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Q12553

- XDH_EMENI

UniProt

Q12553 - XDH_EMENI

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Protein

Xanthine dehydrogenase

Gene

hxA

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli

Functioni

Key enzyme in purine degradation. Catalyzes the oxidation of hypoxanthine to xanthine. Catalyzes the oxidation of xanthine to uric acid (By similarity).By similarity

Catalytic activityi

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

Cofactori

Binds 2 2Fe-2S clusters.By similarity
FAD.By similarity
Binds 1 molybdenum-molybdopterin (Mo-MPT) cofactor per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi73 – 731Iron-sulfur 1By similarity
Metal bindingi78 – 781Iron-sulfur 1By similarity
Metal bindingi81 – 811Iron-sulfur 1By similarity
Metal bindingi103 – 1031Iron-sulfur 1By similarity
Metal bindingi142 – 1421Iron-sulfur 2By similarity
Metal bindingi145 – 1451Iron-sulfur 2By similarity
Metal bindingi177 – 1771Iron-sulfur 2By similarity
Metal bindingi179 – 1791Iron-sulfur 2By similarity
Binding sitei374 – 3741FADBy similarity
Binding sitei397 – 3971FADBy similarity
Binding sitei459 – 4591FADBy similarity
Metal bindingi798 – 7981MolybdenumBy similarity
Metal bindingi829 – 8291Molybdenum; via carbonyl oxygenBy similarity
Binding sitei833 – 8331SubstrateBy similarity
Binding sitei911 – 9111SubstrateBy similarity
Metal bindingi943 – 9431Molybdenum; via amide nitrogenBy similarity
Binding sitei945 – 9451SubstrateBy similarity
Binding sitei1041 – 10411Substrate; via amide nitrogenBy similarity
Metal bindingi1110 – 11101Molybdenum; via amide nitrogenBy similarity
Active sitei1295 – 12951Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi294 – 3018FADBy similarity
Nucleotide bindingi384 – 3885FADBy 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. molybdopterin cofactor binding Source: UniProtKB
  6. UDP-N-acetylmuramate dehydrogenase activity Source: InterPro
  7. xanthine dehydrogenase activity Source: UniProtKB
  8. xanthine oxidase activity Source: InterPro

GO - Biological processi

  1. purine nucleobase catabolic process Source: ASPGD
  2. 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

Names & Taxonomyi

Protein namesi
Recommended name:
Xanthine dehydrogenase (EC:1.17.1.4)
Alternative name(s):
Purine hydroxylase I
Gene namesi
Name:hxA
ORF Names:AN5613
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000000560: Chromosome V

Subcellular locationi

Peroxisome By similarity

GO - Cellular componenti

  1. peroxisome Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13631363Xanthine dehydrogenasePRO_0000166087Add
BLAST

Expressioni

Inductioni

By 2-thiouric acid. Repressed by ammonium.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi162425.CADANIAP00003457.

Structurei

3D structure databases

ProteinModelPortaliQ12553.
SMRiQ12553. Positions 35-193.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini35 – 121872Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST
Domaini266 – 450185FAD-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.
InParanoidiQ12553.
KOiK00106.
OMAiCDETFFA.
OrthoDBiEOG76X67F.

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.
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. 1 hit.
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.
PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51387. FAD_PCMH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q12553 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAPGVLLQPS QSELEAASPP KAAASLLQLT EEWDDTIRFY LNGTKVILDS
60 70 80 90 100
VDPEITLLEY LRGIGLTGTK LGCAEGGCGA CTVVVSQINP TTKKLYHASI
110 120 130 140 150
NACIAPLVAV DGKHVITVEG IGNVKNPHAI QQRLAIGNGS QCGFCTPGIV
160 170 180 190 200
MSLYALLRND PKPSEHAVEE AFDGNLCRCT GYRPILDAAQ SFTSPIGCGK
210 220 230 240 250
ARANGGSGCC MEEQKGTNGC CKGSSEETTE DVKHKFASPD FIEYKPDTEL
260 270 280 290 300
IFPPSLWKHE LRPLAFGNKR KKWYRPVTVQ QLLEIKSIHP DAKLIGGSTE
310 320 330 340 350
TQIEIKFKQM RYGASVYLGD LAELRQFAFH DNYLEIGANI SLTDLESVCD
360 370 380 390 400
QAIERYGSAR GQPFAAIKKQ LRYFAGRQIR NVASPAGNLA TASPISDLNP
410 420 430 440 450
VFVATNTTLV ARSLDKETEI PMTQFFRGYR STALPPDAII SSLRIPTASE
460 470 480 490 500
KGEYLRAYKQ SKRKDDDIAI VNAALRVSLS SSNDVTSVSL VFGGMAPLTV
510 520 530 540 550
SARNAEAFLT GKKFTDPATL EGTMGALEQD FNLKFGVPGG MATYRKSLAL
560 570 580 590 600
GFFYRFYHDV LSQIEARSSD LDNSVVAEIE RAISTGEKDN EASAAYQQRV
610 620 630 640 650
LGRAGPHLSA LKQATGEAQY TDDIPAQKNE LYGCMVLSTK AHAKLLSVNT
660 670 680 690 700
EAALEIPGVI DYVDHKDLPS PRANWWGAPN CDEVFFAVDK VTTAGQPIGM
710 720 730 740 750
ILANTAKAAE EGARAVKVEY EELPVILSIE EAIEAQSFFE RFRYIKNGDP
760 770 780 790 800
ESAFRDADHV FEGVSRMGGQ EHFYLETQAC VAIPKAEDGE MEIWSSTQNP
810 820 830 840 850
TETQSYVAQV TGVAANKIVS RVKRLGGGFG GKETRSVQLA GICATAAAKV
860 870 880 890 900
RRPVRCMLNR DEDIATSGQR HPFYCKWKVG VTREGKLLAL DADVYANGGH
910 920 930 940 950
TQDLSGAVVE RSLSHIDNVY RFPNIYVRGR ICKTNTVSNT AFRGFGGPQG
960 970 980 990 1000
LFFAESIISE VADHLDLQVE QLRILNMYEP GDMTHFNQEL KDWHVPLMYD
1010 1020 1030 1040 1050
QVLQESEYFE RRKAVEEYNR THKWSKRGMA IIPTKFGISF TALFLNQAGA
1060 1070 1080 1090 1100
LVHIYHDGSV LVAHGGVEMG QGLHTKMTMI AAEALGVPLS DVFISETATN
1110 1120 1130 1140 1150
TVANTSSTAA SASSDLNGYA IYNACTQLNE RLKPYREKMP NATLKDLAHA
1160 1170 1180 1190 1200
AYFDRVNLSA QGYYRTPDIG YTWGENKGQM FFYFTQGVTA AEVEIDTLTG
1210 1220 1230 1240 1250
DWTPLRADIK MDVGRTINPS IDYGQIEGAY IQGQGLFTTE ESLWHRTTGQ
1260 1270 1280 1290 1300
IFTKGPGNYK IPGFRDIPQI FNVSLLKDVE WENLRTIQRS RGVGEPPLFM
1310 1320 1330 1340 1350
GSAAFFAIRD ALKAARKEWG VTDVLSLVSP ATPERIRVSC ADPIIERARV
1360
KAEEGEKSFF VAI
Length:1,363
Mass (Da):149,523
Last modified:May 1, 2007 - v2
Checksum:i18D8F50B731EDE4B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti741 – 7411R → H in CAA58034. (PubMed:7876088)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X82827 Genomic DNA. Translation: CAA58034.1.
AACD01000098 Genomic DNA. Translation: EAA62706.1.
BN001305 Genomic DNA. Translation: CBF81549.1.
PIRiA55875.
RefSeqiXP_663217.1. XM_658125.1.

Genome annotation databases

EnsemblFungiiCADANIAT00003457; CADANIAP00003457; CADANIAG00003457.
GeneIDi2871900.
KEGGiani:AN5613.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X82827 Genomic DNA. Translation: CAA58034.1 .
AACD01000098 Genomic DNA. Translation: EAA62706.1 .
BN001305 Genomic DNA. Translation: CBF81549.1 .
PIRi A55875.
RefSeqi XP_663217.1. XM_658125.1.

3D structure databases

ProteinModelPortali Q12553.
SMRi Q12553. Positions 35-193.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 162425.CADANIAP00003457.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADANIAT00003457 ; CADANIAP00003457 ; CADANIAG00003457 .
GeneIDi 2871900.
KEGGi ani:AN5613.2.

Phylogenomic databases

eggNOGi COG4630.
HOGENOMi HOG000191197.
InParanoidi Q12553.
KOi K00106.
OMAi CDETFFA.
OrthoDBi EOG76X67F.

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.
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. 1 hit.
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.
PROSITEi PS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51387. FAD_PCMH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and molecular characterization of hxA, the gene coding for the xanthine dehydrogenase (purine hydroxylase I) of Aspergillus nidulans."
    Glatigny A., Scazzocchio C.
    J. Biol. Chem. 270:3534-3550(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION.
    Strain: biA1.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  3. "The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
    Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G.
    , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
    Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENOME REANNOTATION.
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Entry informationi

Entry nameiXDH_EMENI
AccessioniPrimary (citable) accession number: Q12553
Secondary accession number(s): C8VFY5, Q5B1G7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 1, 2007
Last modified: October 29, 2014
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3