P0AG19 (PURE_ECO57) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
N5-carboxyaminoimidazole ribonucleotide mutase
Short name=N5-CAIR mutase
EC=5.4.99.18

Alternative name(s):
5-(carboxyamino)imidazole ribonucleotide mutase

Gene names

Name:	purE
Ordered Locus Names:	Z0678, ECs0585

Organism

Escherichia coli O157:H7 [Complete proteome] [HAMAP]

Taxonomic identifier

83334 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	169 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide (CAIR) By similarity.
Catalytic activity	5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole = 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate.
Pathway	Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-phospho-D-ribosyl)imidazole (N5-CAIR route): step 2/2.
Subunit structure	Homooctamer By similarity.
Sequence similarities	Belongs to the AIR carboxylase family.

Ontologies

Keywords
Biological process	Purine biosynthesis
Molecular function	Isomerase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	'de novo' IMP biosynthetic process Inferred from electronic annotation. Source: InterPro
Molecular function	5-(carboxyamino)imidazole ribonucleotide mutase activity Inferred from electronic annotation. Source: EC phosphoribosylaminoimidazole carboxylase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 169	168	N5-carboxyaminoimidazole ribonucleotide mutase		PRO_0000074974
Sites
	Binding site	16	1	Substrate By similarity
	Binding site	19	1	Substrate By similarity
	Binding site	46	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P0AG19 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: E8B745B8D86E7D0B	FASTA	169	17,780
	10 20 30 40 50 60 MSSRNNPARV AIVMGSKSDW ATMQFAAEIF EILNVPHHVE VVSAHRTPDK LFSFAESAEE 70 80 90 100 110 120 NGYQVIIAGA GGAAHLPGMI AAKTLVPVLG VPVQSAALSG VDSLYSIVQM PRGIPVGTLA 130 140 150 160 IGKAGAANAA LLAAQILATH DKELHQRLND WRKAQTDEVL ENPDPRGAA

References

[1]

"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R. Nature 409:529-533(2001) [PubMed: 11206551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.

[2]

"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. , Kuhara S., Shiba T., Hattori M., Shinagawa H. DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE005174 Genomic DNA. Translation: AAG54880.1. BA000007 Genomic DNA. Translation: BAB34008.1.
PIR	A90702. D85552.
RefSeq	NP_286272.1. NC_002655.2. NP_308612.1. NC_002695.1.
3D structure databases
ProteinModelPortal	P0AG19.
SMR	P0AG19. Positions 7-168.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000028004; EBESCP00000026897; EBESCG00000027056. EBESCT00000059349; EBESCP00000057177; EBESCG00000058396.
GeneID	916940. 957530.
GenomeReviews	Gene locus Z0678 in contig AE005174_GR. Gene locus ECs0585 in contig BA000007_GR.
KEGG	ece:Z0678. ecs:ECs0585.
PATRIC	18350148. VBIEscCol44059_0594.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000010563.
HOGENOM	HBG301965.
OMA	LIMGSDS.
ProtClustDB	CLSK879691.
Enzyme and pathway databases
BioCyc	ECOL83334:ECS0585-MONOMER.
Family and domain databases
InterPro	IPR024694. N5-CAIR_mutase_PurE. IPR000031. N5-CAIR_Mutase_PurE_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.7700. AIR_carboxyl. 1 hit.
KO	K01588.
Pfam	PF00731. AIRC. 1 hit. [Graphical view]
PIRSF	PIRSF001338. AIR_carboxylase. 1 hit.
SMART	SM01001. AIRC. 1 hit. [Graphical view]
SUPFAM	SSF52255. AIR_carboxyl. 1 hit.
TIGRFAMs	TIGR01162. PurE. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PURE_ECO57

Accession

Primary (citable) accession number: P0AG19
Secondary accession number(s): P09028

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 46 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program