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Protein

Probable xanthine dehydrogenase subunit D

Gene

pucD

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: 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

Mo-molybdopterinBy similarityNote: Binds 1 Mo-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

GO - Biological processi

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 Componenti: 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.
OMAiVWEAMQM.
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:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB15238.1.
PIRiB70017.
RefSeqiNP_391128.1. NC_000964.3.
WP_003243174.1. NZ_JNCM01000033.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB15238.1.
PIRiB70017.
RefSeqiNP_391128.1. NC_000964.3.
WP_003243174.1. NZ_JNCM01000033.1.

3D structure databases

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

Protein-protein interaction databases

STRINGi224308.BSU32480.

Proteomic databases

PaxDbiO32144.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

GenoListiBSU32480. [Micado]

Phylogenomic databases

eggNOGiCOG1529.
HOGENOMiHOG000244715.
InParanoidiO32144.
KOiK00087.
OMAiVWEAMQM.
OrthoDBiEOG6ZSP3F.
PhylomeDBiO32144.

Enzyme and pathway databases

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

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.
ProtoNetiSearch...

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: May 27, 2015
This is version 99 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.