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Database: UniProt
Entry: O32142
LinkDB: O32142
Original site: O32142 
ID   HIUH_BACSU              Reviewed;         114 AA.
AC   O32142;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   14-APR-2009, sequence version 2.
DT   02-JUN-2021, entry version 138.
DE   RecName: Full=5-hydroxyisourate hydrolase;
DE            Short=HIU hydrolase;
DE            Short=HIUHase;
DE            EC=3.5.2.17;
DE   AltName: Full=Transthyretin-related protein;
DE            Short=TRP;
GN   Name=pucM; Synonyms=yunM; OrderedLocusNames=BSU32460;
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   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   CATALYTIC ACTIVITY.
RC   STRAIN=168;
RX   PubMed=16098976; DOI=10.1016/j.febslet.2005.07.056;
RA   Lee Y., Lee D.H., Kho C.W., Lee A.Y., Jang M., Cho S., Lee C.H., Lee J.S.,
RA   Myung P.K., Park B.C., Park S.G.;
RT   "Transthyretin-related proteins function to facilitate the hydrolysis of 5-
RT   hydroxyisourate, the end product of the uricase reaction.";
RL   FEBS Lett. 579:4769-4774(2005).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF APOENZYME AND COMPLEXES WITH
RP   SUBSTRATE ANALOGS, SUBUNIT, REACTION MECHANISM, AND MUTAGENESIS OF HIS-7;
RP   ARG-42; HIS-98; TYR-111; 111-TYR--SER-114 AND SER-114.
RC   STRAIN=168;
RX   PubMed=16782815; DOI=10.1073/pnas.0600523103;
RA   Jung D.-K., Lee Y., Park S.G., Park B.C., Kim G.-H., Rhee S.;
RT   "Structural and functional analysis of PucM, a hydrolase in the ureide
RT   pathway and a member of the transthyretin-related protein family.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:9790-9795(2006).
CC   -!- FUNCTION: Catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo-
CC       4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-hydroxyisourate + H2O = 5-hydroxy-2-oxo-4-ureido-2,5-
CC         dihydro-1H-imidazole-5-carboxylate + H(+); Xref=Rhea:RHEA:23736,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18072,
CC         ChEBI:CHEBI:58639; EC=3.5.2.17;
CC         Evidence={ECO:0000269|PubMed:16098976};
CC   -!- PATHWAY: Purine metabolism; urate degradation; (S)-allantoin from
CC       urate: step 2/3.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:16782815}.
CC   -!- INTERACTION:
CC       O32142; O32142: pucM; NbExp=2; IntAct=EBI-15587837, EBI-15587837;
CC   -!- INDUCTION: Expression is very low in excess nitrogen (glutamate plus
CC       ammonia) and is induced by TnrA during limiting-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 hydrolysis also occurs spontaneously, but more
CC       slowly.
CC   -!- SIMILARITY: Belongs to the transthyretin family. 5-hydroxyisourate
CC       hydrolase subfamily. {ECO:0000305}.
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DR   EMBL; AL009126; CAB15236.2; -; Genomic_DNA.
DR   PIR; H70016; H70016.
DR   RefSeq; NP_391126.2; NC_000964.3.
DR   RefSeq; WP_003244132.1; NZ_JNCM01000033.1.
DR   PDB; 2H0E; X-ray; 2.20 A; A/B=1-114.
DR   PDB; 2H0F; X-ray; 2.70 A; A/B=1-114.
DR   PDB; 2H0J; X-ray; 2.90 A; A/B=1-114.
DR   PDBsum; 2H0E; -.
DR   PDBsum; 2H0F; -.
DR   PDBsum; 2H0J; -.
DR   SMR; O32142; -.
DR   DIP; DIP-61203N; -.
DR   STRING; 224308.BSU32460; -.
DR   TCDB; 9.B.35.2.1; the putative thyronine-transporting transthyretin (transthyretin) family.
DR   PaxDb; O32142; -.
DR   PRIDE; O32142; -.
DR   EnsemblBacteria; CAB15236; CAB15236; BSU_32460.
DR   GeneID; 937977; -.
DR   KEGG; bsu:BSU32460; -.
DR   PATRIC; fig|224308.179.peg.3513; -.
DR   eggNOG; COG2351; Bacteria.
DR   InParanoid; O32142; -.
DR   OMA; DEHYHVP; -.
DR   PhylomeDB; O32142; -.
DR   BioCyc; BSUB:BSU32460-MONOMER; -.
DR   BRENDA; 3.5.2.17; 658.
DR   UniPathway; UPA00394; UER00651.
DR   EvolutionaryTrace; O32142; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0033971; F:hydroxyisourate hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0006144; P:purine nucleobase metabolic process; IBA:GO_Central.
DR   GO; GO:0019628; P:urate catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.60.40.180; -; 1.
DR   InterPro; IPR014306; Hydroxyisourate_hydrolase.
DR   InterPro; IPR023418; Thyroxine_BS.
DR   InterPro; IPR000895; Transthyretin/HIU_hydrolase.
DR   InterPro; IPR023416; Transthyretin/HIU_hydrolase_d.
DR   InterPro; IPR036817; Transthyretin/HIU_hydrolase_sf.
DR   InterPro; IPR023419; Transthyretin_CS.
DR   PANTHER; PTHR10395; PTHR10395; 1.
DR   Pfam; PF00576; Transthyretin; 1.
DR   PRINTS; PR00189; TRNSTHYRETIN.
DR   SUPFAM; SSF49472; SSF49472; 1.
DR   TIGRFAMs; TIGR02962; hdxy_isourate; 1.
DR   PROSITE; PS00768; TRANSTHYRETIN_1; 1.
DR   PROSITE; PS00769; TRANSTHYRETIN_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Hydrolase; Purine metabolism; Reference proteome.
FT   CHAIN           1..114
FT                   /note="5-hydroxyisourate hydrolase"
FT                   /id="PRO_0000050607"
FT   BINDING         7
FT                   /note="Substrate"
FT   BINDING         42
FT                   /note="Substrate"
FT   BINDING         111
FT                   /note="Substrate"
FT   MUTAGEN         7
FT                   /note="H->N: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:16782815"
FT   MUTAGEN         42
FT                   /note="R->E: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:16782815"
FT   MUTAGEN         42
FT                   /note="R->K: No effect on activity."
FT                   /evidence="ECO:0000269|PubMed:16782815"
FT   MUTAGEN         98
FT                   /note="H->N: Reduced activity."
FT                   /evidence="ECO:0000269|PubMed:16782815"
FT   MUTAGEN         111..114
FT                   /note="Missing: Highly reduced activity."
FT                   /evidence="ECO:0000269|PubMed:16782815"
FT   MUTAGEN         111
FT                   /note="Y->F: Reduced activity."
FT                   /evidence="ECO:0000269|PubMed:16782815"
FT   MUTAGEN         114
FT                   /note="S->A: No effect on activity."
FT                   /evidence="ECO:0000269|PubMed:16782815"
FT   STRAND          3..5
FT                   /evidence="ECO:0007829|PDB:2H0E"
FT   STRAND          8..10
FT                   /evidence="ECO:0007829|PDB:2H0E"
FT   TURN            11..13
FT                   /evidence="ECO:0007829|PDB:2H0E"
FT   STRAND          14..16
FT                   /evidence="ECO:0007829|PDB:2H0E"
FT   STRAND          21..26
FT                   /evidence="ECO:0007829|PDB:2H0E"
FT   STRAND          33..36
FT                   /evidence="ECO:0007829|PDB:2H0E"
FT   STRAND          47..49
FT                   /evidence="ECO:0007829|PDB:2H0E"
FT   HELIX           50..52
FT                   /evidence="ECO:0007829|PDB:2H0E"
FT   STRAND          55..62
FT                   /evidence="ECO:0007829|PDB:2H0E"
FT   HELIX           64..69
FT                   /evidence="ECO:0007829|PDB:2H0E"
FT   STRAND          82..90
FT                   /evidence="ECO:0007829|PDB:2H0E"
FT   STRAND          95..98
FT                   /evidence="ECO:0007829|PDB:2H0E"
FT   STRAND          101..104
FT                   /evidence="ECO:0007829|PDB:2H0E"
FT   STRAND          107..110
FT                   /evidence="ECO:0007829|PDB:2H0E"
SQ   SEQUENCE   114 AA;  12635 MW;  ADF152BAF851D91A CRC64;
     MGKLTTHILD LTCGKPAANV KIGLKRLGES IMKEVYTNND GRVDVPLLAG EELMSGEYVM
     EFHAGDYFAS KNMNAADQPF LTIVTVRFQL ADPDAHYHIP LLLSPFGYQV YRGS
//
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