Q82ZQ1 (ALLB_ENTFA) 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:	EF_2999

Organism

Enterococcus faecalis (Streptococcus faecalis)

Taxonomic identifier

1351 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Enterococcaceae › Enterococcus

Protein attributes

Sequence length	454 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 Reference proteome
Gene Ontology (GO)
Biological process	allantoin catabolic process Inferred from electronic annotation. Source: InterPro purine base metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	allantoinase activity Inferred from electronic annotation. Source: EC 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 – 454	454	Allantoinase HAMAP MF_01645		PRO_0000317674
Sites
	Metal binding	58	1	Zinc 1 By similarity
	Metal binding	60	1	Zinc 1 By similarity
	Metal binding	149	1	Zinc 1; via carbamate group By similarity
	Metal binding	149	1	Zinc 2; via carbamate group By similarity
	Metal binding	189	1	Zinc 2 By similarity
	Metal binding	245	1	Zinc 2 By similarity
	Metal binding	318	1	Zinc 1 By similarity
Amino acid modifications
	Modified residue	149	1	N6-carboxylysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q82ZQ1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: B5E4B3F04ED062F4	FASTA	454	48,713
	10 20 30 40 50 60 MQAELVIKNG LVILETGEVI TDVAVQGGKI VAIGQDLSGE RVIDATGLVV SPGMVDAHVH 70 80 90 100 110 120 ITDPGGGYRD EWEGYVTGTA ACAKGGVTTF MEMPLNQIPA TVDKTSLEIK YKAGENKLKV 130 140 150 160 170 180 DVGSFGGVVP TNLADGIQEL DEGGVSGYKC FLGTCGDRSI EGDFQNVDDY SLYEGMKQVA 190 200 210 220 230 240 KTGKVLAIHA ENAPITDKLG AVAYQNGETT LAAYVATRPV FTEVEAIQKA ILFAKETGCR 250 260 270 280 290 300 IHICHVACQE GVEEVLKAQA EGVDVTCETC THYLYFTTDE LDAIGPVVKC SPPIRDADQQ 310 320 330 340 350 360 AALWNHVQTG GIAFVTSDHS PCTPDLKDTT NAFEAWGGIS GVQNNVDVLF DEAVQKRGLS 370 380 390 400 410 420 LKQFADMIAA NPADRYHLAQ KGRISIGKDA DFVLIKPNAP YILKAEDLEY RNKISPYIGR 430 440 450 EIGAQVIQTI LRGETIYAQE TGVTEAFNGV FIKN

References

[1]

"Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus faecalis." Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R., Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., DeBoy R.T., Durkin S.A. , Kolonay J.F., Madupu R., Nelson W.C., Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M., Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M. Science 299:2071-2074(2003) [PubMed: 12663927] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700802 / V583.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016830 Genomic DNA. Translation: AAO82684.1.
RefSeq	NP_816614.1. NC_004668.1.
3D structure databases
HSSP	HSSP built from PDB template 1GKR based on UniProtKB P81006.
ProteinModelPortal	Q82ZQ1.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1201848.
GenomeReviews	Gene locus EF_2999 in contig AE016830_GR.
KEGG	efa:EF2999.
NMPDR	fig|226185.1.peg.2799.
PATRIC	21856167. VBIEntFae7065_2796.
TIGR	EF_2999.
Phylogenomic databases
HOGENOM	HBG724623.
OMA	FHAEVEC.
ProtClustDB	PRK08044.
Enzyme and pathway databases
BioCyc	EFAE226185:EF_2999-MONOMER.
Family and domain databases
HAMAP	MF_01645. Hydantoinase. [Tree]
InterPro	IPR017593. Allantoinase. IPR006680. Amidohydro_1. IPR011059. Metal-dep_hydrolase_composite. [Graphical view]
KO	K01466.
Pfam	PF01979. Amidohydro_1. 1 hit. [Graphical view]
SUPFAM	SSF51338. Metalo_hydrolase. 1 hit.
TIGRFAMs	TIGR03178. Allantoinase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ALLB_ENTFA

Accession

Primary (citable) accession number: Q82ZQ1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	June 1, 2003
Last modified:	January 25, 2012
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program