Reviewed, UniProtKB/Swiss-Prot Q9MYW6 (XDH_FELCA)

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

Felis silvestris catus (Cat)

Taxonomic identifier

9685 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Feliformia › Felidae › Felinae › Felis

Protein attributes

Sequence length	1331 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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 By similarity.
Catalytic activity	Xanthine + NAD+ + H2O = urate + NADH. Hypoxanthine + NAD+ + H2O = xanthine + NADH. Xanthine + H2O + O2 = urate + H2O2.
Cofactor	Binds 2 2Fe-2S clusters By similarity. FAD By similarity. Molybdopterin By similarity.
Subunit structure	Homodimer. Interacts with BTN1A1 By similarity.
Subcellular location	Peroxisome By similarity.
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
PTM	Glycoprotein Phosphoprotein
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
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 1331	1330	Xanthine dehydrogenase/oxidase		PRO_0000246176
Regions
	Domain	4 – 91	88	2Fe-2S ferredoxin-type
	Domain	229 – 412	184	FAD-binding PCMH-type
Sites
	Metal binding	43	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	48	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	51	1	Iron-sulfur (2Fe-2S) By similarity
Amino acid modifications
	Modified residue	222	1	Phosphothreonine By similarity
	Glycosylation	1072	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q9MYW6-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 726C4F72C3B5FB09	FASTA	1,331	146,122
	10 20 30 40 50 60 MTADELVFFV NGKKVVEKNA DPETTLLAYL RRKLGLSGTK LGCGEGGCGA CTVMLSKYDR 70 80 90 100 110 120 FQNKIVHFSA NACLAPICSL HHVAVTTVEG IGSTKSRLHP VQERIAKSHG SQCGFCTPGI 130 140 150 160 170 180 VMSMYTLLRN QPEPTIEEIE DAFQGNLCRC TGYRPILQGF RTFARDGGCC GGSGNDLNCC 190 200 210 220 230 240 MNQKTDHKIT LSPSLFNPEE FTPLDPTQEP IFPPELLRLK DTPQKQLRFE GERVTWIQAS 250 260 270 280 290 300 TLQELLDLKA QDPEAKLVVG NTEIGIEMKF KNMLFPKMVC PAWIPEPVEH GPEGISFGAS 310 320 330 340 350 360 CPLSLVEKTL LDAVANLPAH QTEVFKGVLE QLRWFAGKQV KSVASIGGNI ITASPISDLN 370 380 390 400 410 420 PVFMASGAKL TIVSTGTRRT VRMDHTFFPA YRKTLLAPEE ILLSIEIPYS REGEYFSAFK 430 440 450 460 470 480 QASRREDDIA KVTSGMRVLF NPGTAQVKEL ALCYGGMHDR TVSALQTTRK QISNFWNEEL 490 500 510 520 530 540 LQNVCAGLAE ELSLAPDAPG GMVEFRRTLT LSFFFKFYLT VLQKLGIQNS KDKCGKLDPT 550 560 570 580 590 600 HASATLLFQK DPPANVQLFQ EVPKGQCEED MVGRPLPHLA AAMQASGEAV YCDDIPRYEN 610 620 630 640 650 660 ELSLRLVTST RAHAKIKSID TSEAQKVPGF VCFISADDVP GSNITGIGND EMVFAKDKVT 670 680 690 700 710 720 CIGHIIGAVV TDTREHAQRA AQAVRITYED LPAIITIEDA IAKDSFYEPE LKIEKGNLTK 730 740 750 760 770 780 GFSEADNIVS GELYIGGQEH FYLETHCTIA VPKGEAGEME LFVSTQNTTK TQSFVANMLG 790 800 810 820 830 840 VPANRILVRV KRMGGGFGGK ETRSTVVSTA VPLAAYKTGR PVRCMLDRDE DMLITGGRHP 850 860 870 880 890 900 FLARYKVGFM KTGRVVALKV EHYSNAGNTL DLSQSIMERA LFHMDNCYNI PNIRGTGRIC 910 920 930 940 950 960 KTNLPSNTAF RGFGGPQGML IAEHWMSEVA VTCGLPAEEV RRKNMYKEGD LTHFNQKLEG 970 980 990 1000 1010 1020 FTLPRCWEEC LASSQYHARK READKFNEEN CWKKRGLSII PTKFGISFTV PFLNQAGALV 1030 1040 1050 1060 1070 1080 HVYTDGSVLL THGGTEMGQG LHTKMVQVAS RALKIPTSKI YISETSTNTV PNTSPTAASV 1090 1100 1110 1120 1130 1140 STDINGQAVY EACQTILKRL EPFKKKNPSG SWEDWVTAAY LDAVSLSATG FYKTPNIGYS 1150 1160 1170 1180 1190 1200 FETNSGNPFH YFSYGVACSE VEIDCLTGDH KNLRTDIVMD VGSSLNPAID IGQVEGAFVQ 1210 1220 1230 1240 1250 1260 GLGLFTLEEL HYSPEGSLHT RGPSTYKIPA FGSIPSEFRV SLLRDCPNKK AIYASKAVGE 1270 1280 1290 1300 1310 1320 PPLFLAASIF FAIKDAICAA RAGNPDCKTK KLFQLNSPAT PEKIRNACVD QFTRLCVTGT 1330 AESCKPWSVR V

References

[1]	"Molecular cloning of a cDNA coding for feline liver xanthine dehydrogenase." Tsuchida S., Yamada R., Ikemoto S., Tagawa M. J. Vet. Med. Sci. 63:353-355(2001) [PubMed: 11307944] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF286379 mRNA. Translation: AAF97949.1.
RefSeq	NP_001009217.1.
3D structure databases
HSSP	HSSP built from PDB template 1FIQ based on UniProtKB P80457.
SMR	Q9MYW6. Positions 2-1330, 3-1331.
ModBase	Search...
Genome annotation databases
GeneID	493692.
Phylogenomic databases
HOVERGEN	Q9MYW6.
Enzyme and pathway databases
BRENDA	1.17.1.4. 273949. 1.17.3.2. 273949.
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. 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:3.10.20.30. 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_FELCA

Accession

Primary (citable) accession number: Q9MYW6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 25, 2006
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 44 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)