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Protein

Allantoinase

Gene

allB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of allantoin (5-ureidohydantoin) to allantoic acid by hydrolytic cleavage of the five-member hydantoin ring.2 Publications

Catalytic activityi

(S)-allantoin + H2O = allantoate.1 Publication

Cofactori

Zn2+Curated2 Publications, Ni2+Curated2 Publications, Co2+Curated2 Publications, Mn2+Curated2 PublicationsNote: Binds 2 Zn(2+) ions per subunit. Can also use Ni(2+), Co(2+) or Mn2+.Curated2 Publications

Enzyme regulationi

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.2 Publications

Kineticsi

  1. KM=4.2 mM for allantoin (at 40 degrees Celsius and pH 8.0)2 Publications
  2. KM=17.0 mM for allantoin (in zinc-supplemented medium at 37 degrees Celsius and pH 7.4)2 Publications
  3. KM=19.5 mM for allantoin (in cobalt-supplemented medium at 37 degrees Celsius and pH 7.4)2 Publications
  4. KM=80.0 mM for allantoin (in nickel-supplemented medium at 37 degrees Celsius and pH 7.4)2 Publications

Vmax=101 µmol/min/mg enzyme (in zinc-supplemented medium at 37 degrees Celsius and pH 7.4)2 Publications

Vmax=8.1 µmol/min/mg enzyme (in cobalt-supplemented medium (20mM) at 37 degrees Celsius and pH 7.4)2 Publications

Vmax=6.7 µmol/min/mg enzyme (at 40 degrees Celsius and pH 8.0)2 Publications

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

Vmax=0.7 µmol/min/mg enzyme (without added metal at 37 degrees Celsius and pH 7.4)2 Publications

pH dependencei

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.2 Publications

Temperature dependencei

Optimum temperature is 40-45 degrees Celsius.2 Publications

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi59 – 591Zinc 1By similarity
Metal bindingi61 – 611Zinc 1By similarity
Metal bindingi146 – 1461Zinc 1; via carbamate groupBy similarity
Metal bindingi146 – 1461Zinc 2; via carbamate groupBy similarity
Metal bindingi186 – 1861Zinc 2By similarity
Metal bindingi242 – 2421Zinc 2By similarity
Metal bindingi315 – 3151Zinc 1By similarity

GO - Molecular functioni

  1. allantoinase activity Source: EcoliWiki
  2. cobalt ion binding Source: InterPro
  3. zinc ion binding Source: EcoCyc

GO - Biological processi

  1. allantoin assimilation pathway Source: EcoCyc
  2. purine nucleobase metabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Purine metabolism

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciEcoCyc:G6281-MONOMER.
ECOL316407:JW0500-MONOMER.
MetaCyc:G6281-MONOMER.
BRENDAi3.5.2.5. 2026.
SABIO-RKP77671.
UniPathwayiUPA00395; UER00653.

Names & Taxonomyi

Protein namesi
Recommended name:
Allantoinase (EC:3.5.2.5)
Alternative name(s):
Allantoin-utilizing enzyme
Gene namesi
Name:allB
Synonyms:glxB3, ybbX
Ordered Locus Names:b0512, JW0500
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13619. allB.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: EcoliWiki
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 453453AllantoinasePRO_0000165942Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei146 – 1461N6-carboxylysineBy similarity

Post-translational modificationi

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

Expressioni

Inductioni

By glyoxylate.

Gene expression databases

GenevestigatoriP77671.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

IntActiP77671. 7 interactions.
STRINGi511145.b0512.

Structurei

Secondary structure

1
453
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 97Combined sources
Beta strandi11 – 133Combined sources
Beta strandi18 – 203Combined sources
Beta strandi22 – 265Combined sources
Beta strandi29 – 357Combined sources
Beta strandi40 – 456Combined sources
Beta strandi50 – 534Combined sources
Beta strandi55 – 606Combined sources
Helixi73 – 8210Combined sources
Beta strandi85 – 906Combined sources
Beta strandi93 – 975Combined sources
Helixi102 – 11211Combined sources
Turni113 – 1153Combined sources
Beta strandi117 – 1226Combined sources
Turni131 – 1333Combined sources
Helixi134 – 1407Combined sources
Beta strandi145 – 1484Combined sources
Helixi166 – 17914Combined sources
Beta strandi183 – 1864Combined sources
Helixi190 – 20011Combined sources
Turni201 – 2044Combined sources
Helixi208 – 2136Combined sources
Helixi217 – 23418Combined sources
Beta strandi238 – 2403Combined sources
Helixi246 – 25712Combined sources
Beta strandi262 – 2665Combined sources
Helixi269 – 2724Combined sources
Helixi275 – 2817Combined sources
Helixi283 – 2853Combined sources
Helixi294 – 30512Combined sources
Turni321 – 3244Combined sources
Turni328 – 3303Combined sources
Helixi338 – 3403Combined sources
Helixi341 – 3499Combined sources
Turni350 – 3534Combined sources
Helixi357 – 3648Combined sources
Helixi366 – 3716Combined sources
Beta strandi388 – 3947Combined sources
Helixi401 – 4033Combined sources
Beta strandi406 – 4083Combined sources
Turni412 – 4154Combined sources
Beta strandi417 – 4193Combined sources
Beta strandi421 – 4277Combined sources
Beta strandi430 – 4345Combined sources
Turni435 – 4373Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3E74X-ray2.10A/B/C/D1-453[»]
ProteinModelPortaliP77671.
SMRiP77671. Positions 2-451.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP77671.

Family & Domainsi

Sequence similaritiesi

Belongs to the DHOase family. Allantoinase subfamily.Curated

Phylogenomic databases

eggNOGiCOG0044.
HOGENOMiHOG000219146.
InParanoidiP77671.
KOiK01466.
OMAiHAEMIPP.
OrthoDBiEOG6KHFW6.
PhylomeDBiP77671.

Family and domain databases

Gene3Di2.30.40.10. 1 hit.
HAMAPiMF_01645. Hydantoinase.
InterProiIPR017593. Allantoinase.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
SUPFAMiSSF51338. SSF51338. 2 hits.
TIGRFAMsiTIGR03178. allantoinase. 1 hit.

Sequencei

Sequence statusi: Complete.

P77671-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFDLIIKNG TVILENEARV VDIAVKGGKI AAIGQDLGDA KEVMDASGLV
60 70 80 90 100
VSPGMVDAHT HISEPGRSHW EGYETGTRAA AKGGITTMIE MPLNQLPATV
110 120 130 140 150
DRASIELKFD AAKGKLTIDA AQLGGLVSYN IDRLHELDEV GVVGFKCFVA
160 170 180 190 200
TCGDRGIDND FRDVNDWQFF KGAQKLGELG QPVLVHCENA LICDELGEEA
210 220 230 240 250
KREGRVTAHD YVASRPVFTE VEAIRRVLYL AKVAGCRLHV CHVSSPEGVE
260 270 280 290 300
EVTRARQEGQ DVTCESCPHY FVLDTDQFEE IGTLAKCSPP IRDLENQKGM
310 320 330 340 350
WEKLFNGEID CLVSDHSPCP PEMKAGNIMK AWGGIAGLQS CMDVMFDEAV
360 370 380 390 400
QKRGMSLPMF GKLMATNAAD IFGLQQKGRI APGKDADFVF IQPNSSYVLT
410 420 430 440 450
NDDLEYRHKV SPYVGRTIGA RITKTILRGD VIYDIEQGFP VAPKGQFILK

HQQ
Length:453
Mass (Da):49,602
Last modified:January 31, 1997 - v1
Checksum:i5CFE588F94268AB4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U89279 Genomic DNA. Translation: AAB93853.1.
U82664 Genomic DNA. Translation: AAB40264.1.
U00096 Genomic DNA. Translation: AAC73614.1.
AP009048 Genomic DNA. Translation: BAE76290.1.
PIRiG64782.
RefSeqiNP_415045.1. NC_000913.3.
YP_488802.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC73614; AAC73614; b0512.
BAE76290; BAE76290; BAE76290.
GeneIDi12930868.
945134.
KEGGiecj:Y75_p0498.
eco:b0512.
PATRICi32116181. VBIEscCol129921_0532.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U89279 Genomic DNA. Translation: AAB93853.1.
U82664 Genomic DNA. Translation: AAB40264.1.
U00096 Genomic DNA. Translation: AAC73614.1.
AP009048 Genomic DNA. Translation: BAE76290.1.
PIRiG64782.
RefSeqiNP_415045.1. NC_000913.3.
YP_488802.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3E74X-ray2.10A/B/C/D1-453[»]
ProteinModelPortaliP77671.
SMRiP77671. Positions 2-451.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP77671. 7 interactions.
STRINGi511145.b0512.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73614; AAC73614; b0512.
BAE76290; BAE76290; BAE76290.
GeneIDi12930868.
945134.
KEGGiecj:Y75_p0498.
eco:b0512.
PATRICi32116181. VBIEscCol129921_0532.

Organism-specific databases

EchoBASEiEB3384.
EcoGeneiEG13619. allB.

Phylogenomic databases

eggNOGiCOG0044.
HOGENOMiHOG000219146.
InParanoidiP77671.
KOiK01466.
OMAiHAEMIPP.
OrthoDBiEOG6KHFW6.
PhylomeDBiP77671.

Enzyme and pathway databases

UniPathwayiUPA00395; UER00653.
BioCyciEcoCyc:G6281-MONOMER.
ECOL316407:JW0500-MONOMER.
MetaCyc:G6281-MONOMER.
BRENDAi3.5.2.5. 2026.
SABIO-RKP77671.

Miscellaneous databases

EvolutionaryTraceiP77671.
PROiP77671.

Gene expression databases

GenevestigatoriP77671.

Family and domain databases

Gene3Di2.30.40.10. 1 hit.
HAMAPiMF_01645. Hydantoinase.
InterProiIPR017593. Allantoinase.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
SUPFAMiSSF51338. SSF51338. 2 hits.
TIGRFAMsiTIGR03178. allantoinase. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1998) [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 (DEC-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. 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(2005) [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(1999) [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(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, STEREOSPECIFICITY, COFACTOR.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.

Entry informationi

Entry nameiALLB_ECOLI
AccessioniPrimary (citable) accession number: P77671
Secondary accession number(s): Q2MBR6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 1997
Last sequence update: January 31, 1997
Last modified: March 31, 2015
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.