XDH_RAT
ID XDH_RAT Reviewed; 1331 AA.
AC P22985; Q63157;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 182.
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:15878860, ECO:0000269|PubMed:17301076};
DE Includes:
DE RecName: Full=Xanthine oxidase;
DE Short=XO;
DE EC=1.17.3.2 {ECO:0000269|PubMed:15878860, ECO:0000269|PubMed:17301076};
DE AltName: Full=Xanthine oxidoreductase;
DE Short=XOR;
GN Name=Xdh;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, ACTIVITY REGULATION,
RP PROTEOLYTIC CONVERSION, AND SUBUNIT.
RC TISSUE=Liver;
RX PubMed=2387845; DOI=10.1016/s0021-9258(18)77283-9;
RA Amaya Y., Yamazaki K., Sato M., Noda K., Nishino T., Nishino T.;
RT "Proteolytic conversion of xanthine dehydrogenase from the NAD-dependent
RT type to the O2-dependent type. Amino acid sequence of rat liver xanthine
RT dehydrogenase and identification of the cleavage sites of the enzyme
RT protein during irreversible conversion by trypsin.";
RL J. Biol. Chem. 265:14170-14175(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE OF 1-55.
RC STRAIN=Sprague-Dawley;
RX PubMed=8208609; DOI=10.1093/nar/22.10.1846;
RA Chow C.W., Clark M., Rinaldo J., Chalkley R.;
RT "Identification of the rat xanthine dehydrogenase/oxidase promoter.";
RL Nucleic Acids Res. 22:1846-1854(1994).
RN [3]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11993848; DOI=10.1078/0065-1281-00629;
RA Frederiks W.M., Vreeling-Sindelarova H.;
RT "Ultrastructural localization of xanthine oxidoreductase activity in
RT isolated rat liver cells.";
RL Acta Histochem. 104:29-37(2002).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF MUTANT ALA-535/ARG-992/SER-1324 IN
RP COMPLEX WITH FAD; URIC ACID AND IRON-SULFUR CENTERS, CATALYTIC ACTIVITY,
RP DISULFIDE BOND, ACTIVITY REGULATION, MUTAGENESIS OF CYS-535; CYS-992 AND
RP CYS-1316, AND COFACTOR.
RX PubMed=15878860; DOI=10.1074/jbc.m501830200;
RA Nishino T., Okamoto K., Kawaguchi Y., Hori H., Matsumura T., Eger B.T.,
RA Pai E.F., Nishino T.;
RT "Mechanism of the conversion of xanthine dehydrogenase to xanthine oxidase:
RT identification of the two cysteine disulfide bonds and crystal structure of
RT a non-convertible rat liver xanthine dehydrogenase mutant.";
RL J. Biol. Chem. 280:24888-24894(2005).
RN [5] {ECO:0007744|PDB:2E3T}
RP X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF MUTANT ALA-335/LEU-336 IN COMPLEX
RP WITH FAD AND IRON-SULFUR (2FE-2S), MUTAGENESIS OF 335-TRP-PHE-336,
RP CATALYTIC ACTIVITY, FUNCTION, AND COFACTOR.
RX PubMed=17301076; DOI=10.1093/jb/mvm054;
RA Asai R., Nishino T., Matsumura T., Okamoto K., Igarashi K., Pai E.F.,
RA Nishino T.;
RT "Two mutations convert mammalian xanthine oxidoreductase to highly
RT superoxide-productive xanthine oxidase.";
RL J. Biochem. 141:525-534(2007).
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:0000269|PubMed:17301076}.
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:15878860, ECO:0000269|PubMed:17301076};
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:15878860, ECO:0000269|PubMed:17301076};
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:15878860, ECO:0000269|PubMed:17301076};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000269|PubMed:17301076};
CC Note=Binds 2 [2Fe-2S] clusters per subunit.
CC {ECO:0000269|PubMed:17301076};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:17301076};
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 -!- 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:15878860, ECO:0000269|PubMed:2387845}.
CC -!- SUBUNIT: Homodimer. Interacts with BTN1A1 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:11993848}.
CC Cytoplasm {ECO:0000269|PubMed:11993848}. Secreted {ECO:0000250}.
CC -!- INDUCTION: By interferon.
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}.
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DR EMBL; J05579; AAA42349.1; -; mRNA.
DR EMBL; AH000836; AAA18869.1; -; Unassigned_DNA.
DR RefSeq; NP_058850.1; NM_017154.1.
DR PDB; 1WYG; X-ray; 2.60 A; A=1-1331.
DR PDB; 2E3T; X-ray; 2.28 A; A/B=1-1331.
DR PDB; 3AN1; X-ray; 1.73 A; A/B=1-1331.
DR PDB; 4YRW; X-ray; 1.99 A; A/B=1-1315.
DR PDB; 4YSW; X-ray; 1.99 A; A/B=1-1315.
DR PDB; 4YTY; X-ray; 2.20 A; A/B=1-1331.
DR PDB; 4YTZ; X-ray; 2.30 A; A/B=1-1315.
DR PDB; 6A7X; X-ray; 2.15 A; A/B=1-1331.
DR PDB; 6ABU; X-ray; 1.77 A; A/B=1-1331.
DR PDB; 6AC1; X-ray; 1.77 A; A/B=1-1331.
DR PDB; 6AC4; X-ray; 2.19 A; A/B=1-1331.
DR PDB; 6AD4; X-ray; 1.80 A; A/B=1-1331.
DR PDB; 6ADJ; X-ray; 2.18 A; A/B=1-1331.
DR PDB; 6AJU; X-ray; 1.94 A; A/F=1-1331.
DR PDBsum; 1WYG; -.
DR PDBsum; 2E3T; -.
DR PDBsum; 3AN1; -.
DR PDBsum; 4YRW; -.
DR PDBsum; 4YSW; -.
DR PDBsum; 4YTY; -.
DR PDBsum; 4YTZ; -.
DR PDBsum; 6A7X; -.
DR PDBsum; 6ABU; -.
DR PDBsum; 6AC1; -.
DR PDBsum; 6AC4; -.
DR PDBsum; 6AD4; -.
DR PDBsum; 6ADJ; -.
DR PDBsum; 6AJU; -.
DR AlphaFoldDB; P22985; -.
DR SMR; P22985; -.
DR STRING; 10116.ENSRNOP00000009634; -.
DR BindingDB; P22985; -.
DR ChEMBL; CHEMBL1075246; -.
DR DrugCentral; P22985; -.
DR iPTMnet; P22985; -.
DR PhosphoSitePlus; P22985; -.
DR PaxDb; P22985; -.
DR PRIDE; P22985; -.
DR GeneID; 497811; -.
DR KEGG; rno:497811; -.
DR UCSC; RGD:62043; rat.
DR CTD; 7498; -.
DR RGD; 62043; Xdh.
DR eggNOG; KOG0430; Eukaryota.
DR InParanoid; P22985; -.
DR OrthoDB; 48717at2759; -.
DR PhylomeDB; P22985; -.
DR BioCyc; MetaCyc:MON-15163; -.
DR BRENDA; 1.17.1.4; 5301.
DR BRENDA; 1.17.3.2; 5301.
DR Reactome; R-RNO-74259; Purine catabolism.
DR Reactome; R-RNO-8851680; Butyrophilin (BTN) family interactions.
DR Reactome; R-RNO-9748787; Azathioprine ADME.
DR SABIO-RK; P22985; -.
DR EvolutionaryTrace; P22985; -.
DR PRO; PR:P22985; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0005777; C:peroxisome; IDA:MGI.
DR GO; GO:0016529; C:sarcoplasmic reticulum; ISO:RGD.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:UniProtKB.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:UniProtKB.
DR GO; GO:0070674; F:hypoxanthine dehydrogenase activity; ISO:RGD.
DR GO; GO:0070675; F:hypoxanthine oxidase activity; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IDA:UniProtKB.
DR GO; GO:0050421; F:nitrite reductase (NO-forming) activity; IDA:RGD.
DR GO; GO:0016491; F:oxidoreductase activity; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0004854; F:xanthine dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0004855; F:xanthine oxidase activity; IDA:UniProtKB.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:RGD.
DR GO; GO:0006154; P:adenosine catabolic process; IDA:MGI.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0000255; P:allantoin metabolic process; IDA:MGI.
DR GO; GO:0006196; P:AMP catabolic process; ISO:RGD.
DR GO; GO:0071347; P:cellular response to interleukin-1; IEP:RGD.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:RGD.
DR GO; GO:0046059; P:dAMP catabolic process; ISO:RGD.
DR GO; GO:0006157; P:deoxyadenosine catabolic process; ISO:RGD.
DR GO; GO:0006161; P:deoxyguanosine catabolic process; ISO:RGD.
DR GO; GO:0006149; P:deoxyinosine catabolic process; ISO:RGD.
DR GO; GO:0046055; P:dGMP catabolic process; ISO:RGD.
DR GO; GO:0046038; P:GMP catabolic process; ISO:RGD.
DR GO; GO:0006147; P:guanine catabolic process; IDA:MGI.
DR GO; GO:0009114; P:hypoxanthine catabolic process; IDA:RGD.
DR GO; GO:0006204; P:IMP catabolic process; ISO:RGD.
DR GO; GO:0006148; P:inosine catabolic process; IDA:MGI.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; ISO:RGD.
DR GO; GO:0007595; P:lactation; ISO:RGD.
DR GO; GO:0045602; P:negative regulation of endothelial cell differentiation; ISO:RGD.
DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; ISO:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:0051898; P:negative regulation of protein kinase B signaling; ISO:RGD.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:RGD.
DR GO; GO:1900747; P:negative regulation of vascular endothelial growth factor signaling pathway; ISO:RGD.
DR GO; GO:2001213; P:negative regulation of vasculogenesis; ISO:RGD.
DR GO; GO:1900745; P:positive regulation of p38MAPK cascade; ISO:RGD.
DR GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; ISO:RGD.
DR GO; GO:0030856; P:regulation of epithelial cell differentiation; ISO:RGD.
DR GO; GO:0010044; P:response to aluminum ion; IDA:RGD.
DR GO; GO:0097184; P:response to azide; IEP:RGD.
DR GO; GO:0034465; P:response to carbon monoxide; IEP:RGD.
DR GO; GO:0009408; P:response to heat; IEP:RGD.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEP:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0009115; P:xanthine catabolic process; IDA: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 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 CHAIN 1..1331
FT /note="Xanthine dehydrogenase/oxidase"
FT /id="PRO_0000166086"
FT DOMAIN 4..91
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 228..413
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT ACT_SITE 1261
FT /note="Proton acceptor"
FT BINDING 43
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17301076,
FT ECO:0007744|PDB:2E3T"
FT BINDING 48
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17301076,
FT ECO:0007744|PDB:2E3T"
FT BINDING 51
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17301076,
FT ECO:0007744|PDB:2E3T"
FT BINDING 73
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17301076,
FT ECO:0007744|PDB:2E3T"
FT BINDING 112
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17301076,
FT ECO:0007744|PDB:2E3T"
FT BINDING 115
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17301076,
FT ECO:0007744|PDB:2E3T"
FT BINDING 147
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17301076,
FT ECO:0007744|PDB:2E3T"
FT BINDING 149
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17301076,
FT ECO:0007744|PDB:2E3T"
FT BINDING 256..263
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15878860,
FT ECO:0000269|PubMed:17301076"
FT BINDING 336
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 346..350
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15878860,
FT ECO:0000269|PubMed:17301076"
FT BINDING 359
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15878860,
FT ECO:0000269|PubMed:17301076"
FT BINDING 403
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15878860,
FT ECO:0000269|PubMed:17301076"
FT BINDING 421
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
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:0000250"
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:0000250"
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:0000250"
FT BINDING 914
FT /ligand="substrate"
FT /evidence="ECO:0000250"
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:0000250"
FT DISULFID 535..992
FT /note="In oxidase form"
FT /evidence="ECO:0000305|PubMed:15878860"
FT MUTAGEN 335..336
FT /note="WF->AL: Converts the enzyme 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:17301076"
FT MUTAGEN 535
FT /note="C->A: Slows the conversion from the dehydrogenase
FT form to the oxidase form; when associated with R-992.
FT Abolishes conversion from the dehydrogenase form to the
FT oxidase form; when associated with R-992 and S-1316."
FT /evidence="ECO:0000269|PubMed:15878860"
FT MUTAGEN 992
FT /note="C->R: Slows the conversion from the dehydrogenase
FT form to the oxidase form; when associated with A-535.
FT Abolishes conversion from the dehydrogenase form to the
FT oxidase form; when associated with A-535 and S-1316."
FT /evidence="ECO:0000269|PubMed:15878860"
FT MUTAGEN 1316
FT /note="C->S: Abolishes conversion from the dehydrogenase
FT form to the oxidase form; when associated with A-535 and R-
FT 992."
FT /evidence="ECO:0000269|PubMed:15878860"
FT STRAND 6..10
FT /evidence="ECO:0007829|PDB:3AN1"
FT STRAND 13..17
FT /evidence="ECO:0007829|PDB:3AN1"
FT HELIX 26..32
FT /evidence="ECO:0007829|PDB:3AN1"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:3AN1"
FT STRAND 52..59
FT /evidence="ECO:0007829|PDB:3AN1"
FT TURN 60..63
FT /evidence="ECO:0007829|PDB:3AN1"
FT STRAND 64..71
FT /evidence="ECO:0007829|PDB:3AN1"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:3AN1"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:3AN1"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:3AN1"
FT HELIX 88..91
FT /evidence="ECO:0007829|PDB:3AN1"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:1WYG"
FT HELIX 99..106
FT /evidence="ECO:0007829|PDB:3AN1"
FT HELIX 116..129
FT /evidence="ECO:0007829|PDB:3AN1"
FT HELIX 135..140
FT /evidence="ECO:0007829|PDB:3AN1"
FT TURN 141..144
FT /evidence="ECO:0007829|PDB:3AN1"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:3AN1"
FT HELIX 153..159
FT /evidence="ECO:0007829|PDB:3AN1"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:3AN1"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:3AN1"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:3AN1"
FT HELIX 213..218
FT /evidence="ECO:0007829|PDB:3AN1"
FT STRAND 226..229
FT /evidence="ECO:0007829|PDB:3AN1"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:3AN1"
FT HELIX 241..250
FT /evidence="ECO:0007829|PDB:3AN1"
FT HELIX 263..269
FT /evidence="ECO:0007829|PDB:3AN1"
FT STRAND 275..279
FT /evidence="ECO:0007829|PDB:3AN1"
FT HELIX 284..287
FT /evidence="ECO:0007829|PDB:3AN1"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:3AN1"
FT STRAND 293..299
FT /evidence="ECO:0007829|PDB:3AN1"
FT HELIX 304..317
FT /evidence="ECO:0007829|PDB:3AN1"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:3AN1"
FT HELIX 324..334
FT /evidence="ECO:0007829|PDB:3AN1"
FT HELIX 339..342
FT /evidence="ECO:0007829|PDB:3AN1"
FT HELIX 347..353
FT /evidence="ECO:0007829|PDB:3AN1"
FT HELIX 361..366
FT /evidence="ECO:0007829|PDB:3AN1"
FT STRAND 370..375
FT /evidence="ECO:0007829|PDB:3AN1"
FT STRAND 378..383
FT /evidence="ECO:0007829|PDB:3AN1"
FT HELIX 386..388
FT /evidence="ECO:0007829|PDB:3AN1"
FT STRAND 402..409
FT /evidence="ECO:0007829|PDB:3AN1"
FT STRAND 415..422
FT /evidence="ECO:0007829|PDB:3AN1"
FT STRAND 424..428
FT /evidence="ECO:0007829|PDB:3AN1"
FT STRAND 432..441
FT /evidence="ECO:0007829|PDB:3AN1"
FT STRAND 445..461
FT /evidence="ECO:0007829|PDB:3AN1"
FT TURN 466..468
FT /evidence="ECO:0007829|PDB:3AN1"
FT HELIX 470..472
FT /evidence="ECO:0007829|PDB:3AN1"
FT STRAND 476..478
FT /evidence="ECO:0007829|PDB:3AN1"
FT HELIX 479..492
FT /evidence="ECO:0007829|PDB:3AN1"
FT HELIX 504..528
FT /evidence="ECO:0007829|PDB:3AN1"
FT TURN 529..531
FT /evidence="ECO:0007829|PDB:4YTY"
FT HELIX 532..535
FT /evidence="ECO:0007829|PDB:3AN1"
FT HELIX 540..546
FT /evidence="ECO:0007829|PDB:3AN1"
FT STRAND 555..559
FT /evidence="ECO:0007829|PDB:3AN1"
FT STRAND 565..567
FT /evidence="ECO:0007829|PDB:1WYG"
FT HELIX 582..586
FT /evidence="ECO:0007829|PDB:3AN1"
FT HELIX 593..595
FT /evidence="ECO:0007829|PDB:3AN1"
FT STRAND 603..609
FT /evidence="ECO:0007829|PDB:3AN1"
FT STRAND 611..621
FT /evidence="ECO:0007829|PDB:3AN1"
FT HELIX 625..627
FT /evidence="ECO:0007829|PDB:3AN1"
FT STRAND 631..635
FT /evidence="ECO:0007829|PDB:3AN1"
FT HELIX 637..639
FT /evidence="ECO:0007829|PDB:3AN1"
FT STRAND 645..647
FT /evidence="ECO:0007829|PDB:3AN1"
FT STRAND 652..655
FT /evidence="ECO:0007829|PDB:3AN1"
FT STRAND 658..660
FT /evidence="ECO:0007829|PDB:3AN1"
FT STRAND 666..674
FT /evidence="ECO:0007829|PDB:3AN1"
FT HELIX 675..683
FT /evidence="ECO:0007829|PDB:3AN1"
FT STRAND 686..691
FT /evidence="ECO:0007829|PDB:3AN1"
FT HELIX 698..703
FT /evidence="ECO:0007829|PDB:3AN1"
FT STRAND 707..710
FT /evidence="ECO:0007829|PDB:3AN1"
FT STRAND 712..717
FT /evidence="ECO:0007829|PDB:3AN1"
FT HELIX 719..725
FT /evidence="ECO:0007829|PDB:3AN1"
FT STRAND 727..736
FT /evidence="ECO:0007829|PDB:3AN1"
FT STRAND 748..753
FT /evidence="ECO:0007829|PDB:3AN1"
FT STRAND 760..764
FT /evidence="ECO:0007829|PDB:3AN1"
FT HELIX 769..780
FT /evidence="ECO:0007829|PDB:3AN1"
FT HELIX 784..786
FT /evidence="ECO:0007829|PDB:3AN1"
FT STRAND 787..792
FT /evidence="ECO:0007829|PDB:3AN1"
FT TURN 798..801
FT /evidence="ECO:0007829|PDB:3AN1"
FT STRAND 802..804
FT /evidence="ECO:0007829|PDB:1WYG"
FT HELIX 806..819
FT /evidence="ECO:0007829|PDB:3AN1"
FT STRAND 823..826
FT /evidence="ECO:0007829|PDB:3AN1"
FT HELIX 829..835
FT /evidence="ECO:0007829|PDB:3AN1"
FT STRAND 842..850
FT /evidence="ECO:0007829|PDB:3AN1"
FT STRAND 856..866
FT /evidence="ECO:0007829|PDB:3AN1"
FT HELIX 874..883
FT /evidence="ECO:0007829|PDB:3AN1"
FT TURN 884..888
FT /evidence="ECO:0007829|PDB:3AN1"
FT STRAND 892..901
FT /evidence="ECO:0007829|PDB:3AN1"
FT TURN 912..915
FT /evidence="ECO:0007829|PDB:3AN1"
FT HELIX 916..934
FT /evidence="ECO:0007829|PDB:3AN1"
FT HELIX 938..945
FT /evidence="ECO:0007829|PDB:3AN1"
FT HELIX 964..974
FT /evidence="ECO:0007829|PDB:3AN1"
FT HELIX 977..990
FT /evidence="ECO:0007829|PDB:3AN1"
FT STRAND 992..1008
FT /evidence="ECO:0007829|PDB:3AN1"
FT HELIX 1012..1014
FT /evidence="ECO:0007829|PDB:3AN1"
FT STRAND 1016..1023
FT /evidence="ECO:0007829|PDB:3AN1"
FT STRAND 1029..1034
FT /evidence="ECO:0007829|PDB:3AN1"
FT STRAND 1038..1040
FT /evidence="ECO:0007829|PDB:3AN1"
FT HELIX 1042..1054
FT /evidence="ECO:0007829|PDB:3AN1"
FT HELIX 1058..1060
FT /evidence="ECO:0007829|PDB:3AN1"
FT STRAND 1061..1063
FT /evidence="ECO:0007829|PDB:4YSW"
FT TURN 1068..1070
FT /evidence="ECO:0007829|PDB:3AN1"
FT TURN 1079..1081
FT /evidence="ECO:0007829|PDB:1WYG"
FT HELIX 1082..1107
FT /evidence="ECO:0007829|PDB:3AN1"
FT STRAND 1108..1111
FT /evidence="ECO:0007829|PDB:3AN1"
FT HELIX 1113..1122
FT /evidence="ECO:0007829|PDB:3AN1"
FT STRAND 1128..1134
FT /evidence="ECO:0007829|PDB:3AN1"
FT TURN 1142..1145
FT /evidence="ECO:0007829|PDB:3AN1"
FT STRAND 1151..1165
FT /evidence="ECO:0007829|PDB:3AN1"
FT TURN 1166..1168
FT /evidence="ECO:0007829|PDB:3AN1"
FT STRAND 1171..1181
FT /evidence="ECO:0007829|PDB:3AN1"
FT HELIX 1188..1207
FT /evidence="ECO:0007829|PDB:3AN1"
FT TURN 1224..1226
FT /evidence="ECO:0007829|PDB:3AN1"
FT HELIX 1232..1234
FT /evidence="ECO:0007829|PDB:3AN1"
FT STRAND 1237..1243
FT /evidence="ECO:0007829|PDB:3AN1"
FT TURN 1250..1252
FT /evidence="ECO:0007829|PDB:1WYG"
FT HELIX 1253..1255
FT /evidence="ECO:0007829|PDB:3AN1"
FT HELIX 1264..1267
FT /evidence="ECO:0007829|PDB:3AN1"
FT HELIX 1268..1285
FT /evidence="ECO:0007829|PDB:3AN1"
FT STRAND 1286..1289
FT /evidence="ECO:0007829|PDB:2E3T"
FT HELIX 1301..1307
FT /evidence="ECO:0007829|PDB:3AN1"
FT HELIX 1311..1316
FT /evidence="ECO:0007829|PDB:3AN1"
SQ SEQUENCE 1331 AA; 146243 MW; BF2586A9C63A0B2C CRC64;
MTADELVFFV NGKKVVEKNA DPETTLLVYL RRKLGLCGTK LGCGEGGCGA CTVMISKYDR
LQNKIVHFSV NACLAPICSL HHVAVTTVEG IGNTQKLHPV QERIARSHGS QCGFCTPGIV
MSMYTLLRNQ PEPTVEEIEN AFQGNLCRCT GYRPILQGFR TFAKDGGCCG GSGNNPNCCM
NQTKDQTVSL SPSLFNPEDF KPLDPTQEPI FPPELLRLKD TPQKKLRFEG ERVTWIQAST
MEELLDLKAQ HPDAKLVVGN TEIGIEMKFK NMLFPLIVCP AWIPELNSVV HGPEGISFGA
SCPLSLVESV LAEEIAKLPE QKTEVFRGVM EQLRWFAGKQ VKSVASIGGN IITASPISDL
NPVFMASGAK LTLVSRGTRR TVRMDHTFFP GYRKTLLRPE EILLSIEIPY SKEGEFFSAF
KQASRREDDI AKVTSGMRVL FKPGTIEVQE LSLCFGGMAD RTISALKTTP KQLSKSWNEE
LLQSVCAGLA EELQLAPDAP GGMVEFRRTL TLSFFFKFYL TVLQKLGRAD LEDMCGKLDP
TFASATLLFQ KDPPANVQLF QEVPKDQSEE DMVGRPLPHL AANMQASGEA VYCDDIPRYE
NELSLRLVTS TRAHAKITSI DTSEAKKVPG FVCFLTAEDV PNSNATGLFN DETVFAKDEV
TCVGHIIGAV VADTPEHAQR AARGVKITYE DLPAIITIQD AINNNSFYGS EIKIEKGDLK
KGFSEADNVV SGELYIGGQE HFYLETNCTI AVPKGEAGEM ELFVSTQNTM KTQSFVAKML
GVPDNRIVVR VKRMGGGFGG KETRSTVVST ALALAAHKTG RPVRCMLDRD EDMLITGGRH
PFLAKYKVGF MKTGTVVALE VAHFSNGGNT EDLSRSIMER ALFHMDNAYK IPNIRGTGRI
CKTNLPSNTA FRGFGGPQGM LIAEYWMSEV AITCGLPAEE VRRKNMYKEG DLTHFNQKLE
GFTLPRCWDE CIASSQYLAR KREVEKFNRE NCWKKRGLCI IPTKFGISFT LPFLNQGGAL
VHVYTDGSVL LTHGGTEMGQ GLHTKMVQVA SRALKIPTSK IHISETSTNT VPNTSPTAAS
ASADLNGQGV YEACQTILKR LEPFKKKKPT GPWEAWVMDA YTSAVSLSAT GFYKTPNLGY
SFETNSGNPF HYFSYGVACS EVEIDCLTGD HKNLRTDIVM DVGSSLNPAI DIGQVEGAFV
QGLGLFTMEE LHYSPEGSLH TRGPSTYKIP AFGSIPIEFR VSLLRDCPNK RAIYASKAVG
EPPLFLASSI FFAIKDAIRA ARAQHGDNAK QLFQLDSPAT PEKIRNACVD QFTTLCVTGV
PENCKSWSVR I
