UniProt functional annotation for P0ACP7



	UniProt functional annotation for P0ACP7

UniProt code: P0ACP7.

Organism: Escherichia coli (strain K12).

Taxonomy: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.

Function: Is the main repressor of the genes involved in the de novo synthesis of purine nucleotides, regulating purB, purC, purEK, purF, purHD, purL, purMN and guaBA expression. In addition, it participates in the regulation or coregulation of genes involved in de novo pyrimidine nucleotide biosynthesis, salvage and uptake (pyrC, pyrD, carAB and codBA), and of several genes encoding enzymes necessary for nucleotide and polyamine biosynthesis (prsA, glyA, gcvTHP, speA, glnB). Binds to a 16-bp palindromic sequence located within the promoter region of pur regulon genes. The consensus binding sequence is 5'- ACGCAAACGTTTTCNT-3'. PurR is allosterically activated to bind its cognate DNA by binding the purine corepressors, hypoxanthine or guanine, thereby effecting transcription repression. {ECO:0000269|PubMed:1400170, ECO:0000269|PubMed:14741201, ECO:0000269|PubMed:2211500, ECO:0000269|PubMed:2404765}.

Pathway: Purine metabolism; purine nucleotide biosynthesis [regulation].

Subunit: Homodimer. {ECO:0000269|PubMed:11781089, ECO:0000269|PubMed:1400170, ECO:0000269|PubMed:7973627, ECO:0000269|PubMed:9278422, ECO:0000269|PubMed:9628480, ECO:0000269|Ref.17}.

Induction: Negatively autoregulated. {ECO:0000269|PubMed:2404765}.

Domain: Consists of two structural and functional domains: an N- terminal DNA-binding domain, approximately the first 60 residues, and a larger C-terminal domain, approximately 280 residues, which imparts the function of corepressor binding and oligomerization.

Miscellaneous: The corepressors hypoxanthine and guanine bind cooperatively to single PurR sites in each subunit of the dimer, inducing a conformational change which increases the affinity of PurR for its DNA operator sites.

Annotations taken from UniProtKB at the EBI.


Organism:		Escherichia coli (strain K12).
Taxonomy:		Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.



Function:		Is the main repressor of the genes involved in the de novo synthesis of purine nucleotides, regulating purB, purC, purEK, purF, purHD, purL, purMN and guaBA expression. In addition, it participates in the regulation or coregulation of genes involved in de novo pyrimidine nucleotide biosynthesis, salvage and uptake (pyrC, pyrD, carAB and codBA), and of several genes encoding enzymes necessary for nucleotide and polyamine biosynthesis (prsA, glyA, gcvTHP, speA, glnB). Binds to a 16-bp palindromic sequence located within the promoter region of pur regulon genes. The consensus binding sequence is 5'- ACGCAAACGTTTTCNT-3'. PurR is allosterically activated to bind its cognate DNA by binding the purine corepressors, hypoxanthine or guanine, thereby effecting transcription repression. {ECO:0000269\|PubMed:1400170, ECO:0000269\|PubMed:14741201, ECO:0000269\|PubMed:2211500, ECO:0000269\|PubMed:2404765}.


Pathway:		Purine metabolism; purine nucleotide biosynthesis [regulation].
Subunit:		Homodimer. {ECO:0000269\|PubMed:11781089, ECO:0000269\|PubMed:1400170, ECO:0000269\|PubMed:7973627, ECO:0000269\|PubMed:9278422, ECO:0000269\|PubMed:9628480, ECO:0000269\|Ref.17}.
Induction:		Negatively autoregulated. {ECO:0000269\|PubMed:2404765}.
Domain:		Consists of two structural and functional domains: an N- terminal DNA-binding domain, approximately the first 60 residues, and a larger C-terminal domain, approximately 280 residues, which imparts the function of corepressor binding and oligomerization.
Miscellaneous:		The corepressors hypoxanthine and guanine bind cooperatively to single PurR sites in each subunit of the dimer, inducing a conformational change which increases the affinity of PurR for its DNA operator sites.