XDH_MOUSE
ID XDH_MOUSE Reviewed; 1335 AA.
AC Q00519; E9QLM9;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 5.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Xanthine dehydrogenase/oxidase;
DE Includes:
DE RecName: Full=Xanthine dehydrogenase;
DE Short=XD;
DE EC=1.17.1.4 {ECO:0000250|UniProtKB:P22985};
DE Includes:
DE RecName: Full=Xanthine oxidase;
DE Short=XO;
DE EC=1.17.3.2 {ECO:0000250|UniProtKB:P22985};
DE AltName: Full=Xanthine oxidoreductase;
DE Short=XOR;
GN Name=Xdh;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv; TISSUE=Spleen;
RX PubMed=7835888; DOI=10.1006/geno.1994.1515;
RA Cazzaniga G., Terao M., Lo Schiavo P., Galbiati F., Segalla F.,
RA Seldin M.F., Garattini E.;
RT "Chromosomal mapping, isolation, and characterization of the mouse xanthine
RT dehydrogenase gene.";
RL Genomics 23:390-402(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=1590774; DOI=10.1042/bj2830863;
RA Terao M., Cazzaniga G., Ghezzi P., Bianchi M., Falciani F., Perani P.,
RA Garattini E.;
RT "Molecular cloning of a cDNA coding for mouse liver xanthine dehydrogenase.
RT Regulation of its transcript by interferons in vivo.";
RL Biochem. J. 283:863-870(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP PROTEIN SEQUENCE OF 2-9, AND INTERACTION WITH BTN1A1.
RX PubMed=8541302; DOI=10.1016/0304-4165(95)00102-6;
RA Ishii T., Aoki N., Noda A., Adachi T., Nakamura R., Matsuda T.;
RT "Carboxy-terminal cytoplasmic domain of mouse butyrophilin specifically
RT associates with a 150-kDa protein of mammary epithelial cells and milk fat
RT globule membrane.";
RL Biochim. Biophys. Acta 1245:285-292(1995).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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:0000250|UniProtKB:P22985};
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:0000250|UniProtKB:P22985};
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:0000250|UniProtKB:P22985};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
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 -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000250|UniProtKB:P22985};
CC Note=Binds 2 [2Fe-2S] clusters per subunit.
CC {ECO:0000250|UniProtKB:P22985};
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. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Interacts with BTN1A1.
CC {ECO:0000269|PubMed:8541302}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Peroxisome
CC {ECO:0000250}. 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). {ECO:0000250}.
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). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; X75129; CAA52997.1; -; Genomic_DNA.
DR EMBL; X75128; CAA52997.1; JOINED; Genomic_DNA.
DR EMBL; X75127; CAA52997.1; JOINED; Genomic_DNA.
DR EMBL; X75126; CAA52997.1; JOINED; Genomic_DNA.
DR EMBL; X75125; CAA52997.1; JOINED; Genomic_DNA.
DR EMBL; X75124; CAA52997.1; JOINED; Genomic_DNA.
DR EMBL; X75123; CAA52997.1; JOINED; Genomic_DNA.
DR EMBL; X75122; CAA52997.1; JOINED; Genomic_DNA.
DR EMBL; X75121; CAA52997.1; JOINED; Genomic_DNA.
DR EMBL; X75120; CAA52997.1; JOINED; Genomic_DNA.
DR EMBL; X75119; CAA52997.1; JOINED; Genomic_DNA.
DR EMBL; X75130; CAA52997.1; JOINED; Genomic_DNA.
DR EMBL; X75131; CAA52997.1; JOINED; Genomic_DNA.
DR EMBL; X75132; CAA52997.1; JOINED; Genomic_DNA.
DR EMBL; X75133; CAA52997.1; JOINED; Genomic_DNA.
DR EMBL; X75134; CAA52997.1; JOINED; Genomic_DNA.
DR EMBL; X75135; CAA52997.1; JOINED; Genomic_DNA.
DR EMBL; X75136; CAA52997.1; JOINED; Genomic_DNA.
DR EMBL; X75137; CAA52997.1; JOINED; Genomic_DNA.
DR EMBL; X75138; CAA52997.1; JOINED; Genomic_DNA.
DR EMBL; X75139; CAA52997.1; JOINED; Genomic_DNA.
DR EMBL; X75140; CAA52997.1; JOINED; Genomic_DNA.
DR EMBL; X75141; CAA52997.1; JOINED; Genomic_DNA.
DR EMBL; X75142; CAA52997.1; JOINED; Genomic_DNA.
DR EMBL; X75143; CAA52997.1; JOINED; Genomic_DNA.
DR EMBL; X75151; CAA52997.1; JOINED; Genomic_DNA.
DR EMBL; X75152; CAA52997.1; JOINED; Genomic_DNA.
DR EMBL; X75153; CAA52997.1; JOINED; Genomic_DNA.
DR EMBL; X75154; CAA52997.1; JOINED; Genomic_DNA.
DR EMBL; X75144; CAA52997.1; JOINED; Genomic_DNA.
DR EMBL; X75145; CAA52997.1; JOINED; Genomic_DNA.
DR EMBL; X75146; CAA52997.1; JOINED; Genomic_DNA.
DR EMBL; X75147; CAA52997.1; JOINED; Genomic_DNA.
DR EMBL; X75148; CAA52997.1; JOINED; Genomic_DNA.
DR EMBL; X75149; CAA52997.1; JOINED; Genomic_DNA.
DR EMBL; X75150; CAA52997.1; JOINED; Genomic_DNA.
DR EMBL; X62932; CAA44705.1; -; mRNA.
DR EMBL; AC159187; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT025731; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS28967.1; -.
DR PIR; I48374; XOMSDH.
DR RefSeq; NP_035853.2; NM_011723.3.
DR AlphaFoldDB; Q00519; -.
DR SMR; Q00519; -.
DR BioGRID; 204590; 6.
DR CORUM; Q00519; -.
DR STRING; 10090.ENSMUSP00000024866; -.
DR iPTMnet; Q00519; -.
DR PhosphoSitePlus; Q00519; -.
DR SwissPalm; Q00519; -.
DR CPTAC; non-CPTAC-4057; -.
DR EPD; Q00519; -.
DR jPOST; Q00519; -.
DR MaxQB; Q00519; -.
DR PaxDb; Q00519; -.
DR PeptideAtlas; Q00519; -.
DR PRIDE; Q00519; -.
DR ProteomicsDB; 299780; -.
DR Antibodypedia; 4018; 273 antibodies from 35 providers.
DR DNASU; 22436; -.
DR Ensembl; ENSMUST00000024866; ENSMUSP00000024866; ENSMUSG00000024066.
DR GeneID; 22436; -.
DR KEGG; mmu:22436; -.
DR UCSC; uc008dno.2; mouse.
DR CTD; 7498; -.
DR MGI; MGI:98973; Xdh.
DR VEuPathDB; HostDB:ENSMUSG00000024066; -.
DR eggNOG; KOG0430; Eukaryota.
DR GeneTree; ENSGT00950000183114; -.
DR HOGENOM; CLU_001681_1_2_1; -.
DR InParanoid; Q00519; -.
DR OMA; DIGYVWG; -.
DR OrthoDB; 48717at2759; -.
DR PhylomeDB; Q00519; -.
DR TreeFam; TF353036; -.
DR BioCyc; MetaCyc:MON-14019; -.
DR Reactome; R-MMU-74259; Purine catabolism.
DR Reactome; R-MMU-8851680; Butyrophilin (BTN) family interactions.
DR Reactome; R-MMU-9748787; Azathioprine ADME.
DR SABIO-RK; Q00519; -.
DR BioGRID-ORCS; 22436; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Xdh; mouse.
DR PRO; PR:Q00519; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q00519; protein.
DR Bgee; ENSMUSG00000024066; Expressed in granulocyte and 159 other tissues.
DR ExpressionAtlas; Q00519; baseline and differential.
DR Genevisible; Q00519; MM.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005777; C:peroxisome; ISO:MGI.
DR GO; GO:0016529; C:sarcoplasmic reticulum; IDA:BHF-UCL.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; ISS:UniProtKB.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; ISS:UniProtKB.
DR GO; GO:0070674; F:hypoxanthine dehydrogenase activity; IDA:MGI.
DR GO; GO:0070675; F:hypoxanthine oxidase activity; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR GO; GO:0043546; F:molybdopterin cofactor binding; ISS:UniProtKB.
DR GO; GO:0050421; F:nitrite reductase (NO-forming) activity; ISO:MGI.
DR GO; GO:0016491; F:oxidoreductase activity; IDA:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0004854; F:xanthine dehydrogenase activity; IDA:MGI.
DR GO; GO:0004855; F:xanthine oxidase activity; IDA:MGI.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
DR GO; GO:0006154; P:adenosine catabolic process; IDA:MGI.
DR GO; GO:0000255; P:allantoin metabolic process; IDA:MGI.
DR GO; GO:0006196; P:AMP catabolic process; IDA:MGI.
DR GO; GO:0046059; P:dAMP catabolic process; IDA:MGI.
DR GO; GO:0006157; P:deoxyadenosine catabolic process; IDA:MGI.
DR GO; GO:0006161; P:deoxyguanosine catabolic process; IDA:MGI.
DR GO; GO:0006149; P:deoxyinosine catabolic process; IDA:MGI.
DR GO; GO:0046055; P:dGMP catabolic process; IDA:MGI.
DR GO; GO:0046038; P:GMP catabolic process; IDA:MGI.
DR GO; GO:0006147; P:guanine catabolic process; IDA:MGI.
DR GO; GO:0009114; P:hypoxanthine catabolic process; IDA:MGI.
DR GO; GO:0006204; P:IMP catabolic process; IDA:MGI.
DR GO; GO:0006148; P:inosine catabolic process; IDA:MGI.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IDA:MGI.
DR GO; GO:0007595; P:lactation; IMP:MGI.
DR GO; GO:0045602; P:negative regulation of endothelial cell differentiation; ISO:MGI.
DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:0051898; P:negative regulation of protein kinase B signaling; ISO:MGI.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:1900747; P:negative regulation of vascular endothelial growth factor signaling pathway; ISO:MGI.
DR GO; GO:2001213; P:negative regulation of vasculogenesis; ISO:MGI.
DR GO; GO:1900745; P:positive regulation of p38MAPK cascade; ISO:MGI.
DR GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; ISO:MGI.
DR GO; GO:0030856; P:regulation of epithelial cell differentiation; IMP:MGI.
DR GO; GO:0010044; P:response to aluminum ion; ISO:MGI.
DR GO; GO:0009115; P:xanthine catabolic process; IDA:MGI.
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; IPR014309; Xanthine_DH_Mopterin-bd_su.
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 TIGRFAMs; TIGR02965; xanthine_xdhB; 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; Cytoplasm; Direct protein sequencing; Disulfide bond; FAD;
KW 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:8541302"
FT CHAIN 2..1335
FT /note="Xanthine dehydrogenase/oxidase"
FT /id="PRO_0000166085"
FT DOMAIN 7..94
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 231..416
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT ACT_SITE 1264
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 46
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22985"
FT BINDING 51
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22985"
FT BINDING 54
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22985"
FT BINDING 76
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22985"
FT BINDING 115
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22985"
FT BINDING 118
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22985"
FT BINDING 150
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22985"
FT BINDING 152
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22985"
FT BINDING 259..266
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 339
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 349..353
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 362
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 406
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 424
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 770
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 801
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 805
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 883
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 915
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 917
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1013
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1082
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 538..995
FT /note="In oxidase form"
FT /evidence="ECO:0000250"
FT CONFLICT 241
FT /note="V -> I (in Ref. 2; CAA44705)"
FT /evidence="ECO:0000305"
FT CONFLICT 621
FT /note="M -> T (in Ref. 1; CAA52997)"
FT /evidence="ECO:0000305"
FT CONFLICT 1247
FT /note="L -> V (in Ref. 1; CAA52997 and 2; CAA44705)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1335 AA; 146562 MW; 56AD3E0C75E00F98 CRC64;
MTRTTVDELV FFVNGKKVVE KNADPETTLL VYLRRKLGLC GTKLGCGEGG CGACTVMISK
YDRLQNKIVH FSVNACLTPI CSLHHVAVTT VEGIGNTKKL HPVQERIAKS HGSQCGFCTP
GIVMSMYTLL RNKPEPTVEE IENAFQGNLC RCTGYRPILQ GFRTFAKDGG CCGGSGNNPN
CCMSQTKDQT IAPSSSLFNP EDFKPLDPTQ EPIFPPELLR LKDTPRKTLR FEGERVTWIQ
VSTMEELLDL KAQHPDAKLV VGNTEIGIEM KFKNMLFPLI ICPAWILELT SVAHGPEGIS
FGAACPLSLV ESVLADAIAT LPEQRTEVFR GVMEQLRWFA GKQVKSVASI GGNIITASPI
SDLNPVLMAS RAKLTLASRG TKRTVWMDHT FFPGYRRTLL SPEEILVSIV IPYSRKGEFF
SAFKQASRRE DDIAKVTSGM RVLFKPGTTE VQELSLCFGG MADRTVSALK TTPKQLSKSW
NEELLQDVCA GLAEELHLAP DAPGGMVEFR RTLTLSFFFK FYLTVLQKLG RADLEGMCGK
LDPTFASATL LFQKDPPANV QLFQEVPKGQ SEEDMVGRPM PHLAADMQAS GEAVYCDDIP
RYENELSLRL VTSTRAHAKI MSIDTSEAKK VPGFVCFLTS EDVPGSNITG IFNDETVFAK
DEVTCVGHII GAVVADTPEH AHRAARGVKI TYEDLPAIIT IQDAIKNNSF YGPEVKIEKG
DLKKGFSEAD NVVSGELYIG GQEHFYLETH CTIAVPKGEA GEMELFVSTQ NTMKTQSFIA
KMLGVPDNRI VVRVKRMGGG FGGKETRSTL ISTAVALAAY KTGRPVRCML DRDEDMLITG
GRHPFLAKYK VGFMKTGTIV ALEVAHFSNG GNSEDLSRSI MERAVFHMDN AYKIPNIRGT
GRICKTNLPS NTAFRGFGGP QGMLIAEYWM SEVAVTCGLP AEEVRRKNMY KEGDLTHFNQ
KLEGFTLPRC WDECIASSQY QARKMEVEKF NRENCWKKRG LCIIPTKFGI SFTLSFLNQG
GALVHVYTDG SVLLTHGGTE MGQGLHTKMV QVASRALKIP TSKIHITETS TNTVPNTSPT
AASASADLNG QAIYEACQTI LKRLEPFKKK NPSGSWESWV MDAYTSAVSL SATGFYKTPN
LGYSFETNSG NPFHYFSYGV ACSEVEIDCL TGDHKNLRTD IVMDVGSSLN PAIDIGQVEG
AFVQGLGLFT MEELHYSPEG SLHTRGPSTY KIPAFGSIPI EFRVSLLRDC PNKRAIYASK
AVGEPPLFLA SSIFFAIKDA IRAARAQHGD SNAKQLFQLD SPATPEKIRN ACVDQFTTLC
ATGTPENCKS WSVRI
