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   27-MAR-2024, entry version 145.
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 (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., 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., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., 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   PubMed=11344136; 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 controlled by
RT   the PucR transcription activator.";
RL   J. Bacteriol. 183:3293-3302(2001).
CC   -!- FUNCTION: Oxidizes hypoxanthine and xanthine to uric acid.
CC       {ECO:0000269|PubMed:11344136}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + NAD(+) + xanthine = H(+) + NADH + urate;
CC         Xref=Rhea:RHEA:16669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17712, ChEBI:CHEBI:17775, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.17.1.4;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + hypoxanthine + NAD(+) = H(+) + NADH + xanthine;
CC         Xref=Rhea:RHEA:24670, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17368, ChEBI:CHEBI:17712, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.17.1.4;
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250};
CC       Note=Binds 2 [2Fe-2S] clusters. {ECO:0000250};
CC   -!- PATHWAY: Purine metabolism; hypoxanthine degradation; urate from
CC       hypoxanthine: step 1/2.
CC   -!- PATHWAY: Purine metabolism; hypoxanthine degradation; urate from
CC       hypoxanthine: step 2/2.
CC   -!- SUBUNIT: Could be composed of four subunits: PucA, PucC, PucD and PucE.
CC   -!- INDUCTION: Expression is very low in excess nitrogen (glutamate plus
CC       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; CAB15237.1; -; Genomic_DNA.
DR   PIR; A70017; A70017.
DR   RefSeq; NP_391127.1; NC_000964.3.
DR   RefSeq; WP_003243276.1; NZ_JNCM01000033.1.
DR   AlphaFoldDB; O32143; -.
DR   SMR; O32143; -.
DR   STRING; 224308.BSU32470; -.
DR   PaxDb; 224308-BSU32470; -.
DR   EnsemblBacteria; CAB15237; CAB15237; BSU_32470.
DR   GeneID; 936680; -.
DR   KEGG; bsu:BSU32470; -.
DR   PATRIC; fig|224308.179.peg.3516; -.
DR   eggNOG; COG2080; Bacteria.
DR   InParanoid; O32143; -.
DR   OrthoDB; 9796880at2; -.
DR   PhylomeDB; O32143; -.
DR   BioCyc; BSUB:BSU32470-MONOMER; -.
DR   UniPathway; UPA00604; UER00661.
DR   UniPathway; UPA00604; UER00662.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004854; F:xanthine dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009114; P:hypoxanthine catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.10.20.30; -; 1.
DR   Gene3D; 1.10.150.120; [2Fe-2S]-binding domain; 1.
DR   InterPro; IPR002888; 2Fe-2S-bd.
DR   InterPro; IPR036884; 2Fe-2S-bd_dom_sf.
DR   InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR   InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR   InterPro; IPR006058; 2Fe2S_fd_BS.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR017611; Xanthine_dehydrogenase_esu.
DR   NCBIfam; TIGR03198; pucE; 1.
DR   PANTHER; PTHR44379; OXIDOREDUCTASE WITH IRON-SULFUR SUBUNIT; 1.
DR   PANTHER; PTHR44379:SF5; XANTHINE DEHYDROGENASE SUBUNIT E-RELATED; 1.
DR   Pfam; PF00111; Fer2; 1.
DR   Pfam; PF01799; Fer2_2; 1.
DR   SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR   SUPFAM; SSF47741; CO dehydrogenase ISP C-domain like; 1.
DR   PROSITE; PS00197; 2FE2S_FER_1; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
PE   2: Evidence at transcript level;
KW   2Fe-2S; Iron; Iron-sulfur; Metal-binding; NAD; Oxidoreductase;
KW   Purine metabolism; Reference proteome.
FT   CHAIN           1..173
FT                   /note="Probable xanthine dehydrogenase subunit E"
FT                   /id="PRO_0000166101"
FT   DOMAIN          14..90
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         52
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         57
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         60
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         72
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         110
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         113
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         145
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         147
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
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
//