Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q1J391 (ALLB_DEIGD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Allantoinase

EC=3.5.2.5
Alternative name(s):
Allantoin-utilizing enzyme
Gene names
Name:allB
Ordered Locus Names:Dgeo_2609
Encoded onPlasmid pDSM11300
OrganismDeinococcus geothermalis (strain DSM 11300) [Complete proteome] [HAMAP]
Taxonomic identifier319795 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus

Protein attributes

Sequence length449 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the conversion of allantoin (5-ureidohydantoin) to allantoic acid by hydrolytic cleavage of the five-member hydantoin ring By similarity. HAMAP-Rule MF_01645

Catalytic activity

(S)-allantoin + H2O = allantoate. HAMAP-Rule MF_01645

Cofactor

Binds 2 zinc ions per subunit By similarity. HAMAP-Rule MF_01645

Pathway

Nitrogen metabolism; (S)-allantoin degradation; allantoate from (S)-allantoin: step 1/1. HAMAP-Rule MF_01645

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_01645

Post-translational modification

Carbamylation allows a single lysine to coordinate two zinc ions By similarity. HAMAP-Rule MF_01645

Sequence similarities

Belongs to the DHOase family. Allantoinase subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 449449Allantoinase HAMAP-Rule MF_01645
PRO_0000317672

Sites

Metal binding591Zinc 1 By similarity
Metal binding611Zinc 1 By similarity
Metal binding1461Zinc 1; via carbamate group By similarity
Metal binding1461Zinc 2; via carbamate group By similarity
Metal binding1821Zinc 2 By similarity
Metal binding2381Zinc 2 By similarity
Metal binding3111Zinc 1 By similarity

Amino acid modifications

Modified residue1461N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1J391 [UniParc].

Last modified June 13, 2006. Version 1.
Checksum: F350C1502A58DDA3

FASTA44948,998
        10         20         30         40         50         60 
MYDLLVRGGQ LVREGGVEQA DLGVVEERIV EIAPELMGDA REELDARGLH VFPGAVDIHV 

        70         80         90        100        110        120 
HFNEPGRTDW EGIRTGSRAL VAGGGTVFAD MPLNSTPPVL DRTTFEAKQQ AAERESYADF 

       130        140        150        160        170        180 
ALWGGLTPRN LDRLPELAEA GAVGFKAFMS HSGLEEFESP DDFTLYEGML QARDLGLIVA 

       190        200        210        220        230        240 
LHAESDAITR GLSTRIRREG GTGVRDYLRS RPAIAEVEAV NRALLLAEET GAKLHLVHLS 

       250        260        270        280        290        300 
TGRAVTLAAE ARARGVDVSI ETCPHYLCFT GEDMERLGAV LKCAPPLRDA SEVDALWQAI 

       310        320        330        340        350        360 
RAGHIDTIGS DHSPSTLDLK ERADFFEVWG GIAGVQSTLT VLLTEGRERG LSLPDIARLS 

       370        380        390        400        410        420 
ARTPAGHFGL AGKGRLEPGA DADLVLVDLD REWVHTPEDL HTRWKFSPYL GRTFRGRVVQ 

       430        440 
TRLRGQTVYA EGRFPHPPQG RFLRPAPAS 

« Hide

References

[1]"Complete sequence of plasmid 1 of Deinococcus geothermalis DSM 11300."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Daly M.J., Fredrickson J.K., Makarova K.S., Gaidamakova E.K., Zhai M., Richardson P.
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 11300.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000358 Genomic DNA. Translation: ABF44043.1.
RefSeqYP_594117.1. NC_008010.2.

3D structure databases

ProteinModelPortalQ1J391.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING319795.Dgeo_2609.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABF44043; ABF44043; Dgeo_2609.
GeneID4073840.
KEGGdge:Dgeo_2609.
PATRIC21621500. VBIDeiGeo41128_0409.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0044.
HOGENOMHOG000219146.
KOK01466.
OMACSPWEGH.
OrthoDBEOG6KHFW6.

Enzyme and pathway databases

BioCycDGEO319795:GHMU-2803-MONOMER.
UniPathwayUPA00395; UER00653.

Family and domain databases

Gene3D2.30.40.10. 1 hit.
HAMAPMF_01645. Hydantoinase.
InterProIPR017593. Allantoinase.
IPR004722. DHOase.
IPR002195. Dihydroorotase_CS.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
SUPFAMSSF51338. SSF51338. 2 hits.
TIGRFAMsTIGR03178. allantoinase. 1 hit.
TIGR00857. pyrC_multi. 1 hit.
ProtoNetSearch...

Entry information

Entry nameALLB_DEIGD
AccessionPrimary (citable) accession number: Q1J391
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: June 13, 2006
Last modified: May 14, 2014
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways