ID   PUCL_BACSU              Reviewed;         494 AA.
AC   O32141;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   16-JUN-2009, entry version 65.
DE   RecName: Full=Uric acid degradation bifunctional protein pucL;
DE   Includes:
DE     RecName: Full=2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase;
DE              Short=OHCU decarboxylase;
DE              EC=4.1.1.n1;
DE   Includes:
DE     RecName: Full=Uricase;
DE              EC=1.7.3.3;
DE     AltName: Full=Urate oxidase;
GN   Name=pucL; Synonyms=yunL; OrderedLocusNames=BSU32450;
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 AS A URATE OXIDASE, AND INDUCTION.
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).
RN   [3]
RP   FUNCTION AS A OHCU DECARBOXYLASE, CATALYTIC ACTIVITY, REACTION
RP   MECHANISM, AND MUTAGENESIS OF HIS-68; GLU-84 AND ARG-158.
RX   PubMed=17567580; DOI=10.1074/jbc.M703211200;
RA   Kim K., Park J., Rhee S.;
RT   "Structural and functional basis for (S)-allantoin formation in the
RT   ureide pathway.";
RL   J. Biol. Chem. 282:23457-23464(2007).
CC   -!- FUNCTION: Catalyzes two steps in the degradation of uric acid,
CC       i.e. the oxidation of uric acid to 5-hydroxyisourate (HIU) and the
CC       stereoselective decarboxylation of 2-oxo-4-hydroxy-4-carboxy-5-
CC       ureidoimidazoline (OHCU) to (S)-allantoin.
CC   -!- CATALYTIC ACTIVITY: 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-
CC       imidazole-5-carboxylate = (S)-allantoin + CO(2).
CC   -!- CATALYTIC ACTIVITY: Urate + O(2) + H(2)O = 5-hydroxyisourate +
CC       H(2)O(2).
CC   -!- PATHWAY: Purine metabolism; uric acid degradation; (S)-allantoin
CC       from uric acid: step 1/3.
CC   -!- PATHWAY: Purine metabolism; uric acid degradation; (S)-allantoin
CC       from uric acid: step 3/3.
CC   -!- INDUCTION: Expression is very low in excess nitrogen (glutamate
CC       plus ammonia) and is induced during limiting-nitrogen conditions
CC       (glutamate). Expression is further induced when allantoin or uric
CC       acid are added during limiting-nitrogen conditions.
CC   -!- MISCELLANEOUS: HIU and OHCU are unstable, they spontaneously
CC       decompose to form a racemic mixture of allantoin.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the OHCU
CC       decarboxylase family.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the uricase
CC       family.
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DR   EMBL; AL009126; CAB15235.1; -; Genomic_DNA.
DR   PIR; G70016; G70016.
DR   RefSeq; NP_391125.1; -.
DR   GeneID; 936669; -.
DR   GenomeReviews; AL009126_GR; BSU32450.
DR   KEGG; bsu:BSU32450; -.
DR   NMPDR; fig|224308.1.peg.3251; -.
DR   SubtiList; BG13986; pucL.
DR   HOGENOM; O32141; -.
DR   OMA; O32141; KVYTEPR.
DR   BioCyc; BSUB224308:BSU3242-MON; -.
DR   BRENDA; 1.7.3.3; 150.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004846; F:urate oxidase activity; IEA:EC.
DR   GO; GO:0019428; P:allantoin biosynthetic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006144; P:purine base metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR018020; OHCU_decarboxylase.
DR   InterPro; IPR017580; OHCU_decarboxylase-1.
DR   InterPro; IPR002042; Uricase.
DR   InterPro; IPR019842; Uricase_CS.
DR   Gene3D; G3DSA:3.10.270.10; Uricase; 1.
DR   Pfam; PF09349; OHCU_decarbox; 1.
DR   Pfam; PF01014; Uricase; 2.
DR   PRINTS; PR00093; URICASE.
DR   ProDom; PD003367; Uricase; 2.
DR   TIGRFAMs; TIGR03164; UHCUDC; 1.
DR   TIGRFAMs; TIGR03383; urate_oxi; 1.
DR   PROSITE; PS00366; URICASE; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Decarboxylase; Lyase; Multifunctional enzyme;
KW   Oxidoreductase; Purine metabolism.
FT   CHAIN         1    494       Uric acid degradation bifunctional
FT                                protein pucL.
FT                                /FTId=PRO_0000166006.
FT   REGION        1    174       OHCU decarboxylase.
FT   REGION       81     85       Substrate binding (By similarity).
FT   REGION      116    120       Substrate binding (By similarity).
FT   REGION      175    494       Urate oxidase.
FT   REGION      414    415       Substrate binding (By similarity).
FT   ACT_SITE     68     68       Proton donor; for OHCU decarboxylase
FT                                activity.
FT   ACT_SITE    366    366       Charge relay system; for urate oxidase
FT                                activity (By similarity).
FT   ACT_SITE    415    415       Charge relay system; for urate oxidase
FT                                activity (By similarity).
FT   BINDING      69     69       Substrate; via carbonyl oxygen (By
FT                                similarity).
FT   BINDING     239    239       Substrate (By similarity).
FT   BINDING     366    366       Substrate (By similarity).
FT   MUTAGEN      68     68       H->A: Loss of OHCU decarboxylase
FT                                activity.
FT   MUTAGEN      84     84       E->A: Loss of OHCU decarboxylase
FT                                activity.
FT   MUTAGEN     158    158       R->A: Loss of OHCU decarboxylase
FT                                activity.
SQ   SEQUENCE   494 AA;  56560 MW;  C16D0BB42F67BFC5 CRC64;
     MFTMDDLNQM DTQTLTDTLG SIFEHSSWIA ERSAALRPFS SLSDLHRKMT GIVKAADRET
     QLDLIKKHPR LGTKKTMSDD SVREQQNAGL GKLEQQEYEE FLMLNEHYYD RFGFPFILAV
     KGKTKQDIHQ ALLARLESER ETEFQQALIE IYRIARFRLA DIITEKGETQ MKRTMSYGKG
     NVFAYRTYLK PLTGVKQIPE SSFAGRDNTV VGVDVTCEIG GEAFLPSFTD GDNTLVVATD
     SMKNFIQRHL ASYEGTTTEG FLHYVAHRFL DTYSHMDTIT LTGEDIPFEA MPAYEEKELS
     TSRLVFRRSR NERSRSVLKA ERSGNTITIT EQYSEIMDLQ LVKVSGNSFV GFIRDEYTTL
     PEDGNRPLFV YLNISWQYEN TNDSYASDPA RYVAAEQVRD LASTVFHELE TPSIQNLIYH
     IGCRILARFP QLTDVSFQSQ NHTWDTVVEE IPGSKGKVYT EPRPPYGFQH FTVTREDAEK
     EKQKAAEKCR SLKA
//