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Conserved domains on  [gi|495621754|ref|WP_008346333|]
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MULTISPECIES: xanthine phosphoribosyltransferase [Bacillus]

Protein Classification

xanthine phosphoribosyltransferase( domain architecture ID 10013152)

xanthine phosphoribosyltransferase converts the preformed base xanthine, a product of nucleic acid breakdown, to xanthosine 5'-monophosphate (XMP), so it can be reused for RNA or DNA synthesis

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK09219 PRK09219
xanthine phosphoribosyltransferase; Validated
1-189 2.33e-114

xanthine phosphoribosyltransferase; Validated


:

Pssm-ID: 181705  Cd Length: 189  Bit Score: 323.27  E-value: 2.33e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621754   1 MELLRQKIENEGIVLSNQVLKVDAFLNHQIDPVLMHEIGQEFARLFKHDGITKIITIESSGIAPAVMAGLALHVPVVFAR 80
Cdd:PRK09219   1 MKLLEERILKDGKVLSGNILKVDSFLNHQVDPKLMNEIGKEFARRFKDEGITKILTIEASGIAPAVMAALALGVPVVFAK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621754  81 KRQSLTLTDNLLTASVYSFTKKVESTIAVSNTHLSEDDCVLIIDDFLANGEAAKGLAAIAKQAKAKVAGFGIVIEKSFQP 160
Cdd:PRK09219  81 KKKSLTLTDDVYTATVYSFTKQVTSTVSVSKKFLSEGDRVLIIDDFLANGQAALGLIDIIEQAGAKVAGIGIVIEKSFQD 160
                        170       180
                 ....*....|....*....|....*....
gi 495621754 161 GRKELVQMGYRVESLARIESLEEGKVTFV 189
Cdd:PRK09219 161 GRKLLEEKGYRVESLARIASLENGKVTFV 189
 
Name Accession Description Interval E-value
PRK09219 PRK09219
xanthine phosphoribosyltransferase; Validated
1-189 2.33e-114

xanthine phosphoribosyltransferase; Validated


Pssm-ID: 181705  Cd Length: 189  Bit Score: 323.27  E-value: 2.33e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621754   1 MELLRQKIENEGIVLSNQVLKVDAFLNHQIDPVLMHEIGQEFARLFKHDGITKIITIESSGIAPAVMAGLALHVPVVFAR 80
Cdd:PRK09219   1 MKLLEERILKDGKVLSGNILKVDSFLNHQVDPKLMNEIGKEFARRFKDEGITKILTIEASGIAPAVMAALALGVPVVFAK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621754  81 KRQSLTLTDNLLTASVYSFTKKVESTIAVSNTHLSEDDCVLIIDDFLANGEAAKGLAAIAKQAKAKVAGFGIVIEKSFQP 160
Cdd:PRK09219  81 KKKSLTLTDDVYTATVYSFTKQVTSTVSVSKKFLSEGDRVLIIDDFLANGQAALGLIDIIEQAGAKVAGIGIVIEKSFQD 160
                        170       180
                 ....*....|....*....|....*....
gi 495621754 161 GRKELVQMGYRVESLARIESLEEGKVTFV 189
Cdd:PRK09219 161 GRKLLEEKGYRVESLARIASLENGKVTFV 189
XPRTase TIGR01744
xanthine phosphoribosyltransferase; This model represent a xanthine-specific ...
1-191 2.43e-94

xanthine phosphoribosyltransferase; This model represent a xanthine-specific phosphoribosyltransferase of Bacillus subtilis and closely related proteins from other species, mostly from other Gram-positive bacteria. The adjacent gene is a xanthine transporter; B. subtilis can import xanthine for the purine salvage pathway or for catabolism to obtain nitrogen. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 130805  Cd Length: 191  Bit Score: 272.83  E-value: 2.43e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621754    1 MELLRQKIENEGIVLSNQVLKVDAFLNHQIDPVLMHEIGQEFARLFKHDGITKIITIESSGIAPAVMAGLALHVPVVFAR 80
Cdd:TIGR01744   1 MELLKQKIKEEGVVLPGGILKVDSFLNHQIDPKLMQEVGEEFARRFADDGITKIVTIEASGIAPAIMTGLKLGVPVVFAR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621754   81 KRQSLTLTDNLLTASVYSFTKKVESTIAVSNTHLSEDDCVLIIDDFLANGEAAKGLAAIAKQAKAKVAGFGIVIEKSFQP 160
Cdd:TIGR01744  81 KKKPLTLTDNLLTASVHSFTKQTTSTVAVSGEFLSDQDRVLIIDDFLANGQAAHGLVDIAKQAGAKIAGIGIVIEKSFQN 160
                         170       180       190
                  ....*....|....*....|....*....|.
gi 495621754  161 GRKELVQMGYRVESLARIESLEEGKVTFVRE 191
Cdd:TIGR01744 161 GRQELVELGYRVESLARIQSLEEGKVTFVQE 191
Apt COG0503
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ...
2-178 8.76e-42

Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide transport and metabolism]; Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein is part of the Pathway/BioSystem: Purine salvage


Pssm-ID: 440269  Cd Length: 171  Bit Score: 138.28  E-value: 8.76e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621754   2 ELLRQKIENEGIVLSN--QVLKVDAFLnhqIDPVLMHEIGQEFARLFKHDGITKIITIESSGIAPAVMAGLALHVPVVFA 79
Cdd:COG0503    1 EDLKDLIRDIPDFPKPgiLFRDITPLL---GDPELFRAAGDELAERFADKGIDKVVGIEARGFILAAALAYALGVPFVPA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621754  80 RKRQSLTLtdNLLTASVYS-FTKKveSTIAVSNTHLSEDDCVLIIDDFLANGEAAKGLAAIAKQAKAKVAGFGIVIEKSF 158
Cdd:COG0503   78 RKPGKLPG--ETVSEEYDLeYGTG--DTLELHKDALKPGDRVLIVDDLLATGGTAKAAIKLVEEAGAEVVGIAFLIELGF 153
                        170       180
                 ....*....|....*....|
gi 495621754 159 QPGRKELVqmGYRVESLARI 178
Cdd:COG0503  154 LGGREKLR--DYPVESLLTL 171
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
38-134 8.58e-06

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.


Pssm-ID: 206754 [Multi-domain]  Cd Length: 130  Bit Score: 43.54  E-value: 8.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621754  38 IGQEFARLFKHDG--ITKIITIESSGIAPAVMAGLALHVPVVFARKRQSLtltdnlltasvYSFTKKVESTIAVSNTHLS 115
Cdd:cd06223    1 AGRLLAEEIREDLlePDVVVGILRGGLPLAAALARALGLPLAFIRKERKG-----------PGRTPSEPYGLELPLGGDV 69
                         90
                 ....*....|....*....
gi 495621754 116 EDDCVLIIDDFLANGEAAK 134
Cdd:cd06223   70 KGKRVLLVDDVIATGGTLL 88
 
Name Accession Description Interval E-value
PRK09219 PRK09219
xanthine phosphoribosyltransferase; Validated
1-189 2.33e-114

xanthine phosphoribosyltransferase; Validated


Pssm-ID: 181705  Cd Length: 189  Bit Score: 323.27  E-value: 2.33e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621754   1 MELLRQKIENEGIVLSNQVLKVDAFLNHQIDPVLMHEIGQEFARLFKHDGITKIITIESSGIAPAVMAGLALHVPVVFAR 80
Cdd:PRK09219   1 MKLLEERILKDGKVLSGNILKVDSFLNHQVDPKLMNEIGKEFARRFKDEGITKILTIEASGIAPAVMAALALGVPVVFAK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621754  81 KRQSLTLTDNLLTASVYSFTKKVESTIAVSNTHLSEDDCVLIIDDFLANGEAAKGLAAIAKQAKAKVAGFGIVIEKSFQP 160
Cdd:PRK09219  81 KKKSLTLTDDVYTATVYSFTKQVTSTVSVSKKFLSEGDRVLIIDDFLANGQAALGLIDIIEQAGAKVAGIGIVIEKSFQD 160
                        170       180
                 ....*....|....*....|....*....
gi 495621754 161 GRKELVQMGYRVESLARIESLEEGKVTFV 189
Cdd:PRK09219 161 GRKLLEEKGYRVESLARIASLENGKVTFV 189
XPRTase TIGR01744
xanthine phosphoribosyltransferase; This model represent a xanthine-specific ...
1-191 2.43e-94

xanthine phosphoribosyltransferase; This model represent a xanthine-specific phosphoribosyltransferase of Bacillus subtilis and closely related proteins from other species, mostly from other Gram-positive bacteria. The adjacent gene is a xanthine transporter; B. subtilis can import xanthine for the purine salvage pathway or for catabolism to obtain nitrogen. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 130805  Cd Length: 191  Bit Score: 272.83  E-value: 2.43e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621754    1 MELLRQKIENEGIVLSNQVLKVDAFLNHQIDPVLMHEIGQEFARLFKHDGITKIITIESSGIAPAVMAGLALHVPVVFAR 80
Cdd:TIGR01744   1 MELLKQKIKEEGVVLPGGILKVDSFLNHQIDPKLMQEVGEEFARRFADDGITKIVTIEASGIAPAIMTGLKLGVPVVFAR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621754   81 KRQSLTLTDNLLTASVYSFTKKVESTIAVSNTHLSEDDCVLIIDDFLANGEAAKGLAAIAKQAKAKVAGFGIVIEKSFQP 160
Cdd:TIGR01744  81 KKKPLTLTDNLLTASVHSFTKQTTSTVAVSGEFLSDQDRVLIIDDFLANGQAAHGLVDIAKQAGAKIAGIGIVIEKSFQN 160
                         170       180       190
                  ....*....|....*....|....*....|.
gi 495621754  161 GRKELVQMGYRVESLARIESLEEGKVTFVRE 191
Cdd:TIGR01744 161 GRQELVELGYRVESLARIQSLEEGKVTFVQE 191
Apt COG0503
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ...
2-178 8.76e-42

Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide transport and metabolism]; Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein is part of the Pathway/BioSystem: Purine salvage


Pssm-ID: 440269  Cd Length: 171  Bit Score: 138.28  E-value: 8.76e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621754   2 ELLRQKIENEGIVLSN--QVLKVDAFLnhqIDPVLMHEIGQEFARLFKHDGITKIITIESSGIAPAVMAGLALHVPVVFA 79
Cdd:COG0503    1 EDLKDLIRDIPDFPKPgiLFRDITPLL---GDPELFRAAGDELAERFADKGIDKVVGIEARGFILAAALAYALGVPFVPA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621754  80 RKRQSLTLtdNLLTASVYS-FTKKveSTIAVSNTHLSEDDCVLIIDDFLANGEAAKGLAAIAKQAKAKVAGFGIVIEKSF 158
Cdd:COG0503   78 RKPGKLPG--ETVSEEYDLeYGTG--DTLELHKDALKPGDRVLIVDDLLATGGTAKAAIKLVEEAGAEVVGIAFLIELGF 153
                        170       180
                 ....*....|....*....|
gi 495621754 159 QPGRKELVqmGYRVESLARI 178
Cdd:COG0503  154 LGGREKLR--DYPVESLLTL 171
PRK02304 PRK02304
adenine phosphoribosyltransferase; Provisional
31-179 1.64e-09

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 235028  Cd Length: 175  Bit Score: 54.31  E-value: 1.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621754  31 DPVLMHEIGQEFARLFKHDGITKIITIESSG--IAPAVmaGLALHVPVVFARKRQSLTltdnlltASVYSFTKKVE---S 105
Cdd:PRK02304  32 DPEAFREVIDALVERYKDADIDKIVGIEARGfiFGAAL--AYKLGIGFVPVRKPGKLP-------RETISESYELEygtD 102
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495621754 106 TIAVSNTHLSEDDCVLIIDDFLANGEAAKGLAAIAKQAKAKVAGFGIVIEKSFQPGRKELvqMGYRVESLARIE 179
Cdd:PRK02304 103 TLEIHKDAIKPGDRVLIVDDLLATGGTLEAAIKLLERLGAEVVGAAFVIELPDLGGREKL--EGYPVKSLVKFD 174
PRK08558 PRK08558
adenine phosphoribosyltransferase; Provisional
31-157 8.82e-08

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 181466 [Multi-domain]  Cd Length: 238  Bit Score: 50.38  E-value: 8.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621754  31 DPVLMHEIGQEFARLFKHDGITKIITIESSGIAPAVMAGLALHVPVVFARKRQSlTLTDNLLTASVYSfTKKVESTIAVS 110
Cdd:PRK08558  92 DPSFLRLIAPVVAERFMGLRVDVVLTAATDGIPLAVAIASYFGADLVYAKKSKE-TGVEKFYEEYQRL-ASGIEVTLYLP 169
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 495621754 111 NTHLSEDDCVLIIDDFLANGEAAKGLAAIAKQAKAKVAGFGIVIEKS 157
Cdd:PRK08558 170 ASALKKGDRVLIVDDIIRSGETQRALLDLARQAGADVVGVFFLIAVG 216
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
38-134 8.58e-06

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.


Pssm-ID: 206754 [Multi-domain]  Cd Length: 130  Bit Score: 43.54  E-value: 8.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621754  38 IGQEFARLFKHDG--ITKIITIESSGIAPAVMAGLALHVPVVFARKRQSLtltdnlltasvYSFTKKVESTIAVSNTHLS 115
Cdd:cd06223    1 AGRLLAEEIREDLlePDVVVGILRGGLPLAAALARALGLPLAFIRKERKG-----------PGRTPSEPYGLELPLGGDV 69
                         90
                 ....*....|....*....
gi 495621754 116 EDDCVLIIDDFLANGEAAK 134
Cdd:cd06223   70 KGKRVLLVDDVIATGGTLL 88
PRK12560 PRK12560
adenine phosphoribosyltransferase; Provisional
32-184 3.56e-04

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 183595  Cd Length: 187  Bit Score: 39.77  E-value: 3.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621754  32 PVLMHEIGQEFARLFKHDgITKIITIESSGIAPAVMAGLALHVPVVFARKR--QSLTLTDNLLTASVYSFTKKVESTiav 109
Cdd:PRK12560  34 PKVLKETAKEIIKYIDKD-IDKIVTEEDKGAPLATPVSLLSGKPLAMARWYpySLSELNYNVVEIGSEYFEGVVYLN--- 109
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495621754 110 sntHLSEDDCVLIIDDFLANGEAAKGLAAIAKQAKAKVAGFGIVIEKSFQPGRKELV-QMGYRVESLARIESLEEG 184
Cdd:PRK12560 110 ---GIEKGDRVAIIDDTLSTGGTVIALIKAIENSGGIVSDVICVIEKTQNNGRKKLFtQTGINVKSLVKIDVKPHG 182
 
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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