Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O32145

- XDHC_BACSU

UniProt

O32145 - XDHC_BACSU

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Probable xanthine dehydrogenase subunit C

Gene

pucC

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

FADBy similarity

Pathwayi

GO - Molecular functioni

  1. flavin adenine dinucleotide binding Source: InterPro
  2. oxidoreductase activity, acting on CH-OH group of donors Source: InterPro
  3. 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

FAD, Flavoprotein, NAD

Enzyme and pathway databases

BioCyciBSUB:BSU32490-MONOMER.
UniPathwayiUPA00604; UER00661.
UPA00604; UER00662.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable xanthine dehydrogenase subunit C (EC:1.17.1.4)
Short name:
XDHase subunit C
Gene namesi
Name:pucC
Synonyms:yurD
Ordered Locus Names:BSU32490
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU32490. [Micado]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 277277Probable xanthine dehydrogenase subunit CPRO_0000166099Add
BLAST

Proteomic databases

PaxDbiO32145.

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.BSU32490.

Structurei

3D structure databases

ProteinModelPortaliO32145.
SMRiO32145. Positions 11-276.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 176170FAD-binding PCMH-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 FAD-binding PCMH-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG1319.
HOGENOMiHOG000154870.
InParanoidiO32145.
KOiK00087.
OMAiKARMNIQ.
OrthoDBiEOG686NMM.
PhylomeDBiO32145.

Family and domain databases

Gene3Di3.30.465.10. 1 hit.
InterProiIPR005107. CO_DH_flav_C.
IPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016166. FAD-bd_2.
IPR002346. Mopterin_DH_FAD-bd.
IPR017612. Xanthine_dehydrogenase_csu.
[Graphical view]
PfamiPF00941. FAD_binding_5. 1 hit.
[Graphical view]
SUPFAMiSSF55447. SSF55447. 1 hit.
SSF56176. SSF56176. 1 hit.
TIGRFAMsiTIGR03199. pucC. 1 hit.
PROSITEiPS51387. FAD_PCMH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O32145-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNGQVTKARM NIQLWRPAAL DEAYSLLEKL APDVCAASGS TLLQLQWDKG
60 70 80 90 100
TLPKQHLVSL EGIDEMRGIS TSDTHVSIGG LTSLNECRKN PLIKRALSCF
110 120 130 140 150
SDAASAVAAP GIRSRATIGG NIASKIGDFI PLLLVLGAEL IVYQKELIRL
160 170 180 190 200
PLGAWLSEED FRTAIVTRVI IPRAEGERVF YHKLGRRQAF TGAAAVAAGR
210 220 230 240 250
FLKDGSIRLA AGHADITPRR LLDSEAKWMA PGWDPHELYK TLIHELPFSS
260 270
DVFMSAAYRK KAAANVIMAE LMAEGGE
Length:277
Mass (Da):30,119
Last modified:January 1, 1998 - v1
Checksum:i25D8C75D6D237961
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB15239.1.
PIRiC70017.
RefSeqiNP_391129.1. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB15239; CAB15239; BSU32490.
GeneIDi936685.
KEGGibsu:BSU32490.
PATRICi18978472. VBIBacSub10457_3399.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB15239.1 .
PIRi C70017.
RefSeqi NP_391129.1. NC_000964.3.

3D structure databases

ProteinModelPortali O32145.
SMRi O32145. Positions 11-276.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224308.BSU32490.

Proteomic databases

PaxDbi O32145.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB15239 ; CAB15239 ; BSU32490 .
GeneIDi 936685.
KEGGi bsu:BSU32490.
PATRICi 18978472. VBIBacSub10457_3399.

Organism-specific databases

GenoListi BSU32490. [Micado ]

Phylogenomic databases

eggNOGi COG1319.
HOGENOMi HOG000154870.
InParanoidi O32145.
KOi K00087.
OMAi KARMNIQ.
OrthoDBi EOG686NMM.
PhylomeDBi O32145.

Enzyme and pathway databases

UniPathwayi UPA00604 ; UER00661 .
UPA00604 ; UER00662 .
BioCyci BSUB:BSU32490-MONOMER.

Family and domain databases

Gene3Di 3.30.465.10. 1 hit.
InterProi IPR005107. CO_DH_flav_C.
IPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016166. FAD-bd_2.
IPR002346. Mopterin_DH_FAD-bd.
IPR017612. Xanthine_dehydrogenase_csu.
[Graphical view ]
Pfami PF00941. FAD_binding_5. 1 hit.
[Graphical view ]
SUPFAMi SSF55447. SSF55447. 1 hit.
SSF56176. SSF56176. 1 hit.
TIGRFAMsi TIGR03199. pucC. 1 hit.
PROSITEi PS51387. FAD_PCMH. 1 hit.
[Graphical view ]
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 nameiXDHC_BACSU
AccessioniPrimary (citable) accession number: O32145
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: January 1, 1998
Last modified: November 26, 2014
This is version 97 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