SMART: Pfam domain PAPS

The domain within your query sequence starts at position 303 and ends at position 460; the E-value for the PAPS_reduct domain shown below is 5.2e-25.

QLCVGFNGGKDCTALLHLFHAAVQRKFPDVPKPLQILYIRSISPFPELEQFLQDTIKRYN
LQVLEAEGNMKQALGELQEKHPQLEAVLMGTRRTDPYSCSLSHFSPTDPGWPSFMRINPL
LDWTYRNIWEFLRQLFVPYCILYDRGYTSLGSRENTTQ

PAPS_reduct

PFAM accession number:	PF01507
Interpro abstract (IPR002500):	This domain is found in phosphoadenosine phosphosulphate (PAPS) reductase enzymes or PAPS sulphotransferase. PAPS reductase is part of the adenine nucleotide alpha hydrolases superfamily also including N type ATP PPases and ATP sulphurylases [ (PUBMED:9261082) ]. A highly modified version of the P loop, the fingerprint peptide of mononucleotide-binding proteins, is present in the active site of the protein, which appears to be a positively charged cleft containing a number of conserved arginine and lysine residues. Although PAPS reductase has no ATPase activity, it shows a striking similarity to the structure of the ATP pyrophosphatase (ATP PPase) domain of GMP synthetase, indicating that both enzyme families have evolved from a common ancestral nucleotide-binding fold [ (PUBMED:9261082) ]. The enzyme uses thioredoxin as an electron donor for the reduction of PAPS to phospho-adenosine-phosphate (PAP) [ (PUBMED:9261082) (PUBMED:7588765) ]. It is also found in NodP nodulation protein P from Rhizobium meliloti (Sinorhizobium meliloti) which has ATP sulphurylase activity (sulphate adenylate transferase) [ (PUBMED:2250719) ].
GO function:	catalytic activity (GO:0003824)

PFAM accession number:

PF01507

Interpro abstract (IPR002500):

This domain is found in phosphoadenosine phosphosulphate (PAPS) reductase enzymes or PAPS sulphotransferase. PAPS reductase is part of the adenine nucleotide alpha hydrolases superfamily also including N type ATP PPases and ATP sulphurylases [ (PUBMED:9261082) ].

A highly modified version of the P loop, the fingerprint peptide of mononucleotide-binding proteins, is present in the active site of the protein, which appears to be a positively charged cleft containing a number of conserved arginine and lysine residues. Although PAPS reductase has no ATPase activity, it shows a striking similarity to the structure of the ATP pyrophosphatase (ATP PPase) domain of GMP synthetase, indicating that both enzyme families have evolved from a common ancestral nucleotide-binding fold [ (PUBMED:9261082) ].

The enzyme uses thioredoxin as an electron donor for the reduction of PAPS to phospho-adenosine-phosphate (PAP) [ (PUBMED:9261082) (PUBMED:7588765) ]. It is also found in NodP nodulation protein P from Rhizobium meliloti (Sinorhizobium meliloti) which has ATP sulphurylase activity (sulphate adenylate transferase) [ (PUBMED:2250719) ].

GO function:

catalytic activity (GO:0003824)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry PAPS_reduct