ID   XDHD_BACSU              Reviewed;         745 AA.
AC   O32144;
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 D;
DE            Short=XDHase subunit D;
DE            EC=1.17.1.4;
GN   Name=pucD; Synonyms=yurC; OrderedLocusNames=BSU32480;
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: Molybdopterin (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: Belongs to the xanthine dehydrogenase family.
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DR   EMBL; AL009126; CAB15238.1; -; Genomic_DNA.
DR   PIR; B70017; B70017.
DR   RefSeq; NP_391128.1; -.
DR   GeneID; 936686; -.
DR   GenomeReviews; AL009126_GR; BSU32480.
DR   KEGG; bsu:BSU32480; -.
DR   NMPDR; fig|224308.1.peg.3254; -.
DR   SubtiList; BG13989; pucD.
DR   HOGENOM; O32144; -.
DR   OMA; O32144; RFQLARI.
DR   BioCyc; BSUB224308:BSU3245-MON; -.
DR   BRENDA; 1.17.1.4; 150.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0030151; F:molybdenum ion binding; IEA:UniProtKB-KW.
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; IPR000674; Ald_Oxase/Xan_DH_a/b.
DR   InterPro; IPR008274; AldOxase/xan_DH_Mopterin-bd.
DR   InterPro; IPR017609; Xanthine_dehydrogenase_dsu.
DR   Gene3D; G3DSA:3.30.365.10; Ald_xan_DH_mo_bd; 2.
DR   Gene3D; G3DSA:3.90.1170.50; Aldxan_DH_hamm; 1.
DR   Pfam; PF01315; Ald_Xan_dh_C; 1.
DR   Pfam; PF02738; Ald_Xan_dh_C2; 1.
DR   TIGRFAMs; TIGR03196; pucD; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Molybdenum; NAD; Oxidoreductase; Purine metabolism.
FT   CHAIN         1    745       Probable xanthine dehydrogenase subunit
FT                                D.
FT                                /FTId=PRO_0000166098.
SQ   SEQUENCE   745 AA;  80434 MW;  C4A3EC5F0094EF8D CRC64;
     MIINKPSRVR PDGRGKVTGE LKYMTDLSFP GMLYGKVLRS AYPHAEIVSV CTIKAEKMEG
     VQAVVTHKDV PGLNRFGIVI PDQPVLCEDR VRYVGDAIAA VAAETEEIAE AALELIQVEY
     KELEVMDSPE KALRPNAQRL HEDGNILHRA FFSNGDVEEG FQASDTVFEE TYELPRQMHT
     YMETEGGVAV PEDDGGFTMY AGTQHGYKDR FQLARIFDIP EEKIRIVSSP MGGSFGGKDE
     LNIQPYAALL ALKSGRPVKI HQTRKESVRS GIKRHPMKIT IKTGADHSGN LLAHDVKIVA
     DTGAYATLGP AVLDFSVEHA AGPYRIPNIR TEGISVFTNN GVAGEFRGFG GNQITFALET
     HLDRLSGMLG IDPLELRRKN IRKPHDLGPL EHRIAPTDGA AQVLNAISKS PILKKTSRNC
     GYLQRGTGAA ITMHGGGLGF GRMDAAGGRL SLSSEGKITA SFGFEECGQG ILAAIEQIVM
     EELGCAAEDI SIVIGDTAKV PKSGSSTASR GTSMVWHAIQ RLKKPFLAQL KKRAAEWSGC
     SAENLIPGAA GLRDKNTKAL VVTYKELAEK GPLAEETAFD FPTTPDPVVG GHFLYSFGAA
     AVEVEVDLLT GDVKLIDCEH AIAAGPVVSP QGYRGQIEGG AAMALGYTLM EEAKMTDGRY
     AAENLDHYLI PGIKDVPDMK LIAIEDLMKG DVYGPRGVGE IGTIAITPAI VKAVHDAVGC
     WINKLPISRE ELLEAIDRKG LKQWT
//