Reviewed, UniProtKB/Swiss-Prot P47990 (XDH_CHICK)

Names and origin

Protein names

Recommended name:
    Xanthine dehydrogenase/oxidase
Including the following 2 domains:
    1- Recommended name:
            Xanthine dehydrogenase
                Short name=XD
              EC=1.17.1.4
    2- Recommended name:
            Xanthine oxidase
                Short name=XO
              EC=1.17.3.2
        Alternative name(s):
            Xanthine oxidoreductase

Gene names

Name:

XDH

Organism

Gallus gallus (Chicken)

Taxonomic identifier

9031 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length	1358 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	This enzyme can be converted from the dehydrogenase form (D) to the oxidase form (O) irreversibly by proteolysis or reversibly through the oxidation of sulfhydryl groups.
Catalytic activity	Xanthine + NAD+ + H2O = urate + NADH. Hypoxanthine + NAD+ + H2O = xanthine + NADH. Xanthine + H2O + O2 = urate + H2O2.
Cofactor	Binds 2 2Fe-2S clusters. FAD. Molybdopterin.
Subunit structure	Homodimer.
Subcellular location	Peroxisome.
Sequence similarities	Belongs to the xanthine dehydrogenase family. Contains 1 2Fe-2S ferredoxin-type domain. Contains 1 FAD-binding PCMH-type domain.

Ontologies

Keywords
Cellular component	Peroxisome
Ligand	2Fe-2S FAD Flavoprotein Iron Iron-sulfur Metal-binding Molybdenum NAD
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	peroxisome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW FAD binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW molybdenum ion binding Inferred from electronic annotation. Source: UniProtKB-KW xanthine dehydrogenase activity Inferred from electronic annotation. Source: EC xanthine oxidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1358	1358	Xanthine dehydrogenase/oxidase		PRO_0000166083
Regions
	Domain	8 – 95	88	2Fe-2S ferredoxin-type
	Domain	255 – 440	186	FAD-binding PCMH-type
Sites
	Metal binding	41	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	47	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	52	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	55	1	Iron-sulfur (2Fe-2S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	P47990-1 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: 53B049B38704995F	FASTA	1,358	149,614
	10 20 30 40 50 60 MAPPETGDEL VFFVNGKKVV EKDVDPETTL LTYLRRKLGL CGTKLGCGEG GCGACTVMIS 70 80 90 100 110 120 KYDPFQKKIL HHTANACLFP ICALHHVAVT TVEGIGNTKS RLHPAQERIA KSHGSQCGFC 130 140 150 160 170 180 TPGIVMSMYT LLRNKPKPKM EDIEDAFQGN LCRCTGYRPI LEGYRTFAVD SNCCGKAANG 190 200 210 220 230 240 TGCCHSKGEN SMNGGCCGGK ANGPGCCMNE KENVTMMSSS LFDSSEFQPL DPTQEPIFPP 250 260 270 280 290 300 ELMTQRNKEQ KQVCFKGERV MWIQPTTLQE LVALKSQYPN AKLVVGNTEV GIEMRLKNML 310 320 330 340 350 360 YPVILAPAWI PEMNAVQQTE TGITFGAACT LSSVEEVLRK AVAELPSYKT EIFQAALEQL 370 380 390 400 410 420 RWFAGPQIRN VAALGGNIMT ASPISDLNPV LMASGSKLTL ISMEGKRTVM MDEKFFTGYR 430 440 450 460 470 480 KTIVKPEEVL LSVEIPYSKE GEYFSAFKQA YRREDDIAIV TCGMRVLFQH GTSRVQEVKL 490 500 510 520 530 540 SYGGMAPTTI LALKTCRELA GRDWNEKLLQ DACRLLAGEM DLSPSAPGGM VEFRRTLTLS 550 560 570 580 590 600 FFFKFYLTVL QKLSKDQNGP NNLCEPVPPN YISATELFHK DPIASTQLFQ EVPRGQLVED 610 620 630 640 650 660 TVGRPLVHLS AAKQACGEAV YCDDIPHYEN ELYLTLVTST QAHAKILSID ASEAQSVPGF 670 680 690 700 710 720 VCFVSAKDVP GSNITGIAND ETVFAEDVVT CVGHIIGAVI ADTQEHSRRA AKAVKIKYEE 730 740 750 760 770 780 LKPIVTIQEA IEQQSFIKPI KRIKKGDVNK GFEESDHILE GEMHIGGQEH FYLETHCTLA 790 800 810 820 830 840 VPKGEDGEME LFVSTQNLMK TQEFTASALG VPSNRIVVRV KRMGGGFGGK ETRNTILTTV 850 860 870 880 890 900 VAVAAFKTGR PVRCMLDRDE DMLISGGRHP FLGRYKVGFM KNGKIKSLEV SYYSNGGNSA 910 920 930 940 950 960 DLSHGVMDRA LLHLDNSYNI PNVSIMGFIC KTNLSSNTAF RGFGGPQGMM IAECWMSDLA 970 980 990 1000 1010 1020 RKCGLPPEEV RKINLYHEGD LTHFNQKLEG FTLRRCWDEC LSSSNYHARK KLIEEFNKQN 1030 1040 1050 1060 1070 1080 RWKKRGMCII PTKFGISFTV PFLNQAGALV HVYTDGSVLL THGGTEMGQG LHTKMIQVAS 1090 1100 1110 1120 1130 1140 RSLGIPTSKI YISETSTNTV PNTSPTAASV SADINGMAVH NACQTILKRL EPIKQSNLKG 1150 1160 1170 1180 1190 1200 SWEDWIKTAY ENCISLSATG FYRIPDVGYN FETNKGKPFH YFSYGVACSE VEIDCLTGDH 1210 1220 1230 1240 1250 1260 KNIRTDIVMD VGTSLNPAID IGQIEGAFVQ GIGLFTMEEL RYSPEGNLYT RGPGMYKIPA 1270 1280 1290 1300 1310 1320 FGDIPTEFYV SLLRDCPNSK AIYSSKAVGE PPLFLSASVF YAIKDAIYSA REDSGVTEPF 1330 1340 1350 RLDSPATPER IRNACVDTFT KMCPSAEPGT FKPWSVRA

References

[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: 7852355] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D13221 mRNA. Translation: BAA02502.1.
IPI	IPI00589946.
PIR	XOCHDH. A55711.
RefSeq	NP_990458.1.
UniGene	Gga.43173
3D structure databases
HSSP	HSSP built from PDB template 1FO4 based on UniProtKB P80457.
SMR	P47990. Positions 7-1357.
ModBase	Search...
Genome annotation databases
Ensembl	ENSGALG00000008701. Gallus gallus. [Contig view]
GeneID	396025.
KEGG	gga:396025.
Phylogenomic databases
HOGENOM	P47990.
HOVERGEN	P47990.
Enzyme and pathway databases
BRENDA	1.17.1.4. 4. 1.17.3.2. 4.
Family and domain databases
InterPro	IPR002888. 2Fe-2S_bd. IPR006058. 2Fe2S_fd_BS. IPR000674. Ald_Oxase/Xan_DH_a/b. IPR016208. Ald_Oxase/xanthine_DH. IPR008274. AldOxase/xan_DH_Mopterin-bd. IPR012675. b-grasp_ferredoxin-like. IPR005107. CO_DH_flav_C. IPR016169. CO_DH_flavot_FAD-bd_sub2. IPR016166. FAD-bd_2. IPR016167. FAD-bd_2_sub1. IPR001041. Ferredoxin. IPR002346. Mopterin_DH_FAD-bd. IPR000572. OxRdtase_Mopterin-bd. IPR014309. Xanthine_DH_Mopterin-bd_su. IPR014307. Xanthine_DH_ssu. [Graphical view]
Gene3D	G3DSA:3.30.365.10. Ald_xan_DH_mo_bd. 2 hits. G3DSA:3.90.1170.50. Aldxan_DH_hamm. 1 hit. G3DSA:3.30.390.50. CO_DH_flav_C. 1 hit. G3DSA:3.30.465.10. CO_DH_flavoprot_FAD-bd_sub2. 1 hit. G3DSA:3.30.43.10. FAD-binding_2_sub1. 1 hit. G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit.
Pfam	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]
PIRSF	PIRSF000127. Xanthine_DH. 1 hit.
ProDom	PD186071. 2Fe-2S_bind. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR02963. xanthine_xdhA. 1 hit. TIGR02965. xanthine_xdhB. 1 hit.
PROSITE	PS00197. 2FE2S_FER_1. 1 hit. PS51085. 2FE2S_FER_2. 1 hit. PS51387. FAD_PCMH. 1 hit. PS00559. MOLYBDOPTERIN_EUK. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

XDH_CHICK

Accession

Primary (citable) accession number: P47990

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	June 16, 2009
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)