Allantoinase - Escherichia coli (strain K12)

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P77671 (ALLB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 108. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	453 AA.
Sequence status	Complete.
Protein existence	Evidence 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. HAMAP-Rule MF_01645
Sequence similarities	Belongs to the DHOase family. Allantoinase subfamily.
Biophysicochemical properties	Kinetic parameters: K_M=4.2 mM for allantoin (at 40 degrees Celsius and pH 8.0) Ref.5 Ref.6 K_M=17.0 mM for allantoin (in zinc-supplemented medium at 37 degrees Celsius and pH 7.4) K_M=19.5 mM for allantoin (in cobalt-supplemented medium at 37 degrees Celsius and pH 7.4) K_M=80.0 mM for allantoin (in nickel-supplemented medium at 37 degrees Celsius and pH 7.4) V_max=101 µmol/min/mg enzyme (in zinc-supplemented medium at 37 degrees Celsius and pH 7.4) V_max=8.1 µmol/min/mg enzyme (in cobalt-supplemented medium (20mM) at 37 degrees Celsius and pH 7.4) V_max=6.7 µmol/min/mg enzyme (at 40 degrees Celsius and pH 8.0) V_max=3.9 µmol/min/mg enzyme (in cobalt-supplemented medium (2mM) at 37 degrees Celsius and pH 7.4) V_max=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.

Ontologies

Keywords
Biological process	Purine metabolism
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	allantoin assimilation pathway Inferred from direct assay Ref.6. Source: EcoCyc purine nucleobase metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from direct assay PubMed 19248789. Source: EcoliWiki
Molecular_function	allantoinase activity Inferred from direct assay Ref.6. Source: EcoCyc cobalt ion binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from direct assay Ref.6. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 453

453

Allantoinase HAMAP-Rule MF_01645

PRO_0000165942

Sites

Metal binding

Zinc 1 By similarity

Metal binding

Zinc 1 By similarity

Metal binding

146

Zinc 1; via carbamate group By similarity

Metal binding

146

Zinc 2; via carbamate group By similarity

Metal binding

186

Zinc 2 By similarity

Metal binding

242

Zinc 2 By similarity

Metal binding

315

Zinc 1 By similarity

Amino acid modifications

Modified residue

146

N6-carboxylysine By similarity

Secondary structure

453

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P77671 [UniParc].

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

FASTA

453

49,602

        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' referencesShow '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 277:1453-1474(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.

PIR

G64782.

RefSeq

NP_415045.1. NC_000913.2.
YP_488802.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3E74	X-ray	2.10	A/B/C/D	1-453	[»]

ProteinModelPortal

P77671.

SMR

P77671. Positions 2-451.

ModBase

Search...

Protein-protein interaction databases

IntAct

P77671. 7 interactions.

STRING

511145.b0512.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC73614; AAC73614; b0512.
BAE76290; BAE76290; BAE76290.

GeneID

12930868.
945134.

KEGG

ecj:Y75_p0498.
eco:b0512.

PATRIC

32116181. VBIEscCol129921_0532.

Organism-specific databases

EchoBASE

EB3384.

EcoGene

EG13619. allB.

Phylogenomic databases

eggNOG

COG0044.

HOGENOM

HOG000219146.

K01466.

OMA

CRLHICH.

ProtClustDB

PRK08044.

Enzyme and pathway databases

BioCyc

EcoCyc:G6281-MONOMER.
ECOL316407:JW0500-MONOMER.
MetaCyc:G6281-MONOMER.

SABIO-RK

P77671.

UniPathway

UPA00395; UER00653.

Gene expression databases

Genevestigator

P77671.

Family and domain databases

HAMAP

MF_01645. Hydantoinase.

InterPro

IPR017593. Allantoinase.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]

SUPFAM

SSF51338. Metalo_hydrolase. 1 hit.

TIGRFAMs

TIGR03178. allantoinase. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P77671.

Entry information

Entry name

ALLB_ECOLI

Accession

Primary (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 1, 2013
This is version 108 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

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

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

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents