ID   XDHC_BACSU              Reviewed;         277 AA.
AC   O32145;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   16-JUN-2009, entry version 57.
DE   RecName: Full=Probable xanthine dehydrogenase subunit C;
DE            Short=XDHase subunit C;
DE            EC=1.17.1.4;
GN   Name=pucC; Synonyms=yurD; OrderedLocusNames=BSU32490;
OS   Bacillus subtilis.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   MEDLINE=98044033; PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
RA   Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA   Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA   Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA   Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA   Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA   Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA   Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA   Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA   Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA   Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA   Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA   Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA   Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
RA   Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA   Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA   Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA   Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA   Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA   Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA   Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA   Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [2]
RP   FUNCTION.
RC   STRAIN=168;
RX   MEDLINE=21242727; PubMed=11344136;
RX   DOI=10.1128/JB.183.11.3293-3302.2001;
RA   Schultz A.C., Nygaard P., Saxild H.H.;
RT   "Functional analysis of 14 genes that constitute the purine catabolic
RT   pathway in Bacillus subtilis and evidence for a novel regulon
RT   controlled by the PucR transcription activator.";
RL   J. Bacteriol. 183:3293-3302(2001).
CC   -!- FUNCTION: Oxidizes hypoxanthine and xanthine to uric acid.
CC   -!- CATALYTIC ACTIVITY: Xanthine + NAD(+) + H(2)O = urate + NADH.
CC   -!- CATALYTIC ACTIVITY: Hypoxanthine + NAD(+) + H(2)O = xanthine +
CC       NADH.
CC   -!- COFACTOR: FAD (By similarity).
CC   -!- PATHWAY: Purine metabolism; hypoxanthine degradation; uric acid
CC       from hypoxanthine: step 1/2.
CC   -!- PATHWAY: Purine metabolism; hypoxanthine degradation; uric acid
CC       from hypoxanthine: step 2/2.
CC   -!- SUBUNIT: Could be composed of four subunits: pucA, pucC, pucD and
CC       pucE.
CC   -!- INDUCTION: Expression is very low in excess nitrogen (glutamate
CC       plus ammonia) and is induced during limiting-nitrogen conditions
CC       (glutamate). Expression decreases when allantoin is added during
CC       limiting-nitrogen conditions.
CC   -!- SIMILARITY: Contains 1 FAD-binding PCMH-type domain.
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DR   EMBL; AL009126; CAB15239.1; -; Genomic_DNA.
DR   PIR; C70017; C70017.
DR   RefSeq; NP_391129.1; -.
DR   GeneID; 936685; -.
DR   GenomeReviews; AL009126_GR; BSU32490.
DR   KEGG; bsu:BSU32490; -.
DR   NMPDR; fig|224308.1.peg.3255; -.
DR   SubtiList; BG13990; pucC.
DR   HOGENOM; O32145; -.
DR   OMA; O32145; LEGIDEM.
DR   BioCyc; BSUB224308:BSU3246-MON; -.
DR   BRENDA; 1.17.1.4; 150.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0050660; F:FAD binding; IEA:InterPro.
DR   GO; GO:0004854; F:xanthine dehydrogenase activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006144; P:purine base metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR016169; CO_DH_flavot_FAD-bd_sub2.
DR   InterPro; IPR016166; FAD-bd_2.
DR   InterPro; IPR002346; Mopterin_DH_FAD-bd.
DR   InterPro; IPR017612; Xanthine_dehydrogenase_csu.
DR   Gene3D; G3DSA:3.30.465.10; CO_DH_flavoprot_FAD-bd_sub2; 1.
DR   Pfam; PF00941; FAD_binding_5; 1.
DR   TIGRFAMs; TIGR03199; pucC; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; FAD; Flavoprotein; NAD; Oxidoreductase;
KW   Purine metabolism.
FT   CHAIN         1    277       Probable xanthine dehydrogenase subunit
FT                                C.
FT                                /FTId=PRO_0000166099.
FT   DOMAIN        7    176       FAD-binding PCMH-type.
SQ   SEQUENCE   277 AA;  30119 MW;  25D8C75D6D237961 CRC64;
     MNGQVTKARM NIQLWRPAAL DEAYSLLEKL APDVCAASGS TLLQLQWDKG TLPKQHLVSL
     EGIDEMRGIS TSDTHVSIGG LTSLNECRKN PLIKRALSCF SDAASAVAAP GIRSRATIGG
     NIASKIGDFI PLLLVLGAEL IVYQKELIRL PLGAWLSEED FRTAIVTRVI IPRAEGERVF
     YHKLGRRQAF TGAAAVAAGR FLKDGSIRLA AGHADITPRR LLDSEAKWMA PGWDPHELYK
     TLIHELPFSS DVFMSAAYRK KAAANVIMAE LMAEGGE
//