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Protein

5-hydroxyisourate hydrolase

Gene

pucM

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 5 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

Pathwayi: urate degradation

This protein is involved in step 2 of the subpathway that synthesizes (S)-allantoin from urate.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Uric acid degradation bifunctional protein PucL (pucL)
  2. 5-hydroxyisourate hydrolase (pucM)
  3. Uric acid degradation bifunctional protein PucL (pucL)
This subpathway is part of the pathway urate degradation, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-allantoin from urate, the pathway urate degradation and in Purine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei7Substrate1
Binding sitei42Substrate1
Binding sitei111Substrate1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Purine metabolism

Enzyme and pathway databases

BioCyciBSUB:BSU32460-MONOMER.
BRENDAi3.5.2.17. 658.
UniPathwayiUPA00394; UER00651.

Protein family/group databases

TCDBi9.B.35.2.1. the putative thyronine-transporting transthyretin (transthyretin) family.

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-related protein
Short name:
TRP
Gene namesi
Name:pucM
Synonyms:yunM
Ordered Locus Names:BSU32460
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi7H → N: Loss of activity. 1 Publication1
Mutagenesisi42R → E: Loss of activity. 1 Publication1
Mutagenesisi42R → K: No effect on activity. 1 Publication1
Mutagenesisi98H → N: Reduced activity. 1 Publication1
Mutagenesisi111 – 114Missing : Highly reduced activity. 1 Publication4
Mutagenesisi111Y → F: Reduced activity. 1 Publication1
Mutagenesisi114S → A: No effect on activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000506071 – 1145-hydroxyisourate hydrolaseAdd BLAST114

Proteomic databases

PaxDbiO32142.

Expressioni

Inductioni

Expression is very low in excess nitrogen (glutamate plus ammonia) and is induced by TnrA during limiting-nitrogen conditions (glutamate). Expression is further induced when allantoin or uric acid are added during limiting-nitrogen conditions.2 Publications

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

DIPiDIP-61203N.
STRINGi224308.Bsubs1_010100017606.

Structurei

Secondary structure

1114
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 5Combined sources3
Beta strandi8 – 10Combined sources3
Turni11 – 13Combined sources3
Beta strandi14 – 16Combined sources3
Beta strandi21 – 26Combined sources6
Beta strandi33 – 36Combined sources4
Beta strandi47 – 49Combined sources3
Helixi50 – 52Combined sources3
Beta strandi55 – 62Combined sources8
Helixi64 – 69Combined sources6
Beta strandi82 – 90Combined sources9
Beta strandi95 – 98Combined sources4
Beta strandi101 – 104Combined sources4
Beta strandi107 – 110Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2H0EX-ray2.20A/B1-114[»]
2H0FX-ray2.70A/B1-114[»]
2H0JX-ray2.90A/B1-114[»]
ProteinModelPortaliO32142.
SMRiO32142.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO32142.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105VT2. Bacteria.
COG2351. LUCA.
HOGENOMiHOG000251776.
InParanoidiO32142.
KOiK07127.
OMAiPWAYSTY.
PhylomeDBiO32142.

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.
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.

O32142-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKLTTHILD LTCGKPAANV KIGLKRLGES IMKEVYTNND GRVDVPLLAG
60 70 80 90 100
EELMSGEYVM EFHAGDYFAS KNMNAADQPF LTIVTVRFQL ADPDAHYHIP
110
LLLSPFGYQV YRGS
Length:114
Mass (Da):12,635
Last modified:April 14, 2009 - v2
Checksum:iADF152BAF851D91A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB15236.2.
PIRiH70016.
RefSeqiNP_391126.2. NC_000964.3.
WP_003244132.1. NZ_JNCM01000033.1.

Genome annotation databases

EnsemblBacteriaiCAB15236; CAB15236; BSU32460.
GeneIDi937977.
KEGGibsu:BSU32460.
PATRICi18978464. VBIBacSub10457_3395.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB15236.2.
PIRiH70016.
RefSeqiNP_391126.2. NC_000964.3.
WP_003244132.1. NZ_JNCM01000033.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2H0EX-ray2.20A/B1-114[»]
2H0FX-ray2.70A/B1-114[»]
2H0JX-ray2.90A/B1-114[»]
ProteinModelPortaliO32142.
SMRiO32142.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-61203N.
STRINGi224308.Bsubs1_010100017606.

Protein family/group databases

TCDBi9.B.35.2.1. the putative thyronine-transporting transthyretin (transthyretin) family.

Proteomic databases

PaxDbiO32142.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15236; CAB15236; BSU32460.
GeneIDi937977.
KEGGibsu:BSU32460.
PATRICi18978464. VBIBacSub10457_3395.

Phylogenomic databases

eggNOGiENOG4105VT2. Bacteria.
COG2351. LUCA.
HOGENOMiHOG000251776.
InParanoidiO32142.
KOiK07127.
OMAiPWAYSTY.
PhylomeDBiO32142.

Enzyme and pathway databases

UniPathwayiUPA00394; UER00651.
BioCyciBSUB:BSU32460-MONOMER.
BRENDAi3.5.2.17. 658.

Miscellaneous databases

EvolutionaryTraceiO32142.

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.
SUPFAMiSSF49472. SSF49472. 1 hit.
TIGRFAMsiTIGR02962. hdxy_isourate. 1 hit.
PROSITEiPS00768. TRANSTHYRETIN_1. 1 hit.
PS00769. TRANSTHYRETIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHIUH_BACSU
AccessioniPrimary (citable) accession number: O32142
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: April 14, 2009
Last modified: November 2, 2016
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

HIU hydrolysis also occurs spontaneously, but more slowly.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.