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B5BD11

- ALLB_SALPK

UniProt

B5BD11 - ALLB_SALPK

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Protein

Allantoinase

Gene
allB, SSPA2045
Organism
Salmonella paratyphi A (strain AKU_12601)
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

BioCyciSENT554290:GJDA-2192-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:SSPA2045
OrganismiSalmonella paratyphi A (strain AKU_12601)
Taxonomic identifieri554290 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
ProteomesiUP000001869: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 453453AllantoinaseUniRule annotationPRO_1000186932Add
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

PRIDEiB5BD11.

Interactioni

Subunit structurei

Homotetramer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi554290.SSPA2045.

Structurei

3D structure databases

ProteinModelPortaliB5BD11.

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.

B5BD11-1 [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:September 23, 2008 - v1
Checksum:i223BFADF6257891E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
FM200053 Genomic DNA. Translation: CAR60253.1.
RefSeqiYP_002142882.1. NC_011147.1.

Genome annotation databases

EnsemblBacteriaiCAR60253; CAR60253; SSPA2045.
PATRICi32344257. VBISalEnt134303_2345.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
FM200053 Genomic DNA. Translation: CAR60253.1 .
RefSeqi YP_002142882.1. NC_011147.1.

3D structure databases

ProteinModelPortali B5BD11.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 554290.SSPA2045.

Proteomic databases

PRIDEi B5BD11.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAR60253 ; CAR60253 ; SSPA2045 .
PATRICi 32344257. VBISalEnt134303_2345.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00395 ; UER00653 .
BioCyci SENT554290:GJDA-2192-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. "Pseudogene accumulation in the evolutionary histories of Salmonella enterica serovars Paratyphi A and Typhi."
    Holt K.E., Thomson N.R., Wain J., Langridge G.C., Hasan R., Bhutta Z.A., Quail M.A., Norbertczak H., Walker D., Simmonds M., White B., Bason N., Mungall K., Dougan G., Parkhill J.
    BMC Genomics 10:36-36(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: AKU_12601.

Entry informationi

Entry nameiALLB_SALPK
AccessioniPrimary (citable) accession number: B5BD11
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: September 23, 2008
Last modified: May 14, 2014
This is version 40 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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