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Q9KAH8 (ALLB_BACHD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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 lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

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 MF_01645

Catalytic activity

(S)-allantoin + H2O = allantoate. HAMAP MF_01645

Cofactor

Binds 2 zinc ions per subunit By similarity. HAMAP MF_01645

Pathway

Nitrogen metabolism; (S)-allantoin degradation; allantoate from (S)-allantoin: step 1/1. HAMAP MF_01645

Subunit structure

Homotetramer By similarity. HAMAP MF_01645

Post-translational modification

Carbamylation allows a single lysine to coordinate two zinc ions By similarity. HAMAP MF_01645

Sequence similarities

Belongs to the DHOase family. Allantoinase subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 438438Allantoinase HAMAP 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

1 ................................................................................ 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: 11058132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.
+Additional computationally mapped references.

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...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000051936; EBBACP00000050575; EBBACG00000051927.
GeneID892154.
GenomeReviewsGene locus BH2309 in contig BA000004_GR.
KEGGbha:BH2309.
NMPDRfig|272558.1.peg.2309.
PATRIC18941796. VBIBacHal18977_2411.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000001626.
HOGENOMHBG724623.
PhylomeDBQ9KAH8.
ProtClustDBPRK06189.

Enzyme and pathway databases

BioCycBHAL272558:BH2309-MONOMER.

Family and domain databases

HAMAPMF_01645. Hydantoinase.
[Tree]
InterProIPR017593. Allantoinase.
IPR006680. Amidohydro_1.
IPR002195. Dihydroorotase_CS.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
KOK01466.
PfamPF01979. Amidohydro_1. 1 hit.
[Graphical view]
SUPFAMSSF51338. Metalo_hydrolase. 1 hit.
TIGRFAMsTIGR03178. Allantoinase. 1 hit.
ProtoNetSearch...

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: January 25, 2012
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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