|
Name |
Accession |
Description |
Interval |
E-value |
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
1-486 |
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: 579.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 1 MCGVLGICLADQtaaVAPELFDGCLFLQHRGQDAAGISTCgQRGRLYQCKGNGMARDVFTQQRMAGLVGSMGIAHLRYPT 80
Cdd:COG0034 7 ECGVFGIYGHED---VAQLTYYGLYALQHRGQESAGIATS-DGGRFHLHKGMGLVSDVFDEEDLERLKGNIAIGHVRYST 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 81 AGSSANSEAQPFYVNSPYG-ICMGHNGNLVNTQAIQRYMdEDVHRHINTDSDSELLLNIFAAELEKynkyrvnnDDIFHA 159
Cdd:COG0034 83 TGSSSLENAQPFYVNSPFGsIALAHNGNLTNAEELREEL-EEEGAIFQTTSDTEVILHLIARELTK--------EDLEEA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 160 LEGVYRLCRGGYACVGMVaGFAMIGFRDPNGIRPLLFGTRTNAdgtkdYMLASESVVLKAHNFNDFRDLKPGEAVIVpkd 239
Cdd:COG0034 154 IKEALRRVKGAYSLVILT-GDGLIAARDPNGIRPLVLGKLEDG-----YVVASESCALDILGAEFVRDVEPGEIVVI--- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 240 cSKSEPEFRQVVPVNSYRPDLFEYVYFARPDSVLDGISVYHTRLAMGVKLAE----------SVlksikPEdvdvvvsvp 309
Cdd:COG0034 225 -DEDGLRSRQFAEKPRPAPCIFEYVYFARPDSVIDGRSVYEARKRMGRELAReapvdadvviPV-----PD--------- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 310 dTARTCALECANTLNKPYREGFVKNRYVGRTFIMPNQKERVSSVRRKLNPMESEFKGKRVLIVDDSIVRGTTSKEIINMA 389
Cdd:COG0034 290 -SGRPAAIGYAEESGIPYEEGLIKNRYVGRTFIQPTQELRELGVRLKLNPIREVVKGKRVVLVDDSIVRGTTSRRIVKML 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 390 RESGALKVYFASAAPAIRFNHIYGIDLADTKQLVAYDKTEEEIQHELGCDEVIYQSLDDLIDCCKTPqIQKFEVGVFTGQ 469
Cdd:COG0034 369 REAGAKEVHFRIASPPIRYPCYYGIDTPTREELIAANRSVEEIREYIGADSLGYLSLEGLIEAVGEP-IEGFCTACFTGD 447
|
490
....*....|....*..
gi 50303009 470 YVTGVEDGYLLELEKAR 486
Cdd:COG0034 448 YPTGIPDEEKKRLELLR 464
|
|
| purF |
TIGR01134 |
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ... |
2-471 |
5.15e-176 |
|
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: 502.24 E-value: 5.15e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 2 CGVLGIclADQTAAVAPELFDGCLFLQHRGQDAAGISTCGqRGRLYQCKGNGMARDVFTQQRMAGLVGSMGIAHLRYPTA 81
Cdd:TIGR01134 1 CGVVGI--YGQEEVAASLTYYGLYALQHRGQESAGISVFD-GNRFRLHKGNGLVSDVFNEEHLQRLKGNVGIGHVRYSTA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 82 GSSANSEAQPFYVNSPYG-ICMGHNGNLVNTQAIQRYMdEDVHRHINTDSDSELLLNIFAAELEKynkyrvnNDDIFHAL 160
Cdd:TIGR01134 78 GSSGLENAQPFVVNSPYGgLALAHNGNLVNADELRREL-EEEGRHFNTTSDSEVLLHLLAHNDES-------KDDLFDAV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 161 EGVYRLCRGGYACVGMVAGFaMIGFRDPNGIRPLLFGTRtnADGtkdYMLASESVVLKAHNFNDFRDLKPGEAVIVpkdc 240
Cdd:TIGR01134 150 ARVLERVRGAYALVLMTEDG-LVAVRDPHGIRPLVLGRR--GDG---YVVASESCALDILGAEFVRDVEPGEVVVI---- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 241 sKSEPEFRQVVPVNSYRPDLFEYVYFARPDSVLDGISVYHTRLAMGVKLAESvlksiKPEDVDVVVSVPDTARTCALECA 320
Cdd:TIGR01134 220 -FDGGLESRQCARRPRAPCVFEYVYFARPDSVIDGISVYYARKRMGKELARE-----SPVEADVVVPVPDSGRSAALGFA 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 321 NTLNKPYREGFVKNRYVGRTFIMPNQKERVSSVRRKLNPMESEFKGKRVLIVDDSIVRGTTSKEIINMARESGALKVYFA 400
Cdd:TIGR01134 294 QASGIPYREGLIKNRYVGRTFIMPTQELRELSVRLKLNPVRAVFEGKRVVLVDDSIVRGTTSRQIVEMLRDAGAKEVHVR 373
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50303009 401 SAAPAIRFNHIYGIDLADTKQLVAYDKTEEEIQhELGCDEVIYQSLDDLIDCCKTPqIQKFEVGVFTGQYV 471
Cdd:TIGR01134 374 IASPPIRYPCYYGIDMPTREELIAARRTVEEIR-KIGADSLAYLSLEGLKEAVGNP-ESDLCLACFTGEYP 442
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
1-499 |
1.46e-174 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 499.97 E-value: 1.46e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 1 MCGVLGICladQTAAVAPELFDGCLFLQHRGQDAAGISTCGqRGRLYQCKGNGMARDVFTQQRMAGLVGSMGIAHLRYPT 80
Cdd:PLN02440 1 ECGVVGIF---GDPEASRLCYLGLHALQHRGQEGAGIVTVD-GNRLQSITGNGLVSDVFDESKLDQLPGDIAIGHVRYST 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 81 AGSSANSEAQPFYVNSPYG-ICMGHNGNLVNTQAIqRYMDEDVHRHINTDSDSELLLNIFAAELEKYnkyrvnnddIFHA 159
Cdd:PLN02440 77 AGASSLKNVQPFVANYRFGsIGVAHNGNLVNYEEL-RAKLEENGSIFNTSSDTEVLLHLIAISKARP---------FFSR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 160 LEGVYRLCRGGYACVGMVAGFaMIGFRDPNGIRPLLFGTRTNADgtkdYMLASESVVLKAHNFNDFRDLKPGEAVIVPKD 239
Cdd:PLN02440 147 IVDACEKLKGAYSMVFLTEDK-LVAVRDPHGFRPLVMGRRSNGA----VVFASETCALDLIGATYEREVNPGEVIVVDKD 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 240 CSKSepefRQ-VVPVNSYRPDLFEYVYFARPDSVLDGISVYHTRLAMGVKLAESVlksikPEDVDVVVSVPDTARTCALE 318
Cdd:PLN02440 222 KGVS----SQcLMPHPEPKPCIFEHIYFARPNSIVFGRSVYESRLEFGEILATEI-----PVDCDVVIPVPDSGRVAALG 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 319 CANTLNKPYREGFVKNRYVGRTFIMPNQKERVSSVRRKLNPMESEFKGKRVLIVDDSIVRGTTSKEIINMARESGALKVY 398
Cdd:PLN02440 293 YAAKLGVPFQQGLIRSHYVGRTFIEPSQKIRDFSVKLKLNPVRSVLEGKRVVVVDDSIVRGTTSSKIVRMLREAGAKEVH 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 399 FASAAPAIRFNHIYGIDLADTKQLVAYDKTEEEIQHELGCDEVIYQSLDDLIDCCKtPQIQKFEVGVFTGQYVT------ 472
Cdd:PLN02440 373 MRIASPPIIASCYYGVDTPSREELISNRMSVEEIRKFIGCDSLAFLPLEDLKKSLG-EESPRFCYACFSGDYPVlpkrvg 451
|
490 500
....*....|....*....|....*...
gi 50303009 473 -GVEDGYLLELEKARAMNVlKASAKAES 499
Cdd:PLN02440 452 gDIDDGYLESLEEAGRGWG-RKGRRQEA 478
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
2-274 |
6.20e-114 |
|
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: 336.74 E-value: 6.20e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 2 CGVLGICLADQtaaVAPELFDGCLFLQHRGQDAAGISTCGQrGRLYQCKGNGMARDVFTQQRMAGLVGSMGIAHLRYPTA 81
Cdd:cd00715 1 CGVFGIYGAED---AARLTYLGLYALQHRGQESAGIATSDG-KRFHTHKGMGLVSDVFDEEKLRRLPGNIAIGHVRYSTA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 82 GSSANSEAQPFYVNSP-YGICMGHNGNLVNTQAIQRYMDEDvHRHINTDSDSELLLNIFAAELEKynkyrvnnDDIFHAL 160
Cdd:cd00715 77 GSSSLENAQPFVVNSPlGGIALAHNGNLVNAKELREELEEE-GRIFQTTSDSEVILHLIARSLAK--------DDLFEAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 161 EGVYRLCRGGYACVGMVAgFAMIGFRDPNGIRPLLFGTRtnadGTKDYMLASESVVLKAHNFNDFRDLKPGEAVIVPKDC 240
Cdd:cd00715 148 IDALERVKGAYSLVIMTA-DGLIAVRDPHGIRPLVLGKL----EGDGYVVASESCALDIIGAEFVRDVEPGEIVVIDDDG 222
|
250 260 270
....*....|....*....|....*....|....
gi 50303009 241 SKSEpefrQVVPVNSYRPDLFEYVYFARPDSVLD 274
Cdd:cd00715 223 LESS----QRAPKPKPAPCIFEYVYFARPDSVID 252
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
69-213 |
1.43e-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: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 69 GSMGIAHLRYPTAGSSaNSEAQPFYvnSPYG-ICMGHNGNLVNTQAIQRYMdEDVHRHINTDSDSELLLNIfaaelekyn 147
Cdd:pfam13522 10 GGVALGHVRLAIVDLP-DAGNQPML--SRDGrLVLVHNGEIYNYGELREEL-ADLGHAFRSRSDTEVLLAL--------- 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50303009 148 kYRVNNDDIFHALEGVYRLC-----RGGYACVgmvagfamigfRDPNGIRPLLFGTRTNAdgtkdYMLASE 213
Cdd:pfam13522 77 -YEEWGEDCLERLRGMFAFAiwdrrRRTLFLA-----------RDRLGIKPLYYGILGGG-----FVFASE 130
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
1-486 |
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: 579.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 1 MCGVLGICLADQtaaVAPELFDGCLFLQHRGQDAAGISTCgQRGRLYQCKGNGMARDVFTQQRMAGLVGSMGIAHLRYPT 80
Cdd:COG0034 7 ECGVFGIYGHED---VAQLTYYGLYALQHRGQESAGIATS-DGGRFHLHKGMGLVSDVFDEEDLERLKGNIAIGHVRYST 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 81 AGSSANSEAQPFYVNSPYG-ICMGHNGNLVNTQAIQRYMdEDVHRHINTDSDSELLLNIFAAELEKynkyrvnnDDIFHA 159
Cdd:COG0034 83 TGSSSLENAQPFYVNSPFGsIALAHNGNLTNAEELREEL-EEEGAIFQTTSDTEVILHLIARELTK--------EDLEEA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 160 LEGVYRLCRGGYACVGMVaGFAMIGFRDPNGIRPLLFGTRTNAdgtkdYMLASESVVLKAHNFNDFRDLKPGEAVIVpkd 239
Cdd:COG0034 154 IKEALRRVKGAYSLVILT-GDGLIAARDPNGIRPLVLGKLEDG-----YVVASESCALDILGAEFVRDVEPGEIVVI--- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 240 cSKSEPEFRQVVPVNSYRPDLFEYVYFARPDSVLDGISVYHTRLAMGVKLAE----------SVlksikPEdvdvvvsvp 309
Cdd:COG0034 225 -DEDGLRSRQFAEKPRPAPCIFEYVYFARPDSVIDGRSVYEARKRMGRELAReapvdadvviPV-----PD--------- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 310 dTARTCALECANTLNKPYREGFVKNRYVGRTFIMPNQKERVSSVRRKLNPMESEFKGKRVLIVDDSIVRGTTSKEIINMA 389
Cdd:COG0034 290 -SGRPAAIGYAEESGIPYEEGLIKNRYVGRTFIQPTQELRELGVRLKLNPIREVVKGKRVVLVDDSIVRGTTSRRIVKML 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 390 RESGALKVYFASAAPAIRFNHIYGIDLADTKQLVAYDKTEEEIQHELGCDEVIYQSLDDLIDCCKTPqIQKFEVGVFTGQ 469
Cdd:COG0034 369 REAGAKEVHFRIASPPIRYPCYYGIDTPTREELIAANRSVEEIREYIGADSLGYLSLEGLIEAVGEP-IEGFCTACFTGD 447
|
490
....*....|....*..
gi 50303009 470 YVTGVEDGYLLELEKAR 486
Cdd:COG0034 448 YPTGIPDEEKKRLELLR 464
|
|
| purF |
TIGR01134 |
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ... |
2-471 |
5.15e-176 |
|
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: 502.24 E-value: 5.15e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 2 CGVLGIclADQTAAVAPELFDGCLFLQHRGQDAAGISTCGqRGRLYQCKGNGMARDVFTQQRMAGLVGSMGIAHLRYPTA 81
Cdd:TIGR01134 1 CGVVGI--YGQEEVAASLTYYGLYALQHRGQESAGISVFD-GNRFRLHKGNGLVSDVFNEEHLQRLKGNVGIGHVRYSTA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 82 GSSANSEAQPFYVNSPYG-ICMGHNGNLVNTQAIQRYMdEDVHRHINTDSDSELLLNIFAAELEKynkyrvnNDDIFHAL 160
Cdd:TIGR01134 78 GSSGLENAQPFVVNSPYGgLALAHNGNLVNADELRREL-EEEGRHFNTTSDSEVLLHLLAHNDES-------KDDLFDAV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 161 EGVYRLCRGGYACVGMVAGFaMIGFRDPNGIRPLLFGTRtnADGtkdYMLASESVVLKAHNFNDFRDLKPGEAVIVpkdc 240
Cdd:TIGR01134 150 ARVLERVRGAYALVLMTEDG-LVAVRDPHGIRPLVLGRR--GDG---YVVASESCALDILGAEFVRDVEPGEVVVI---- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 241 sKSEPEFRQVVPVNSYRPDLFEYVYFARPDSVLDGISVYHTRLAMGVKLAESvlksiKPEDVDVVVSVPDTARTCALECA 320
Cdd:TIGR01134 220 -FDGGLESRQCARRPRAPCVFEYVYFARPDSVIDGISVYYARKRMGKELARE-----SPVEADVVVPVPDSGRSAALGFA 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 321 NTLNKPYREGFVKNRYVGRTFIMPNQKERVSSVRRKLNPMESEFKGKRVLIVDDSIVRGTTSKEIINMARESGALKVYFA 400
Cdd:TIGR01134 294 QASGIPYREGLIKNRYVGRTFIMPTQELRELSVRLKLNPVRAVFEGKRVVLVDDSIVRGTTSRQIVEMLRDAGAKEVHVR 373
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50303009 401 SAAPAIRFNHIYGIDLADTKQLVAYDKTEEEIQhELGCDEVIYQSLDDLIDCCKTPqIQKFEVGVFTGQYV 471
Cdd:TIGR01134 374 IASPPIRYPCYYGIDMPTREELIAARRTVEEIR-KIGADSLAYLSLEGLKEAVGNP-ESDLCLACFTGEYP 442
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
1-499 |
1.46e-174 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 499.97 E-value: 1.46e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 1 MCGVLGICladQTAAVAPELFDGCLFLQHRGQDAAGISTCGqRGRLYQCKGNGMARDVFTQQRMAGLVGSMGIAHLRYPT 80
Cdd:PLN02440 1 ECGVVGIF---GDPEASRLCYLGLHALQHRGQEGAGIVTVD-GNRLQSITGNGLVSDVFDESKLDQLPGDIAIGHVRYST 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 81 AGSSANSEAQPFYVNSPYG-ICMGHNGNLVNTQAIqRYMDEDVHRHINTDSDSELLLNIFAAELEKYnkyrvnnddIFHA 159
Cdd:PLN02440 77 AGASSLKNVQPFVANYRFGsIGVAHNGNLVNYEEL-RAKLEENGSIFNTSSDTEVLLHLIAISKARP---------FFSR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 160 LEGVYRLCRGGYACVGMVAGFaMIGFRDPNGIRPLLFGTRTNADgtkdYMLASESVVLKAHNFNDFRDLKPGEAVIVPKD 239
Cdd:PLN02440 147 IVDACEKLKGAYSMVFLTEDK-LVAVRDPHGFRPLVMGRRSNGA----VVFASETCALDLIGATYEREVNPGEVIVVDKD 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 240 CSKSepefRQ-VVPVNSYRPDLFEYVYFARPDSVLDGISVYHTRLAMGVKLAESVlksikPEDVDVVVSVPDTARTCALE 318
Cdd:PLN02440 222 KGVS----SQcLMPHPEPKPCIFEHIYFARPNSIVFGRSVYESRLEFGEILATEI-----PVDCDVVIPVPDSGRVAALG 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 319 CANTLNKPYREGFVKNRYVGRTFIMPNQKERVSSVRRKLNPMESEFKGKRVLIVDDSIVRGTTSKEIINMARESGALKVY 398
Cdd:PLN02440 293 YAAKLGVPFQQGLIRSHYVGRTFIEPSQKIRDFSVKLKLNPVRSVLEGKRVVVVDDSIVRGTTSSKIVRMLREAGAKEVH 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 399 FASAAPAIRFNHIYGIDLADTKQLVAYDKTEEEIQHELGCDEVIYQSLDDLIDCCKtPQIQKFEVGVFTGQYVT------ 472
Cdd:PLN02440 373 MRIASPPIIASCYYGVDTPSREELISNRMSVEEIRKFIGCDSLAFLPLEDLKKSLG-EESPRFCYACFSGDYPVlpkrvg 451
|
490 500
....*....|....*....|....*...
gi 50303009 473 -GVEDGYLLELEKARAMNVlKASAKAES 499
Cdd:PLN02440 452 gDIDDGYLESLEEAGRGWG-RKGRRQEA 478
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
2-274 |
6.20e-114 |
|
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: 336.74 E-value: 6.20e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 2 CGVLGICLADQtaaVAPELFDGCLFLQHRGQDAAGISTCGQrGRLYQCKGNGMARDVFTQQRMAGLVGSMGIAHLRYPTA 81
Cdd:cd00715 1 CGVFGIYGAED---AARLTYLGLYALQHRGQESAGIATSDG-KRFHTHKGMGLVSDVFDEEKLRRLPGNIAIGHVRYSTA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 82 GSSANSEAQPFYVNSP-YGICMGHNGNLVNTQAIQRYMDEDvHRHINTDSDSELLLNIFAAELEKynkyrvnnDDIFHAL 160
Cdd:cd00715 77 GSSSLENAQPFVVNSPlGGIALAHNGNLVNAKELREELEEE-GRIFQTTSDSEVILHLIARSLAK--------DDLFEAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 161 EGVYRLCRGGYACVGMVAgFAMIGFRDPNGIRPLLFGTRtnadGTKDYMLASESVVLKAHNFNDFRDLKPGEAVIVPKDC 240
Cdd:cd00715 148 IDALERVKGAYSLVIMTA-DGLIAVRDPHGIRPLVLGKL----EGDGYVVASESCALDIIGAEFVRDVEPGEIVVIDDDG 222
|
250 260 270
....*....|....*....|....*....|....
gi 50303009 241 SKSEpefrQVVPVNSYRPDLFEYVYFARPDSVLD 274
Cdd:cd00715 223 LESS----QRAPKPKPAPCIFEYVYFARPDSVID 252
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
2-481 |
4.31e-112 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 340.09 E-value: 4.31e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 2 CGVLGIcLADQTAAVAPELFDGCLFLQHRGQDAAGISTcgQRGRLYQC-KGNGMARDVFTQQRMAGLVGSMGIAHLRYPT 80
Cdd:PRK05793 15 CGVFGV-FSKNNIDVASLTYYGLYALQHRGQESAGIAV--SDGEKIKVhKGMGLVSEVFSKEKLKGLKGNSAIGHVRYST 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 81 AGSSANSEAQPFYVNSPYG-ICMGHNGNLVNTQAIQRYMdEDVHRHINTDSDSELLLNIFAaeleKYNKYrvnndDIFHA 159
Cdd:PRK05793 92 TGASDLDNAQPLVANYKLGsIAIAHNGNLVNADVIRELL-EDGGRIFQTSIDSEVILNLIA----RSAKK-----GLEKA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 160 LEGVYRLCRGGYACVGMVAGfAMIGFRDPNGIRPLLFGTRTNadgtkDYMLASESVVLKAHNFNDFRDLKPGEAVIVPKD 239
Cdd:PRK05793 162 LVDAIQAIKGSYALVILTED-KLIGVRDPHGIRPLCLGKLGD-----DYILSSESCALDTIGAEFIRDVEPGEIVIIDED 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 240 CSKSEPEFRQVVPvnsyRPDLFEYVYFARPDSVLDGISVYHTRLAMGVKLAESvlksiKPEDVDVVVSVPDTARTCALEC 319
Cdd:PRK05793 236 GIKSIKFAEKTKC----QTCAFEYIYFARPDSVIDGISVYESRVRAGRQLYKE-----YPVDADIVIGVPDSGIPAAIGY 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 320 ANTLNKPYREGFVKNRYVGRTFIMPNQKERVSSVRRKLNPMESEFKGKRVLIVDDSIVRGTTSKEIINMARESGALKVYF 399
Cdd:PRK05793 307 AEASGIPYGIGFIKNKYVGRTFIAPSQELRERAVRVKLNPLKVNVEGKRVVLIDDSIVRGTTSKRLVELLRKAGAKEVHF 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 400 ASAAPAIRFNHIYGIDLADTKQLVAYDKTEEEIQHELGCDEVIYQSLDDLIDCCktPQIQKFEVGVFTGQYVTGV---ED 476
Cdd:PRK05793 387 RVSSPPVKYPCYFGIDTPYRKELIGANMSVEEIREMIGADSLGYLSIEGLLESL--NGDKGFCLGCFNGVYPVSApkeGP 464
|
....*
gi 50303009 477 GYLLE 481
Cdd:PRK05793 465 KYLLE 469
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
2-234 |
1.12e-46 |
|
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: 161.85 E-value: 1.12e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 2 CGVLGICLADQTAA-VAPELFDGCLFLQHRGQDAAGISTCGQRGRLYQcKGNGMARDVFTQQRMAGLVGSMGIAHLRYPT 80
Cdd:cd00352 1 CGIFGIVGADGAASlLLLLLLRGLAALEHRGPDGAGIAVYDGDGLFVE-KRAGPVSDVALDLLDEPLKSGVALGHVRLAT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 81 AGSSANSEAQPFYVNSpYGICMGHNGNLVNTQAIQRYMDEDVHrHINTDSDSELLLNIFAAELEKynkyrvnnDDIFHAL 160
Cdd:cd00352 80 NGLPSEANAQPFRSED-GRIALVHNGEIYNYRELREELEARGY-RFEGESDSEVILHLLERLGRE--------GGLFEAV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50303009 161 EGVYRLCRGGYACVGM-VAGFAMIGFRDPNGIRPLLFGTRtnADGTkdYMLASESVVLKAHNFNDFRDLKPGEAV 234
Cdd:cd00352 150 EDALKRLDGPFAFALWdGKPDRLFAARDRFGIRPLYYGIT--KDGG--LVFASEPKALLALPFKGVRRLPPGELL 220
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
2-235 |
2.60e-15 |
|
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: 75.77 E-value: 2.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 2 CGVLGICLADQTAAVAPELFDGCLFLQHRG-QDAAGISTCGQ-RGRLYQC-------KGNGMARDVFTQQRMAGLVGSMG 72
Cdd:cd01907 1 CGIFGIMSKDGEPFVGALLVEMLDAMQERGpGDGAGFALYGDpDAFVYSSgkdmevfKGVGYPEDIARRYDLEEYKGYHW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 73 IAHLRYPTagssaNSE-----AQPFyvnSPYGICMGHNGNLVNTQAIQRYMdEDVHRHINTDSDSELLLNIFAAELEKY- 146
Cdd:cd01907 81 IAHTRQPT-----NSAvwwygAHPF---SIGDIAVVHNGEISNYGSNREYL-ERFGYKFETETDTEVIAYYLDLLLRKGg 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 147 ---------NKYRVNNDDIFHALEGVYRLCR--GGYACVGMVAGfAMIGFRDPNGIRPLLFGtrtnadGTKDYM-LASE- 213
Cdd:cd01907 152 lpleyykhiIRMPEEERELLLALRLTYRLADldGPFTIIVGTPD-GFIVIRDRIKLRPAVVA------ETDDYVaIASEe 224
|
250 260
....*....|....*....|....*
gi 50303009 214 ---SVVLKAHNFNDFrDLKPGEAVI 235
Cdd:cd01907 225 caiREIPDRDNAKVW-EPRPGEYVI 248
|
|
| PRTases_typeI |
cd06223 |
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ... |
316-405 |
4.61e-13 |
|
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: 66.27 E-value: 4.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 316 ALECANTLNKPYREGFVKNRYVGRTFIMPNQKErvssvrrklNPMESEFKGKRVLIVDDSIVRGTTSKEIINMARESGAL 395
Cdd:cd06223 30 AAALARALGLPLAFIRKERKGPGRTPSEPYGLE---------LPLGGDVKGKRVLLVDDVIATGGTLLAAIELLKEAGAK 100
|
90
....*....|
gi 50303009 396 KVYFASAAPA 405
Cdd:cd06223 101 VVGVAVLLDK 110
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-232 |
1.01e-10 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 64.27 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 1 MCGVLGIcLADQTAAVApeLFDGCLFLQHRGQDAAGISTCGQRGRLY--QCKGNGMARDVFTQQRMAGL---VGS-MGIA 74
Cdd:PTZ00295 24 CCGIVGY-LGNEDASKI--LLEGIEILQNRGYDSCGISTISSGGELKttKYASDGTTSDSIEILKEKLLdshKNStIGIA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 75 HLRYPTAGSSANSEAQPfYVNSPYGICMGHNGNLVNTQAIQRYMdedVHRHIN--TDSDSELLLNIFAAELEKynkyrvn 152
Cdd:PTZ00295 101 HTRWATHGGKTDENAHP-HCDYKKRIALVHNGTIENYVELKSEL---IAKGIKfrSETDSEVIANLIGLELDQ------- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 153 NDDIFHALEGVYRLCRGGYacvgmvaGFAMIGFRDPNGI------RPLLFGTrtnadGTKDYMLASESVVLkAHNFNDFR 226
Cdd:PTZ00295 170 GEDFQEAVKSAISRLQGTW-------GLCIIHKDNPDSLivarngSPLLVGI-----GDDSIYVASEPSAF-AKYTNEYI 236
|
....*.
gi 50303009 227 DLKPGE 232
Cdd:PTZ00295 237 SLKDGE 242
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
2-236 |
3.66e-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: 53.99 E-value: 3.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 2 CGVLGICLADQtaaVAPELFDGCLFLQHRGQDAAGISTCGQrGRLYQCKGNGMARDVFTQQRMAGLVGSMGIAHLRYPTA 81
Cdd:cd00714 1 CGIVGYIGKRE---AVDILLEGLKRLEYRGYDSAGIAVIGD-GSLEVVKAVGKVANLEEKLAEKPLSGHVGIGHTRWATH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 82 G--SSANseAQPfYVNSPYGICMGHNGNLVNTQAIQRYMDEDVHRhINTDSDSELLLNIFAAELEKynkyrvnNDDIFHA 159
Cdd:cd00714 77 GepTDVN--AHP-HRSCDGEIAVVHNGIIENYAELKEELEAKGYK-FESETDTEVIAHLIEYYYDG-------GLDLLEA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 50303009 160 LEGVYRLCRGGYACVGMVAGF--AMIGFRdpNGiRPLLFGTrtnadGTKDYMLASESVVLKAHNfNDFRDLKPGEAVIV 236
Cdd:cd00714 146 VKKALKRLEGAYALAVISKDEpdEIVAAR--NG-SPLVIGI-----GDGENFVASDAPALLEHT-RRVIYLEDGDIAVI 215
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
69-213 |
1.43e-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: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 69 GSMGIAHLRYPTAGSSaNSEAQPFYvnSPYG-ICMGHNGNLVNTQAIQRYMdEDVHRHINTDSDSELLLNIfaaelekyn 147
Cdd:pfam13522 10 GGVALGHVRLAIVDLP-DAGNQPML--SRDGrLVLVHNGEIYNYGELREEL-ADLGHAFRSRSDTEVLLAL--------- 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50303009 148 kYRVNNDDIFHALEGVYRLC-----RGGYACVgmvagfamigfRDPNGIRPLLFGTRTNAdgtkdYMLASE 213
Cdd:pfam13522 77 -YEEWGEDCLERLRGMFAFAiwdrrRRTLFLA-----------RDRLGIKPLYYGILGGG-----FVFASE 130
|
|
| YafJ |
cd01908 |
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ... |
73-236 |
1.59e-06 |
|
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: 49.69 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 73 IAHLRYPTAGSSANSEAQPFYVNSpygICMGHNGNLVNTQAIQRYMDEDVHRHINTDSDSELLLNIFAAELEkyNKYRVN 152
Cdd:cd01908 84 LAHVRAATVGPVSLENCHPFTRGR---WLFAHNGQLDGFRLLRRRLLRLLPRLPVGTTDSELAFALLLSRLL--ERDPLD 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 153 NDDIFHALEGVYR----LCRGGYACVGMVAGFAMIGFRDP---------------NGIRPLLFGTRTNADGtkdYMLASE 213
Cdd:cd01908 159 PAELLDAILQTLRelaaLAPPGRLNLLLSDGEYLIATRYAsapslyyltrrapfgCARLLFRSVTTPNDDG---VVVASE 235
|
170 180
....*....|....*....|...
gi 50303009 214 SVVLKahnfNDFRDLKPGEAVIV 236
Cdd:cd01908 236 PLTDD----EGWTEVPPGELVVV 254
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
1-231 |
1.87e-06 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 50.48 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 1 MCGVLGIC-LADQTAAVAPELFDGCLFLQHRGQDAAGISTCGQRGRLYQCkgngmardvftqqrmaglvgsmgIAHLRYP 79
Cdd:PTZ00077 1 MCGILAIFnSKGERHELRRKALELSKRLRHRGPDWSGIIVLENSPGTYNI-----------------------LAHERLA 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 80 TAGSSanSEAQPFYVNSpYGICMGHNGNLVNTQAIQRYMDEDVHRhINTDSDSELLLNIFaaelEKYNKyrvnnDDIFHA 159
Cdd:PTZ00077 58 IVDLS--DGKQPLLDDD-ETVALMQNGEIYNHWEIRPELEKEGYK-FSSNSDCEIIGHLY----KEYGP-----KDFWNH 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50303009 160 LEGVYrlcrgGYACVGMVAGfAMIGFRDPNGIRPLLFGtrTNADGTkdYMLASESVVLKAhNFNDFRDLKPG 231
Cdd:PTZ00077 125 LDGMF-----ATVIYDMKTN-TFFAARDHIGIIPLYIG--YAKDGS--IWFSSELKALHD-QCVEVKQFPPG 185
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-219 |
2.75e-06 |
|
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine synthetase B catalyses the ATP-dependent conversion of aspartate to asparagine. This enzyme is a homodimer, with each monomer composed of a glutaminase domain and a synthetase domain. The N-terminal glutaminase domain hydrolyzes glutamine to glutamic acid and ammonia.
Pssm-ID: 238364 [Multi-domain] Cd Length: 220 Bit Score: 48.32 E-value: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 2 CGVLGICLADQTAAVAPELFDGCLFLQHRGQDAAGIstcgqrgrlYQCKGNGMArdvftQQRMAglvgSMGIAHlrypta 81
Cdd:cd00712 1 CGIAGIIGLDGASVDRATLERMLDALAHRGPDGSGI---------WIDEGVALG-----HRRLS----IIDLSG------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 82 gssansEAQPFYVNSPyGICMGHNGNLVNTQAIQRYMDEDVHRHiNTDSDSELLLnifaaelekynkyrvnnddifHALE 161
Cdd:cd00712 57 ------GAQPMVSEDG-RLVLVFNGEIYNYRELRAELEALGHRF-RTHSDTEVIL---------------------HLYE 107
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 162 gvyrlcRGGYACV----GMVAgFA--------MIGFRDPNGIRPLLFGTRtnaDGTkdYMLASEsvvLKA 219
Cdd:cd00712 108 ------EWGEDCLerlnGMFA-FAlwdkrkrrLFLARDRFGIKPLYYGRD---GGG--LAFASE---LKA 162
|
|
| YafJ |
COG0121 |
Predicted glutamine amidotransferase YafJ [General function prediction only]; |
73-236 |
6.94e-06 |
|
Predicted glutamine amidotransferase YafJ [General function prediction only];
Pssm-ID: 439891 [Multi-domain] Cd Length: 248 Bit Score: 47.65 E-value: 6.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 73 IAHLRYPTAGSSANSEAQPFYvnSPYGICMgHNGNLVNTQAIQR----YMDEDVHRHINTDSDSELLLNIFAAELEkyNK 148
Cdd:COG0121 80 IAHVRKATVGPVSLENTHPFR--GGRWLFA-HNGQLDGFDRLRRrlaeELPDELYFQPVGTTDSELAFALLLSRLR--DG 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 149 YRVNNDDIFHALEGVYRLCRG-GYACVGMVAGFAMIGFRDPNGIRP--LLFGTRTNADGTKdYMLASESvvLKAHnfNDF 225
Cdd:COG0121 155 GPDPAEALAEALRELAELARApGRLNLLLSDGERLYATRYTSDDPYptLYYLTRTTPDDRV-VVVASEP--LTDD--EGW 229
|
170
....*....|.
gi 50303009 226 RDLKPGEAVIV 236
Cdd:COG0121 230 TEVPPGELLVV 240
|
|
| PRK00934 |
PRK00934 |
ribose-phosphate pyrophosphokinase; Provisional |
346-432 |
1.18e-05 |
|
ribose-phosphate pyrophosphokinase; Provisional
Pssm-ID: 234868 [Multi-domain] Cd Length: 285 Bit Score: 47.22 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 346 QKERVSSVRRKLNPMESEFKGKRVLIVDDSIVRGTTSKEIINMARESGALKVYFASAAPAIRFNHIYGIDLADTKQLVAY 425
Cdd:PRK00934 184 EKTRISPTEVEIAPKNLDVKGKDVLIVDDIISTGGTMATAIKILKEQGAKKVYVACVHPVLVGDAILKLYNAGVDEIIVT 263
|
....*..
gi 50303009 426 DKTEEEI 432
Cdd:PRK00934 264 DTLESEV 270
|
|
| Hpt1 |
COG2236 |
Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine ... |
359-400 |
2.65e-05 |
|
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: 44.45 E-value: 2.65e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 50303009 359 PMESEFKGKRVLIVDDSIVRGTTSKEIINMARESGALKVYFA 400
Cdd:COG2236 81 PLDEDLAGKRVLIVDDVADTGRTLEAVRDLLKEAGPAEVRTA 122
|
|
| PRK02277 |
PRK02277 |
orotate phosphoribosyltransferase-like protein; Provisional |
365-394 |
4.67e-04 |
|
orotate phosphoribosyltransferase-like protein; Provisional
Pssm-ID: 235023 [Multi-domain] Cd Length: 200 Bit Score: 41.39 E-value: 4.67e-04
10 20 30
....*....|....*....|....*....|
gi 50303009 365 KGKRVLIVDDSIVRGTTSKEIINMARESGA 394
Cdd:PRK02277 139 EGKRCVIVDDVITSGTTMKETIEYLKEHGG 168
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
89-219 |
7.72e-04 |
|
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: 39.42 E-value: 7.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 89 AQPFYVNSPYGICMGHNGNLVNTQAIQRYMDEDVHRHiNTDSDSELLLNIFAAElekynkyrvnnddifhalegvyrlcr 168
Cdd:pfam13537 13 AQPMVSSEDGRYVIVFNGEIYNYRELRAELEAKGYRF-RTHSDTEVILHLYEAE-------------------------- 65
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50303009 169 GGYACV----GMVAgFA--------MIGFRDPNGIRPLLFGtRTNADGtkdYMLASEsvvLKA 219
Cdd:pfam13537 66 WGEDCVdrlnGMFA-FAiwdrrrqrLFLARDRFGIKPLYYG-RDDGGR---LLFASE---LKA 120
|
|
| PLN02549 |
PLN02549 |
asparagine synthase (glutamine-hydrolyzing) |
1-197 |
3.37e-03 |
|
asparagine synthase (glutamine-hydrolyzing)
Pssm-ID: 178164 [Multi-domain] Cd Length: 578 Bit Score: 40.13 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 1 MCGVLGIC-LADQTAAVAPELFDGCLFLQHRGQDAAGistcgqrgrLYQCKGNGMArdvftQQRMAglvgsmgiahLRYP 79
Cdd:PLN02549 1 MCGILAVLgCSDDSQAKRSRVLELSRRLRHRGPDWSG---------LYGNEDCYLA-----HERLA----------IMDP 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303009 80 TAGSsanseaQPFYvNSPYGICMGHNGNLVNTQAIQRYMDEDVHRhinTDSDSELLLNIfaaelekynkYRVNNDDIFHA 159
Cdd:PLN02549 57 ESGD------QPLY-NEDKTIVVTANGEIYNHKELREKLKLHKFR---TGSDCEVIAHL----------YEEHGEEFVDM 116
|
170 180 190
....*....|....*....|....*....|....*...
gi 50303009 160 LEGVYrlcrgGYACVGMvAGFAMIGFRDPNGIRPLLFG 197
Cdd:PLN02549 117 LDGMF-----SFVLLDT-RDNSFIAARDHIGITPLYIG 148
|
|
| PRK09162 |
PRK09162 |
hypoxanthine-guanine phosphoribosyltransferase; Provisional |
356-400 |
3.80e-03 |
|
hypoxanthine-guanine phosphoribosyltransferase; Provisional
Pssm-ID: 181675 Cd Length: 181 Bit Score: 38.30 E-value: 3.80e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 50303009 356 KLNPMESeFKGKRVLIVDDSIVRGTTSKEIINMARESGALKVYFA 400
Cdd:PRK09162 88 KVKPRES-LKGRTVLVVDDILDEGHTLAAIRDRCLEMGAAEVYSA 131
|
|
| PyrE |
COG0461 |
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ... |
365-394 |
7.58e-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: 37.83 E-value: 7.58e-03
10 20 30
....*....|....*....|....*....|
gi 50303009 365 KGKRVLIVDDSIVRGTTSKEIINMARESGA 394
Cdd:COG0461 111 PGERVLVVEDVITTGGSVLEAVEALREAGA 140
|
|
| PRK08558 |
PRK08558 |
adenine phosphoribosyltransferase; Provisional |
365-394 |
8.93e-03 |
|
adenine phosphoribosyltransferase; Provisional
Pssm-ID: 181466 [Multi-domain] Cd Length: 238 Bit Score: 38.05 E-value: 8.93e-03
10 20 30
....*....|....*....|....*....|
gi 50303009 365 KGKRVLIVDDSIVRGTTSKEIINMARESGA 394
Cdd:PRK08558 175 KGDRVLIVDDIIRSGETQRALLDLARQAGA 204
|
|
| |
