Q82LL4 (ALLB_STRAW) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 69.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Allantoinase EC=3.5.2.5 Alternative name(s): Allantoin-utilizing enzyme | ||||||
| Gene names |
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| Organism | Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 227882 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces › ![]() |
Protein attributes
| Sequence length | 445 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred 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. |
| Pathway | Nitrogen metabolism; (S)-allantoin degradation; allantoate from (S)-allantoin: step 1/1. HAMAP-Rule MF_01645 |
| Subunit structure | Homotetramer By similarity. |
| 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 process | Purine metabolism |
| Ligand | Metal-binding Zinc |
| Molecular function | Hydrolase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | allantoin catabolic process Inferred from electronic annotation. Source: HAMAP purine nucleobase metabolic processInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular_function | allantoinase activity Inferred from electronic annotation. Source: HAMAP cobalt ion bindingInferred from electronic annotation. Source: InterPro zinc ion bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 445 | 445 | Allantoinase HAMAP-Rule MF_01645 | PRO_0000317687 | |||||
Sites | |||||||||
| Metal binding | 63 | 1 | Zinc 1 By similarity | ||||||
| Metal binding | 65 | 1 | Zinc 1 By similarity | ||||||
| Metal binding | 150 | 1 | Zinc 1; via carbamate group By similarity | ||||||
| Metal binding | 150 | 1 | Zinc 2; via carbamate group By similarity | ||||||
| Metal binding | 186 | 1 | Zinc 2 By similarity | ||||||
| Metal binding | 238 | 1 | Zinc 2 By similarity | ||||||
| Metal binding | 311 | 1 | Zinc 1 By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 150 | 1 | N6-carboxylysine By similarity | ||||||
Sequences
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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. |
| RefSeq | NP_823172.1. NC_003155.4. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1GKR based on UniProtKB P81006. |
| ProteinModelPortal | Q82LL4. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 227882.SAV_1996. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | BAC69707; BAC69707; SAV_1996. |
| GeneID | 1210332. |
| KEGG | sma:SAV_1996. |
| PATRIC | 23717441. VBIStrAve112782_2134. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0044. |
| HOGENOM | HOG000219146. |
| KO | K01466. |
| OMA | DMPLNSF. |
| ProtClustDB | CLSK2519400. |
Enzyme and pathway databases | |
| BioCyc | SAVE227882:GJU1-2009-MONOMER. |
| UniPathway | UPA00395; UER00653. |
Family and domain databases | |
| HAMAP | MF_01645. Hydantoinase. |
| InterPro | IPR017593. Allantoinase. IPR011059. Metal-dep_hydrolase_composite. [Graphical view] |
| SUPFAM | SSF51338. Metalo_hydrolase. 1 hit. |
| TIGRFAMs | TIGR03178. allantoinase. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | ALLB_STRAW | ||||||||
| Accession | Primary (citable) accession number: Q82LL4 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
