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P40757 (ALN_LITCT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 81. 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, mitochondrial

EC=3.5.2.5
Gene names
Name:ALN
OrganismLithobates catesbeiana (American bullfrog) (Rana catesbeiana)
Taxonomic identifier8400 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraNeobatrachiaRanoideaRanidaeRanaAquarana

Protein attributes

Sequence length484 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

(S)-allantoin + H2O = allantoate.

Cofactor

Binds 2 zinc ions per subunit By similarity.

Pathway

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

Subunit structure

Homotetramer By similarity.

Subcellular location

Mitochondrion.

Tissue specificity

Liver and kidney.

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
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processallantoin catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionallantoinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

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

Transit peptide1 – ?Mitochondrion Potential
Chain? – 484Allantoinase, mitochondrialPRO_0000007371

Sites

Metal binding761Zinc 1 By similarity
Metal binding781Zinc 1 By similarity
Metal binding1631Zinc 1; via carbamate group By similarity
Metal binding1631Zinc 2; via carbamate group By similarity
Metal binding1991Zinc 2 By similarity
Metal binding2511Zinc 2 By similarity
Metal binding3241Zinc 1 By similarity

Amino acid modifications

Modified residue1631N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P40757 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: A2DC377B850DC402

FASTA48453,257
        10         20         30         40         50         60 
MALKSKPGIM NITPGSKISV IRSKRVIQAN TISSCDIIIS DGKISSVLAW GKHVTSGAKL 

        70         80         90        100        110        120 
LDVGDLVVMA GIIDPHVHVN EPGRTDWEGY RTATLAAAAG GITAIVDMPL NSLPPTTSVT 

       130        140        150        160        170        180 
NFHTKLQAAK RQCYVDVAFW GGVIPDNQVE LIPMLQAGVA GFKCFLINSG VPEFPHVSVT 

       190        200        210        220        230        240 
DLHTAMSELQ GTNSVLLFHA ELEIAKPAPE IGDSTLYQTF LDSRPDDMEI AAVQLVADLC 

       250        260        270        280        290        300 
QQYKVRCHIV HLSSAQSLTI IRKAKEAGAP LTVETTHHYL SLSSEHIPPG ATYFKCCPPV 

       310        320        330        340        350        360 
RGHRNKEALW NALLQGHIDM VVSDHSPCTP DLKLLKEGDY MKAWGGISSL QFGLPLFWTS 

       370        380        390        400        410        420 
ARTRGFSLTD VSQLLSSNTA KLCGLGIVKE PLKWVMMLIW SSGILTKSFR CKKMIFITRI 

       430        440        450        460        470        480 
SSPHIWDSFF KEKSWLLLFE GLLFISKGSM LPNQLENLFL YTLWSLVKPV HPVHPIIRKN 


LPHI 

« Hide

References

[1]"Amphibian allantoinase. Molecular cloning, tissue distribution, and functional expression."
Hayashi S., Jain S., Chu R., Alvares K., Xu B., Erfurth F., Usuda N., Rao M.S., Reddy S.K., Noguchi T., Reddy J.K., Yeldandi A.Y.
J. Biol. Chem. 269:12269-12276(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 365-381.
Tissue: Liver.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U03471 mRNA. Translation: AAA19116.1.
PIRA53595.

3D structure databases

ProteinModelPortalP40757.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG004211.

Enzyme and pathway databases

UniPathwayUPA00395; UER00653.

Family and domain databases

Gene3D2.30.40.10. 1 hit.
InterProIPR017593. Allantoinase.
IPR002195. Dihydroorotase_CS.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
SUPFAMSSF51338. SSF51338. 1 hit.
TIGRFAMsTIGR03178. allantoinase. 1 hit.
PROSITEPS00482. DIHYDROOROTASE_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameALN_LITCT
AccessionPrimary (citable) accession number: P40757
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: April 16, 2014
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways