Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9KAH8 (ALLB_BACHD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:BH2309
OrganismBacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) [Complete proteome] [HAMAP]
Taxonomic identifier272558 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length438 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 term3D-structure
Complete 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 – 438438Allantoinase HAMAP-Rule MF_01645
PRO_0000317670

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 binding2421Zinc 2 By similarity
Metal binding3151Zinc 1 By similarity

Amino acid modifications

Modified residue1501N6-carboxylysine By similarity

Secondary structure

.................................................................................... 438
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9KAH8 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 47A24DD790AF947F

FASTA43848,542
        10         20         30         40         50         60 
MKRFDLIIRS STVVTETTTY RADVAIRNGI VSAITEPGSI SSDDGPAIDG TGLHLFPGMV 

        70         80         90        100        110        120 
DVHVHFNEPG RTEWEGFASG SKSLAAGGVT TYFDMPLNSN PPTITREELD KKRQLANEKS 

       130        140        150        160        170        180 
LVDYRFWGGL VPGNIDHLQD LHDGGVIGFK AFMSECGTDD FQFSHDETLL KGMKKIAALG 

       190        200        210        220        230        240 
SILAVHAESN EMVNALTTIA IEEQRLTVKD YSEARPIVSE LEAVERILRF AQLTCCPIHI 

       250        260        270        280        290        300 
CHVSSRKVLK RIKQAKGEGV NVSVETCPHY LLFSLDEFAE IGYLAKCAPP LRERQEVEDL 

       310        320        330        340        350        360 
WDGLMAGEID LISSDHSPSL PQMKTGKTIF EVWGGIAGCQ NTLAVMLTEG YHKRKMPLTQ 

       370        380        390        400        410        420 
IVQLLSTEPA KRFGLYPQKG TIQVGAEASF TLIDLNESYT LNASDLYYRH PISPYVGQRF 

       430 
RGKVKHTICQ GKHVYQDH 

« Hide

References

[1]"Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis."
Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.
Nucleic Acids Res. 28:4317-4331(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000004 Genomic DNA. Translation: BAB06028.1.
PIRE83938.
RefSeqNP_243175.1. NC_002570.2.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3HM7X-ray2.60A/B/C/D/E/F2-438[»]
ProteinModelPortalQ9KAH8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272558.BH2309.

Protocols and materials databases

DNASU892154.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB06028; BAB06028; BAB06028.
GeneID892154.
KEGGbha:BH2309.
PATRIC18941796. VBIBacHal18977_2411.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0044.
HOGENOMHOG000219146.
KOK01466.
OMACSPWEGH.
OrthoDBEOG6KHFW6.

Enzyme and pathway databases

BioCycBHAL272558:GJC5-2393-MONOMER.
UniPathwayUPA00395; UER00653.

Family and domain databases

Gene3D2.30.40.10. 1 hit.
HAMAPMF_01645. Hydantoinase.
InterProIPR017593. Allantoinase.
IPR002195. Dihydroorotase_CS.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
SUPFAMSSF51338. SSF51338. 2 hits.
TIGRFAMsTIGR03178. allantoinase. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ9KAH8.

Entry information

Entry nameALLB_BACHD
AccessionPrimary (citable) accession number: Q9KAH8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 1, 2000
Last modified: May 14, 2014
This is version 86 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways