ID   XDHE_BACSU              Reviewed;         173 AA.
AC   O32143;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   16-JUN-2009, entry version 63.
DE   RecName: Full=Probable xanthine dehydrogenase subunit E;
DE            Short=XDHase subunit E;
DE            EC=1.17.1.4;
GN   Name=pucE; Synonyms=yurB; OrderedLocusNames=BSU32470;
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: Binds 2 2Fe-2S clusters (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 2Fe-2S ferredoxin-type domain.
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DR   EMBL; AL009126; CAB15237.1; -; Genomic_DNA.
DR   PIR; A70017; A70017.
DR   RefSeq; NP_391127.1; -.
DR   HSSP; Q46509; 1HLR.
DR   GeneID; 936680; -.
DR   GenomeReviews; AL009126_GR; BSU32470.
DR   KEGG; bsu:BSU32470; -.
DR   NMPDR; fig|224308.1.peg.3253; -.
DR   SubtiList; BG13988; pucE.
DR   HOGENOM; O32143; -.
DR   OMA; O32143; MAVWANG.
DR   BioCyc; BSUB224308:BSU3244-MON; -.
DR   BRENDA; 1.17.1.4; 150.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0005506; F:iron 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; IPR002888; 2Fe-2S_bd.
DR   InterPro; IPR006058; 2Fe2S_fd_BS.
DR   InterPro; IPR001041; Ferredoxin.
DR   InterPro; IPR017611; Xanthine_dehydrogenase_esu.
DR   Pfam; PF00111; Fer2; 1.
DR   Pfam; PF01799; Fer2_2; 1.
DR   ProDom; PD186071; 2Fe-2S_bind; 1.
DR   TIGRFAMs; TIGR03198; pucE; 1.
DR   PROSITE; PS00197; 2FE2S_FER_1; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
PE   2: Evidence at transcript level;
KW   2Fe-2S; Complete proteome; Iron; Iron-sulfur; Metal-binding; NAD;
KW   Oxidoreductase; Purine metabolism.
FT   CHAIN         1    173       Probable xanthine dehydrogenase subunit
FT                                E.
FT                                /FTId=PRO_0000166101.
FT   DOMAIN       14     90       2Fe-2S ferredoxin-type.
FT   METAL        52     52       Iron-sulfur (2Fe-2S) (Potential).
FT   METAL        57     57       Iron-sulfur (2Fe-2S) (Potential).
FT   METAL        60     60       Iron-sulfur (2Fe-2S) (Potential).
FT   METAL        72     72       Iron-sulfur (2Fe-2S) (Potential).
FT   METAL       110    110       Iron-sulfur (2Fe-2S) (Potential).
FT   METAL       113    113       Iron-sulfur (2Fe-2S) (Potential).
FT   METAL       145    145       Iron-sulfur (2Fe-2S) (Potential).
FT   METAL       147    147       Iron-sulfur (2Fe-2S) (Potential).
SQ   SEQUENCE   173 AA;  18838 MW;  48E7D4CBB76BB321 CRC64;
     MDIKEAGPFP VKKEQFRMTV NGQAWEVAAV PTTHLSDLLR KEFQLTGTKV SCGIGRCGAC
     SILIDGKLAN ACMTMAYQAD GHSITTIEGL QKEELDMCQT AFLEEGGFQC GYCTPGMIIA
     LKALFRETPQ PSDKDIEEGL AGNLCRCTGY GGIMRSACRI RRELNGGRRE SGF
//