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P77671 (ALLB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:glxB3, ybbX
Ordered Locus Names:b0512, JW0500
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length453 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. Ref.1 Ref.5

Catalytic activity

(S)-allantoin + H2O = allantoate. Ref.5

Cofactor

Binds 2 zinc ions per subunit Probable. Can also use nickel, cobalt or manganese. Ref.5 Ref.6

Enzyme regulation

Severely inhibited by copper, and competitively inhibited by dithiothreitol (DTT). Zinc concentrations above 2.5 mM and cobalt or nickel concentrations above 1 mM are inhibitors. Ref.5 Ref.6

Pathway

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

Subunit structure

Homotetramer. Ref.5

Induction

By glyoxylate. Ref.5 Ref.6

Post-translational modification

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

Miscellaneous

The zinc-containing form utilizes only the (S)-isomer of allantoin, whereas the cobalt-containing form prefers the (S)-isomer, but also hydrolyzes the (R)-isomer at about 1/10 the rate.

Sequence similarities

Belongs to the DHOase family. Allantoinase subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=4.2 mM for allantoin (at 40 degrees Celsius and pH 8.0) Ref.5 Ref.6

KM=17.0 mM for allantoin (in zinc-supplemented medium at 37 degrees Celsius and pH 7.4)

KM=19.5 mM for allantoin (in cobalt-supplemented medium at 37 degrees Celsius and pH 7.4)

KM=80.0 mM for allantoin (in nickel-supplemented medium at 37 degrees Celsius and pH 7.4)

Vmax=101 µmol/min/mg enzyme (in zinc-supplemented medium at 37 degrees Celsius and pH 7.4)

Vmax=8.1 µmol/min/mg enzyme (in cobalt-supplemented medium (20mM) at 37 degrees Celsius and pH 7.4)

Vmax=6.7 µmol/min/mg enzyme (at 40 degrees Celsius and pH 8.0)

Vmax=3.9 µmol/min/mg enzyme (in cobalt-supplemented medium (2mM) at 37 degrees Celsius and pH 7.4)

Vmax=0.7 µmol/min/mg enzyme (without added metal at 37 degrees Celsius and pH 7.4)

pH dependence:

Optimum pH is 7.5-8.0. The optimal activity is at pH 8.8 for zinc-containing form and pH 9.0 for cobalt-containing form.

Temperature dependence:

Optimum temperature is 40-45 degrees Celsius.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 453453Allantoinase HAMAP-Rule MF_01645
PRO_0000165942

Sites

Metal binding591Zinc 1 By similarity
Metal binding611Zinc 1 By similarity
Metal binding1461Zinc 1; via carbamate group By similarity
Metal binding1461Zinc 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 residue1461N6-carboxylysine By similarity

Secondary structure

..................................................................................... 453
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P77671 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 5CFE588F94268AB4

FASTA45349,602
        10         20         30         40         50         60 
MSFDLIIKNG TVILENEARV VDIAVKGGKI AAIGQDLGDA KEVMDASGLV VSPGMVDAHT 

        70         80         90        100        110        120 
HISEPGRSHW EGYETGTRAA AKGGITTMIE MPLNQLPATV DRASIELKFD AAKGKLTIDA 

       130        140        150        160        170        180 
AQLGGLVSYN IDRLHELDEV GVVGFKCFVA TCGDRGIDND FRDVNDWQFF KGAQKLGELG 

       190        200        210        220        230        240 
QPVLVHCENA LICDELGEEA KREGRVTAHD YVASRPVFTE VEAIRRVLYL AKVAGCRLHV 

       250        260        270        280        290        300 
CHVSSPEGVE EVTRARQEGQ DVTCESCPHY FVLDTDQFEE IGTLAKCSPP IRDLENQKGM 

       310        320        330        340        350        360 
WEKLFNGEID CLVSDHSPCP PEMKAGNIMK AWGGIAGLQS CMDVMFDEAV QKRGMSLPMF 

       370        380        390        400        410        420 
GKLMATNAAD IFGLQQKGRI APGKDADFVF IQPNSSYVLT NDDLEYRHKV SPYVGRTIGA 

       430        440        450 
RITKTILRGD VIYDIEQGFP VAPKGQFILK HQQ 

« Hide

References

« Hide 'large scale' references
[1]"Genetic analysis of a chromosomal region containing genes required for assimilation of allantoin nitrogen and linked glyoxylate metabolism in Escherichia coli."
Cusa E., Obradors N., Baldoma L., Badia J., Aguilar J.
J. Bacteriol. 181:7479-7484(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
Strain: K12 / ECL1.
[2]"Sequence of minutes 4-25 of Escherichia coli."
Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Functional expression and characterization of the two cyclic amidohydrolase enzymes, allantoinase and a novel phenylhydantoinase, from Escherichia coli."
Kim G.J., Lee D.E., Kim H.-S.
J. Bacteriol. 182:7021-7028(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF N-TERMINUS, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, ENZYME REGULATION, FUNCTION, SUBUNIT.
Strain: K12.
[6]"Metal ion dependence of recombinant Escherichia coli allantoinase."
Mulrooney S.B., Hausinger R.P.
J. Bacteriol. 185:126-134(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, STEREOSPECIFICITY, COFACTOR.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U89279 Genomic DNA. Translation: AAB93853.1.
U82664 Genomic DNA. Translation: AAB40264.1.
U00096 Genomic DNA. Translation: AAC73614.1.
AP009048 Genomic DNA. Translation: BAE76290.1.
PIRG64782.
RefSeqNP_415045.1. NC_000913.3.
YP_488802.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3E74X-ray2.10A/B/C/D1-453[»]
ProteinModelPortalP77671.
SMRP77671. Positions 2-451.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP77671. 7 interactions.
STRING511145.b0512.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73614; AAC73614; b0512.
BAE76290; BAE76290; BAE76290.
GeneID12930868.
945134.
KEGGecj:Y75_p0498.
eco:b0512.
PATRIC32116181. VBIEscCol129921_0532.

Organism-specific databases

EchoBASEEB3384.
EcoGeneEG13619. allB.

Phylogenomic databases

eggNOGCOG0044.
HOGENOMHOG000219146.
KOK01466.
OMACSPWEGH.
OrthoDBEOG6KHFW6.
PhylomeDBP77671.

Enzyme and pathway databases

BioCycEcoCyc:G6281-MONOMER.
ECOL316407:JW0500-MONOMER.
MetaCyc:G6281-MONOMER.
SABIO-RKP77671.
UniPathwayUPA00395; UER00653.

Gene expression databases

GenevestigatorP77671.

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...

Other

EvolutionaryTraceP77671.
PROP77671.

Entry information

Entry nameALLB_ECOLI
AccessionPrimary (citable) accession number: P77671
Secondary accession number(s): Q2MBR6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: May 14, 2014
This is version 115 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

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene