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B5FLN3

- ALLB_SALDC

UniProt

B5FLN3 - ALLB_SALDC

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Protein

Allantoinase

Gene
allB, SeD_A0571
Organism
Salmonella dublin (strain CT_02021853)
Status
Reviewed - 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 By similarity.UniRule annotation

Catalytic activityi

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

Cofactori

Binds 2 zinc ions per subunit By similarity.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi59 – 591Zinc 1 By similarity
Metal bindingi61 – 611Zinc 1 By similarity
Metal bindingi146 – 1461Zinc 1; via carbamate group By similarity
Metal bindingi146 – 1461Zinc 2; via carbamate group By similarity
Metal bindingi186 – 1861Zinc 2 By similarity
Metal bindingi242 – 2421Zinc 2 By similarity
Metal bindingi315 – 3151Zinc 1 By similarity

GO - Molecular functioni

  1. allantoinase activity Source: UniProtKB-HAMAP
  2. cobalt ion binding Source: InterPro
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. allantoin catabolic process Source: UniProtKB-HAMAP
  2. purine nucleobase metabolic process Source: UniProtKB-KW
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:
Allantoinase (EC:3.5.2.5)
Alternative name(s):
Allantoin-utilizing enzyme
Gene namesi
Name:allB
Ordered Locus Names:SeD_A0571
OrganismiSalmonella dublin (strain CT_02021853)
Taxonomic identifieri439851 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
ProteomesiUP000008322: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 453453AllantoinaseUniRule annotationPRO_1000186927Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei146 – 1461N6-carboxylysine By similarity

Post-translational modificationi

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

Proteomic databases

PRIDEiB5FLN3.

Interactioni

Subunit structurei

Homotetramer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi439851.SeD_A0571.

Structurei

3D structure databases

ProteinModelPortaliB5FLN3.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0044.
HOGENOMiHOG000219146.
OMAiCSPWEGH.
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

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MSFDLIIKNG TVILENEARV IDIAVQGGKI AAIGENLGEA KNVLDATGLI    50
VSPGMVDAHT HISEPGRTHW EGYETGTRAA AKGGITTMIE MPLNQLPATV 100
DRETIELKFD AAKGKLTIDA AQLGGLVSYN LDRLHELDEV GVVGFKCFVA 150
TCGDRGIDND FRDVNDWQFY KGAQKLGEMD QTVLVHCENA LICDELGEEA 200
KREGRVTAHD YVASRPVFTE VEAIRRVLYL AKAAGCRLHV CHISSPEGVE 250
EVTRARQEGQ DVTCESCPHY FVLDTDQFEE IGTLAKCSPP IRDQENQKGM 300
WEKLFNGEID CLVSDHSPCP PEMKAGNIMQ AWGGIAGLQN CMDVMFDEAV 350
QKRGMSLPMF GKLMATNAAD IFGLKHKGRI APGKDADLVF IQPDSSYVLK 400
NEDLEYRHKV SPYVGRTIGA RITKTILRGD VIYDIEHGFP VPPKGQFILK 450
HQQ 453
Length:453
Mass (Da):49,887
Last modified:October 14, 2008 - v1
Checksum:i223BFADF6257891E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001144 Genomic DNA. Translation: ACH74684.1.
RefSeqiYP_002214478.1. NC_011205.1.

Genome annotation databases

EnsemblBacteriaiACH74684; ACH74684; SeD_A0571.
PATRICi18489356. VBISalEnt111443_0645.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001144 Genomic DNA. Translation: ACH74684.1 .
RefSeqi YP_002214478.1. NC_011205.1.

3D structure databases

ProteinModelPortali B5FLN3.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 439851.SeD_A0571.

Proteomic databases

PRIDEi B5FLN3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACH74684 ; ACH74684 ; SeD_A0571 .
PATRICi 18489356. VBISalEnt111443_0645.

Phylogenomic databases

eggNOGi COG0044.
HOGENOMi HOG000219146.
OMAi CSPWEGH.
OrthoDBi EOG6KHFW6.

Enzyme and pathway databases

UniPathwayi UPA00395 ; UER00653 .
BioCyci SENT439851:GH2Z-563-MONOMER.

Family and domain databases

Gene3Di 2.30.40.10. 1 hit.
HAMAPi MF_01645. Hydantoinase.
InterProi IPR017593. Allantoinase.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view ]
SUPFAMi SSF51338. SSF51338. 2 hits.
TIGRFAMsi TIGR03178. allantoinase. 1 hit.
ProtoNeti Search...

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 9, 2014
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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