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Protein

5-hydroxyisourate hydrolase

Gene

hiuH

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU).

Catalytic activityi

5-hydroxyisourate + H2O = 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei32 – 321SubstrateBy similarity
Binding sitei70 – 701SubstrateBy similarity
Binding sitei134 – 1341SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Purine metabolism

Enzyme and pathway databases

BioCyciEcoCyc:G7058-MONOMER.
ECOL316407:JW1953-MONOMER.
BRENDAi3.5.2.17. 2026.

Names & Taxonomyi

Protein namesi
Recommended name:
5-hydroxyisourate hydrolase (EC:3.5.2.17)
Short name:
HIU hydrolase
Short name:
HIUHase
Alternative name(s):
Transthyretin-like protein
Short name:
TLP
Transthyretin-related protein
Short name:
TRP
Gene namesi
Name:hiuH
Synonyms:yedX
Ordered Locus Names:b1970, JW1953
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG14046. hiuH.

Subcellular locationi

  • Periplasm 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 23232 PublicationsAdd
BLAST
Chaini24 – 1371145-hydroxyisourate hydrolasePRO_0000035772Add
BLAST

Proteomic databases

PaxDbiP76341.

Interactioni

Subunit structurei

Homotetramer.2 Publications

Protein-protein interaction databases

BioGridi4260382. 3 interactions.
DIPiDIP-11854N.
IntActiP76341. 1 interaction.
STRINGi511145.b1970.

Structurei

Secondary structure

1
137
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi29 – 357Combined sources
Turni36 – 394Combined sources
Beta strandi46 – 527Combined sources
Beta strandi54 – 6411Combined sources
Beta strandi69 – 724Combined sources
Beta strandi82 – 898Combined sources
Helixi91 – 977Combined sources
Beta strandi107 – 1159Combined sources
Beta strandi120 – 1278Combined sources
Beta strandi130 – 1345Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2G2NX-ray1.65A/B/C/D24-137[»]
2G2PX-ray2.10A/B/C/D24-137[»]
2IGLX-ray1.80A/B/C/D24-137[»]
ProteinModelPortaliP76341.
SMRiP76341. Positions 26-137.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP76341.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105VT2. Bacteria.
COG2351. LUCA.
HOGENOMiHOG000251776.
InParanoidiP76341.
KOiK07127.
OMAiADADSHY.
OrthoDBiEOG6F55J8.
PhylomeDBiP76341.

Family and domain databases

Gene3Di2.60.40.180. 1 hit.
InterProiIPR014306. Hydroxyisourate_hydrolase.
IPR023418. Thyroxine_BS.
IPR000895. Transthyretin/HIU_hydrolase.
IPR023416. Transthyretin/HIU_hydrolase_SF.
IPR023419. Transthyretin_CS.
[Graphical view]
PfamiPF00576. Transthyretin. 1 hit.
[Graphical view]
PRINTSiPR00189. TRNSTHYRETIN.
SMARTiSM00095. TR_THY. 1 hit.
[Graphical view]
SUPFAMiSSF49472. SSF49472. 1 hit.
TIGRFAMsiTIGR02962. hdxy_isourate. 1 hit.
PROSITEiPS00768. TRANSTHYRETIN_1. 1 hit.
PS00769. TRANSTHYRETIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P76341-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLKRYLVLSV ATAAFSLPSL VNAAQQNILS VHILNQQTGK PAADVTVTLE
60 70 80 90 100
KKADNGWLQL NTAKTDKDGR IKALWPEQTA TTGDYRVVFK TGDYFKKQNL
110 120 130
ESFFPEIPVE FHINKVNEHY HVPLLLSQYG YSTYRGS
Length:137
Mass (Da):15,460
Last modified:February 1, 1997 - v1
Checksum:iB58A534051DDDC5E
GO

Mass spectrometryi

Molecular mass is 13013 Da from positions 24 - 137. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC75036.1.
AP009048 Genomic DNA. Translation: BAE76558.1.
PIRiF64961.
RefSeqiNP_416479.1. NC_000913.3.
WP_000920120.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75036; AAC75036; b1970.
BAE76558; BAE76558; BAE76558.
GeneIDi946485.
KEGGiecj:JW1953.
eco:b1970.
PATRICi32119271. VBIEscCol129921_2050.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC75036.1.
AP009048 Genomic DNA. Translation: BAE76558.1.
PIRiF64961.
RefSeqiNP_416479.1. NC_000913.3.
WP_000920120.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2G2NX-ray1.65A/B/C/D24-137[»]
2G2PX-ray2.10A/B/C/D24-137[»]
2IGLX-ray1.80A/B/C/D24-137[»]
ProteinModelPortaliP76341.
SMRiP76341. Positions 26-137.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260382. 3 interactions.
DIPiDIP-11854N.
IntActiP76341. 1 interaction.
STRINGi511145.b1970.

Proteomic databases

PaxDbiP76341.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75036; AAC75036; b1970.
BAE76558; BAE76558; BAE76558.
GeneIDi946485.
KEGGiecj:JW1953.
eco:b1970.
PATRICi32119271. VBIEscCol129921_2050.

Organism-specific databases

EchoBASEiEB3799.
EcoGeneiEG14046. hiuH.

Phylogenomic databases

eggNOGiENOG4105VT2. Bacteria.
COG2351. LUCA.
HOGENOMiHOG000251776.
InParanoidiP76341.
KOiK07127.
OMAiADADSHY.
OrthoDBiEOG6F55J8.
PhylomeDBiP76341.

Enzyme and pathway databases

BioCyciEcoCyc:G7058-MONOMER.
ECOL316407:JW1953-MONOMER.
BRENDAi3.5.2.17. 2026.

Miscellaneous databases

EvolutionaryTraceiP76341.
PROiP76341.

Family and domain databases

Gene3Di2.60.40.180. 1 hit.
InterProiIPR014306. Hydroxyisourate_hydrolase.
IPR023418. Thyroxine_BS.
IPR000895. Transthyretin/HIU_hydrolase.
IPR023416. Transthyretin/HIU_hydrolase_SF.
IPR023419. Transthyretin_CS.
[Graphical view]
PfamiPF00576. Transthyretin. 1 hit.
[Graphical view]
PRINTSiPR00189. TRNSTHYRETIN.
SMARTiSM00095. TR_THY. 1 hit.
[Graphical view]
SUPFAMiSSF49472. SSF49472. 1 hit.
TIGRFAMsiTIGR02962. hdxy_isourate. 1 hit.
PROSITEiPS00768. TRANSTHYRETIN_1. 1 hit.
PS00769. TRANSTHYRETIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  2. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Rudd K.E.
    Unpublished observations (AUG-1999)
    Cited for: PROTEIN SEQUENCE OF N-TERMINUS, SUBCELLULAR LOCATION.
  4. Cited for: PROTEIN SEQUENCE OF N-TERMINUS, LACK OF THYROID HORMONE BINDING, MASS SPECTROMETRY, SUBUNIT.
    Strain: K12 / MG1655 / ATCC 47076.
  5. "Transthyretin-related proteins function to facilitate the hydrolysis of 5-hydroxyisourate, the end product of the uricase reaction."
    Lee Y., Lee D.H., Kho C.W., Lee A.Y., Jang M., Cho S., Lee C.H., Lee J.S., Myung P.K., Park B.C., Park S.G.
    FEBS Lett. 579:4769-4774(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY.
  6. "The transthyretin-related protein: structural investigation of a novel protein family."
    Lundberg E., Baeckstroem S., Sauer U.H., Sauer-Eriksson A.E.
    J. Struct. Biol. 155:445-457(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 24-137, SUBUNIT.
  7. "Expression, purification and structure determination of yedX, a transthyretin-related protein from Escherichia coli."
    Zuo Y., Malhotra A.
    Submitted (OCT-2007) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 24-137.

Entry informationi

Entry nameiHIUH_ECOLI
AccessioniPrimary (citable) accession number: P76341
Secondary accession number(s): Q2MAZ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: February 1, 1997
Last modified: January 20, 2016
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Despite its homology to transthyretins, is not able to bind to the thyroid hormones thyroxine (T4) and triiodothyronine (T3).
Although some crystallographic structures were found to contain zinc, the purified protein does not contain bound metal ions, and does not require zinc or other metal ions for enzyme activity.
HIU hydrolysis also occurs spontaneously, but more slowly.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.