ID   XDHA_BACSU              Reviewed;         330 AA.
AC   O32147;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   16-JUN-2009, entry version 49.
DE   RecName: Full=Probable xanthine dehydrogenase subunit A;
DE            Short=XDHase subunit A;
DE            EC=1.17.1.4;
GN   Name=pucA; Synonyms=yurF; OrderedLocusNames=BSU32510;
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. PucA
CC       subunit could exert a molybdenum cofactor recruiting function.
CC   -!- CATALYTIC ACTIVITY: Xanthine + NAD(+) + H(2)O = urate + NADH.
CC   -!- CATALYTIC ACTIVITY: Hypoxanthine + NAD(+) + H(2)O = xanthine +
CC       NADH.
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.
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DR   EMBL; AL009126; CAB15241.1; -; Genomic_DNA.
DR   PIR; E70017; E70017.
DR   RefSeq; NP_391131.1; -.
DR   GeneID; 938865; -.
DR   GenomeReviews; AL009126_GR; BSU32510.
DR   KEGG; bsu:BSU32510; -.
DR   NMPDR; fig|224308.1.peg.3257; -.
DR   SubtiList; BG13992; pucA.
DR   HOGENOM; O32147; -.
DR   OMA; O32147; EDDLSWG.
DR   BioCyc; BSUB224308:BSU3248-MON; -.
DR   BRENDA; 1.17.1.4; 150.
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; IPR003777; XdhC_CoxI.
DR   Pfam; PF02625; XdhC_CoxI; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; NAD; Oxidoreductase; Purine metabolism.
FT   CHAIN         1    330       Probable xanthine dehydrogenase subunit
FT                                A.
FT                                /FTId=PRO_0000166100.
SQ   SEQUENCE   330 AA;  36746 MW;  E4A70B2155BE1902 CRC64;
     MGNFHTMLDA LLEDQEEAVL ATIVQVEGSA YRKAGASMLF KKKGRRIGLL SGGCVEEDVF
     QRISALGDQL TSTLIPYDMR SEDDLSWGMG AGCNGIIHVH AERITQEKRR HYEKVRDCLH
     SGKAVTSVIK IESSHYLFLT ENGHFGNWPD APLQDIQRTV STLHLPHFDQ TTNMFIQRIE
     PKPRLILFGA GPDNVPLANL AADTGFSVIV TDWRPAYCTS SLFPKADQLI TAFPEQMLSE
     FQFFPHDAAV VATHHYQHDQ TIINFLFSQN LHYIGLLGSA NRTKRLLSGK HPPSHFYSPV
     GLKIGAEGPE EIAVSVVAEI IQTRKRVAVV
//