HIUH_BACSU
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 03-AUG-2022, entry version 142.
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}.
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; 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 AlphaFoldDB; O32142; -.
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 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; ENQNYHI; -.
DR PhylomeDB; O32142; -.
DR BioCyc; BSUB:BSU32460-MON; -.
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 /ligand="substrate"
FT BINDING 42
FT /ligand="substrate"
FT BINDING 111
FT /ligand="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
