ID   PUCB_BACSU              Reviewed;         205 AA.
AC   O32146;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 2.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Purine catabolism protein PucB;
GN   Name=pucB; Synonyms=yurE; OrderedLocusNames=BSU32500;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; 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   SEQUENCE REVISION TO C-TERMINUS.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
RN   [3]
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: Required for xanthine dehydrogenase activity. Could be
CC       involved in formation of the molybdenum cofactor required by xanthine
CC       dehydrogenase. {ECO:0000269|PubMed:11344136}.
CC   -!- PATHWAY: Purine metabolism; hypoxanthine degradation.
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; CAB15240.2; -; Genomic_DNA.
DR   PIR; D70017; D70017.
DR   RefSeq; NP_391130.2; NC_000964.3.
DR   RefSeq; WP_003228645.1; NZ_JNCM01000033.1.
DR   AlphaFoldDB; O32146; -.
DR   SMR; O32146; -.
DR   STRING; 224308.BSU32500; -.
DR   PaxDb; O32146; -.
DR   PRIDE; O32146; -.
DR   EnsemblBacteria; CAB15240; CAB15240; BSU_32500.
DR   GeneID; 936486; -.
DR   KEGG; bsu:BSU32500; -.
DR   PATRIC; fig|224308.179.peg.3519; -.
DR   eggNOG; COG2068; Bacteria.
DR   InParanoid; O32146; -.
DR   OMA; WSLHVCQ; -.
DR   PhylomeDB; O32146; -.
DR   BioCyc; BSUB:BSU32500-MON; -.
DR   UniPathway; UPA00604; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0009114; P:hypoxanthine catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR025877; MobA-like_NTP_Trfase.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR017615; Xanthine_dehydrogenase_PucB.
DR   Pfam; PF12804; NTP_transf_3; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
DR   TIGRFAMs; TIGR03202; pucB; 1.
PE   2: Evidence at transcript level;
KW   Purine metabolism; Reference proteome.
FT   CHAIN           1..205
FT                   /note="Purine catabolism protein PucB"
FT                   /id="PRO_0000097098"
SQ   SEQUENCE   205 AA;  22092 MW;  7F98E03296BBBE20 CRC64;
     MRSPYLIGVF LAAGKSRRMG QNKLALPLKG ENIGSLSLKT ALSSRLDHVL VVERTEHASL
     EWIGAPYHAP PFQKRWSLHV CQDAEKGQGH SVSSGVRKAE SMGADGIVIL LADQPQLSVD
     HLNALVALAP ESFAVSSFLG AFTPPIYFSS TCFPYVKGLK GDEGARRLLK SGQLGAGAVL
     EAKDSGELDD IDTPEEYDMV RRAMS