX           505..527
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   TURN            540..542
FT                   /evidence="ECO:0007829|PDB:3UNC"
FT   HELIX           543..546
FT                   /evidence="ECO:0007829|PDB:3UNC"
FT   STRAND          555..559
FT                   /evidence="ECO:0007829|PDB:3UNC"
FT   HELIX           582..586
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   HELIX           593..595
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   STRAND          603..609
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   STRAND          611..621
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   HELIX           625..627
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   STRAND          631..635
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   HELIX           637..639
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   STRAND          644..647
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   STRAND          652..655
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   STRAND          658..660
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   STRAND          666..674
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   HELIX           675..683
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   STRAND          686..691
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   HELIX           698..703
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   STRAND          707..717
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   HELIX           719..725
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   STRAND          727..736
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   STRAND          748..753
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   STRAND          760..764
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   HELIX           769..780
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   HELIX           784..786
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   STRAND          787..791
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   TURN            798..801
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   HELIX           806..819
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   STRAND          823..826
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   HELIX           829..835
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   STRAND          842..850
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   STRAND          856..866
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   HELIX           874..883
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   TURN            884..888
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   STRAND          892..901
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   TURN            912..915
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   HELIX           916..934
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   HELIX           938..945
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   HELIX           964..974
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   HELIX           977..990
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   STRAND          992..1008
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   HELIX           1012..1014
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   STRAND          1016..1023
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   STRAND          1029..1034
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   STRAND          1038..1040
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   HELIX           1042..1054
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   HELIX           1058..1060
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   STRAND          1061..1063
FT                   /evidence="ECO:0007829|PDB:3SR6"
FT   TURN            1068..1070
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   TURN            1079..1081
FT                   /evidence="ECO:0007829|PDB:3B9J"
FT   HELIX           1082..1107
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   HELIX           1113..1122
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   STRAND          1128..1134
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   TURN            1142..1145
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   STRAND          1151..1165
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   TURN            1166..1168
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   STRAND          1171..1181
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   HELIX           1188..1207
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   TURN            1224..1226
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   HELIX           1232..1234
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   STRAND          1237..1243
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   HELIX           1253..1255
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   HELIX           1264..1267
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   HELIX           1268..1285
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   HELIX           1302..1308
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   TURN            1312..1314
FT                   /evidence="ECO:0007829|PDB:3NVW"
FT   HELIX           1317..1319
FT                   /evidence="ECO:0007829|PDB:3NVW"
SQ   SEQUENCE   1332 AA;  146790 MW;  744BA523471948B7 CRC64;
     MTADELVFFV NGKKVVEKNA DPETTLLAYL RRKLGLRGTK LGCGEGGCGA CTVMLSKYDR
     LQDKIIHFSA NACLAPICTL HHVAVTTVEG IGSTKTRLHP VQERIAKSHG SQCGFCTPGI
     VMSMYTLLRN QPEPTVEEIE DAFQGNLCRC TGYRPILQGF RTFAKNGGCC GGNGNNPNCC
     MNQKKDHTVT LSPSLFNPEE FMPLDPTQEP IFPPELLRLK DVPPKQLRFE GERVTWIQAS
     TLKELLDLKA QHPEAKLVVG NTEIGIEMKF KNQLFPMIIC PAWIPELNAV EHGPEGISFG
     AACALSSVEK TLLEAVAKLP TQKTEVFRGV LEQLRWFAGK QVKSVASLGG NIITASPISD
     LNPVFMASGT KLTIVSRGTR RTVPMDHTFF PSYRKTLLGP EEILLSIEIP YSREDEFFSA
     FKQASRREDD IAKVTCGMRV LFQPGSMQVK ELALCYGGMA DRTISALKTT QKQLSKFWNE
     KLLQDVCAGL AEELSLSPDA PGGMIEFRRT LTLSFFFKFY LTVLKKLGKD SKDKCGKLDP
     TYTSATLLFQ KDPPANIQLF QEVPNGQSKE DTVGRPLPHL AAAMQASGEA VYCDDIPRYE
     NELFLRLVTS TRAHAKIKSI DVSEAQKVPG FVCFLSADDI PGSNETGLFN DETVFAKDTV
     TCVGHIIGAV VADTPEHAER AAHVVKVTYE DLPAIITIED AIKNNSFYGS ELKIEKGDLK
     KGFSEADNVV SGELYIGGQD HFYLETHCTI AIPKGEEGEM ELFVSTQNAM KTQSFVAKML
     GVPVNRILVR VKRMGGGFGG KETRSTLVSV AVALAAYKTG HPVRCMLDRN EDMLITGGRH
     PFLARYKVGF MKTGTIVALE VDHYSNAGNS RDLSHSIMER ALFHMDNCYK IPNIRGTGRL
     CKTNLSSNTA FRGFGGPQAL FIAENWMSEV AVTCGLPAEE VRWKNMYKEG DLTHFNQRLE
     GFSVPRCWDE CLKSSQYYAR KSEVDKFNKE NCWKKRGLCI IPTKFGISFT VPFLNQAGAL
     IHVYTDGSVL VSHGGTEMGQ GLHTKMVQVA SKALKIPISK IYISETSTNT VPNSSPTAAS
     VSTDIYGQAV YEACQTILKR LEPFKKKNPD GSWEDWVMAA YQDRVSLSTT GFYRTPNLGY
     SFETNSGNAF HYFTYGVACS EVEIDCLTGD HKNLRTDIVM DVGSSLNPAI DIGQVEGAFV
     QGLGLFTLEE LHYSPEGSLH TRGPSTYKIP AFGSIPTEFR VSLLRDCPNK KAIYASKAVG
     EPPLFLGASV FFAIKDAIRA ARAQHTNNNT KELFRLDSPA TPEKIRNACV DKFTTLCVTG
     APGNCKPWSL RV
//