Q9RKU5 (ALLB_STRCO) 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:	SCO6247
ORF Names:	SCAH10.12, STAH10.12

Organism

Streptomyces coelicolor

Taxonomic identifier

1902 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

Protein attributes

Sequence length	445 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 – 445	445	Allantoinase HAMAP MF_01645		PRO_0000165943
Sites
	Metal binding	63	1	Zinc 1 By similarity
	Metal binding	65	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	186	1	Zinc 2 By similarity
	Metal binding	238	1	Zinc 2 By similarity
	Metal binding	311	1	Zinc 1 By similarity
Amino acid modifications
	Modified residue	150	1	N6-carboxylysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9RKU5 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 75955C5F98632570	FASTA	445	47,492
	10 20 30 40 50 60 MSEAELVLRS TRVITPEGTR AASVAVTGEK ITAVLPYDAP VPAGARLEDV GDHVVLPGLV 70 80 90 100 110 120 DTHVHVNDPG RTEWEGFWTA TRAAAAGGIT TLVDMPLNSI PPTTTVDNLR TKREVAADKA 130 140 150 160 170 180 HIDVGFWGGA LPDNVKDLRP LHEAGVFGFK AFLSPSGVDE FPHLDQEQLA RSLAEIAAFD 190 200 210 220 230 240 GLLIVHAEDP HHLAAAPQQG GPKYTHFLAS RPRDAEDTAI ATLLAQAKRF NARVHVLHLS 250 260 270 280 290 300 SSDALPLIAE ARADGVRVTV ETCPHYLTLT AEEVPDGASE FKCCPPIREA ANQDLLWQAL 310 320 330 340 350 360 ADGTIDCVVT DHSPSTADLK TDDFATAWGG IAGLQLSLPA MWTAARGRGL GLEDVVRWMS 370 380 390 400 410 420 ERTAALVGLD ARKGAIAPGH DADFAVLAPD ETFTVDPAAL QHRNRVTAYA GKTLYGVVKS 430 440 TWLRGERIVA DGAFTDPKGQ LLDRA

References

[1]

"Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2)." Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L., Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A., Fraser A., Goble A. , Hidalgo J., Hornsby T., Howarth S., Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A. Nature 417:141-147(2002) [PubMed: 12000953] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-471 / A3(2) / M145.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL939126 Genomic DNA. Translation: CAB60166.1.
RefSeq	NP_630347.1. NC_003888.3.
3D structure databases
ProteinModelPortal	Q9RKU5.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1101688.
GenomeReviews	Gene locus SCO6247 in contig AL645882_GR.
KEGG	sco:SCO6247.
NMPDR	fig|100226.1.peg.6192.
PATRIC	23742428. VBIStrCoe124346_6361.
Phylogenomic databases
HOGENOM	HBG724623.
OMA	FHAEVEC.
PhylomeDB	Q9RKU5.
ProtClustDB	CLSK2519400.
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_STRCO

Accession

Primary (citable) accession number: Q9RKU5

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	May 1, 2000
Last modified:	January 25, 2012
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program