Allantoinase - Escherichia coli (strain K12)

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Reviewed, UniProtKB/Swiss-Prot P77671 (ALLB_ECOLI)

Last modified June 16, 2009. Version 75. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length	453 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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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.
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 MF_01645
Subunit structure	Homotetramer. Ref.5
Induction	By glyoxylate. HAMAP MF_01645
Post-translational modification	Carbamylation allows a single lysine to coordinate two zinc ions By similarity.
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 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) HAMAP MF_01645 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.

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Ontologies

Keywords
Biological process	Purine metabolism
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	allantoin catabolic process Inferred from electronic annotation. Source: HAMAP purine base metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	allantoinase activity Inferred from electronic annotation. Source: HAMAP zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 453

453

Allantoinase HAMAP 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

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Sequences

Sequence

Length

Mass (Da)

Tools

P77671-1 [UniParc].

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

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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: 10601204] [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: 9278503] [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: 16738553] [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: 11092864] [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: 12486048] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, STEREOSPECIFICITY, COFACTOR. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.

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Cross-references

Sequence databases

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

AP_001160.1.
NP_415045.1.

3D structure databases

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

ModBase

Search...

Genome annotation databases

GeneID

945134.

GenomeReviews

Gene locus JW0500 in contig AP009048_GR.
Gene locus b0512 in contig U00096_GR.

KEGG

ecj:JW0500.
eco:b0512.

Organism-specific databases

EchoBASE

EB3384.

EcoGene

EG13619. allB.

CMR

Search...

Phylogenomic databases

HOGENOM

P77671.

OMA

P77671. FEAWGGI.

Enzyme and pathway databases

BioCyc

EcoCyc:G6281-MON.
MetaCyc:G6281-MON.

Family and domain databases

HAMAP

MF_01645.
[Tree]

InterPro

IPR017593. Allantoinase.
IPR006680. Amidohydro_1.
[Graphical view]

Pfam

PF01979. Amidohydro_1. 2 hits.
[Graphical view]

ProDom

PD000518. DHOase. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR03178. allantoinase. 1 hit.

ProtoNet

Search...

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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:	June 16, 2009
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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