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Q65LN0 (ALLB_BACLD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 72. 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
Synonyms:pucH
Ordered Locus Names:BLi01126, BL01094
OrganismBacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP]
Taxonomic identifier279010 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length454 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 – 454454Allantoinase HAMAP-Rule MF_01645
PRO_0000317671

Sites

Metal binding591Zinc 1 By similarity
Metal binding611Zinc 1 By similarity
Metal binding1501Zinc 1; via carbamate group By similarity
Metal binding1501Zinc 2; via carbamate group By similarity
Metal binding1901Zinc 2 By similarity
Metal binding2461Zinc 2 By similarity
Metal binding3191Zinc 1 By similarity

Amino acid modifications

Modified residue1501N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q65LN0 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: DE1502556AD04420

FASTA45449,488
        10         20         30         40         50         60 
MNFDSIIKNG LVILENGEQE VEVGIKDGKI AAIGQDLGTS AKIIDAKGSI VSPGMIDAHV 

        70         80         90        100        110        120 
HITEPGGGYR DEWEGYDTGT RAAAKGGVTT FIEMPLNQVP ATVDEESIQE KFKAGKGKLS 

       130        140        150        160        170        180 
VDVASYGGLV PFDLDGGIQE LDSNGVVAYK CFLATCGDRS IEGDFMNVDD YSLYEGMKQI 

       190        200        210        220        230        240 
AKTGKILSIH AENAAITDKL GEIASKNGET SLRAYVDSRP VFTEVEPIRK IILFAKETGC 

       250        260        270        280        290        300 
RVHIVHIACE EGVDEIVKAQ QEGVDITCET CTHYLYFYKE ELDHIGPVVK CSPPIREQSR 

       310        320        330        340        350        360 
LEGMWNRVLN GDISFVTSDH SPCTPDLKAT DNAFEAWGGI AGLQNNVDVL FDEGVQKRNM 

       370        380        390        400        410        420 
PLSKFAAIIA TNPAKRFNLA SKGSIAVGKD ADFVFIKKDA PYELKAEDLA YRHKISPYIG 

       430        440        450 
RKIGAQVVKT ILRGVEIYDK EKGISNEKVG RFIP 

« Hide

References

[1]"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential."
Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.
J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.
[2]"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species."
Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. expand/collapse author list , Galleron N., Ehrlich S.D., Berka R.M.
Genome Biol. 5:R77.1-R77.12(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000002 Genomic DNA. Translation: AAU22686.1.
AE017333 Genomic DNA. Translation: AAU40034.1.
RefSeqYP_006712506.1. NC_006322.1.
YP_078324.1. NC_006270.3.

3D structure databases

ProteinModelPortalQ65LN0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING279010.BL01094.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAU22686; AAU22686; BL01094.
AAU40034; AAU40034; BLi01126.
GeneID3030063.
3098142.
KEGGbld:BLi01126.
bli:BL01094.
PATRIC18947811. VBIBacLic203714_1110.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0044.
HOGENOMHOG000219146.
KOK01466.
OMACSPWEGH.
OrthoDBEOG6KHFW6.

Enzyme and pathway databases

BioCycBLIC279010:GJ2P-1115-MONOMER.
UniPathwayUPA00395; UER00653.

Family and domain databases

Gene3D2.30.40.10. 1 hit.
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_BACLD
AccessionPrimary (citable) accession number: Q65LN0
Secondary accession number(s): Q62X22
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 25, 2004
Last modified: May 14, 2014
This is version 72 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