Q9RV76 (ALLB_DEIRA) 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:	DR_1153

Organism

Deinococcus radiodurans

Taxonomic identifier

1299 [NCBI]

Taxonomic lineage

Bacteria › Deinococcus-Thermus › Deinococci › Deinococcales › Deinococcaceae › Deinococcus

Protein attributes

Sequence length	448 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 – 448	448	Allantoinase HAMAP MF_01645		PRO_0000165941
Sites
	Metal binding	60	1	Zinc 1 By similarity
	Metal binding	62	1	Zinc 1 By similarity
	Metal binding	147	1	Zinc 1; via carbamate group By similarity
	Metal binding	147	1	Zinc 2; via carbamate group By similarity
	Metal binding	183	1	Zinc 2 By similarity
	Metal binding	239	1	Zinc 2 By similarity
	Metal binding	312	1	Zinc 1 By similarity
Amino acid modifications
	Modified residue	147	1	N6-carboxylysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9RV76 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 3215965D0613AF86	FASTA	448	48,559
	10 20 30 40 50 60 MSLDLLLRGA VLVTPEGERR ADLGIVGGQI AELTDEIATP AAQTLDVSGL HVFPGVLDDH 70 80 90 100 110 120 VHLNEPGRTH WEGFETGTQA LAAGGATSFL DMPLNSSPPV LTRERFEDKA RLGEEKSLID 130 140 150 160 170 180 FGLWGGLTPL NLDQLDDLAE CGVIGLKAFM SHSGLDEFPA ADDLTLYEGM RTAKRHGLVV 190 200 210 220 230 240 ATHAESNEFT RRLTETARAQ GKSGVRDYLE SRPVVTELEA VQRALLFAQD TGAALHLVHV 250 260 270 280 290 300 SSGAAVALAY EGKQKGIDVT IETCPHYLHF TGEDVERVGA ALKCAPPLRD PAVQEELWRE 310 320 330 340 350 360 LLAGHIDTVG SDHSPAPPDM KTSEDFFSLW GGISGAQSTL NVMLEDGYAQ RGLPLEIIAA 370 380 390 400 410 420 LLALNPAQRF GLPQKGRLAV GADADFALVA LGEKFTLDTL YDRWQQNPYR GQSFQGRVHA 430 440 TYLRGQPVYQ NGEFTGTPRG RLLRPRSL

References

[1]

"Genome sequence of the radioresistant bacterium Deinococcus radiodurans R1." White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D., Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L., Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M., Vamathevan J.J., Lam P. , McDonald L.A., Utterback T.R., Zalewski C., Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D., Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M. Science 286:1571-1577(1999) [PubMed: 10567266] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000513 Genomic DNA. Translation: AAF10727.1.
PIR	E75429.
RefSeq	NP_294877.1. NC_001263.1.
3D structure databases
ProteinModelPortal	Q9RV76.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1798402.
GenomeReviews	Gene locus DR_1153 in contig AE000513_GR.
KEGG	dra:DR_1153.
NMPDR	fig|243230.1.peg.1336.
PATRIC	21629898. VBIDeiRad64572_1350.
TIGR	DR_1153.
Phylogenomic databases
HOGENOM	HBG724623.
OMA	LKCAPPL.
PhylomeDB	Q9RV76.
ProtClustDB	PRK06189.
Enzyme and pathway databases
BioCyc	DRAD243230:DR_1153-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_DEIRA

Accession

Primary (citable) accession number: Q9RV76

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	May 1, 2000
Last modified:	January 25, 2012
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program