HIUH_ECOLI
ID HIUH_ECOLI Reviewed; 137 AA.
AC P76341; Q2MAZ8;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=5-hydroxyisourate hydrolase;
DE Short=HIU hydrolase;
DE Short=HIUHase;
DE EC=3.5.2.17 {ECO:0000269|PubMed:16098976};
DE AltName: Full=Transthyretin-like protein;
DE Short=TLP;
DE AltName: Full=Transthyretin-related protein;
DE Short=TRP;
DE Flags: Precursor;
GN Name=hiuH; Synonyms=yedX; OrderedLocusNames=b1970, JW1953;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP PROTEIN SEQUENCE OF N-TERMINUS, AND SUBCELLULAR LOCATION.
RA Rudd K.E.;
RL Unpublished observations (AUG-1999).
RN [4]
RP PROTEIN SEQUENCE OF N-TERMINUS, LACK OF THYROID HORMONE BINDING, MASS
RP SPECTROMETRY, AND SUBUNIT.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=12542701; DOI=10.1046/j.1432-1033.2003.03408.x;
RA Eneqvist T., Lundberg E., Nilsson L., Abagyan R., Sauer-Eriksson A.E.;
RT "The transthyretin-related protein family.";
RL Eur. J. Biochem. 270:518-532(2003).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
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 [6]
RP INDUCTION.
RX PubMed=25568260; DOI=10.1099/mic.0.000026;
RA Urano H., Umezawa Y., Yamamoto K., Ishihama A., Ogasawara H.;
RT "Cooperative regulation of the common target genes between H(2)O(2)-sensing
RT YedVW and Cu2+-sensing CusSR in Escherichia coli.";
RL Microbiology 161:729-738(2015).
RN [7]
RP INDUCTION.
RX PubMed=27983483; DOI=10.1099/mic.0.000410;
RA Urano H., Yoshida M., Ogawa A., Yamamoto K., Ishihama A., Ogasawara H.;
RT "Cross-regulation between two common ancestral response regulators, HprR
RT and CusR, in Escherichia coli.";
RL Microbiology 163:243-252(2017).
RN [8] {ECO:0007744|PDB:2G2N, ECO:0007744|PDB:2G2P}
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 24-137, AND SUBUNIT.
RX PubMed=16723258; DOI=10.1016/j.jsb.2006.04.002;
RA Lundberg E., Baeckstroem S., Sauer U.H., Sauer-Eriksson A.E.;
RT "The transthyretin-related protein: structural investigation of a novel
RT protein family.";
RL J. Struct. Biol. 155:445-457(2006).
RN [9] {ECO:0007744|PDB:2IGL}
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 24-137.
RA Zuo Y., Malhotra A.;
RT "Expression, purification and structure determination of yedX, a
RT transthyretin-related protein from Escherichia coli.";
RL Submitted (OCT-2007) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo-
CC 4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU).
CC {ECO:0000269|PubMed:16098976}.
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 -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:12542701,
CC ECO:0000269|PubMed:16723258}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|Ref.3}.
CC -!- INDUCTION: Induced by H(2)O(2), via the HprR/HprS two-component system,
CC and by Cu(2+), via the CusS/CusR two-component system. HprR and CusR
CC bind to essentially the same sequence within the hiuH promoter region.
CC {ECO:0000269|PubMed:25568260, ECO:0000269|PubMed:27983483}.
CC -!- MASS SPECTROMETRY: Mass=13013; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:12542701};
CC -!- MISCELLANEOUS: Despite its homology to transthyretins, is not able to
CC bind to the thyroid hormones thyroxine (T4) and triiodothyronine (T3).
CC -!- MISCELLANEOUS: Although some crystallographic structures were found to
CC contain zinc, the purified protein does not contain bound metal ions,
CC and does not require zinc or other metal ions for enzyme activity.
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; U00096; AAC75036.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76558.1; -; Genomic_DNA.
DR PIR; F64961; F64961.
DR RefSeq; NP_416479.1; NC_000913.3.
DR RefSeq; WP_000920120.1; NZ_LN832404.1.
DR PDB; 2G2N; X-ray; 1.65 A; A/B/C/D=24-137.
DR PDB; 2G2P; X-ray; 2.10 A; A/B/C/D=24-137.
DR PDB; 2IGL; X-ray; 1.80 A; A/B/C/D=24-137.
DR PDBsum; 2G2N; -.
DR PDBsum; 2G2P; -.
DR PDBsum; 2IGL; -.
DR AlphaFoldDB; P76341; -.
DR SMR; P76341; -.
DR BioGRID; 4260382; 14.
DR BioGRID; 850836; 1.
DR DIP; DIP-11854N; -.
DR IntAct; P76341; 1.
DR STRING; 511145.b1970; -.
DR jPOST; P76341; -.
DR PaxDb; P76341; -.
DR PRIDE; P76341; -.
DR EnsemblBacteria; AAC75036; AAC75036; b1970.
DR EnsemblBacteria; BAE76558; BAE76558; BAE76558.
DR GeneID; 66674140; -.
DR GeneID; 946485; -.
DR KEGG; ecj:JW1953; -.
DR KEGG; eco:b1970; -.
DR PATRIC; fig|1411691.4.peg.280; -.
DR EchoBASE; EB3799; -.
DR eggNOG; COG2351; Bacteria.
DR HOGENOM; CLU_115536_3_0_6; -.
DR InParanoid; P76341; -.
DR OMA; ENQNYHI; -.
DR PhylomeDB; P76341; -.
DR BioCyc; EcoCyc:G7058-MON; -.
DR BioCyc; MetaCyc:G7058-MON; -.
DR BRENDA; 3.5.2.17; 2026.
DR EvolutionaryTrace; P76341; -.
DR PRO; PR:P76341; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IDA:EcoCyc.
DR GO; GO:0033971; F:hydroxyisourate hydrolase activity; IDA:EcoCyc.
DR GO; GO:0006144; P:purine nucleobase metabolic process; IBA:GO_Central.
DR CDD; cd05822; TLP_HIUase; 1.
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 SMART; SM00095; TR_THY; 1.
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; Direct protein sequencing; Hydrolase; Periplasm;
KW Purine metabolism; Reference proteome; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:12542701, ECO:0000269|Ref.3"
FT CHAIN 24..137
FT /note="5-hydroxyisourate hydrolase"
FT /id="PRO_0000035772"
FT BINDING 32
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT STRAND 29..35
FT /evidence="ECO:0007829|PDB:2G2N"
FT TURN 36..39
FT /evidence="ECO:0007829|PDB:2G2N"
FT STRAND 46..52
FT /evidence="ECO:0007829|PDB:2G2N"
FT STRAND 54..64
FT /evidence="ECO:0007829|PDB:2G2N"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:2G2N"
FT STRAND 82..89
FT /evidence="ECO:0007829|PDB:2G2N"
FT HELIX 91..97
FT /evidence="ECO:0007829|PDB:2G2N"
FT STRAND 107..115
FT /evidence="ECO:0007829|PDB:2G2N"
FT STRAND 120..127
FT /evidence="ECO:0007829|PDB:2G2N"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:2G2N"
SQ SEQUENCE 137 AA; 15460 MW; B58A534051DDDC5E CRC64;
MLKRYLVLSV ATAAFSLPSL VNAAQQNILS VHILNQQTGK PAADVTVTLE KKADNGWLQL
NTAKTDKDGR IKALWPEQTA TTGDYRVVFK TGDYFKKQNL ESFFPEIPVE FHINKVNEHY
HVPLLLSQYG YSTYRGS
