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Reviewed, UniProtKB/Swiss-Prot Q1J391 (ALLB_DEIGD)

Last modified November 3, 2009. Version 27. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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.
Sequence processingThe displayed sequence is not processed.
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.

Catalytic activity

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

Cofactor

Binds 2 zinc ions per subunit By similarity.

Pathway

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

Subunit structure

Homotetramer By similarity.

Post-translational modification

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

Sequence similarities

Belongs to the DHOase family. Allantoinase subfamily.

Ontologies

Keywords
   Biological processPurine metabolism
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
   Technical termComplete proteome
Plasmid
Gene Ontology (GO)
   Biological processallantoin catabolic process

Inferred from electronic annotation. Source: HAMAP

purine base metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionallantoinase activity

Inferred from electronic annotation. Source: HAMAP

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 449449Allantoinase HAMAP 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
Q1J391-1 [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].

Cross-references

Sequence databases

CP000358 Genomic DNA. Translation: ABF44043.1.
RefSeqYP_594117.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ1J391.

Genome annotation databases

GeneID4073840.
GenomeReviewsGene locus Dgeo_2609 in contig CP000358_GR.
KEGGdge:Dgeo_2609.
NMPDRfig|68909.1.peg.21.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ1J391.
OMALKCAPPL.

Enzyme and pathway databases

BioCycDGEO319795:DGEO_2609-MON.

Family and domain databases

HAMAPMF_01645.
[Tree]
InterProIPR017593. Allantoinase.
IPR006680. Amidohydro_1.
IPR004722. DHOmult.
[Graphical view]
PfamPF01979. Amidohydro_1. 1 hit.
[Graphical view]
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: November 3, 2009
This is version 27 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents