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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}.
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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
 
 
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