Reviewed, UniProtKB/Swiss-Prot P63486 (ALLA_ECO57)

Names and origin

Protein names

Recommended name:
    Ureidoglycolate hydrolase
    EC=3.5.3.19

Gene names

Name:	allA
Ordered Locus Names:	Z0659, ECs0566

Organism

Escherichia coli O157:H7 [Complete proteome] [HAMAP]

Taxonomic identifier

83334 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	160 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Involved in the anaerobic utilization of allantoin. Reinforces the induction of genes involved in the degradation of allantoin and glyoxylate by producing glyoxylate By similarity. HAMAP MF_00616
Catalytic activity	(S)-ureidoglycolate + H2O = glyoxylate + 2 NH3 + CO2. HAMAP MF_00616
Pathway	Nitrogen metabolism; (S)-allantoin degradation; glyoxylate from (S)-ureidoglycolate: step 1/1. HAMAP MF_00616
Subunit structure	Homodimer. Ref.3
Sequence similarities	Belongs to the ureidoglycolate hydrolase family.

Ontologies

Keywords
Biological process	Purine metabolism
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	allantoin catabolic process Inferred from electronic annotation. Source: InterPro purine base catabolic process Inferred from electronic annotation. Source: HAMAP
Molecular function	ureidoglycolate hydrolase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 160

160

Ureidoglycolate hydrolase HAMAP MF_00616

PRO_0000120549

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

160

Helix Strand Turn

Details...

Beta strand

2 – 7

6

Helix

10 – 13

4

Turn

14 – 16

3

Beta strand

17 – 20

4

Beta strand

27 – 30

4

Turn

31 – 34

4

Beta strand

35 – 43

9

Beta strand

46 – 48

3

Helix

49 – 51

3

Beta strand

53 – 59

7

Beta strand

67 – 73

7

Beta strand

79 – 86

8

Beta strand

90 – 94

5

Beta strand

97 – 99

3

Beta strand

106 – 109

4

Beta strand

115 – 118

4

Beta strand

129 – 132

4

Beta strand

134 – 140

7

Beta strand

148 – 158

11

Sequences

	Sequence		Length	Mass (Da)
	P63486-1 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: E39014610FE93FC6	FASTA	160	18,223
	10 20 30 40 50 60 MKLQVLPLSQ EAFSAYGDVI ETQQRDFFHI NNGLVERYHD LALVEILEQD RTLISINRAQ 70 80 90 100 110 120 PANLPLTIHE LERHPLGTQA FIPMKGEVFV VVVALGDDKP DLSTLRAFIT NGEQGVNYHR 130 140 150 160 NVWHHPLFAW QRVTDFLTID RGGSDNCDVE SIPEQELCFA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R. Nature 409:529-533(2001) [PubMed: 11206551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
[2]	"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. , Kuhara S., Shiba T., Hattori M., Shinagawa H. DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.
[3]	"Crystal structure of ureidoglycolate hydrolase (AllA) from Escherichia coli O157:H7." Raymond S., Tocilj A., Ajamian E., Li Y., Hung M.-N., Matte A., Cygler M. Proteins 61:454-459(2005) [PubMed: 16114032] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS), SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE005174 Genomic DNA. Translation: AAG54861.1.
BA000007 Genomic DNA. Translation: BAB33989.1.

PIR

A85550.
F90699.

RefSeq

NP_286253.1.
NP_308593.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1YQC	X-ray	1.71	A/B	1-160	[»]

ModBase

Search...

Genome annotation databases

GeneID

915530.
957495.

GenomeReviews

Gene locus Z0659 in contig AE005174_GR.
Gene locus ECs0566 in contig BA000007_GR.

KEGG

ece:Z0659.
ecs:ECs0566.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

HBG289179.

OMA

MRFHRLA.

Enzyme and pathway databases

BioCyc

ECOL83334:ECS0566-MONOMER.

BRENDA

3.5.3.19. 246.

Family and domain databases

HAMAP

MF_00616. Ureidogly_hydro.
[Tree]

InterPro

IPR007247. Ureidogly_hydro.
[Graphical view]

PANTHER

PTHR21221. Ureidogly_hydro. 1 hit.

Pfam

PF04115. Ureidogly_hydro. 1 hit.
[Graphical view]

PIRSF

PIRSF017306. Ureidogly_hydro. 1 hit.

ProtoNet

Search...

Entry information

Entry name

ALLA_ECO57

Accession

Primary (citable) accession number: P63486
Secondary accession number(s): Q8XCX8

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	October 11, 2004
Last modified:	January 19, 2010
This is version 40 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)