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O32144

- XDHD_BACSU

UniProt

O32144 - XDHD_BACSU

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Protein

Probable xanthine dehydrogenase subunit D

Gene

pucD

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli

Functioni

Oxidizes hypoxanthine and xanthine to uric acid.1 Publication

Catalytic activityi

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

Cofactori

Binds 1 molybdenum-molybdopterin (Mo-MPT) cofactor per subunit.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi204 – 2041MolybdenumSequence Analysis
Metal bindingi235 – 2351Molybdenum; via carbonyl oxygenSequence Analysis
Metal bindingi508 – 5081Molybdenum; via amide nitrogenSequence Analysis

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. xanthine dehydrogenase activity Source: UniProtKB-EC

GO - Biological processi

  1. hypoxanthine catabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Purine metabolism

Keywords - Ligandi

Metal-binding, Molybdenum, NAD

Enzyme and pathway databases

BioCyciBSUB:BSU32480-MONOMER.
UniPathwayiUPA00604; UER00661.
UPA00604; UER00662.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable xanthine dehydrogenase subunit D (EC:1.17.1.4)
Short name:
XDHase subunit D
Gene namesi
Name:pucD
Synonyms:yurC
Ordered Locus Names:BSU32480
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU32480. [Micado]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 745745Probable xanthine dehydrogenase subunit DPRO_0000166098Add
BLAST

Proteomic databases

PaxDbiO32144.

Expressioni

Inductioni

Expression is very low in excess nitrogen (glutamate plus ammonia) and is induced during limiting-nitrogen conditions (glutamate). Expression decreases when allantoin is added during limiting-nitrogen conditions.

Interactioni

Subunit structurei

Could be composed of four subunits: PucA, PucC, PucD and PucE.

Protein-protein interaction databases

STRINGi224308.BSU32480.

Structurei

3D structure databases

ProteinModelPortaliO32144.
SMRiO32144. Positions 2-740.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the xanthine dehydrogenase family.Curated

Phylogenomic databases

eggNOGiCOG1529.
HOGENOMiHOG000244715.
InParanoidiO32144.
KOiK00087.
OMAiDGNFRKK.
OrthoDBiEOG6ZSP3F.
PhylomeDBiO32144.

Family and domain databases

Gene3Di3.30.365.10. 6 hits.
3.90.1170.50. 1 hit.
InterProiIPR000674. Ald_Oxase/Xan_DH_a/b.
IPR008274. AldOxase/xan_DH_Mopterin-bd.
IPR017609. Xanthine_dehydrogenase_dsu.
[Graphical view]
PfamiPF01315. Ald_Xan_dh_C. 1 hit.
PF02738. Ald_Xan_dh_C2. 1 hit.
[Graphical view]
SMARTiSM01008. Ald_Xan_dh_C. 1 hit.
[Graphical view]
SUPFAMiSSF54665. SSF54665. 1 hit.
SSF56003. SSF56003. 1 hit.
TIGRFAMsiTIGR03196. pucD. 1 hit.

Sequencei

Sequence statusi: Complete.

O32144-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MIINKPSRVR PDGRGKVTGE LKYMTDLSFP GMLYGKVLRS AYPHAEIVSV
60 70 80 90 100
CTIKAEKMEG VQAVVTHKDV PGLNRFGIVI PDQPVLCEDR VRYVGDAIAA
110 120 130 140 150
VAAETEEIAE AALELIQVEY KELEVMDSPE KALRPNAQRL HEDGNILHRA
160 170 180 190 200
FFSNGDVEEG FQASDTVFEE TYELPRQMHT YMETEGGVAV PEDDGGFTMY
210 220 230 240 250
AGTQHGYKDR FQLARIFDIP EEKIRIVSSP MGGSFGGKDE LNIQPYAALL
260 270 280 290 300
ALKSGRPVKI HQTRKESVRS GIKRHPMKIT IKTGADHSGN LLAHDVKIVA
310 320 330 340 350
DTGAYATLGP AVLDFSVEHA AGPYRIPNIR TEGISVFTNN GVAGEFRGFG
360 370 380 390 400
GNQITFALET HLDRLSGMLG IDPLELRRKN IRKPHDLGPL EHRIAPTDGA
410 420 430 440 450
AQVLNAISKS PILKKTSRNC GYLQRGTGAA ITMHGGGLGF GRMDAAGGRL
460 470 480 490 500
SLSSEGKITA SFGFEECGQG ILAAIEQIVM EELGCAAEDI SIVIGDTAKV
510 520 530 540 550
PKSGSSTASR GTSMVWHAIQ RLKKPFLAQL KKRAAEWSGC SAENLIPGAA
560 570 580 590 600
GLRDKNTKAL VVTYKELAEK GPLAEETAFD FPTTPDPVVG GHFLYSFGAA
610 620 630 640 650
AVEVEVDLLT GDVKLIDCEH AIAAGPVVSP QGYRGQIEGG AAMALGYTLM
660 670 680 690 700
EEAKMTDGRY AAENLDHYLI PGIKDVPDMK LIAIEDLMKG DVYGPRGVGE
710 720 730 740
IGTIAITPAI VKAVHDAVGC WINKLPISRE ELLEAIDRKG LKQWT
Length:745
Mass (Da):80,434
Last modified:January 1, 1998 - v1
Checksum:iC4A3EC5F0094EF8D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL009126 Genomic DNA. Translation: CAB15238.1.
PIRiB70017.
RefSeqiNP_391128.1. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB15238; CAB15238; BSU32480.
GeneIDi936686.
KEGGibsu:BSU32480.
PATRICi18978470. VBIBacSub10457_3398.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL009126 Genomic DNA. Translation: CAB15238.1 .
PIRi B70017.
RefSeqi NP_391128.1. NC_000964.3.

3D structure databases

ProteinModelPortali O32144.
SMRi O32144. Positions 2-740.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224308.BSU32480.

Proteomic databases

PaxDbi O32144.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB15238 ; CAB15238 ; BSU32480 .
GeneIDi 936686.
KEGGi bsu:BSU32480.
PATRICi 18978470. VBIBacSub10457_3398.

Organism-specific databases

GenoListi BSU32480. [Micado ]

Phylogenomic databases

eggNOGi COG1529.
HOGENOMi HOG000244715.
InParanoidi O32144.
KOi K00087.
OMAi DGNFRKK.
OrthoDBi EOG6ZSP3F.
PhylomeDBi O32144.

Enzyme and pathway databases

UniPathwayi UPA00604 ; UER00661 .
UPA00604 ; UER00662 .
BioCyci BSUB:BSU32480-MONOMER.

Family and domain databases

Gene3Di 3.30.365.10. 6 hits.
3.90.1170.50. 1 hit.
InterProi IPR000674. Ald_Oxase/Xan_DH_a/b.
IPR008274. AldOxase/xan_DH_Mopterin-bd.
IPR017609. Xanthine_dehydrogenase_dsu.
[Graphical view ]
Pfami PF01315. Ald_Xan_dh_C. 1 hit.
PF02738. Ald_Xan_dh_C2. 1 hit.
[Graphical view ]
SMARTi SM01008. Ald_Xan_dh_C. 1 hit.
[Graphical view ]
SUPFAMi SSF54665. SSF54665. 1 hit.
SSF56003. SSF56003. 1 hit.
TIGRFAMsi TIGR03196. pucD. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  2. "Functional analysis of 14 genes that constitute the purine catabolic pathway in Bacillus subtilis and evidence for a novel regulon controlled by the PucR transcription activator."
    Schultz A.C., Nygaard P., Saxild H.H.
    J. Bacteriol. 183:3293-3302(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: 168.

Entry informationi

Entry nameiXDHD_BACSU
AccessioniPrimary (citable) accession number: O32144
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: January 1, 1998
Last modified: October 29, 2014
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3