XDH_BOVIN
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 03-AUG-2022, entry version 176.
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.1432-1033.1995.646zz.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; 7D6O; X-ray; 1.99 A; A/B=1-1332.
DR PDB; 7DNV; 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; 7D6O; -.
DR PDBsum; 7DNV; -.
DR AlphaFoldDB; P80457; -.
DR SMR; P80457; -.
DR IntAct; P80457; 1.
DR STRING; 9913.ENSBTAP00000016620; -.
DR BindingDB; P80457; -.
DR ChEMBL; CHEMBL3649; -.
DR DrugCentral; P80457; -.
DR PaxDb; P80457; -.
DR PeptideAtlas; P80457; -.
DR PRIDE; P80457; -.
DR GeneID; 280960; -.
DR KEGG; bta:280960; -.
DR CTD; 7498; -.
DR eggNOG; KOG0430; Eukaryota.
DR InParanoid; P80457; -.
DR OrthoDB; 48717at2759; -.
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:0016491; F:oxidoreductase activity; IBA:GO_Central.
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; 3.30.43.10; -; 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 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
