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P47990

- XDH_CHICK

UniProt

P47990 - XDH_CHICK

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Protein

Xanthine dehydrogenase/oxidase

Gene

XDH

Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Key enzyme in purine degradation. Catalyzes the oxidation of hypoxanthine to xanthine. Catalyzes the oxidation of xanthine to uric acid. Contributes to the generation of reactive oxygen species (By similarity).By similarity

Catalytic activityi

Xanthine + NAD+ + H2O = urate + NADH.
Hypoxanthine + NAD+ + H2O = xanthine + NADH.
Xanthine + H2O + O2 = urate + H2O2.

Cofactori

Protein has several cofactor binding sites:
  • [2Fe-2S] clusterBy similarityNote: Binds 2 [2Fe-2S] clusters.By similarity
  • FADBy similarity
  • Mo-molybdopterinBy similarityNote: Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi47 – 471Iron-sulfur 1By similarity
Metal bindingi52 – 521Iron-sulfur 1By similarity
Metal bindingi55 – 551Iron-sulfur 1By similarity
Metal bindingi77 – 771Iron-sulfur 1By similarity
Metal bindingi117 – 1171Iron-sulfur 2By similarity
Metal bindingi120 – 1201Iron-sulfur 2By similarity
Metal bindingi152 – 1521Iron-sulfur 2By similarity
Metal bindingi154 – 1541Iron-sulfur 2By similarity
Binding sitei363 – 3631FADBy similarity
Binding sitei386 – 3861FADBy similarity
Binding sitei430 – 4301FAD; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei448 – 4481FADBy similarity
Metal bindingi796 – 7961MolybdenumBy similarity
Metal bindingi827 – 8271Molybdenum; via carbonyl oxygenBy similarity
Binding sitei831 – 8311SubstrateBy similarity
Binding sitei909 – 9091SubstrateBy similarity
Metal bindingi941 – 9411Molybdenum; via amide nitrogenBy similarity
Binding sitei943 – 9431SubstrateBy similarity
Binding sitei1039 – 10391Substrate; via amide nitrogenBy similarity
Metal bindingi1108 – 11081Molybdenum; via amide nitrogenBy similarity
Active sitei1290 – 12901Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi283 – 2908FADBy similarity
Nucleotide bindingi373 – 3775FADBy similarity

GO - Molecular functioni

  1. 2 iron, 2 sulfur cluster binding Source: UniProtKB
  2. electron carrier activity Source: InterPro
  3. flavin adenine dinucleotide binding Source: UniProtKB
  4. iron ion binding Source: InterPro
  5. molybdenum ion binding Source: InterPro
  6. molybdopterin cofactor binding Source: UniProtKB
  7. UDP-N-acetylmuramate dehydrogenase activity Source: InterPro
  8. xanthine dehydrogenase activity Source: UniProtKB
  9. xanthine oxidase activity Source: UniProtKB

GO - Biological processi

  1. nucleobase-containing small molecule metabolic process Source: Reactome
  2. purine nucleobase metabolic process Source: Reactome
  3. small molecule metabolic process Source: Reactome
  4. urate biosynthetic process Source: Reactome
  5. xanthine catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

2Fe-2S, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding, Molybdenum, NAD

Enzyme and pathway databases

ReactomeiREACT_115590. Urate synthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Xanthine dehydrogenase/oxidase
Including the following 2 domains:
Xanthine dehydrogenase (EC:1.17.1.4)
Short name:
XD
Xanthine oxidase (EC:1.17.3.2)
Short name:
XO
Alternative name(s):
Xanthine oxidoreductase
Short name:
XOR
Gene namesi
Name:XDH
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539: Unplaced

Subcellular locationi

Peroxisome By similarity. Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. peroxisome Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13581358Xanthine dehydrogenase/oxidasePRO_0000166083Add
BLAST

Proteomic databases

PaxDbiP47990.

Expressioni

Tissue specificityi

Detected in liver (at protein level).1 Publication

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi9031.ENSGALP00000014144.

Structurei

3D structure databases

ProteinModelPortaliP47990.
SMRiP47990. Positions 600-1343.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini8 – 95882Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST
Domaini255 – 440186FAD-binding PCMH-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the xanthine dehydrogenase family.Curated
Contains 1 2Fe-2S ferredoxin-type domain.PROSITE-ProRule annotation
Contains 1 FAD-binding PCMH-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG4630.
HOGENOMiHOG000191197.
HOVERGENiHBG004182.
InParanoidiP47990.
KOiK00106.
PhylomeDBiP47990.

Family and domain databases

Gene3Di1.10.150.120. 1 hit.
3.10.20.30. 1 hit.
3.30.365.10. 6 hits.
3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
3.90.1170.50. 1 hit.
InterProiIPR002888. 2Fe-2S-bd.
IPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR000674. Ald_Oxase/Xan_DH_a/b.
IPR016208. Ald_Oxase/xanthine_DH.
IPR008274. AldOxase/xan_DH_Mopterin-bd.
IPR012675. Beta-grasp_dom.
IPR005107. CO_DH_flav_C.
IPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR002346. Mopterin_DH_FAD-bd.
IPR022407. OxRdtase_Mopterin_BS.
IPR014309. Xanthine_DH_Mopterin-bd_su.
IPR014307. Xanthine_DH_ssu.
[Graphical view]
PfamiPF01315. Ald_Xan_dh_C. 1 hit.
PF02738. Ald_Xan_dh_C2. 1 hit.
PF03450. CO_deh_flav_C. 1 hit.
PF00941. FAD_binding_5. 1 hit.
PF00111. Fer2. 1 hit.
PF01799. Fer2_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000127. Xanthine_DH. 1 hit.
SMARTiSM01008. Ald_Xan_dh_C. 1 hit.
SM01092. CO_deh_flav_C. 1 hit.
[Graphical view]
SUPFAMiSSF47741. SSF47741. 2 hits.
SSF54292. SSF54292. 1 hit.
SSF54665. SSF54665. 1 hit.
SSF55447. SSF55447. 1 hit.
SSF56003. SSF56003. 1 hit.
SSF56176. SSF56176. 1 hit.
TIGRFAMsiTIGR02963. xanthine_xdhA. 1 hit.
TIGR02965. xanthine_xdhB. 1 hit.
PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51387. FAD_PCMH. 1 hit.
PS00559. MOLYBDOPTERIN_EUK. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P47990-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAPPETGDEL VFFVNGKKVV EKDVDPETTL LTYLRRKLGL CGTKLGCGEG
60 70 80 90 100
GCGACTVMIS KYDPFQKKIL HHTANACLFP ICALHHVAVT TVEGIGNTKS
110 120 130 140 150
RLHPAQERIA KSHGSQCGFC TPGIVMSMYT LLRNKPKPKM EDIEDAFQGN
160 170 180 190 200
LCRCTGYRPI LEGYRTFAVD SNCCGKAANG TGCCHSKGEN SMNGGCCGGK
210 220 230 240 250
ANGPGCCMNE KENVTMMSSS LFDSSEFQPL DPTQEPIFPP ELMTQRNKEQ
260 270 280 290 300
KQVCFKGERV MWIQPTTLQE LVALKSQYPN AKLVVGNTEV GIEMRLKNML
310 320 330 340 350
YPVILAPAWI PEMNAVQQTE TGITFGAACT LSSVEEVLRK AVAELPSYKT
360 370 380 390 400
EIFQAALEQL RWFAGPQIRN VAALGGNIMT ASPISDLNPV LMASGSKLTL
410 420 430 440 450
ISMEGKRTVM MDEKFFTGYR KTIVKPEEVL LSVEIPYSKE GEYFSAFKQA
460 470 480 490 500
YRREDDIAIV TCGMRVLFQH GTSRVQEVKL SYGGMAPTTI LALKTCRELA
510 520 530 540 550
GRDWNEKLLQ DACRLLAGEM DLSPSAPGGM VEFRRTLTLS FFFKFYLTVL
560 570 580 590 600
QKLSKDQNGP NNLCEPVPPN YISATELFHK DPIASTQLFQ EVPRGQLVED
610 620 630 640 650
TVGRPLVHLS AAKQACGEAV YCDDIPHYEN ELYLTLVTST QAHAKILSID
660 670 680 690 700
ASEAQSVPGF VCFVSAKDVP GSNITGIAND ETVFAEDVVT CVGHIIGAVI
710 720 730 740 750
ADTQEHSRRA AKAVKIKYEE LKPIVTIQEA IEQQSFIKPI KRIKKGDVNK
760 770 780 790 800
GFEESDHILE GEMHIGGQEH FYLETHCTLA VPKGEDGEME LFVSTQNLMK
810 820 830 840 850
TQEFTASALG VPSNRIVVRV KRMGGGFGGK ETRNTILTTV VAVAAFKTGR
860 870 880 890 900
PVRCMLDRDE DMLISGGRHP FLGRYKVGFM KNGKIKSLEV SYYSNGGNSA
910 920 930 940 950
DLSHGVMDRA LLHLDNSYNI PNVSIMGFIC KTNLSSNTAF RGFGGPQGMM
960 970 980 990 1000
IAECWMSDLA RKCGLPPEEV RKINLYHEGD LTHFNQKLEG FTLRRCWDEC
1010 1020 1030 1040 1050
LSSSNYHARK KLIEEFNKQN RWKKRGMCII PTKFGISFTV PFLNQAGALV
1060 1070 1080 1090 1100
HVYTDGSVLL THGGTEMGQG LHTKMIQVAS RSLGIPTSKI YISETSTNTV
1110 1120 1130 1140 1150
PNTSPTAASV SADINGMAVH NACQTILKRL EPIKQSNLKG SWEDWIKTAY
1160 1170 1180 1190 1200
ENCISLSATG FYRIPDVGYN FETNKGKPFH YFSYGVACSE VEIDCLTGDH
1210 1220 1230 1240 1250
KNIRTDIVMD VGTSLNPAID IGQIEGAFVQ GIGLFTMEEL RYSPEGNLYT
1260 1270 1280 1290 1300
RGPGMYKIPA FGDIPTEFYV SLLRDCPNSK AIYSSKAVGE PPLFLSASVF
1310 1320 1330 1340 1350
YAIKDAIYSA REDSGVTEPF RLDSPATPER IRNACVDTFT KMCPSAEPGT

FKPWSVRA
Length:1,358
Mass (Da):149,614
Last modified:February 1, 1996 - v1
Checksum:i53B049B38704995F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13221 mRNA. Translation: BAA02502.1.
PIRiA55711. XOCHDH.
RefSeqiNP_990458.1. NM_205127.1.
UniGeneiGga.2494.

Genome annotation databases

GeneIDi396025.
KEGGigga:396025.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13221 mRNA. Translation: BAA02502.1 .
PIRi A55711. XOCHDH.
RefSeqi NP_990458.1. NM_205127.1.
UniGenei Gga.2494.

3D structure databases

ProteinModelPortali P47990.
SMRi P47990. Positions 600-1343.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9031.ENSGALP00000014144.

Proteomic databases

PaxDbi P47990.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 396025.
KEGGi gga:396025.

Organism-specific databases

CTDi 7498.

Phylogenomic databases

eggNOGi COG4630.
HOGENOMi HOG000191197.
HOVERGENi HBG004182.
InParanoidi P47990.
KOi K00106.
PhylomeDBi P47990.

Enzyme and pathway databases

Reactomei REACT_115590. Urate synthesis.

Miscellaneous databases

NextBioi 20816087.
PROi P47990.

Family and domain databases

Gene3Di 1.10.150.120. 1 hit.
3.10.20.30. 1 hit.
3.30.365.10. 6 hits.
3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
3.90.1170.50. 1 hit.
InterProi IPR002888. 2Fe-2S-bd.
IPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR000674. Ald_Oxase/Xan_DH_a/b.
IPR016208. Ald_Oxase/xanthine_DH.
IPR008274. AldOxase/xan_DH_Mopterin-bd.
IPR012675. Beta-grasp_dom.
IPR005107. CO_DH_flav_C.
IPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR002346. Mopterin_DH_FAD-bd.
IPR022407. OxRdtase_Mopterin_BS.
IPR014309. Xanthine_DH_Mopterin-bd_su.
IPR014307. Xanthine_DH_ssu.
[Graphical view ]
Pfami PF01315. Ald_Xan_dh_C. 1 hit.
PF02738. Ald_Xan_dh_C2. 1 hit.
PF03450. CO_deh_flav_C. 1 hit.
PF00941. FAD_binding_5. 1 hit.
PF00111. Fer2. 1 hit.
PF01799. Fer2_2. 1 hit.
[Graphical view ]
PIRSFi PIRSF000127. Xanthine_DH. 1 hit.
SMARTi SM01008. Ald_Xan_dh_C. 1 hit.
SM01092. CO_deh_flav_C. 1 hit.
[Graphical view ]
SUPFAMi SSF47741. SSF47741. 2 hits.
SSF54292. SSF54292. 1 hit.
SSF54665. SSF54665. 1 hit.
SSF55447. SSF55447. 1 hit.
SSF56003. SSF56003. 1 hit.
SSF56176. SSF56176. 1 hit.
TIGRFAMsi TIGR02963. xanthine_xdhA. 1 hit.
TIGR02965. xanthine_xdhB. 1 hit.
PROSITEi PS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51387. FAD_PCMH. 1 hit.
PS00559. MOLYBDOPTERIN_EUK. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The structure of chicken liver xanthine dehydrogenase. cDNA cloning and the domain structure."
    Satoh A., Amaya Y., Noda K., Nishino T.
    J. Biol. Chem. 270:2818-2826(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, CATALYTIC ACTIVITY.
    Tissue: Liver.
  2. "Subcellular localization of chicken liver xanthine dehydrogenase. A possible source of cytoplasmic reducing equivalents."
    Coolbear K.P., Herzberg G.R., Brosnan J.T.
    Biochem. J. 202:555-558(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, CATALYTIC ACTIVITY.

Entry informationi

Entry nameiXDH_CHICK
AccessioniPrimary (citable) accession number: P47990
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: November 26, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3