Reviewed, UniProtKB/Swiss-Prot A7ZIR8 (ALLB_ECO24)

Names and origin

Protein names

Recommended name:
    Allantoinase
    EC=3.5.2.5
Alternative name(s):
    Allantoin-utilizing enzyme

Gene names

Name:	allB
Ordered Locus Names:	EcE24377A_0548

Organism

Escherichia coli O139:H28 (strain E24377A / ETEC) [Complete proteome] [HAMAP]

Taxonomic identifier

331111 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	453 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalyzes the conversion of allantoin (5-ureidohydantoin) to allantoic acid by hydrolytic cleavage of the five-member hydantoin ring By similarity. HAMAP MF_01645
Catalytic activity	(S)-allantoin + H2O = allantoate. HAMAP MF_01645
Cofactor	Binds 2 zinc ions per subunit By similarity. HAMAP MF_01645
Pathway	Nitrogen metabolism; (S)-allantoin degradation; allantoate from (S)-allantoin: step 1/1. HAMAP MF_01645
Subunit structure	Homotetramer By similarity. HAMAP MF_01645
Post-translational modification	Carbamylation allows a single lysine to coordinate two zinc ions By similarity. HAMAP MF_01645
Sequence similarities	Belongs to the DHOase family. Allantoinase subfamily.

Ontologies

Keywords
Biological process	Purine metabolism
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
Technical term	Complete proteome
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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 453	453	Allantoinase HAMAP MF_01645		PRO_0000317676
Sites
	Metal binding	59	1	Zinc 1 By similarity
	Metal binding	61	1	Zinc 1 By similarity
	Metal binding	146	1	Zinc 1; via carbamate group By similarity
	Metal binding	146	1	Zinc 2; via carbamate group By similarity
	Metal binding	186	1	Zinc 2 By similarity
	Metal binding	242	1	Zinc 2 By similarity
	Metal binding	315	1	Zinc 1 By similarity
Amino acid modifications
	Modified residue	146	1	N6-carboxylysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A7ZIR8-1 [UniParc]. Last modified October 23, 2007. Version 1. Checksum: 3EF2096AF5A022B6	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 LICDALGEEA KREGRVTAHD YVASRPVFTE VEAIRRVLYL AKVAGCRLHV 250 260 270 280 290 300 CHISSPEGVE EVTRARQEGQ DVTCESCPHY FVLDTDQFEE IGTLAKCSPP IRDLENQKGM 310 320 330 340 350 360 WEKLFNGEID CLVSDHSPCP PEMKAGNIME AWGGIAGLQN CMDVMFDEAV QKRGMSLPMF 370 380 390 400 410 420 GKLMATNAAD IFGLQQKGRI ALGKDADFVF IQPNSSYVLT NDDLEYRHKV SPYVGRTIGA 430 440 450 RITKTILRGD VIYDIEQGFP VAPKGQFILK HQQ

References

[1]

"The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates." Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J. J. Bacteriol. 190:6881-6893(2008) [PubMed: 18676672] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000800 Genomic DNA. Translation: ABV17665.1.
RefSeq	YP_001461697.1.
3D structure databases
SMR	A7ZIR8. Positions 3-449.
ModBase	Search...
Protein-protein interaction databases
STRING	A7ZIR8.
Genome annotation databases
GeneID	5586304.
GenomeReviews	Gene locus EcE24377A_0548 in contig CP000800_GR.
KEGG	ecw:EcE24377A_0548.
NMPDR	fig|331111.3.peg.3083.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0044.
HOGENOM	HBG724623.
OMA	HICHISS.
Family and domain databases
HAMAP	MF_01645. Hydantoinase. [Tree]
InterPro	IPR017593. Allantoinase. IPR006680. Amidohydro_1. IPR011059. Metal-dep_hydrolase_composite. [Graphical view]
Pfam	PF01979. Amidohydro_1. 1 hit. [Graphical view]
TIGRFAMs	TIGR03178. allantoinase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ALLB_ECO24

Accession

Primary (citable) accession number: A7ZIR8

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	October 23, 2007
Last modified:	February 9, 2010
This is version 19 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)