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Conserved domains on  [gi|446465217|ref|WP_000543071|]
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MULTISPECIES: xanthine phosphoribosyltransferase [Acinetobacter]

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

EC:  2.4.2.22
Gene Ontology:  GO:0016763|GO:0046110|GO:0043101|GO:0000310
PubMed:  16716072|9100006|11933250

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK09219 PRK09219
xanthine phosphoribosyltransferase; Validated
 1-189 2.52e-124

xanthine phosphoribosyltransferase; Validated


:

Pssm-ID: 181705  Cd Length: 189  Bit Score: 348.31  E-value: 2.52e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446465217   1 MHALEQKILTEGIVLSDQVLKVDAFLNHQIDPVLMQQIGKEFAARFKDAGITKIITIEASGIAPAIMAGLELGVPVIFAR 80
Cdd:PRK09219   1 MKLLEERILKDGKVLSGNILKVDSFLNHQVDPKLMNEIGKEFARRFKDEGITKILTIEASGIAPAVMAALALGVPVVFAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446465217  81 KYQSLTLKDDLYRAKVFSFTKQTESTIAISNKHINSSDKALVIDDFLANGQAALGLIDLIHQANAEVVGVGIVIEKSFQP 160
Cdd:PRK09219  81 KKKSLTLTDDVYTATVYSFTKQVTSTVSVSKKFLSEGDRVLIIDDFLANGQAALGLIDIIEQAGAKVAGIGIVIEKSFQD 160

                        170       180
                 ....*....|....*....|....*....
gi 446465217 161 GRDLLLEKGYRVESLARVQSLADGTVTFV 189
Cdd:PRK09219 161 GRKLLEEKGYRVESLARIASLENGKVTFV 189
 
Name Accession Description Interval E-value
PRK09219 PRK09219
xanthine phosphoribosyltransferase; Validated
 1-189 2.52e-124

xanthine phosphoribosyltransferase; Validated


Pssm-ID: 181705  Cd Length: 189  Bit Score: 348.31  E-value: 2.52e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446465217   1 MHALEQKILTEGIVLSDQVLKVDAFLNHQIDPVLMQQIGKEFAARFKDAGITKIITIEASGIAPAIMAGLELGVPVIFAR 80
Cdd:PRK09219   1 MKLLEERILKDGKVLSGNILKVDSFLNHQVDPKLMNEIGKEFARRFKDEGITKILTIEASGIAPAVMAALALGVPVVFAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446465217  81 KYQSLTLKDDLYRAKVFSFTKQTESTIAISNKHINSSDKALVIDDFLANGQAALGLIDLIHQANAEVVGVGIVIEKSFQP 160
Cdd:PRK09219  81 KKKSLTLTDDVYTATVYSFTKQVTSTVSVSKKFLSEGDRVLIIDDFLANGQAALGLIDIIEQAGAKVAGIGIVIEKSFQD 160

                        170       180
                 ....*....|....*....|....*....
gi 446465217 161 GRDLLLEKGYRVESLARVQSLADGTVTFV 189
Cdd:PRK09219 161 GRKLLEEKGYRVESLARIASLENGKVTFV 189
XPRTase TIGR01744
xanthine phosphoribosyltransferase; This model represent a xanthine-specific ...
 1-191 9.55e-93

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: 268.60  E-value: 9.55e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446465217    1 MHALEQKILTEGIVLSDQVLKVDAFLNHQIDPVLMQQIGKEFAARFKDAGITKIITIEASGIAPAIMAGLELGVPVIFAR 80
Cdd:TIGR01744   1 MELLKQKIKEEGVVLPGGILKVDSFLNHQIDPKLMQEVGEEFARRFADDGITKIVTIEASGIAPAIMTGLKLGVPVVFAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446465217   81 KYQSLTLKDDLYRAKVFSFTKQTESTIAISNKHINSSDKALVIDDFLANGQAALGLIDLIHQANAEVVGVGIVIEKSFQP 160
Cdd:TIGR01744  81 KKKPLTLTDNLLTASVHSFTKQTTSTVAVSGEFLSDQDRVLIIDDFLANGQAAHGLVDIAKQAGAKIAGIGIVIEKSFQN 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 446465217  161 GRDLLLEKGYRVESLARVQSLADGTVTFVKE 191
Cdd:TIGR01744 161 GRQELVELGYRVESLARIQSLEEGKVTFVQE 191
Apt COG0503
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ...
 4-178 1.35e-52

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: 166.02  E-value: 1.35e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446465217   4 LEQKILTEGIVLSD--QVLKVDAFLnhqIDPVLMQQIGKEFAARFKDAGITKIITIEASGIAPAIMAGLELGVPVIFARK 81
Cdd:COG0503    3 LKDLIRDIPDFPKPgiLFRDITPLL---GDPELFRAAGDELAERFADKGIDKVVGIEARGFILAAALAYALGVPFVPARK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446465217  82 YQSLTLkdDLYRAKVFS-FTKQteSTIAISNKHINSSDKALVIDDFLANGQAALGLIDLIHQANAEVVGVGIVIEKSFQP 160
Cdd:COG0503   80 PGKLPG--ETVSEEYDLeYGTG--DTLELHKDALKPGDRVLIVDDLLATGGTAKAAIKLVEEAGAEVVGIAFLIELGFLG 155

                        170
                 ....*....|....*...
gi 446465217 161 GRDLLleKGYRVESLARV 178
Cdd:COG0503  156 GREKL--RDYPVESLLTL 171
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 38-176 1.72e-12

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: 61.64  E-value: 1.72e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446465217  38 IGKEFAARFKDAG--ITKIITIEASGIAPAIMAGLELGVPVIFARKyqsltlkddlyRAKVFSFTKQTESTIAISNKHIN 115
Cdd:cd06223    1 AGRLLAEEIREDLlePDVVVGILRGGLPLAAALARALGLPLAFIRK-----------ERKGPGRTPSEPYGLELPLGGDV 69

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446465217 116 SSDKALVIDDFLANGQAALGLIDLIHQANAEVVGVGIVIEKsFQPGRDLLLEKGYRVESLA 176
Cdd:cd06223   70 KGKRVLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVLLDK-PEGGARELASPGDPVYSLF 129
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 51-156 8.90e-04

Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl transferase enzymes. This family includes: Adenine phosphoribosyl-transferase EC:2.4.2.7. Hypoxanthine-guanine-xanthine phosphoribosyl-transferase. Hypoxanthine phosphoribosyl-transferase EC:2.4.2.8. Ribose-phosphate pyrophosphokinase i EC:2.7.6.1. Amidophosphoribosyltransferase EC:2.4.2.14. Orotate phosphoribosyl-transferase EC:2.4.2.10. Uracil phosphoribosyl-transferase EC:2.4.2.9. Xanthine-guanine phosphoribosyl-transferase EC:2.4.2.22. In Arabidopsis, At the very N-terminus of this domain is the P-Loop NTPase domain.


Pssm-ID: 425489 [Multi-domain]  Cd Length: 150  Bit Score: 38.11  E-value: 8.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446465217   51 ITKIITIEASGIAPAIMAGLELGVPVIFARKyqsltlkddlyrakVFSFTKQTESTIAISNKHINSSDKALVIDDFLANG 130
Cdd:pfam00156  30 PDVVVGILRGGLPFAGILARRLDVPLAFVRK--------------VSYNPDTSEVMKTSSALPDLKGKTVLIVDDILDTG 95

                          90       100
                  ....*....|....*....|....*.
gi 446465217  131 QAALGLIDLIHQANAEVVGVGIVIEK 156
Cdd:pfam00156  96 GTLLKVLELLKNVGPKEVKIAVLIDK 121
 
Name Accession Description Interval E-value
PRK09219 PRK09219
xanthine phosphoribosyltransferase; Validated
 1-189 2.52e-124

xanthine phosphoribosyltransferase; Validated


Pssm-ID: 181705  Cd Length: 189  Bit Score: 348.31  E-value: 2.52e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446465217   1 MHALEQKILTEGIVLSDQVLKVDAFLNHQIDPVLMQQIGKEFAARFKDAGITKIITIEASGIAPAIMAGLELGVPVIFAR 80
Cdd:PRK09219   1 MKLLEERILKDGKVLSGNILKVDSFLNHQVDPKLMNEIGKEFARRFKDEGITKILTIEASGIAPAVMAALALGVPVVFAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446465217  81 KYQSLTLKDDLYRAKVFSFTKQTESTIAISNKHINSSDKALVIDDFLANGQAALGLIDLIHQANAEVVGVGIVIEKSFQP 160
Cdd:PRK09219  81 KKKSLTLTDDVYTATVYSFTKQVTSTVSVSKKFLSEGDRVLIIDDFLANGQAALGLIDIIEQAGAKVAGIGIVIEKSFQD 160

                        170       180
                 ....*....|....*....|....*....
gi 446465217 161 GRDLLLEKGYRVESLARVQSLADGTVTFV 189
Cdd:PRK09219 161 GRKLLEEKGYRVESLARIASLENGKVTFV 189
XPRTase TIGR01744
xanthine phosphoribosyltransferase; This model represent a xanthine-specific ...
 1-191 9.55e-93

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: 268.60  E-value: 9.55e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446465217    1 MHALEQKILTEGIVLSDQVLKVDAFLNHQIDPVLMQQIGKEFAARFKDAGITKIITIEASGIAPAIMAGLELGVPVIFAR 80
Cdd:TIGR01744   1 MELLKQKIKEEGVVLPGGILKVDSFLNHQIDPKLMQEVGEEFARRFADDGITKIVTIEASGIAPAIMTGLKLGVPVVFAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446465217   81 KYQSLTLKDDLYRAKVFSFTKQTESTIAISNKHINSSDKALVIDDFLANGQAALGLIDLIHQANAEVVGVGIVIEKSFQP 160
Cdd:TIGR01744  81 KKKPLTLTDNLLTASVHSFTKQTTSTVAVSGEFLSDQDRVLIIDDFLANGQAAHGLVDIAKQAGAKIAGIGIVIEKSFQN 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 446465217  161 GRDLLLEKGYRVESLARVQSLADGTVTFVKE 191
Cdd:TIGR01744 161 GRQELVELGYRVESLARIQSLEEGKVTFVQE 191
Apt COG0503
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ...
 4-178 1.35e-52

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: 166.02  E-value: 1.35e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446465217   4 LEQKILTEGIVLSD--QVLKVDAFLnhqIDPVLMQQIGKEFAARFKDAGITKIITIEASGIAPAIMAGLELGVPVIFARK 81
Cdd:COG0503    3 LKDLIRDIPDFPKPgiLFRDITPLL---GDPELFRAAGDELAERFADKGIDKVVGIEARGFILAAALAYALGVPFVPARK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446465217  82 YQSLTLkdDLYRAKVFS-FTKQteSTIAISNKHINSSDKALVIDDFLANGQAALGLIDLIHQANAEVVGVGIVIEKSFQP 160
Cdd:COG0503   80 PGKLPG--ETVSEEYDLeYGTG--DTLELHKDALKPGDRVLIVDDLLATGGTAKAAIKLVEEAGAEVVGIAFLIELGFLG 155

                        170
                 ....*....|....*...
gi 446465217 161 GRDLLleKGYRVESLARV 178
Cdd:COG0503  156 GREKL--RDYPVESLLTL 171
PRK02304 PRK02304
adenine phosphoribosyltransferase; Provisional
 31-175 2.75e-20

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 235028  Cd Length: 175  Bit Score: 83.20  E-value: 2.75e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446465217  31 DPVLMQQIGKEFAARFKDAGITKIITIEASGIapaIMAG---LELGVPVIFARKYQSLTlkddlyrAKVFSFTKQTE--- 104
Cdd:PRK02304  32 DPEAFREVIDALVERYKDADIDKIVGIEARGF---IFGAalaYKLGIGFVPVRKPGKLP-------RETISESYELEygt 101

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446465217 105 STIAISNKHINSSDKALVIDDFLANGQAALGLIDLIHQANAEVVGVGIVIEKSFQPGRDLLleKGYRVESL 175
Cdd:PRK02304 102 DTLEIHKDAIKPGDRVLIVDDLLATGGTLEAAIKLLERLGAEVVGAAFVIELPDLGGREKL--EGYPVKSL 170
PRK08558 PRK08558
adenine phosphoribosyltransferase; Provisional
 31-157 4.44e-16

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 181466 [Multi-domain]  Cd Length: 238  Bit Score: 73.49  E-value: 4.44e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446465217  31 DPVLMQQIGKEFAARFKDAGITKIITIEASGIAPAIMAGLELGVPVIFARKYQSlTLKDDLYRAKVfSFTKQTESTIAIS 110
Cdd:PRK08558  92 DPSFLRLIAPVVAERFMGLRVDVVLTAATDGIPLAVAIASYFGADLVYAKKSKE-TGVEKFYEEYQ-RLASGIEVTLYLP 169

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 446465217 111 NKHINSSDKALVIDDFLANGQAALGLIDLIHQANAEVVGVGIVIEKS 157
Cdd:PRK08558 170 ASALKKGDRVLIVDDIIRSGETQRALLDLARQAGADVVGVFFLIAVG 216
PRK12560 PRK12560
adenine phosphoribosyltransferase; Provisional
 32-190 7.43e-14

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 183595  Cd Length: 187  Bit Score: 66.35  E-value: 7.43e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446465217  32 PVLMQQIGKEFAaRFKDAGITKIITIEASGIAPAIMAGLELGVPVIFARKYQSLTLKDDlyRAKVFSFTKQTESTIAISN 111
Cdd:PRK12560  34 PKVLKETAKEII-KYIDKDIDKIVTEEDKGAPLATPVSLLSGKPLAMARWYPYSLSELN--YNVVEIGSEYFEGVVYLNG 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446465217 112 khINSSDKALVIDDFLANGQAALGLIDLIHQANAEVVGVGIVIEKSFQPGRD-LLLEKGYRVESLARVQSLADGtVTFVK 190
Cdd:PRK12560 111 --IEKGDRVAIIDDTLSTGGTVIALIKAIENSGGIVSDVICVIEKTQNNGRKkLFTQTGINVKSLVKIDVKPHG-VDIIE 187
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 38-176 1.72e-12

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: 61.64  E-value: 1.72e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446465217  38 IGKEFAARFKDAG--ITKIITIEASGIAPAIMAGLELGVPVIFARKyqsltlkddlyRAKVFSFTKQTESTIAISNKHIN 115
Cdd:cd06223    1 AGRLLAEEIREDLlePDVVVGILRGGLPLAAALARALGLPLAFIRK-----------ERKGPGRTPSEPYGLELPLGGDV 69

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446465217 116 SSDKALVIDDFLANGQAALGLIDLIHQANAEVVGVGIVIEKsFQPGRDLLLEKGYRVESLA 176
Cdd:cd06223   70 KGKRVLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVLLDK-PEGGARELASPGDPVYSLF 129
PLN02293 PLN02293
adenine phosphoribosyltransferase
 31-168 1.11e-11

adenine phosphoribosyltransferase


Pssm-ID: 177930  Cd Length: 187  Bit Score: 60.46  E-value: 1.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446465217  31 DPVLMQQIGKEFAARFKDAGITKIITIEASG--IAPAImaGLELGVPVIFARKYQSLTlkddlyrAKVFSFTKQTE---S 105
Cdd:PLN02293  43 DPKAFKDTIDLFVERYRDMGISVVAGIEARGfiFGPPI--ALAIGAKFVPLRKPGKLP-------GEVISEEYVLEygtD 113

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446465217 106 TIAISNKHINSSDKALVIDDFLANGQAALGLIDLIHQANAEVVGVGIVIEKSFQPGRDLLLEK 168
Cdd:PLN02293 114 CLEMHVGAVEPGERALVIDDLIATGGTLCAAINLLERAGAEVVECACVIELPELKGREKLNGK 176
PyrE COG0461
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ...
 31-181 3.33e-10

Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate phosphoribosyltransferase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 440229  Cd Length: 201  Bit Score: 56.70  E-value: 3.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446465217  31 DPVLMQQIGKEFAARFKDAG--ITKIITIEASGIAPAIMAGLELGVPVIFARKyqsltlkddlyRAKVFSFTKQTEStia 108
Cdd:COG0461   42 YPEALELLGEALAELIKELGpeFDAVAGPATGGIPLAAAVARALGLPAIFVRK-----------EAKDHGTGGQIEG--- 107

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446465217 109 isnkHINSSDKALVIDDFLANGQAALGLIDLIHQANAEVVGVGIVIEKSfQPGRDLLLEKGYRVESLARVQSL 181
Cdd:COG0461  108 ----GLLPGERVLVVEDVITTGGSVLEAVEALREAGAEVVGVAVIVDRE-EGAAENLEEAGVPLHSLLTLDDL 175
pyrE PRK00455
orotate phosphoribosyltransferase; Validated
 31-178 2.28e-04

orotate phosphoribosyltransferase; Validated


Pssm-ID: 234771  Cd Length: 202  Bit Score: 40.14  E-value: 2.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446465217  31 DPVLMQQIGKEFAARFKDAG--ITKIITIEASGIAPAIMAGLELGVPVIFARKyqsltlkddlyRAKVFSFTKQTEstia 108
Cdd:PRK00455  43 YPEALALLGRFLAEAIKDSGieFDVVAGPATGGIPLAAAVARALDLPAIFVRK-----------EAKDHGEGGQIE---- 107

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446465217 109 isnKHINSSDKALVIDDFLANGQAALGLIDLIHQANAEVVGVGIVIEKSfQPGRDLLLEKGYRVESLARV 178
Cdd:PRK00455 108 ---GRRLFGKRVLVVEDVITTGGSVLEAVEAIRAAGAEVVGVAVIVDRQ-SAAQEVFADAGVPLISLITL 173
PRK07322 PRK07322
adenine phosphoribosyltransferase; Provisional
 31-150 2.45e-04

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 180928  Cd Length: 178  Bit Score: 39.96  E-value: 2.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446465217  31 DPVLMQQIGKEFAARFKDaGITKIITIEASGIAPAIMAGLELGVPVIFARKYQSLTLKDDLYRaKVFSFTKQTESTIAIS 110
Cdd:PRK07322  34 DTELTEAAAEALAKRLPT-EVDVLVTPETKGIPLAHALSRRLGKPYVVARKSRKPYMQDPIIQ-EVVSITTGKPQLLVLD 111

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 446465217 111 NKHINS--SDKALVIDDFLANGQAALGLIDLIHQANAEVVGV 150
Cdd:PRK07322 112 GADAEKlkGKRVAIVDDVVSTGGTLTALERLVERAGGQVVAK 153
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 51-156 8.90e-04

Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl transferase enzymes. This family includes: Adenine phosphoribosyl-transferase EC:2.4.2.7. Hypoxanthine-guanine-xanthine phosphoribosyl-transferase. Hypoxanthine phosphoribosyl-transferase EC:2.4.2.8. Ribose-phosphate pyrophosphokinase i EC:2.7.6.1. Amidophosphoribosyltransferase EC:2.4.2.14. Orotate phosphoribosyl-transferase EC:2.4.2.10. Uracil phosphoribosyl-transferase EC:2.4.2.9. Xanthine-guanine phosphoribosyl-transferase EC:2.4.2.22. In Arabidopsis, At the very N-terminus of this domain is the P-Loop NTPase domain.


Pssm-ID: 425489 [Multi-domain]  Cd Length: 150  Bit Score: 38.11  E-value: 8.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446465217   51 ITKIITIEASGIAPAIMAGLELGVPVIFARKyqsltlkddlyrakVFSFTKQTESTIAISNKHINSSDKALVIDDFLANG 130
Cdd:pfam00156  30 PDVVVGILRGGLPFAGILARRLDVPLAFVRK--------------VSYNPDTSEVMKTSSALPDLKGKTVLIVDDILDTG 95

                          90       100
                  ....*....|....*....|....*.
gi 446465217  131 QAALGLIDLIHQANAEVVGVGIVIEK 156
Cdd:pfam00156  96 GTLLKVLELLKNVGPKEVKIAVLIDK 121
 
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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