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Protein

Allantoinase

Gene

allB

Organism
Salmonella dublin (strain CT_02021853)
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

Pathway:i(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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi59 – 591Zinc 1UniRule annotation
Metal bindingi61 – 611Zinc 1UniRule annotation
Metal bindingi146 – 1461Zinc 1; via carbamate groupUniRule annotation
Metal bindingi146 – 1461Zinc 2; via carbamate groupUniRule annotation
Metal bindingi186 – 1861Zinc 2UniRule annotation
Metal bindingi242 – 2421Zinc 2UniRule annotation
Metal bindingi315 – 3151Zinc 1UniRule annotation

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

BioCyciSENT439851:GH2Z-563-MONOMER.
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:SeD_A0571
OrganismiSalmonella dublin (strain CT_02021853)
Taxonomic identifieri439851 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 453453AllantoinasePRO_1000186927Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei146 – 1461N6-carboxylysineUniRule annotation

Post-translational modificationi

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

Proteomic databases

PRIDEiB5FLN3.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliB5FLN3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the DHOase family. Allantoinase subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG0044.
HOGENOMiHOG000219146.
KOiK01466.
OMAiVYLAEFT.
OrthoDBiEOG6KHFW6.

Family and domain databases

Gene3Di2.30.40.10. 1 hit.
HAMAPiMF_01645. Hydantoinase.
InterProiIPR017593. Allantoinase.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
SUPFAMiSSF51338. SSF51338. 2 hits.
TIGRFAMsiTIGR03178. allantoinase. 1 hit.

Sequencei

Sequence statusi: Complete.

B5FLN3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFDLIIKNG TVILENEARV IDIAVQGGKI AAIGENLGEA KNVLDATGLI
60 70 80 90 100
VSPGMVDAHT HISEPGRTHW EGYETGTRAA AKGGITTMIE MPLNQLPATV
110 120 130 140 150
DRETIELKFD AAKGKLTIDA AQLGGLVSYN LDRLHELDEV GVVGFKCFVA
160 170 180 190 200
TCGDRGIDND FRDVNDWQFY KGAQKLGEMD QTVLVHCENA LICDELGEEA
210 220 230 240 250
KREGRVTAHD YVASRPVFTE VEAIRRVLYL AKAAGCRLHV CHISSPEGVE
260 270 280 290 300
EVTRARQEGQ DVTCESCPHY FVLDTDQFEE IGTLAKCSPP IRDQENQKGM
310 320 330 340 350
WEKLFNGEID CLVSDHSPCP PEMKAGNIMQ AWGGIAGLQN CMDVMFDEAV
360 370 380 390 400
QKRGMSLPMF GKLMATNAAD IFGLKHKGRI APGKDADLVF IQPDSSYVLK
410 420 430 440 450
NEDLEYRHKV SPYVGRTIGA RITKTILRGD VIYDIEHGFP VPPKGQFILK

HQQ
Length:453
Mass (Da):49,887
Last modified:October 14, 2008 - v1
Checksum:i223BFADF6257891E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001144 Genomic DNA. Translation: ACH74684.1.
RefSeqiWP_000006865.1. NC_011205.1.
YP_002214478.1. NC_011205.1.

Genome annotation databases

EnsemblBacteriaiACH74684; ACH74684; SeD_A0571.
KEGGised:SeD_A0571.
PATRICi18489356. VBISalEnt111443_0645.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001144 Genomic DNA. Translation: ACH74684.1.
RefSeqiWP_000006865.1. NC_011205.1.
YP_002214478.1. NC_011205.1.

3D structure databases

ProteinModelPortaliB5FLN3.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiB5FLN3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACH74684; ACH74684; SeD_A0571.
KEGGised:SeD_A0571.
PATRICi18489356. VBISalEnt111443_0645.

Phylogenomic databases

eggNOGiCOG0044.
HOGENOMiHOG000219146.
KOiK01466.
OMAiVYLAEFT.
OrthoDBiEOG6KHFW6.

Enzyme and pathway databases

UniPathwayiUPA00395; UER00653.
BioCyciSENT439851:GH2Z-563-MONOMER.

Family and domain databases

Gene3Di2.30.40.10. 1 hit.
HAMAPiMF_01645. Hydantoinase.
InterProiIPR017593. Allantoinase.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
SUPFAMiSSF51338. SSF51338. 2 hits.
TIGRFAMsiTIGR03178. allantoinase. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Comparative genomics of 28 Salmonella enterica isolates: evidence for CRISPR-mediated adaptive sublineage evolution."
    Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G., Leclerc J.E., Ravel J., Cebula T.A.
    J. Bacteriol. 193:3556-3568(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CT_02021853.

Entry informationi

Entry nameiALLB_SALDC
AccessioniPrimary (citable) accession number: B5FLN3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: October 14, 2008
Last modified: July 22, 2015
This is version 49 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

External Data

Dasty 3

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 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.