Reviewed, UniProtKB/Swiss-Prot Q82LL4 (ALLB_STRAW)

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, sav1996
Ordered Locus Names:	SAV_1996

Organism

Streptomyces avermitilis [Complete proteome] [HAMAP]

Taxonomic identifier

33903 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	445 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 – 445	445	Allantoinase HAMAP MF_01645		PRO_0000317687
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)
	Q82LL4-1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 3C75AF72F136425C	FASTA	445	47,582
	10 20 30 40 50 60 MSDVELVLRS TRVITPEGTR PAAVAVAAGK ITAVLPHDAE VPAGARLEDL GDDVLLPGLV 70 80 90 100 110 120 DTHVHVNDPG RTHWEGFWTA TRAAAAGGIT TLVDMPLNSL PPTTTVGNLR TKRDVAADKA 130 140 150 160 170 180 HIDVGFWGGA LPDNVKDLRP LHDAGVFGFK AFLSPSGVDE FPELDQERLA RSMAEIAGFG 190 200 210 220 230 240 GLLIVHAEDP HHLAAAPQRG GPRYTDFLAS RPRDAEDTAI ANLLAQAKRL NARVHVLHLS 250 260 270 280 290 300 SSDALPLIAG AKAEGVRVTV ETCPHYLTLT AEEVPDGASE FKCCPPIREA ANQDLLWQAL 310 320 330 340 350 360 ADGTIDCVVT DHSPSTADLK TDDFATAWGG ISGLQLSLPA IWTEARRRGH SLEDVVRWMS 370 380 390 400 410 420 ARTARLVGLA QKGAIEAGRD ADFAVLAPDE TFTVDPAALQ HRNRVTAYAG KTLSGVVKST 430 440 WLRGERIMAD GEFTEPKGRL LSREP

References

[1]

"Genome sequence of an industrial microorganism Streptomyces avermitilis: deducing the ability of producing secondary metabolites." Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M., Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T., Sakaki Y., Hattori M. Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001) [PubMed: 11572948] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165.

[2]

"Complete genome sequence and comparative analysis of the industrial microorganism Streptomyces avermitilis." Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T., Sakaki Y., Hattori M., Omura S. Nat. Biotechnol. 21:526-531(2003) [PubMed: 12692562] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BA000030 Genomic DNA. Translation: BAC69707.1.
RefSeq	NP_823172.1.
3D structure databases
HSSP	HSSP built from PDB template 1GKR based on UniProtKB P81006.
ModBase	Search...
Genome annotation databases
GeneID	1210332.
GenomeReviews	Gene locus SAV_1996 in contig BA000030_GR.
KEGG	sma:SAV_1996.
NMPDR	fig|227882.1.peg.1998.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q82LL4.
OMA	HSGVEEF.
Enzyme and pathway databases
BioCyc	SAVE227882:SAV1996-MON.
BRENDA	3.5.2.5. 140873.
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_STRAW

Accession

Primary (citable) accession number: Q82LL4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	June 1, 2003
Last modified:	November 3, 2009
This is version 43 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)