PUCL_BACSU
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 03-AUG-2022, entry version 139.
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=4.1.1.97;
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 (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 FUNCTION AS A URATE OXIDASE, AND INDUCTION.
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).
RN [3]
RP INDUCTION BY TNRA.
RX PubMed=12823818; DOI=10.1046/j.1365-2958.2003.03567.x;
RA Yoshida K., Yamaguchi H., Kinehara M., Ohki Y.-H., Nakaura Y., Fujita Y.;
RT "Identification of additional TnrA-regulated genes of Bacillus subtilis
RT associated with a TnrA box.";
RL Mol. Microbiol. 49:157-165(2003).
RN [4]
RP FUNCTION AS A OHCU DECARBOXYLASE, CATALYTIC ACTIVITY, REACTION MECHANISM,
RP 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 ureide
RT pathway.";
RL J. Biol. Chem. 282:23457-23464(2007).
RN [5]
RP FUNCTION AS URATE OXIDASE, CATALYTIC ACTIVITY, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=168 / NCCB 69003;
RX PubMed=20168977; DOI=10.1155/2010/674908;
RA Pfrimer P., de Moraes L.M., Galdino A.S., Salles L.P., Reis V.C.,
RA De Marco J.L., Prates M.V., Bloch C. Jr., Torres F.A.;
RT "Cloning, purification, and partial characterization of Bacillus subtilis
RT urate oxidase expressed in Escherichia coli.";
RL J. Biomed. Biotechnol. 2010:674908-674908(2010).
CC -!- FUNCTION: Catalyzes two steps in the degradation of uric acid, i.e. the
CC 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 {ECO:0000269|PubMed:11344136, ECO:0000269|PubMed:17567580,
CC ECO:0000269|PubMed:20168977}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-
CC carboxylate + H(+) = (S)-allantoin + CO2; Xref=Rhea:RHEA:26301,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15678, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:58639; EC=4.1.1.97;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O2 + urate = 5-hydroxyisourate + H2O2;
CC Xref=Rhea:RHEA:21368, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:17775, ChEBI:CHEBI:18072; EC=1.7.3.3;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8. {ECO:0000269|PubMed:20168977};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius. Retains 90% of its
CC activity after 72 hours of incubation at 20 degrees Celsius or -4
CC degrees Celsius, but loses 50% of its activity after 12 hours of
CC incubation at 37 degrees Celsius. {ECO:0000269|PubMed:20168977};
CC -!- PATHWAY: Purine metabolism; urate degradation; (S)-allantoin from
CC urate: step 1/3.
CC -!- PATHWAY: Purine metabolism; urate degradation; (S)-allantoin from
CC urate: step 3/3.
CC -!- INDUCTION: Expression is very low in excess nitrogen (glutamate plus
CC ammonia) and is induced by TnrA during imiting-nitrogen conditions
CC (glutamate). Expression is further induced when allantoin or uric acid
CC are added during limiting-nitrogen conditions.
CC {ECO:0000269|PubMed:11344136, ECO:0000269|PubMed:12823818}.
CC -!- MISCELLANEOUS: HIU and OHCU are unstable, they spontaneously decompose
CC to form a racemic mixture of allantoin.
CC -!- SIMILARITY: In the N-terminal section; belongs to the OHCU
CC decarboxylase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the uricase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL009126; CAB15235.1; -; Genomic_DNA.
DR PIR; G70016; G70016.
DR RefSeq; NP_391125.1; NC_000964.3.
DR RefSeq; WP_003242600.1; NZ_JNCM01000033.1.
DR PDB; 6A4M; X-ray; 2.60 A; A=175-479.
DR PDBsum; 6A4M; -.
DR AlphaFoldDB; O32141; -.
DR SMR; O32141; -.
DR STRING; 224308.BSU32450; -.
DR PaxDb; O32141; -.
DR PRIDE; O32141; -.
DR EnsemblBacteria; CAB15235; CAB15235; BSU_32450.
DR GeneID; 936669; -.
DR KEGG; bsu:BSU32450; -.
DR PATRIC; fig|224308.179.peg.3512; -.
DR eggNOG; COG3195; Bacteria.
DR eggNOG; COG3648; Bacteria.
DR InParanoid; O32141; -.
DR OMA; THRWTRM; -.
DR PhylomeDB; O32141; -.
DR BioCyc; BSUB:BSU32450-MON; -.
DR SABIO-RK; O32141; -.
DR UniPathway; UPA00394; UER00650.
DR UniPathway; UPA00394; UER00652.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR GO; GO:0051997; F:2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase activity; IBA:GO_Central.
DR GO; GO:0004846; F:urate oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0000255; P:allantoin metabolic process; IEA:InterPro.
DR GO; GO:0006144; P:purine nucleobase metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0019628; P:urate catabolic process; IBA:GO_Central.
DR Gene3D; 1.10.3330.10; -; 1.
DR InterPro; IPR018020; OHCU_decarboxylase.
DR InterPro; IPR017580; OHCU_decarboxylase-1.
DR InterPro; IPR036778; OHCU_decarboxylase_sf.
DR InterPro; IPR002042; Uricase.
DR InterPro; IPR019842; Uricase_CS.
DR Pfam; PF09349; OHCU_decarbox; 1.
DR Pfam; PF01014; Uricase; 2.
DR PRINTS; PR00093; URICASE.
DR SUPFAM; SSF158694; SSF158694; 1.
DR TIGRFAMs; TIGR03164; UHCUDC; 1.
DR TIGRFAMs; TIGR03383; urate_oxi; 1.
DR PROSITE; PS00366; URICASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Decarboxylase; Lyase; Multifunctional enzyme; Oxidoreductase;
KW Purine metabolism; Reference proteome.
FT CHAIN 1..494
FT /note="Uric acid degradation bifunctional protein PucL"
FT /id="PRO_0000166006"
FT REGION 1..174
FT /note="OHCU decarboxylase"
FT REGION 175..494
FT /note="Urate oxidase"
FT ACT_SITE 68
FT /note="Proton donor; for OHCU decarboxylase activity"
FT /evidence="ECO:0000305|PubMed:17567580"
FT ACT_SITE 179
FT /note="Charge relay system; for urate oxidase activity"
FT /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT ACT_SITE 239
FT /note="Charge relay system; for urate oxidase activity"
FT /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT BINDING 69
FT /ligand="5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-
FT 5-carboxylate"
FT /ligand_id="ChEBI:CHEBI:58639"
FT /evidence="ECO:0000250"
FT BINDING 81..85
FT /ligand="5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-
FT 5-carboxylate"
FT /ligand_id="ChEBI:CHEBI:58639"
FT /evidence="ECO:0000305|PubMed:17567580"
FT BINDING 116..120
FT /ligand="5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-
FT 5-carboxylate"
FT /ligand_id="ChEBI:CHEBI:58639"
FT /evidence="ECO:0000250"
FT BINDING 239..240
FT /ligand="urate"
FT /ligand_id="ChEBI:CHEBI:17775"
FT /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT BINDING 349
FT /ligand="urate"
FT /ligand_id="ChEBI:CHEBI:17775"
FT /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT BINDING 366
FT /ligand="urate"
FT /ligand_id="ChEBI:CHEBI:17775"
FT /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT BINDING 414..415
FT /ligand="urate"
FT /ligand_id="ChEBI:CHEBI:17775"
FT /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT MUTAGEN 68
FT /note="H->A: Loss of OHCU decarboxylase activity."
FT /evidence="ECO:0000269|PubMed:17567580"
FT MUTAGEN 84
FT /note="E->A: Loss of OHCU decarboxylase activity."
FT /evidence="ECO:0000269|PubMed:17567580"
FT MUTAGEN 158
FT /note="R->A: Loss of OHCU decarboxylase activity."
FT /evidence="ECO:0000269|PubMed:17567580"
FT STRAND 177..188
FT /evidence="ECO:0007829|PDB:6A4M"
FT STRAND 209..220
FT /evidence="ECO:0007829|PDB:6A4M"
FT HELIX 238..252
FT /evidence="ECO:0007829|PDB:6A4M"
FT HELIX 258..272
FT /evidence="ECO:0007829|PDB:6A4M"
FT STRAND 278..286
FT /evidence="ECO:0007829|PDB:6A4M"
FT STRAND 288..295
FT /evidence="ECO:0007829|PDB:6A4M"
FT STRAND 298..308
FT /evidence="ECO:0007829|PDB:6A4M"
FT STRAND 313..322
FT /evidence="ECO:0007829|PDB:6A4M"
FT STRAND 324..343
FT /evidence="ECO:0007829|PDB:6A4M"
FT STRAND 368..380
FT /evidence="ECO:0007829|PDB:6A4M"
FT HELIX 381..385
FT /evidence="ECO:0007829|PDB:6A4M"
FT HELIX 389..391
FT /evidence="ECO:0007829|PDB:6A4M"
FT HELIX 395..407
FT /evidence="ECO:0007829|PDB:6A4M"
FT STRAND 408..411
FT /evidence="ECO:0007829|PDB:6A4M"
FT HELIX 414..428
FT /evidence="ECO:0007829|PDB:6A4M"
FT STRAND 432..441
FT /evidence="ECO:0007829|PDB:6A4M"
FT STRAND 445..448
FT /evidence="ECO:0007829|PDB:6A4M"
FT STRAND 458..460
FT /evidence="ECO:0007829|PDB:6A4M"
FT STRAND 467..474
FT /evidence="ECO:0007829|PDB:6A4M"
FT TURN 475..477
FT /evidence="ECO:0007829|PDB:6A4M"
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
