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Conserved domains on  [gi|658753047|ref|WP_029772562|]
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amidophosphoribosyltransferase, partial [Pseudoalteromonas sp. TB51]

Protein Classification

amidophosphoribosyltransferase( domain architecture ID 11414536)

amidophosphoribosyltransferase catalyzes the conversion of 5-phosphoribosyl-1-pyrophosphate (PRPP) into 5-phosphoribosyl-1-amine (PRA) by using the ammonia group from a glutamine side-chain, which is the committing step in de novo purine synthesis

CATH:  3.60.20.10|3.40.50.2020
EC:  2.4.2.14
Gene Ontology:  GO:0004044|GO:0046872|GO:0006164|GO:0051539|GO:0009113
PubMed:  9914248
SCOP:  4000253

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PurF COG0034
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ...
 1-410 0e+00

Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; Glutamine phosphoribosylpyrophosphate amidotransferase is part of the Pathway/BioSystem: Purine biosynthesis


:

Pssm-ID: 439804 [Multi-domain]  Cd Length: 464  Bit Score: 628.21  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047   1 VRYPTAGSSSSSEAQPFYVNSPFG-IALAHNGNLTNAETLKQQLFSEARrHVNTTSDSEILLNIMAHELSKsdklhldaE 79
Cdd:COG0034   78 VRYSTTGSSSLENAQPFYVNSPFGsIALAHNGNLTNAEELREELEEEGA-IFQTTSDTEVILHLIARELTK--------E 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047  80 DIFTAVTEVNNKVTGGYAAIAMIiGHGVLAFRDPNGIRPLVFGKRETpkgtEYMFASESVALKPDGFEFVRDVAPGEAIY 159
Cdd:COG0034  149 DLEEAIKEALRRVKGAYSLVILT-GDGLIAARDPNGIRPLVLGKLED----GYVVASESCALDILGAEFVRDVEPGEIVV 223

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047 160 VTEDGqFHSQSCAEKASYAPCIFEFVYFARPDSTIDRMSVYATRVNMGTKLgekiAREwSDKDIDVVIPIPETSCDVALE 239
Cdd:COG0034  224 IDEDG-LRSRQFAEKPRPAPCIFEYVYFARPDSVIDGRSVYEARKRMGREL----ARE-APVDADVVIPVPDSGRPAAIG 297

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047 240 IARMLDLPYRQGFVKNRYIGRTFIMPGQEMRKKSVRQKLNAIDREFKGKNVLLVDDSIVRGTTSAQIVEMAREAGAKNVY 319
Cdd:COG0034  298 YAEESGIPYEEGLIKNRYVGRTFIQPTQELRELGVRLKLNPIREVVKGKRVVLVDDSIVRGTTSRRIVKMLREAGAKEVH 377

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047 320 FASAAPEIRFPNVYGIDMPSAAELIAHGREVEDINQSISADGLIFQSLNDLIAAVSQENPEitkFETSVFDGQYITGdID 399
Cdd:COG0034  378 FRIASPPIRYPCYYGIDTPTREELIAANRSVEEIREYIGADSLGYLSLEGLIEAVGEPIEG---FCTACFTGDYPTG-IP 453

                        410
                 ....*....|.
gi 658753047 400 QDYLNHIDQLR 410
Cdd:COG0034  454 DEEKKRLELLR 464
 
Name Accession Description Interval E-value
PurF COG0034
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ...
 1-410 0e+00

Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; Glutamine phosphoribosylpyrophosphate amidotransferase is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 439804 [Multi-domain]  Cd Length: 464  Bit Score: 628.21  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047   1 VRYPTAGSSSSSEAQPFYVNSPFG-IALAHNGNLTNAETLKQQLFSEARrHVNTTSDSEILLNIMAHELSKsdklhldaE 79
Cdd:COG0034   78 VRYSTTGSSSLENAQPFYVNSPFGsIALAHNGNLTNAEELREELEEEGA-IFQTTSDTEVILHLIARELTK--------E 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047  80 DIFTAVTEVNNKVTGGYAAIAMIiGHGVLAFRDPNGIRPLVFGKRETpkgtEYMFASESVALKPDGFEFVRDVAPGEAIY 159
Cdd:COG0034  149 DLEEAIKEALRRVKGAYSLVILT-GDGLIAARDPNGIRPLVLGKLED----GYVVASESCALDILGAEFVRDVEPGEIVV 223

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047 160 VTEDGqFHSQSCAEKASYAPCIFEFVYFARPDSTIDRMSVYATRVNMGTKLgekiAREwSDKDIDVVIPIPETSCDVALE 239
Cdd:COG0034  224 IDEDG-LRSRQFAEKPRPAPCIFEYVYFARPDSVIDGRSVYEARKRMGREL----ARE-APVDADVVIPVPDSGRPAAIG 297

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047 240 IARMLDLPYRQGFVKNRYIGRTFIMPGQEMRKKSVRQKLNAIDREFKGKNVLLVDDSIVRGTTSAQIVEMAREAGAKNVY 319
Cdd:COG0034  298 YAEESGIPYEEGLIKNRYVGRTFIQPTQELRELGVRLKLNPIREVVKGKRVVLVDDSIVRGTTSRRIVKMLREAGAKEVH 377

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047 320 FASAAPEIRFPNVYGIDMPSAAELIAHGREVEDINQSISADGLIFQSLNDLIAAVSQENPEitkFETSVFDGQYITGdID 399
Cdd:COG0034  378 FRIASPPIRYPCYYGIDTPTREELIAANRSVEEIREYIGADSLGYLSLEGLIEAVGEPIEG---FCTACFTGDYPTG-IP 453

                        410
                 ....*....|.
gi 658753047 400 QDYLNHIDQLR 410
Cdd:COG0034  454 DEEKKRLELLR 464
purF TIGR01134
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ...
 1-393 0e+00

amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) amidotransferase. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273461 [Multi-domain]  Cd Length: 442  Bit Score: 539.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047    1 VRYPTAGSSSSSEAQPFYVNSPFG-IALAHNGNLTNAETLKQQLFSEaRRHVNTTSDSEILLNIMAHELSKSDklhldae 79
Cdd:TIGR01134  72 VRYSTAGSSGLENAQPFVVNSPYGgLALAHNGNLVNADELRRELEEE-GRHFNTTSDSEVLLHLLAHNDESKD------- 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047   80 DIFTAVTEVNNKVTGGYAAIAMIiGHGVLAFRDPNGIRPLVFGKRETpkgtEYMFASESVALKPDGFEFVRDVAPGEAIy 159
Cdd:TIGR01134 144 DLFDAVARVLERVRGAYALVLMT-EDGLVAVRDPHGIRPLVLGRRGD----GYVVASESCALDILGAEFVRDVEPGEVV- 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047  160 VTEDGQFHSQSCaEKASYAPCIFEFVYFARPDSTIDRMSVYATRVNMGTKLGEKiarewSDKDIDVVIPIPETSCDVALE 239
Cdd:TIGR01134 218 VIFDGGLESRQC-ARRPRAPCVFEYVYFARPDSVIDGISVYYARKRMGKELARE-----SPVEADVVVPVPDSGRSAALG 291

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047  240 IARMLDLPYRQGFVKNRYIGRTFIMPGQEMRKKSVRQKLNAIDREFKGKNVLLVDDSIVRGTTSAQIVEMAREAGAKNVY 319
Cdd:TIGR01134 292 FAQASGIPYREGLIKNRYVGRTFIMPTQELRELSVRLKLNPVRAVFEGKRVVLVDDSIVRGTTSRQIVEMLRDAGAKEVH 371

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658753047  320 FASAAPEIRFPNVYGIDMPSAAELIAHGREVEDInQSISADGLIFQSLNDLIAAVSQENPeitKFETSVFDGQY 393
Cdd:TIGR01134 372 VRIASPPIRYPCYYGIDMPTREELIAARRTVEEI-RKIGADSLAYLSLEGLKEAVGNPES---DLCLACFTGEY 441
PLN02440 PLN02440
amidophosphoribosyltransferase
 1-418 1.37e-178

amidophosphoribosyltransferase


Pssm-ID: 215241 [Multi-domain]  Cd Length: 479  Bit Score: 507.29  E-value: 1.37e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047   1 VRYPTAGSSSSSEAQPFYVNSPFG-IALAHNGNLTNAETLKQQLfSEARRHVNTTSDSEILLNIMAHELSKSdklhldae 79
Cdd:PLN02440  72 VRYSTAGASSLKNVQPFVANYRFGsIGVAHNGNLVNYEELRAKL-EENGSIFNTSSDTEVLLHLIAISKARP-------- 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047  80 dIFTAVTEVNNKVTGGYAAIAMIIGHgVLAFRDPNGIRPLVFGKRetpKGTEYMFASESVALKPDGFEFVRDVAPGEAIY 159
Cdd:PLN02440 143 -FFSRIVDACEKLKGAYSMVFLTEDK-LVAVRDPHGFRPLVMGRR---SNGAVVFASETCALDLIGATYEREVNPGEVIV 217

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047 160 VTEDGQFHSQSCAEKASYAPCIFEFVYFARPDSTIDRMSVYATRVNMGTKLGEKIARewsdkDIDVVIPIPETSCDVALE 239
Cdd:PLN02440 218 VDKDKGVSSQCLMPHPEPKPCIFEHIYFARPNSIVFGRSVYESRLEFGEILATEIPV-----DCDVVIPVPDSGRVAALG 292

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047 240 IARMLDLPYRQGFVKNRYIGRTFIMPGQEMRKKSVRQKLNAIDREFKGKNVLLVDDSIVRGTTSAQIVEMAREAGAKNVY 319
Cdd:PLN02440 293 YAAKLGVPFQQGLIRSHYVGRTFIEPSQKIRDFSVKLKLNPVRSVLEGKRVVVVDDSIVRGTTSSKIVRMLREAGAKEVH 372

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047 320 FASAAPEIRFPNVYGIDMPSAAELIAHGREVEDINQSISADGLIFQSLNDLIAAVSQENPeitKFETSVFDGQY------ 393
Cdd:PLN02440 373 MRIASPPIIASCYYGVDTPSREELISNRMSVEEIRKFIGCDSLAFLPLEDLKKSLGEESP---RFCYACFSGDYpvlpkr 449

                        410       420
                 ....*....|....*....|....*
gi 658753047 394 ITGDIDQDYLNHIDQLRNDSAKSNR 418
Cdd:PLN02440 450 VGGDIDDGYLESLEEAGRGWGRKGR 474
GPATase_N cd00715
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ...
 1-195 1.06e-93

Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the N-terminus of glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase) . The glutaminase domain catalyzes amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. GPATase catalyzes the first step in purine biosynthesis, an amide transfer from glutamine to PRPP, resulting in phosphoribosylamine, pyrophosphate and glutamate. GPATase crystalizes as a homotetramer, but can also exist as a homdimer.


Pssm-ID: 238367 [Multi-domain]  Cd Length: 252  Bit Score: 282.81  E-value: 1.06e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047   1 VRYPTAGSSSSSEAQPFYVNSPFG-IALAHNGNLTNAETLKQQLFSEARrHVNTTSDSEILLNIMAHELSKsdklhldaE 79
Cdd:cd00715   71 VRYSTAGSSSLENAQPFVVNSPLGgIALAHNGNLVNAKELREELEEEGR-IFQTTSDSEVILHLIARSLAK--------D 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047  80 DIFTAVTEVNNKVTGGYAAIAMIIgHGVLAFRDPNGIRPLVFGKREtpkGTEYMFASESVALKPDGFEFVRDVAPGEAIY 159
Cdd:cd00715  142 DLFEAIIDALERVKGAYSLVIMTA-DGLIAVRDPHGIRPLVLGKLE---GDGYVVASESCALDIIGAEFVRDVEPGEIVV 217

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 658753047 160 VTEDGQFHSQsCAEKASYAPCIFEFVYFARPDSTID 195
Cdd:cd00715  218 IDDDGLESSQ-RAPKPKPAPCIFEYVYFARPDSVID 252
GATase_7 pfam13537
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ...
 10-143 1.55e-11

Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain found in a variety of enzymes such as asparagine synthetase and glutamine-fructose-6-phosphate transaminase.


Pssm-ID: 433289 [Multi-domain]  Cd Length: 123  Bit Score: 61.38  E-value: 1.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047   10 SSSEAQPFyVNSPFG-IALAHNGNLTNAETLKQQLfsEARRHV-NTTSDSEILLNIMAHElsksdklhlDAEDIFtavte 87
Cdd:pfam13537   9 LEGGAQPM-VSSEDGrYVIVFNGEIYNYRELRAEL--EAKGYRfRTHSDTEVILHLYEAE---------WGEDCV----- 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 658753047   88 vnNKVTGGYA-AIAMIIGHGVLAFRDPNGIRPLVFGKRetpKGTEYMFASESVALKP 143
Cdd:pfam13537  72 --DRLNGMFAfAIWDRRRQRLFLARDRFGIKPLYYGRD---DGGRLLFASELKALLA 123
 
Name Accession Description Interval E-value
PurF COG0034
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ...
 1-410 0e+00

Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; Glutamine phosphoribosylpyrophosphate amidotransferase is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 439804 [Multi-domain]  Cd Length: 464  Bit Score: 628.21  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047   1 VRYPTAGSSSSSEAQPFYVNSPFG-IALAHNGNLTNAETLKQQLFSEARrHVNTTSDSEILLNIMAHELSKsdklhldaE 79
Cdd:COG0034   78 VRYSTTGSSSLENAQPFYVNSPFGsIALAHNGNLTNAEELREELEEEGA-IFQTTSDTEVILHLIARELTK--------E 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047  80 DIFTAVTEVNNKVTGGYAAIAMIiGHGVLAFRDPNGIRPLVFGKRETpkgtEYMFASESVALKPDGFEFVRDVAPGEAIY 159
Cdd:COG0034  149 DLEEAIKEALRRVKGAYSLVILT-GDGLIAARDPNGIRPLVLGKLED----GYVVASESCALDILGAEFVRDVEPGEIVV 223

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047 160 VTEDGqFHSQSCAEKASYAPCIFEFVYFARPDSTIDRMSVYATRVNMGTKLgekiAREwSDKDIDVVIPIPETSCDVALE 239
Cdd:COG0034  224 IDEDG-LRSRQFAEKPRPAPCIFEYVYFARPDSVIDGRSVYEARKRMGREL----ARE-APVDADVVIPVPDSGRPAAIG 297

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047 240 IARMLDLPYRQGFVKNRYIGRTFIMPGQEMRKKSVRQKLNAIDREFKGKNVLLVDDSIVRGTTSAQIVEMAREAGAKNVY 319
Cdd:COG0034  298 YAEESGIPYEEGLIKNRYVGRTFIQPTQELRELGVRLKLNPIREVVKGKRVVLVDDSIVRGTTSRRIVKMLREAGAKEVH 377

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047 320 FASAAPEIRFPNVYGIDMPSAAELIAHGREVEDINQSISADGLIFQSLNDLIAAVSQENPEitkFETSVFDGQYITGdID 399
Cdd:COG0034  378 FRIASPPIRYPCYYGIDTPTREELIAANRSVEEIREYIGADSLGYLSLEGLIEAVGEPIEG---FCTACFTGDYPTG-IP 453

                        410
                 ....*....|.
gi 658753047 400 QDYLNHIDQLR 410
Cdd:COG0034  454 DEEKKRLELLR 464
purF TIGR01134
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ...
 1-393 0e+00

amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) amidotransferase. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273461 [Multi-domain]  Cd Length: 442  Bit Score: 539.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047    1 VRYPTAGSSSSSEAQPFYVNSPFG-IALAHNGNLTNAETLKQQLFSEaRRHVNTTSDSEILLNIMAHELSKSDklhldae 79
Cdd:TIGR01134  72 VRYSTAGSSGLENAQPFVVNSPYGgLALAHNGNLVNADELRRELEEE-GRHFNTTSDSEVLLHLLAHNDESKD------- 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047   80 DIFTAVTEVNNKVTGGYAAIAMIiGHGVLAFRDPNGIRPLVFGKRETpkgtEYMFASESVALKPDGFEFVRDVAPGEAIy 159
Cdd:TIGR01134 144 DLFDAVARVLERVRGAYALVLMT-EDGLVAVRDPHGIRPLVLGRRGD----GYVVASESCALDILGAEFVRDVEPGEVV- 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047  160 VTEDGQFHSQSCaEKASYAPCIFEFVYFARPDSTIDRMSVYATRVNMGTKLGEKiarewSDKDIDVVIPIPETSCDVALE 239
Cdd:TIGR01134 218 VIFDGGLESRQC-ARRPRAPCVFEYVYFARPDSVIDGISVYYARKRMGKELARE-----SPVEADVVVPVPDSGRSAALG 291

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047  240 IARMLDLPYRQGFVKNRYIGRTFIMPGQEMRKKSVRQKLNAIDREFKGKNVLLVDDSIVRGTTSAQIVEMAREAGAKNVY 319
Cdd:TIGR01134 292 FAQASGIPYREGLIKNRYVGRTFIMPTQELRELSVRLKLNPVRAVFEGKRVVLVDDSIVRGTTSRQIVEMLRDAGAKEVH 371

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658753047  320 FASAAPEIRFPNVYGIDMPSAAELIAHGREVEDInQSISADGLIFQSLNDLIAAVSQENPeitKFETSVFDGQY 393
Cdd:TIGR01134 372 VRIASPPIRYPCYYGIDMPTREELIAARRTVEEI-RKIGADSLAYLSLEGLKEAVGNPES---DLCLACFTGEY 441
PLN02440 PLN02440
amidophosphoribosyltransferase
 1-418 1.37e-178

amidophosphoribosyltransferase


Pssm-ID: 215241 [Multi-domain]  Cd Length: 479  Bit Score: 507.29  E-value: 1.37e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047   1 VRYPTAGSSSSSEAQPFYVNSPFG-IALAHNGNLTNAETLKQQLfSEARRHVNTTSDSEILLNIMAHELSKSdklhldae 79
Cdd:PLN02440  72 VRYSTAGASSLKNVQPFVANYRFGsIGVAHNGNLVNYEELRAKL-EENGSIFNTSSDTEVLLHLIAISKARP-------- 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047  80 dIFTAVTEVNNKVTGGYAAIAMIIGHgVLAFRDPNGIRPLVFGKRetpKGTEYMFASESVALKPDGFEFVRDVAPGEAIY 159
Cdd:PLN02440 143 -FFSRIVDACEKLKGAYSMVFLTEDK-LVAVRDPHGFRPLVMGRR---SNGAVVFASETCALDLIGATYEREVNPGEVIV 217

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047 160 VTEDGQFHSQSCAEKASYAPCIFEFVYFARPDSTIDRMSVYATRVNMGTKLGEKIARewsdkDIDVVIPIPETSCDVALE 239
Cdd:PLN02440 218 VDKDKGVSSQCLMPHPEPKPCIFEHIYFARPNSIVFGRSVYESRLEFGEILATEIPV-----DCDVVIPVPDSGRVAALG 292

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047 240 IARMLDLPYRQGFVKNRYIGRTFIMPGQEMRKKSVRQKLNAIDREFKGKNVLLVDDSIVRGTTSAQIVEMAREAGAKNVY 319
Cdd:PLN02440 293 YAAKLGVPFQQGLIRSHYVGRTFIEPSQKIRDFSVKLKLNPVRSVLEGKRVVVVDDSIVRGTTSSKIVRMLREAGAKEVH 372

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047 320 FASAAPEIRFPNVYGIDMPSAAELIAHGREVEDINQSISADGLIFQSLNDLIAAVSQENPeitKFETSVFDGQY------ 393
Cdd:PLN02440 373 MRIASPPIIASCYYGVDTPSREELISNRMSVEEIRKFIGCDSLAFLPLEDLKKSLGEESP---RFCYACFSGDYpvlpkr 449

                        410       420
                 ....*....|....*....|....*
gi 658753047 394 ITGDIDQDYLNHIDQLRNDSAKSNR 418
Cdd:PLN02440 450 VGGDIDDGYLESLEEAGRGWGRKGR 474
PRK05793 PRK05793
amidophosphoribosyltransferase; Provisional
 1-393 3.07e-122

amidophosphoribosyltransferase; Provisional


Pssm-ID: 235611 [Multi-domain]  Cd Length: 469  Bit Score: 363.58  E-value: 3.07e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047   1 VRYPTAGSSSSSEAQPFYVNSPFG-IALAHNGNLTNAETLKQQLfSEARRHVNTTSDSEILLNIMAHELSKsdklhldae 79
Cdd:PRK05793  87 VRYSTTGASDLDNAQPLVANYKLGsIAIAHNGNLVNADVIRELL-EDGGRIFQTSIDSEVILNLIARSAKK--------- 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047  80 DIFTAVTEVNNKVTGGYAaIAMIIGHGVLAFRDPNGIRPLVFGKretpKGTEYMFASESVALKPDGFEFVRDVAPGEAIY 159
Cdd:PRK05793 157 GLEKALVDAIQAIKGSYA-LVILTEDKLIGVRDPHGIRPLCLGK----LGDDYILSSESCALDTIGAEFIRDVEPGEIVI 231

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047 160 VTEDGqFHSQSCAEKASYAPCIFEFVYFARPDSTIDRMSVYATRVNMGtklgEKIAREwSDKDIDVVIPIPETSCDVALE 239
Cdd:PRK05793 232 IDEDG-IKSIKFAEKTKCQTCAFEYIYFARPDSVIDGISVYESRVRAG----RQLYKE-YPVDADIVIGVPDSGIPAAIG 305

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047 240 IARMLDLPYRQGFVKNRYIGRTFIMPGQEMRKKSVRQKLNAIDREFKGKNVLLVDDSIVRGTTSAQIVEMAREAGAKNVY 319
Cdd:PRK05793 306 YAEASGIPYGIGFIKNKYVGRTFIAPSQELRERAVRVKLNPLKVNVEGKRVVLIDDSIVRGTTSKRLVELLRKAGAKEVH 385

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658753047 320 FASAAPEIRFPNVYGIDMPSAAELIAHGREVEDINQSISADGLIFQSLNDLIAAVSQENpeitKFETSVFDGQY 393
Cdd:PRK05793 386 FRVSSPPVKYPCYFGIDTPYRKELIGANMSVEEIREMIGADSLGYLSIEGLLESLNGDK----GFCLGCFNGVY 455
GPATase_N cd00715
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ...
 1-195 1.06e-93

Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the N-terminus of glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase) . The glutaminase domain catalyzes amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. GPATase catalyzes the first step in purine biosynthesis, an amide transfer from glutamine to PRPP, resulting in phosphoribosylamine, pyrophosphate and glutamate. GPATase crystalizes as a homotetramer, but can also exist as a homdimer.


Pssm-ID: 238367 [Multi-domain]  Cd Length: 252  Bit Score: 282.81  E-value: 1.06e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047   1 VRYPTAGSSSSSEAQPFYVNSPFG-IALAHNGNLTNAETLKQQLFSEARrHVNTTSDSEILLNIMAHELSKsdklhldaE 79
Cdd:cd00715   71 VRYSTAGSSSLENAQPFVVNSPLGgIALAHNGNLVNAKELREELEEEGR-IFQTTSDSEVILHLIARSLAK--------D 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047  80 DIFTAVTEVNNKVTGGYAAIAMIIgHGVLAFRDPNGIRPLVFGKREtpkGTEYMFASESVALKPDGFEFVRDVAPGEAIY 159
Cdd:cd00715  142 DLFEAIIDALERVKGAYSLVIMTA-DGLIAVRDPHGIRPLVLGKLE---GDGYVVASESCALDIIGAEFVRDVEPGEIVV 217

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 658753047 160 VTEDGQFHSQsCAEKASYAPCIFEFVYFARPDSTID 195
Cdd:cd00715  218 IDDDGLESSQ-RAPKPKPAPCIFEYVYFARPDSVID 252
Gn_AT_II cd00352
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ...
 1-158 1.18e-35

Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. This domain is related to members of the Ntn (N-terminal nucleophile) hydrolase superfamily and is found at the N-terminus of enzymes such as glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). GLMS catalyzes the formation of glucosamine 6-phosphate from fructose 6-phosphate and glutamine in amino sugar synthesis. GPATase catalyzes the first step in purine biosynthesis, an amide transfer from glutamine to PRPP, resulting in phosphoribosylamine, pyrophosphate and glutamate. Asparagine synthetase B synthesizes asparagine from aspartate and glutamine. Beta-LS catalyzes the formation of the beta-lactam ring in the beta-lactamase inhibitor clavulanic acid. GltS synthesizes L-glutamate from 2-oxoglutarate and L-glutamine. These enzymes are generally dimers, but GPATase also exists as a homotetramer.


Pssm-ID: 238212 [Multi-domain]  Cd Length: 220  Bit Score: 131.03  E-value: 1.18e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047   1 VRYPTAGSSSSSEAQPFYVNSPfGIALAHNGNLTNAETLKQQLFSEaRRHVNTTSDSEILLNIMAHelsksdklHLDAED 80
Cdd:cd00352   75 VRLATNGLPSEANAQPFRSEDG-RIALVHNGEIYNYRELREELEAR-GYRFEGESDSEVILHLLER--------LGREGG 144

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658753047  81 IFTAVTEVNNKVTGGYAAIAMIIG-HGVLAFRDPNGIRPLVFGKRetpKGTEYMFASESVALKPDGFEFVRDVAPGEAI 158
Cdd:cd00352  145 LFEAVEDALKRLDGPFAFALWDGKpDRLFAARDRFGIRPLYYGIT---KDGGLVFASEPKALLALPFKGVRRLPPGELL 220
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 210-325 2.25e-19

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: 83.60  E-value: 2.25e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047 210 LGEKIAREWSDK--DIDVVIPIPETSCDVALEIARMLDLPYRQGFVKNRYIGRTFIMPgqemrkksvRQKLNAIDREFKG 287
Cdd:cd06223    1 AGRLLAEEIREDllEPDVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSEP---------YGLELPLGGDVKG 71

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 658753047 288 KNVLLVDDSIVRGTTSAQIVEMAREAGAKNVYFASAAP 325
Cdd:cd06223   72 KRVLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVLLD 109
GATase_7 pfam13537
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ...
 10-143 1.55e-11

Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain found in a variety of enzymes such as asparagine synthetase and glutamine-fructose-6-phosphate transaminase.


Pssm-ID: 433289 [Multi-domain]  Cd Length: 123  Bit Score: 61.38  E-value: 1.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047   10 SSSEAQPFyVNSPFG-IALAHNGNLTNAETLKQQLfsEARRHV-NTTSDSEILLNIMAHElsksdklhlDAEDIFtavte 87
Cdd:pfam13537   9 LEGGAQPM-VSSEDGrYVIVFNGEIYNYRELRAEL--EAKGYRfRTHSDTEVILHLYEAE---------WGEDCV----- 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 658753047   88 vnNKVTGGYA-AIAMIIGHGVLAFRDPNGIRPLVFGKRetpKGTEYMFASESVALKP 143
Cdd:pfam13537  72 --DRLNGMFAfAIWDRRRQRLFLARDRFGIKPLYYGRD---DGGRLLFASELKALLA 123
YafJ COG0121
Predicted glutamine amidotransferase YafJ [General function prediction only];
1-168 2.38e-09

Predicted glutamine amidotransferase YafJ [General function prediction only];


Pssm-ID: 439891 [Multi-domain]  Cd Length: 248  Bit Score: 57.67  E-value: 2.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047   1 VRYPTAGSSSSSEAQPFYVnspFGIALAHNGNLTNAETLKQQLFS----EARRHVNTTSDSEILLNIMAHELSKSDklHL 76
Cdd:COG0121   83 VRKATVGPVSLENTHPFRG---GRWLFAHNGQLDGFDRLRRRLAEelpdELYFQPVGTTDSELAFALLLSRLRDGG--PD 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047  77 DAEDIFTAVTEVnNKVTGGYAAIAMII--GHGVLAFRDPNGIRP--LVFGKRETPKGTEYMFASESVALKPDGfefvRDV 152
Cdd:COG0121  158 PAEALAEALREL-AELARAPGRLNLLLsdGERLYATRYTSDDPYptLYYLTRTTPDDRVVVVASEPLTDDEGW----TEV 232

                        170
                 ....*....|....*.
gi 658753047 153 APGEAIYVTEDGQFHS 168
Cdd:COG0121  233 PPGELLVVRDGLEVEV 248
GFAT cd00714
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ...
 25-166 1.72e-08

Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus of glucosamine-6P synthase (GlmS, or GFAT in humans). The glutaminase domain catalyzes amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. In humans, GFAT catalyzes the first and rate-limiting step of hexosamine metabolism, the conversion of D-fructose-6P (Fru6P) into D-glucosamine-6P using L-glutamine as a nitrogen source. The end product of this pathway, UDP-N-acetyl glucosamine, is a major building block of the bacterial peptidoglycan and fungal chitin.


Pssm-ID: 238366 [Multi-domain]  Cd Length: 215  Bit Score: 54.38  E-value: 1.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047  25 IALAHNGNLTNAETLKQQLfsEARRHV-NTTSDSEILLNIMAHELSKSdklhldaEDIFTAVTEVNNKVTGGYAAIAMII 103
Cdd:cd00714   94 IAVVHNGIIENYAELKEEL--EAKGYKfESETDTEVIAHLIEYYYDGG-------LDLLEAVKKALKRLEGAYALAVISK 164

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658753047 104 GHgvlafrdPNGI---R---PLVFGKREtpkgTEYMFASESVALkpdgFEFVRDVapgeaIYVtEDGQF 166
Cdd:cd00714  165 DE-------PDEIvaaRngsPLVIGIGD----GENFVASDAPAL----LEHTRRV-----IYL-EDGDI 212
YafJ cd01908
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ...
 1-163 1.00e-07

Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine amidotransferase-like protein of unknown function found in prokaryotes, eukaryotes and archaea. YafJ has a conserved structural fold similar to those of other class II glutamine amidotransferases including glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). The YafJ fold is also somewhat similar to the Ntn (N-terminal nucleophile) hydrolase fold of the proteasomal alpha and beta subunits.


Pssm-ID: 238889 [Multi-domain]  Cd Length: 257  Bit Score: 52.78  E-value: 1.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047   1 VRYPTAGSSSSSEAQPFYVNSpfgIALAHNGNLTNAETLKQQLFSEARRHVNTTSDSE-ILLNIMAHELSKSDKLHLDAE 79
Cdd:cd01908   87 VRAATVGPVSLENCHPFTRGR---WLFAHNGQLDGFRLLRRRLLRLLPRLPVGTTDSElAFALLLSRLLERDPLDPAELL 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047  80 D-IFTAVTEVNNKVTGGYAAIAMIIGHGVLAFR-------------DPNGIRPLVFGKRETPKGTEYMFASEsvalkPDG 145
Cdd:cd01908  164 DaILQTLRELAALAPPGRLNLLLSDGEYLIATRyasapslyyltrrAPFGCARLLFRSVTTPNDDGVVVASE-----PLT 238

                        170
                 ....*....|....*....
gi 658753047 146 FEF-VRDVAPGEAIYVTED 163
Cdd:cd01908  239 DDEgWTEVPPGELVVVSEG 257
GlxB cd01907
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ...
 2-142 1.28e-07

Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine amidotransferase-like protein of unknown function found in bacteria and archaea. GlxB has a structural fold similar to that of other class II glutamine amidotransferases including glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). The GlxB fold is also somewhat similar to the Ntn (N-terminal nucleophile) hydrolase fold of the proteasomal alpha and beta subunits.


Pssm-ID: 238888 [Multi-domain]  Cd Length: 249  Bit Score: 52.27  E-value: 1.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047   2 RYPTAGSSSSSEAQPFyvnSPFGIALAHNGNLTNAETLKQQLFSEaRRHVNTTSDSEILLNIMAHELSKSDKLHLDAEDI 81
Cdd:cd01907   85 RQPTNSAVWWYGAHPF---SIGDIAVVHNGEISNYGSNREYLERF-GYKFETETDTEVIAYYLDLLLRKGGLPLEYYKHI 160

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658753047  82 FTAVTEVNN-----KVTGGYAAI----AMIIGH--GVLAFRDPNGIRPLVFGKREtpkgTEYMFASESVALK 142
Cdd:cd01907  161 IRMPEEERElllalRLTYRLADLdgpfTIIVGTpdGFIVIRDRIKLRPAVVAETD----DYVAIASEECAIR 228
ComFC COG1040
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General ...
 210-324 7.39e-07

DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General function prediction only];


Pssm-ID: 440662 [Multi-domain]  Cd Length: 196  Bit Score: 49.44  E-value: 7.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047 210 LGEKIAREWSD---KDIDVVIPIP-----------ETSCDVALEIARMLDLPYR-QGFVKNRY----IGRTfimpgQEMR 270
Cdd:COG1040   63 LARLLARALREallPRPDLIVPVPlhrrrlrrrgfNQAELLARALARALGIPVLpDLLRRVRAtpsqAGLS-----RAER 137

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 658753047 271 KKSVRQKLNAIDRE-FKGKNVLLVDDsIVrgTTSAQIVEMAR---EAGAKNVYFASAA 324
Cdd:COG1040  138 RRNLRGAFAVRPPArLAGKHVLLVDD-VL--TTGATLAEAARalkAAGAARVDVLVLA 192
GATase_6 pfam13522
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ...
 10-137 1.55e-06

Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain found in a variety of enzymes, such as asparagine synthetase and glutamine--fructose-6-phosphate transaminase.


Pssm-ID: 433279 [Multi-domain]  Cd Length: 130  Bit Score: 47.30  E-value: 1.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047   10 SSSEAQPFYVNSPfGIALAHNGNLTNAETLKQQLfSEARRHVNTTSDSEILLNImAHELSKSDKLHLDaediftavtevn 89
Cdd:pfam13522  25 PDAGNQPMLSRDG-RLVLVHNGEIYNYGELREEL-ADLGHAFRSRSDTEVLLAL-YEEWGEDCLERLR------------ 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 658753047   90 nkvtgGYAAIAMII---GHGVLAfRDPNGIRPLVFGKretpKGTEYMFASE 137
Cdd:pfam13522  90 -----GMFAFAIWDrrrRTLFLA-RDRLGIKPLYYGI----LGGGFVFASE 130
asnB PRK09431
asparagine synthetase B; Provisional
 11-167 2.18e-05

asparagine synthetase B; Provisional


Pssm-ID: 236513 [Multi-domain]  Cd Length: 554  Bit Score: 46.83  E-value: 2.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047  11 SSEAQPFYvNSPFGIALAHNGNLTNAETLKQQLfseARRHV-NTTSDSEILLnimahelsksdklHLDAEDIFTAVTEVN 89
Cdd:PRK09431  57 NGGAQPLY-NEDGTHVLAVNGEIYNHQELRAEL---GDKYAfQTGSDCEVIL-------------ALYQEKGPDFLDDLD 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047  90 nkvtgGYAAIAMIIGHG--VLAFRDPNGIRPLVFGKRETPKgteYMFASESVALKPdgfeFVRDVA---PGEaIYVTEDG 164
Cdd:PRK09431 120 -----GMFAFALYDSEKdaYLIARDPIGIIPLYYGYDEHGN---LYFASEMKALVP----VCKTIKefpPGH-YYWSKDG 186


                 ...
gi 658753047 165 QFH 167
Cdd:PRK09431 187 EFV 189
HptA COG0634
Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism]; ...
 209-322 3.14e-05

Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism]; Hypoxanthine-guanine phosphoribosyltransferase is part of the Pathway/BioSystem: Purine salvage


Pssm-ID: 440399  Cd Length: 176  Bit Score: 44.25  E-value: 3.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047 209 KLGEKIAREWSDKDIdVVIPIPETSCDVALEIARMLDLPYRQGFVK-NRYigrtfimpGQEMRKKSVRQKLNAIDREFKG 287
Cdd:COG0634   21 ELAAQITADYAGKEP-LVVGVLKGAFVFMADLLRALDFPLEIDFMHvSSY--------GGGTESSGEVRILKDLDEDIEG 91

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 658753047 288 KNVLLVDDsIVR-GTTSAQIVEMAREAGAKNVYFAS 322
Cdd:COG0634   92 RDVLIVED-IIDtGLTLSYLLELLKSRGPASVKIAT 126
Hpt1 COG2236
Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine ...
 209-321 2.51e-04

Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine phosphoribosyltransferase is part of the Pathway/BioSystem: Purine salvage


Pssm-ID: 441837 [Multi-domain]  Cd Length: 153  Bit Score: 41.37  E-value: 2.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047 209 KLGEKIARewSDKDIDVVIPI-----PetscdVALEIARMLDLPYRQGFVKNRYIGrtfimPGQEMRKKSVRQKLnaiDR 283
Cdd:COG2236   20 RLAEQILE--SGFRPDVIVAIargglV-----PARILADALGVPDLASIRVSSYTG-----TAKRLEEPVVKGPL---DE 84

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 658753047 284 EFKGKNVLLVDDSIVRGTTSAQIVEMAREAGAKNVYFA 321
Cdd:COG2236   85 DLAGKRVLIVDDVADTGRTLEAVRDLLKEAGPAEVRTA 122
PRK00934 PRK00934
ribose-phosphate pyrophosphokinase; Provisional
 237-321 2.76e-04

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 234868 [Multi-domain]  Cd Length: 285  Bit Score: 42.59  E-value: 2.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047 237 ALEIARMLDLPYRQgFVKNRYIGRTFimpgqEMRKKSVrqklnaidrEFKGKNVLLVDDSIVRGTTSAQIVEMAREAGAK 316
Cdd:PRK00934 169 AKEAAEILGCEYDY-LEKTRISPTEV-----EIAPKNL---------DVKGKDVLIVDDIISTGGTMATAIKILKEQGAK 233


                 ....*
gi 658753047 317 NVYFA 321
Cdd:PRK00934 234 KVYVA 238
Apt COG0503
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ...
 209-316 5.46e-04

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: 40.44  E-value: 5.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047 209 KLGEKIAREWSDKDIDVVIPIpETS-CDVALEIARMLDLPyrqgFV---KNRYIGRTFImpGQEMR-KKSVRQKLnAIDR 283
Cdd:COG0503   35 AAGDELAERFADKGIDKVVGI-EARgFILAAALAYALGVP----FVparKPGKLPGETV--SEEYDlEYGTGDTL-ELHK 106

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 658753047 284 EF--KGKNVLLVDDSIVRGTTSAQIVEMAREAGAK 316
Cdd:COG0503  107 DAlkPGDRVLIVDDLLATGGTAKAAIKLVEEAGAE 141
PRK00331 PRK00331
isomerizing glutamine--fructose-6-phosphate transaminase;
25-164 1.02e-03

isomerizing glutamine--fructose-6-phosphate transaminase;


Pssm-ID: 234729 [Multi-domain]  Cd Length: 604  Bit Score: 41.57  E-value: 1.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047  25 IALAHNGNLTNAETLKQQLfsEARRHV-NTTSDSEILLNIMAHELSKSDklhldaeDIFTAVTEVNNKVTGGYaAIAMII 103
Cdd:PRK00331  95 IAVVHNGIIENYAELKEEL--LAKGHVfKSETDTEVIAHLIEEELKEGG-------DLLEAVRKALKRLEGAY-ALAVID 164

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658753047 104 GhgvlafRDPNGIrplVFGKRETP----KG-TEYMFASESVALkpdgFEFVRDVAP---GEAIYVTEDG 164
Cdd:PRK00331 165 K------DEPDTI---VAARNGSPlvigLGeGENFLASDALAL----LPYTRRVIYledGEIAVLTRDG 220
PRK08558 PRK08558
adenine phosphoribosyltransferase; Provisional
 210-318 1.13e-03

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 181466 [Multi-domain]  Cd Length: 238  Bit Score: 40.36  E-value: 1.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047 210 LGEKIAREWSDKDIDVVIPIPETSCDVALEIARMLDLP------YRQGFVKNRYIGRTFIMPGQEMrkkSVRQKLNAIDR 283
Cdd:PRK08558  99 IAPVVAERFMGLRVDVVLTAATDGIPLAVAIASYFGADlvyakkSKETGVEKFYEEYQRLASGIEV---TLYLPASALKK 175

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 658753047 284 efkGKNVLLVDDSIVRGTTSAQIVEMAREAGAKNV 318
Cdd:PRK08558 176 ---GDRVLIVDDIIRSGETQRALLDLARQAGADVV 207
PTZ00295 PTZ00295
glucosamine-fructose-6-phosphate aminotransferase; Provisional
 2-141 1.13e-03

glucosamine-fructose-6-phosphate aminotransferase; Provisional


Pssm-ID: 240349 [Multi-domain]  Cd Length: 640  Bit Score: 41.16  E-value: 1.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047   2 RYPTAGSSSSSEAQPfYVNSPFGIALAHNGNLTNAETLKQQLFSEARRHVNTTsDSEILLNIMAHELSksdklhlDAEDI 81
Cdd:PTZ00295 103 RWATHGGKTDENAHP-HCDYKKRIALVHNGTIENYVELKSELIAKGIKFRSET-DSEVIANLIGLELD-------QGEDF 173

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 658753047  82 FTAVTEVNNKVTGGYAAIAMIIGHGVLAFRDPNGiRPLVFGkretpKGTEYMF-ASESVAL 141
Cdd:PTZ00295 174 QEAVKSAISRLQGTWGLCIIHKDNPDSLIVARNG-SPLLVG-----IGDDSIYvASEPSAF 228
PyrE COG0461
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ...
 209-316 1.17e-03

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


Pssm-ID: 440229  Cd Length: 201  Bit Score: 40.14  E-value: 1.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047 209 KLGEKIAREWSDK--DIDVV-------IPIpetscdvALEIARMLDLPYrqGFVknryigrtfimpgqemRKKSVRQ-KL 278
Cdd:COG0461   48 LLGEALAELIKELgpEFDAVagpatggIPL-------AAAVARALGLPA--IFV----------------RKEAKDHgTG 102

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 658753047 279 NAIDREF-KGKNVLLVDDSIVRGTTSAQIVEMAREAGAK 316
Cdd:COG0461  103 GQIEGGLlPGERVLVVEDVITTGGSVLEAVEALREAGAE 141
ribP_PPkin TIGR01251
ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In ...
 279-321 1.25e-03

ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In some systems, close homologs lacking enzymatic activity exist and perform regulatory functions. The model is designated subfamily rather than equivalog for this reason. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273523 [Multi-domain]  Cd Length: 308  Bit Score: 40.73  E-value: 1.25e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 658753047  279 NAIDREFKGKNVLLVDDSIVRGTTSAQIVEMAREAGAKNVYFA 321
Cdd:TIGR01251 202 MNLVGDVEGKDVVIVDDIIDTGGTIAKAAEILKSAGAKRVIAA 244
PRK07322 PRK07322
adenine phosphoribosyltransferase; Provisional
 206-318 1.55e-03

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 180928  Cd Length: 178  Bit Score: 39.19  E-value: 1.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047 206 MG-TKLGEKIAREWSDK---DIDVVIpIPETS-CDVALEIARMLDLPYrqgFV--KNR--YIGRTFIMPGQEMrKKSVRQ 276
Cdd:PRK07322  32 LGdTELTEAAAEALAKRlptEVDVLV-TPETKgIPLAHALSRRLGKPY---VVarKSRkpYMQDPIIQEVVSI-TTGKPQ 106

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 658753047 277 K--LNAIDRE-FKGKNVLLVDDSIVRGTTSAQIVEMAREAGAKNV 318
Cdd:PRK07322 107 LlvLDGADAEkLKGKRVAIVDDVVSTGGTLTALERLVERAGGQVV 151
pyrE PRK00455
orotate phosphoribosyltransferase; Validated
 209-316 1.88e-03

orotate phosphoribosyltransferase; Validated


Pssm-ID: 234771  Cd Length: 202  Bit Score: 39.37  E-value: 1.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753047 209 KLGEKIAREWSDK--DIDVVI-P----IPetscdVALEIARMLDLPYrqGFVknryigrtfimpgqemRKKSVRQKLNA- 280
Cdd:PRK00455  49 LLGRFLAEAIKDSgiEFDVVAgPatggIP-----LAAAVARALDLPA--IFV----------------RKEAKDHGEGGq 105

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 658753047 281 -IDREFKGKNVLLVDDSIVRGTTSAQIVEMAREAGAK 316
Cdd:PRK00455 106 iEGRRLFGKRVLVVEDVITTGGSVLEAVEAIRAAGAE 142
PrsA COG0462
Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; ...
 284-321 3.05e-03

Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; Phosphoribosylpyrophosphate synthetase is part of the Pathway/BioSystem: Histidine biosynthesis, Purine biosynthesis


Pssm-ID: 440230 [Multi-domain]  Cd Length: 311  Bit Score: 39.27  E-value: 3.05e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 658753047 284 EFKGKNVLLVDDSIVRGTTSAQIVEMAREAGAKNVYFA 321
Cdd:COG0462  208 DVEGKTCIIVDDMIDTGGTLVEAAEALKEAGAKSVYAA 245
AsnB COG0367
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ...
 10-61 7.18e-03

Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; Asparagine synthetase B (glutamine-hydrolyzing) is part of the Pathway/BioSystem: Asparagine biosynthesis


Pssm-ID: 440136 [Multi-domain]  Cd Length: 558  Bit Score: 38.66  E-value: 7.18e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 658753047  10 SSSEAQPFyVNSPFGIALAHNGNLTNAETLKQQLfsEARRHV-NTTSDSEILL 61
Cdd:COG0367   55 SEGGHQPM-VSEDGRYVLVFNGEIYNYRELRAEL--EALGHRfRTHSDTEVIL 104
 
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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