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Q82LL4 (ALLB_STRAW) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 75. 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, sav1996
Ordered Locus Names:SAV_1996
OrganismStreptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680) [Complete proteome] [HAMAP]
Taxonomic identifier227882 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length445 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 – 445445Allantoinase HAMAP-Rule MF_01645
PRO_0000317687

Sites

Metal binding631Zinc 1 By similarity
Metal binding651Zinc 1 By similarity
Metal binding1501Zinc 1; via carbamate group By similarity
Metal binding1501Zinc 2; via carbamate group By similarity
Metal binding1861Zinc 2 By similarity
Metal binding2381Zinc 2 By similarity
Metal binding3111Zinc 1 By similarity

Amino acid modifications

Modified residue1501N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q82LL4 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 3C75AF72F136425C

FASTA44547,582
        10         20         30         40         50         60 
MSDVELVLRS TRVITPEGTR PAAVAVAAGK ITAVLPHDAE VPAGARLEDL GDDVLLPGLV 

        70         80         90        100        110        120 
DTHVHVNDPG RTHWEGFWTA TRAAAAGGIT TLVDMPLNSL PPTTTVGNLR TKRDVAADKA 

       130        140        150        160        170        180 
HIDVGFWGGA LPDNVKDLRP LHDAGVFGFK AFLSPSGVDE FPELDQERLA RSMAEIAGFG 

       190        200        210        220        230        240 
GLLIVHAEDP HHLAAAPQRG GPRYTDFLAS RPRDAEDTAI ANLLAQAKRL NARVHVLHLS 

       250        260        270        280        290        300 
SSDALPLIAG AKAEGVRVTV ETCPHYLTLT AEEVPDGASE FKCCPPIREA ANQDLLWQAL 

       310        320        330        340        350        360 
ADGTIDCVVT DHSPSTADLK TDDFATAWGG ISGLQLSLPA IWTEARRRGH SLEDVVRWMS 

       370        380        390        400        410        420 
ARTARLVGLA QKGAIEAGRD ADFAVLAPDE TFTVDPAALQ HRNRVTAYAG KTLSGVVKST 

       430        440 
WLRGERIMAD GEFTEPKGRL LSREP 

« Hide

References

[1]"Genome sequence of an industrial microorganism Streptomyces avermitilis: deducing the ability of producing secondary metabolites."
Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M., Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T., Sakaki Y., Hattori M.
Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680.
[2]"Complete genome sequence and comparative analysis of the industrial microorganism Streptomyces avermitilis."
Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T., Sakaki Y., Hattori M., Omura S.
Nat. Biotechnol. 21:526-531(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000030 Genomic DNA. Translation: BAC69707.1.
RefSeqNP_823172.1. NC_003155.4.

3D structure databases

ProteinModelPortalQ82LL4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING227882.SAV_1996.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC69707; BAC69707; SAV_1996.
GeneID1210332.
KEGGsma:SAV_1996.
PATRIC23717441. VBIStrAve112782_2134.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0044.
HOGENOMHOG000219146.
KOK01466.
OMARWMSTAP.
OrthoDBEOG6KHFW6.

Enzyme and pathway databases

BioCycSAVE227882:GJU1-2009-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_STRAW
AccessionPrimary (citable) accession number: Q82LL4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: June 1, 2003
Last modified: May 14, 2014
This is version 75 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