Reviewed, UniProtKB/Swiss-Prot Q5PCG0 (ALLB_SALPA)

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:	SPA2200

Organism

Salmonella paratyphi A [Complete proteome] [HAMAP]

Taxonomic identifier

54388 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella

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_0000317683
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)
	Q5PCG0-1 [UniParc]. Last modified January 4, 2005. 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]

"Comparison of genome degradation in Paratyphi A and Typhi, human-restricted serovars of Salmonella enterica that cause typhoid." McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S., Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R., Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F. , Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W., Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M., Warren W., Florea L., Spieth J., Wilson R.K. Nat. Genet. 36:1268-1274(2004) [PubMed: 15531882] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 9150 / SARB42.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000026 Genomic DNA. Translation: AAV78088.1.
RefSeq	YP_151400.1.
3D structure databases
HSSP	HSSP built from PDB template 1GKR based on UniProtKB P81006.
SMR	Q5PCG0. Positions 3-449.
ModBase	Search...
Proteomic databases
PRIDE	Q5PCG0.
Genome annotation databases
GeneID	3178003.
GenomeReviews	Gene locus SPA2200 in contig CP000026_GR.
KEGG	spt:SPA2200.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG724623.
OMA	HICHISS.
Enzyme and pathway databases
BioCyc	SENT295319:SPA2200-MONOMER.
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_SALPA

Accession

Primary (citable) accession number: Q5PCG0

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	January 4, 2005
Last modified:	February 9, 2010
This is version 33 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)