B1LKD0 (ALLB_ECOSM) Reviewed, UniProtKB/Swiss-Prot

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:	EcSMS35_0554

Organism

Escherichia coli (strain SMS-3-5 / SECEC) [Complete proteome] [HAMAP]

Taxonomic identifier

439855 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

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-Rule MF_01645
Catalytic activity	(S)-allantoin + H2O = allantoate. HAMAP-Rule MF_01645
Cofactor	Binds 2 zinc ions per subunit By similarity.
Pathway	Nitrogen metabolism; (S)-allantoin degradation; allantoate from (S)-allantoin: step 1/1. HAMAP-Rule MF_01645
Subunit structure	Homotetramer By similarity.
Post-translational modification	Carbamylation allows a single lysine to coordinate two zinc ions By similarity. HAMAP-Rule 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 nucleobase metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	allantoinase activity Inferred from electronic annotation. Source: HAMAP cobalt ion binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
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_1000186925
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)
	B1LKD0 [UniParc]. Last modified April 29, 2008. Version 1. Checksum: 960C3FEFF05B8DF3	FASTA	453	49,602
	10 20 30 40 50 60 MSFDLIIKNG TVILENEARV VDVAVKGGKI 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 CHISSPEGVE 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

References

[1]

"Insights into the environmental resistance gene pool from the genome sequence of the multidrug-resistant environmental isolate Escherichia coli SMS-3-5." Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C., Ravel J., Stepanauskas R. J. Bacteriol. 190:6779-6794(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SMS-3-5 / SECEC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000970 Genomic DNA. Translation: ACB18542.1.
RefSeq	YP_001742655.1. NC_010498.1.
3D structure databases
ProteinModelPortal	B1LKD0.
SMR	B1LKD0. Positions 2-451.
ModBase	Search...
Protein-protein interaction databases
STRING	439855.EcSMS35_0554.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ACB18542; ACB18542; EcSMS35_0554.
GeneID	6144951.
KEGG	ecm:EcSMS35_0554.
PATRIC	18429947. VBIEscCol6161_0725.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0044.
HOGENOM	HOG000219146.
KO	K01466.
OMA	CRLHICH.
ProtClustDB	PRK08044.
Enzyme and pathway databases
BioCyc	ECOL439855:GHHB-3122-MONOMER.
UniPathway	UPA00395; UER00653.
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...

Entry information

Entry name

ALLB_ECOSM

Accession

Primary (citable) accession number: B1LKD0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 28, 2009
Last sequence update:	April 29, 2008
Last modified:	May 1, 2013
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program