Reviewed, UniProtKB/Swiss-Prot Q8XGS6 (ALLB_SALTI)

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:	STY0571, t2338

Organism

Salmonella typhi [Complete proteome] [HAMAP]

Taxonomic identifier

90370 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella

Protein attributes

Sequence length	453 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Catalytic activity	(S)-allantoin + H2O = allantoate. HAMAP 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 MF_01645
Subunit structure	Homotetramer By similarity.
Post-translational modification	Carbamylation allows a single lysine to coordinate two zinc ions By similarity.
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_0000317684
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)
	Q8XGS6-1 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 223BFADF6257891E	FASTA	453	49,887
	10 20 30 40 50 60 MSFDLIIKNG TVILENEARV IDIAVQGGKI 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 EVTRARQEGQ 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]

"Complete genome sequence of a multiple drug resistant Salmonella enterica serovar Typhi CT18." Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J., Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M., Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A., Davis P. , Davies R.M., Dowd L., White N., Farrar J., Feltwell T., Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A., Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S., Barrell B.G. Nature 413:848-852(2001) [PubMed: 11677608] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CT18.

[2]

"Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and CT18." Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V., Kodoyianni V., Schwartz D.C., Blattner F.R. J. Bacteriol. 185:2330-2337(2003) [PubMed: 12644504] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700931 / Ty2.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AL627267 Genomic DNA. Translation: CAD05007.1. AE014613 Genomic DNA. Translation: AAO69932.1.
RefSeq	NP_455115.1. NP_806072.1.
3D structure databases
HSSP	HSSP built from PDB template 1GKR based on UniProtKB P81006.
ModBase	Search...
Proteomic databases
PRIDE	Q8XGS6.
Genome annotation databases
GeneID	1067348. 1247039.
GenomeReviews	Gene locus t2338 in contig AE014613_GR. Gene locus STY0571 in contig AL513382_GR.
KEGG	stt:t2338. sty:STY0571.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q8XGS6.
OMA	FEAWGGI.
Enzyme and pathway databases
BioCyc	SENT209261:T2338-MON. SENT220341:STY0571-MON.
BRENDA	3.5.2.5. 3716.
Family and domain databases
HAMAP	MF_01645. [Tree]
InterPro	IPR017593. Allantoinase. IPR006680. Amidohydro_1. [Graphical view]
Pfam	PF01979. Amidohydro_1. 1 hit. [Graphical view]
ProDom	PD000518. DHOase. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR03178. allantoinase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ALLB_SALTI

Accession

Primary (citable) accession number: Q8XGS6
Secondary accession number(s): Q7ANE4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	March 1, 2002
Last modified:	November 3, 2009
This is version 52 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)