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Q5WBJ6

- ALLB_BACSK

UniProt

Q5WBJ6 - ALLB_BACSK

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Protein
Allantoinase
Gene
allB, pucH, ABC3732
Organism
Bacillus clausii (strain KSM-K16)
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 bindingi185 – 1851Zinc 2 By similarity
Metal bindingi239 – 2391Zinc 2 By similarity
Metal bindingi312 – 3121Zinc 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

BioCyciBCLA66692:GHMP-3813-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
Synonyms:pucH
Ordered Locus Names:ABC3732
OrganismiBacillus clausii (strain KSM-K16)
Taxonomic identifieri66692 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001168: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 448448AllantoinaseUniRule annotation
PRO_0000317669Add
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

Interactioni

Subunit structurei

Homotetramer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi66692.ABC3732.

Structurei

3D structure databases

ProteinModelPortaliQ5WBJ6.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0044.
HOGENOMiHOG000219146.
KOiK01466.
OMAiCSPWEGH.
OrthoDBiEOG6KHFW6.

Family and domain databases

Gene3Di2.30.40.10. 1 hit.
HAMAPiMF_01645. Hydantoinase.
InterProiIPR017593. Allantoinase.
IPR013108. Amidohydro_3.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
PfamiPF07969. Amidohydro_3. 1 hit.
[Graphical view]
SUPFAMiSSF51338. SSF51338. 2 hits.
TIGRFAMsiTIGR03178. allantoinase. 1 hit.

Sequencei

Sequence statusi: Complete.

Q5WBJ6-1 [UniParc]FASTAAdd to Basket

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MLDLCITGGR VVLPSGVEET DVGIQAGKIA RIGPINKKEA RCIMNANGQY    50
VFPGAVDTHV HFSEPGRTEW EGFFTGSRSL AAGGTTTYVE MPLNALPATT 100
NRANLQRKLE AAKGQNYVDY SFYGGLVPTN LHELADLSAS GVVAFKCFLS 150
PCGSDIPGDF RNVDLNGLRA GMRLLAEKGQ LLCVHAEDPS MISQLEAKLL 200
SPVGADAYVA SRPVEAEVKA VCDTLAAARE TGCRIHFVHI SSAAAIEAIE 250
RAKEEGVDVT VESCPHYFLL SAEELAELGP LAKCQPPLRP KQEQAKLWAC 300
LLDGQIDWLA SDHSPCTPDL KDGDFLTAWG GISGCQNNID IMFDAAVKRR 350
GMPPEQLARL IATNPAKRMN LREKGEIAIG KDADFAFVDD RQSYTLTKEQ 400
LYYKNKHSPY VGRTIGCKVR RVLLRGQTIY TEEKGIIGKP SGELLHIH 448
Length:448
Mass (Da):48,711
Last modified:November 23, 2004 - v1
Checksum:i903BD489E7C7ACF5
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP006627 Genomic DNA. Translation: BAD66264.1.
RefSeqiYP_177225.1. NC_006582.1.

Genome annotation databases

EnsemblBacteriaiBAD66264; BAD66264; ABC3732.
GeneIDi3202800.
KEGGibcl:ABC3732.
PATRICi18927260. VBIBacCla58185_3978.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP006627 Genomic DNA. Translation: BAD66264.1 .
RefSeqi YP_177225.1. NC_006582.1.

3D structure databases

ProteinModelPortali Q5WBJ6.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 66692.ABC3732.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAD66264 ; BAD66264 ; ABC3732 .
GeneIDi 3202800.
KEGGi bcl:ABC3732.
PATRICi 18927260. VBIBacCla58185_3978.

Phylogenomic databases

eggNOGi COG0044.
HOGENOMi HOG000219146.
KOi K01466.
OMAi CSPWEGH.
OrthoDBi EOG6KHFW6.

Enzyme and pathway databases

UniPathwayi UPA00395 ; UER00653 .
BioCyci BCLA66692:GHMP-3813-MONOMER.

Family and domain databases

Gene3Di 2.30.40.10. 1 hit.
HAMAPi MF_01645. Hydantoinase.
InterProi IPR017593. Allantoinase.
IPR013108. Amidohydro_3.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view ]
Pfami PF07969. Amidohydro_3. 1 hit.
[Graphical view ]
SUPFAMi SSF51338. SSF51338. 2 hits.
TIGRFAMsi TIGR03178. allantoinase. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "The complete genome sequence of the alkaliphilic Bacillus clausii KSM-K16."
    Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y., Kawai S., Ito S., Horikoshi K.
    Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: KSM-K16.

Entry informationi

Entry nameiALLB_BACSK
AccessioniPrimary (citable) accession number: Q5WBJ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: November 23, 2004
Last modified: May 14, 2014
This is version 64 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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