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B8G120 (ALLB_DESHD) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 36. 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:Dhaf_1177
OrganismDesulfitobacterium hafniense (strain DCB-2 / DSM 10664) [Complete proteome] [HAMAP]
Taxonomic identifier272564 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesPeptococcaceaeDesulfitobacterium

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.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-HAMAP

purine nucleobase metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionallantoinase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

cobalt ion binding

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 449449Allantoinase HAMAP-Rule MF_01645
PRO_1000186916

Sites

Metal binding611Zinc 1 By similarity
Metal binding631Zinc 1 By similarity
Metal binding1481Zinc 1; via carbamate group By similarity
Metal binding1481Zinc 2; via carbamate group By similarity
Metal binding1841Zinc 2 By similarity
Metal binding2401Zinc 2 By similarity
Metal binding3131Zinc 1 By similarity

Amino acid modifications

Modified residue1481N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B8G120 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: 1FBD355BCE3138D3

FASTA44949,300
        10         20         30         40         50         60 
MSHYDLILRN GNVVCPDGVR KADIAVSDGK IVLIAEEIPG DAKEIIDAAG KHIFPGITDG 

        70         80         90        100        110        120 
HVHFNDPGRT EWETITTGSS ALAAGGGVAY FDMPLNCSPC TLDAVNFNNK LAVAQKDSLV 

       130        140        150        160        170        180 
DYGFWGGLTS ANLDKLDELA ECGVIGFKAF ACHSGIDEFP RMDDYTALVG MEKLAKLGLP 

       190        200        210        220        230        240 
LMVHCENAEI TKELTELSLA NNRTGVRDYF AARPPITEIE NVSRMITFAE ETGCKLIIAH 

       250        260        270        280        290        300 
ISTAKAVELV AQARARGVDV YCETIGHYLY LTGDDVERLG TVAKCSPPIR DGENQLQMWG 

       310        320        330        340        350        360 
RLFNDNIAFV SSDHSPCDPK LKNGEFMRVW GGISACQTTL QGLLTHAYHD RKFPLVKIAQ 

       370        380        390        400        410        420 
LTAQHVNEIF KIKDKGQIAL GYDADFALVD LDHEFTLQAE DLFYKHKVSP YVGDRFRGSV 

       430        440 
SQTILRGTTI YKDGKIVSQP IGKHLRPHQ 

« Hide

References

[1]"Complete sequence of Desulfitobacterium hafniense DCB-2."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Kuske C.R., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Ovchinnikova G., Madsen T., Christiansen N., Ahring B., Marsh T., Harzman C., Davis J.K., Kim S.-H., Tiedje J.M.
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DCB-2 / DSM 10664.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001336 Genomic DNA. Translation: ACL19235.1.
RefSeqYP_002457671.1. NC_011830.1.

3D structure databases

ProteinModelPortalB8G120.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272564.Dhaf_1177.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACL19235; ACL19235; Dhaf_1177.
GeneID7258147.
KEGGdhd:Dhaf_1177.
PATRIC21660051. VBIDesHaf15223_1226.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0044.
HOGENOMHOG000219146.
KOK01466.
OMAHAEMIPP.
OrthoDBEOG6KHFW6.
ProtClustDBCLSK2466964.

Enzyme and pathway databases

BioCycDHAF272564:GCV8-1203-MONOMER.
UniPathwayUPA00395; UER00653.

Family and domain databases

HAMAPMF_01645. Hydantoinase.
InterProIPR017593. Allantoinase.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
SUPFAMSSF51338. SSF51338. 2 hits.
TIGRFAMsTIGR03178. allantoinase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameALLB_DESHD
AccessionPrimary (citable) accession number: B8G120
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: February 19, 2014
This is version 36 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