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Conserved domains on  [gi|2315541554|dbj|GIV44774|]
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MAG: hypothetical protein KatS3mg035_1897 [Bacteroidia bacterium]

Protein Classification

type I phosphoribosyltransferase( domain architecture ID 27)

type I phosphoribosyltransferase similar to phosphoribosyltransferases with specificities for hypoxanthine, guanine, and/or xanthine

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRTases_typeI super family cl00309
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 4-40 1.75e-05

Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The type I PRTases are identified by a conserved PRPP binding motif which features two adjacent acidic residues surrounded by one or more hydrophobic residue. PRTases catalyze the displacement of the alpha-1'-pyrophosphate of 5-phosphoribosyl-alpha1-pyrophosphate (PRPP) by a nitrogen-containing nucleophile. The reaction products are an alpha-1 substituted ribose-5'-phosphate and a free pyrophosphate (PP). PRPP, an activated form of ribose-5-phosphate, is a key metabolite connecting nucleotide synthesis and salvage pathways. The type I PRTase family includes a range of diverse phosphoribosyl transferase enzymes and regulatory proteins of the nucleotide synthesis and salvage pathways, including adenine phosphoribosyltransferase EC:2.4.2.7., hypoxanthine-guanine-xanthine phosphoribosyltransferase, hypoxanthine phosphoribosyltransferase EC:2.4.2.8., ribose-phosphate pyrophosphokinase EC:2.7.6.1., amidophosphoribosyltransferase EC:2.4.2.14., orotate phosphoribosyltransferase EC:2.4.2.10., uracil phosphoribosyltransferase EC:2.4.2.9., and xanthine-guanine phosphoribosyltransferase EC:2.4.2.22.


The actual alignment was detected with superfamily member PRK05205:

Pssm-ID: 444823  Cd Length: 176  Bit Score: 39.72  E-value: 1.75e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2315541554   4 QKVVILNAHQIEQKIKRIAYQIYENNVNESELIIAGI 40
Cdd:PRK05205    2 MKKEILDAEALRRALTRIAHEIIERNKGLDNLVLVGI 38
 
Name Accession Description Interval E-value
PRK05205 PRK05205
bifunctional pyr operon transcriptional regulator/uracil phosphoribosyltransferase PyrR;
4-40 1.75e-05

bifunctional pyr operon transcriptional regulator/uracil phosphoribosyltransferase PyrR;


Pssm-ID: 235365  Cd Length: 176  Bit Score: 39.72  E-value: 1.75e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2315541554   4 QKVVILNAHQIEQKIKRIAYQIYENNVNESELIIAGI 40
Cdd:PRK05205    2 MKKEILDAEALRRALTRIAHEIIERNKGLDNLVLVGI 38
 
Name Accession Description Interval E-value
PRK05205 PRK05205
bifunctional pyr operon transcriptional regulator/uracil phosphoribosyltransferase PyrR;
4-40 1.75e-05

bifunctional pyr operon transcriptional regulator/uracil phosphoribosyltransferase PyrR;


Pssm-ID: 235365  Cd Length: 176  Bit Score: 39.72  E-value: 1.75e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2315541554   4 QKVVILNAHQIEQKIKRIAYQIYENNVNESELIIAGI 40
Cdd:PRK05205    2 MKKEILDAEALRRALTRIAHEIIERNKGLDNLVLVGI 38
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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