Q65LN0 (ALLB_BACLD) 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
Synonyms:	pucH
Ordered Locus Names:	BLi01126, BL01094

Organism

Bacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP]

Taxonomic identifier

279010 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus subtilis group › Bacillus licheniformis

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-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 – 454	454	Allantoinase HAMAP-Rule MF_01645		PRO_0000317671
Sites
	Metal binding	59	1	Zinc 1 By similarity
	Metal binding	61	1	Zinc 1 By similarity
	Metal binding	150	1	Zinc 1; via carbamate group By similarity
	Metal binding	150	1	Zinc 2; via carbamate group By similarity
	Metal binding	190	1	Zinc 2 By similarity
	Metal binding	246	1	Zinc 2 By similarity
	Metal binding	319	1	Zinc 1 By similarity
Amino acid modifications
	Modified residue	150	1	N6-carboxylysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q65LN0 [UniParc]. Last modified October 25, 2004. Version 1. Checksum: DE1502556AD04420	FASTA	454	49,488
	10 20 30 40 50 60 MNFDSIIKNG LVILENGEQE VEVGIKDGKI AAIGQDLGTS AKIIDAKGSI VSPGMIDAHV 70 80 90 100 110 120 HITEPGGGYR DEWEGYDTGT RAAAKGGVTT FIEMPLNQVP ATVDEESIQE KFKAGKGKLS 130 140 150 160 170 180 VDVASYGGLV PFDLDGGIQE LDSNGVVAYK CFLATCGDRS IEGDFMNVDD YSLYEGMKQI 190 200 210 220 230 240 AKTGKILSIH AENAAITDKL GEIASKNGET SLRAYVDSRP VFTEVEPIRK IILFAKETGC 250 260 270 280 290 300 RVHIVHIACE EGVDEIVKAQ QEGVDITCET CTHYLYFYKE ELDHIGPVVK CSPPIREQSR 310 320 330 340 350 360 LEGMWNRVLN GDISFVTSDH SPCTPDLKAT DNAFEAWGGI AGLQNNVDVL FDEGVQKRNM 370 380 390 400 410 420 PLSKFAAIIA TNPAKRFNLA SKGSIAVGKD ADFVFIKKDA PYELKAEDLA YRHKISPYIG 430 440 450 RKIGAQVVKT ILRGVEIYDK EKGISNEKVG RFIP

References

[1]

"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential." Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G. J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 13 / ATCC 14580.

[2]

"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species." Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. , Galleron N., Ehrlich S.D., Berka R.M. Genome Biol. 5:R77.1-R77.12(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 13 / ATCC 14580.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000002 Genomic DNA. Translation: AAU22686.1. AE017333 Genomic DNA. Translation: AAU40034.1.
RefSeq	YP_006712506.1. NC_006322.1. YP_078324.1. NC_006270.3.
3D structure databases
HSSP	HSSP built from PDB template 1GKR based on UniProtKB P81006.
ProteinModelPortal	Q65LN0.
ModBase	Search...
Protein-protein interaction databases
STRING	279010.BL01094.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAU22686; AAU22686; BL01094. AAU40034; AAU40034; BLi01126.
GeneID	3030063. 3098142.
KEGG	bld:BLi01126. bli:BL01094.
PATRIC	18947811. VBIBacLic203714_1110.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0044.
HOGENOM	HOG000219146.
KO	K01466.
OMA	LLMFHAE.
ProtClustDB	PRK08044.
Enzyme and pathway databases
BioCyc	BLIC279010:GJ2P-1115-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_BACLD

Accession

Primary (citable) accession number: Q65LN0
Secondary accession number(s): Q62X22

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	October 25, 2004
Last modified:	May 1, 2013
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program