B5R646 (ALLB_SALG2) 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:	SG0535

Organism

Salmonella gallinarum (strain 287/91 / NCTC 13346) [Complete proteome] [HAMAP]

Taxonomic identifier

550538 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella › Salmonella choleraesuis › Salmonella enterica I › Salmonella gallinarum

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_1000186929
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)
	B5R646 [UniParc]. Last modified November 4, 2008. Version 1. Checksum: 965209A59078ADDF	FASTA	453	49,901
	10 20 30 40 50 60 MSFDLIIKNG TVILENEARV IDIAAQGGKI AAIGENLGEA KNVLDATGLI VSPGMVDAHT 70 80 90 100 110 120 HISEPGRTHW EGYETGTRAA AKGGITTMIE MPLNQLPATV DRETIELKFD AAKGKLTIDA 130 140 150 160 170 180 AQLGGLVSYN LDRLHELDEV GVVGFKCFVA TCGDRGIDND FRDVNDWQFY KGAQKLGEMD 190 200 210 220 230 240 QTVLVHCENA LICDELGEEA KREGRVTAHD YVASRPVFTE VEAIRRVLYL AKAAGCRLHV 250 260 270 280 290 300 CHISSPEGVE EVTRARQEVQ DVTCESCPHY FVLDTDQFEE IGTLAKCSPP IRDQENQKGM 310 320 330 340 350 360 WEKLFNGEID CLVSDHSPCP PEMKAGNIMQ AWGGIAGLQN CMDVMFDEAV QKRGMSLPMF 370 380 390 400 410 420 GKLMATNAAD IFGLKHKGRI APGKDADLVF IQPDSSYVLK NEDLEYRHKV SPYVGRTIGA 430 440 450 RITKTILRGD VIYDIEHGFP VPPKGQFILK HQQ

References

[1]

"Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella gallinarum 287/91 provides insights into evolutionary and host adaptation pathways." Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S., Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A., Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B., Ormond D. , Abdellah Z., Brooks K., Cherevach I., Chillingworth T., Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S., Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D., Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J. Genome Res. 18:1624-1637(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 287/91 / NCTC 13346.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM933173 Genomic DNA. Translation: CAR36431.1.
RefSeq	YP_002225626.1. NC_011274.1.
3D structure databases
ProteinModelPortal	B5R646.
ModBase	Search...
Protein-protein interaction databases
STRING	550538.SG0535.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAR36431; CAR36431; SG0535.
GeneID	6923067.
KEGG	seg:SG0535.
PATRIC	18499266. VBISalEnt1629_0584.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0044.
HOGENOM	HOG000267552.
KO	K01466.
OMA	CRLHICH.
ProtClustDB	PRK08044.
Enzyme and pathway databases
BioCyc	SENT550538:GJ93-529-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_SALG2

Accession

Primary (citable) accession number: B5R646

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 28, 2009
Last sequence update:	November 4, 2008
Last modified:	May 1, 2013
This is version 37 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program