Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Allantoinase

Gene

allB

Organism
Escherichia coli O9:H4 (strain HS)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the conversion of allantoin (5-ureidohydantoin) to allantoic acid by hydrolytic cleavage of the five-member hydantoin ring.UniRule annotation

Catalytic activityi

(S)-allantoin + H2O = allantoate.UniRule annotation

Cofactori

Zn2+UniRule annotationNote: Binds 2 Zn2+ ions per subunit.UniRule annotation

Pathwayi: (S)-allantoin degradation

This protein is involved in step 1 of the subpathway that synthesizes allantoate from (S)-allantoin.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Allantoinase (allB)
This subpathway is part of the pathway (S)-allantoin degradation, which is itself part of Nitrogen metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes allantoate from (S)-allantoin, the pathway (S)-allantoin degradation and in Nitrogen metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi59Zinc 1UniRule annotation1
Metal bindingi61Zinc 1UniRule annotation1
Metal bindingi146Zinc 1; via carbamate groupUniRule annotation1
Metal bindingi146Zinc 2; via carbamate groupUniRule annotation1
Metal bindingi186Zinc 2UniRule annotation1
Metal bindingi242Zinc 2UniRule annotation1
Metal bindingi315Zinc 1UniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Purine metabolism

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00395; UER00653.

Names & Taxonomyi

Protein namesi
Recommended name:
AllantoinaseUniRule annotation (EC:3.5.2.5UniRule annotation)
Alternative name(s):
Allantoin-utilizing enzymeUniRule annotation
Gene namesi
Name:allBUniRule annotation
Ordered Locus Names:EcHS_A0585
OrganismiEscherichia coli O9:H4 (strain HS)
Taxonomic identifieri331112 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003176801 – 453AllantoinaseAdd BLAST453

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei146N6-carboxylysineUniRule annotation1

Post-translational modificationi

Carbamylation allows a single lysine to coordinate two zinc ions.UniRule annotation

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliA7ZXG5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the DHOase family. Allantoinase subfamily.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000219146.
KOiK01466.
OMAiEMIPPIT.

Family and domain databases

Gene3Di2.30.40.10. 1 hit.
HAMAPiMF_01645. Hydantoinase. 1 hit.
InterProiIPR017593. Allantoinase.
IPR006680. Amidohydro-rel.
IPR011059. Metal-dep_hydrolase_composite.
IPR032466. Metal_Hydrolase.
[Graphical view]
PfamiPF01979. Amidohydro_1. 1 hit.
[Graphical view]
SUPFAMiSSF51338. SSF51338. 2 hits.
SSF51556. SSF51556. 1 hit.
TIGRFAMsiTIGR03178. allantoinase. 1 hit.

Sequencei

Sequence statusi: Complete.

A7ZXG5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFDLIIKNG TVILENEARV VDIAVKGGKI AAIGQDLGDA KEVMDASGLV
60 70 80 90 100
VSPGMVDAHT HISEPGRSHW EGYETGTRAA AKGGITTMIE MPLNQLPATV
110 120 130 140 150
DRASIELKFD AAKGKLTIDA AQLGGLVSYN IDRLHELDEV GVVGFKCFVA
160 170 180 190 200
TCGDRGIDND FRDVNDWQFF KGAQKLGELG QPVLVHCENA LICDALGEEA
210 220 230 240 250
KSEGRVTAHD YVASRPVFTE VEAIRRVLYL AKVAGCRLHI CHISSPEGVE
260 270 280 290 300
EVTRARQEGQ DVTCESCPHY FVLDTDQFEE IGTLAKCSPP IRDLENQKGM
310 320 330 340 350
WEKLFNGEID CLVSDHSPCP PEMKAGNIME AWGGIAGLQN CMDVMFDEAV
360 370 380 390 400
QKRGMSLPMF GKLMATNAAD IFGLQQKGRI APGKDAEFVF IQPNSSYVLT
410 420 430 440 450
NDDLEYRHKV SPYVGRTIGA RITKTILRGD VIYDIEQGFP VAPKGQFILK

HQQ
Length:453
Mass (Da):49,545
Last modified:October 23, 2007 - v1
Checksum:iC9FFEF190D58F74D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000802 Genomic DNA. Translation: ABV04969.1.
RefSeqiWP_000006891.1. NC_009800.1.

Genome annotation databases

EnsemblBacteriaiABV04969; ABV04969; EcHS_A0585.
KEGGiecx:EcHS_A0585.
PATRICi18311156. VBIEscCol77814_0572.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000802 Genomic DNA. Translation: ABV04969.1.
RefSeqiWP_000006891.1. NC_009800.1.

3D structure databases

ProteinModelPortaliA7ZXG5.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABV04969; ABV04969; EcHS_A0585.
KEGGiecx:EcHS_A0585.
PATRICi18311156. VBIEscCol77814_0572.

Phylogenomic databases

HOGENOMiHOG000219146.
KOiK01466.
OMAiEMIPPIT.

Enzyme and pathway databases

UniPathwayiUPA00395; UER00653.

Family and domain databases

Gene3Di2.30.40.10. 1 hit.
HAMAPiMF_01645. Hydantoinase. 1 hit.
InterProiIPR017593. Allantoinase.
IPR006680. Amidohydro-rel.
IPR011059. Metal-dep_hydrolase_composite.
IPR032466. Metal_Hydrolase.
[Graphical view]
PfamiPF01979. Amidohydro_1. 1 hit.
[Graphical view]
SUPFAMiSSF51338. SSF51338. 2 hits.
SSF51556. SSF51556. 1 hit.
TIGRFAMsiTIGR03178. allantoinase. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiALLB_ECOHS
AccessioniPrimary (citable) accession number: A7ZXG5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 23, 2007
Last modified: November 2, 2016
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.