|
Name |
Accession |
Description |
Interval |
E-value |
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
1-478 |
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: 769.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 1 MCGIVGIAGVMPVNQSIYDALTVLQHRGQDAAGIITIDaNNCFRLRKANGLVSDVFEARHMQRLQGNMGIGHVRYPTAGS 80
Cdd:COG0034 7 ECGVFGIYGHEDVAQLTYYGLYALQHRGQESAGIATSD-GGRFHLHKGMGLVSDVFDEEDLERLKGNIAIGHVRYSTTGS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 81 SSASEAQPFYVNSPYG-ITLAHNGNLTNAHELRKKLFEEKRrHINTTSDSEILLNIFASELdnfrhyplEADNIFAAIAA 159
Cdd:COG0034 86 SSLENAQPFYVNSPFGsIALAHNGNLTNAEELREELEEEGA-IFQTTSDTEVILHLIAREL--------TKEDLEEAIKE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 160 TNRLIRGAYACVAMIiGHGMVAFRDPNGIRPLVLGKRDidenrTEYMVASESVALDTLGFDFLRDVAPGEAIYITEEGqL 239
Cdd:COG0034 157 ALRRVKGAYSLVILT-GDGLIAARDPNGIRPLVLGKLE-----DGYVVASESCALDILGAEFVRDVEPGEIVVIDEDG-L 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 240 FTRQCADNPVSNPCLFEYVYFARPDSFIDKISVYSARVNMGTKLgekiAREwEDLDIDVVIPIPETSCDIALEIARILGK 319
Cdd:COG0034 230 RSRQFAEKPRPAPCIFEYVYFARPDSVIDGRSVYEARKRMGREL----ARE-APVDADVVIPVPDSGRPAAIGYAEESGI 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 320 PYRQGFVKNRYVGRTFIMPGQQLRRKSVRRKLNANRAEFRDKNVLLVDDSIVRGTTSEQIIEMAREAGAKKVYLASAAPE 399
Cdd:COG0034 305 PYEEGLIKNRYVGRTFIQPTQELRELGVRLKLNPIREVVKGKRVVLVDDSIVRGTTSRRIVKMLREAGAKEVHFRIASPP 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130247 400 IRFPNVYGIDMPSATELIAHGREVDEIRQIIGADGLIFQDLNDLIDAVRAenpDIQQFECSVFNGVYVTKDVDQGYLDF 478
Cdd:COG0034 385 IRYPCYYGIDTPTREELIAANRSVEEIREYIGADSLGYLSLEGLIEAVGE---PIEGFCTACFTGDYPTGIPDEEKKRL 460
|
|
| purF |
TIGR01134 |
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ... |
2-467 |
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: 703.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 2 CGIVGIAGVMPVNQS-IYDALTVLQHRGQDAAGIITIDaNNCFRLRKANGLVSDVFEARHMQRLQGNMGIGHVRYPTAGS 80
Cdd:TIGR01134 1 CGVVGIYGQEEVAASlTYYGLYALQHRGQESAGISVFD-GNRFRLHKGNGLVSDVFNEEHLQRLKGNVGIGHVRYSTAGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 81 SSASEAQPFYVNSPYG-ITLAHNGNLTNAHELRKKLfEEKRRHINTTSDSEILLNIFAseldnfrHYPLEADNIFAAIAA 159
Cdd:TIGR01134 80 SGLENAQPFVVNSPYGgLALAHNGNLVNADELRREL-EEEGRHFNTTSDSEVLLHLLA-------HNDESKDDLFDAVAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 160 TNRLIRGAYACVAMIiGHGMVAFRDPNGIRPLVLGKRDidenrTEYMVASESVALDTLGFDFLRDVAPGEAIYITEEGqL 239
Cdd:TIGR01134 152 VLERVRGAYALVLMT-EDGLVAVRDPHGIRPLVLGRRG-----DGYVVASESCALDILGAEFVRDVEPGEVVVIFDGG-L 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 240 FTRQCADNPVsNPCLFEYVYFARPDSFIDKISVYSARVNMGTKLGEKiarewEDLDIDVVIPIPETSCDIALEIARILGK 319
Cdd:TIGR01134 225 ESRQCARRPR-APCVFEYVYFARPDSVIDGISVYYARKRMGKELARE-----SPVEADVVVPVPDSGRSAALGFAQASGI 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 320 PYRQGFVKNRYVGRTFIMPGQQLRRKSVRRKLNANRAEFRDKNVLLVDDSIVRGTTSEQIIEMAREAGAKKVYLASAAPE 399
Cdd:TIGR01134 299 PYREGLIKNRYVGRTFIMPTQELRELSVRLKLNPVRAVFEGKRVVLVDDSIVRGTTSRQIVEMLRDAGAKEVHVRIASPP 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130247 400 IRFPNVYGIDMPSATELIAHGREVDEIRQiIGADGLIFQDLNDLIDAVRAenpDIQQFECSVFNGVYV 467
Cdd:TIGR01134 379 IRYPCYYGIDMPTREELIAARRTVEEIRK-IGADSLAYLSLEGLKEAVGN---PESDLCLACFTGEYP 442
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
1-495 |
0e+00 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 621.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 1 MCGIVGIAGVMPVNQSIYDALTVLQHRGQDAAGIITIDANNcFRLRKANGLVSDVFEARHMQRLQGNMGIGHVRYPTAGS 80
Cdd:PLN02440 1 ECGVVGIFGDPEASRLCYLGLHALQHRGQEGAGIVTVDGNR-LQSITGNGLVSDVFDESKLDQLPGDIAIGHVRYSTAGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 81 SSASEAQPFYVNSPYG-ITLAHNGNLTNAHELRKKLfEEKRRHINTTSDSEILLNIFASELdnfrhypleADNIFAAIAA 159
Cdd:PLN02440 80 SSLKNVQPFVANYRFGsIGVAHNGNLVNYEELRAKL-EENGSIFNTSSDTEVLLHLIAISK---------ARPFFSRIVD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 160 TNRLIRGAYACVAMIIGHgMVAFRDPNGIRPLVLGKRDIDEnrteYMVASESVALDTLGFDFLRDVAPGEAIYITEeGQL 239
Cdd:PLN02440 150 ACEKLKGAYSMVFLTEDK-LVAVRDPHGFRPLVMGRRSNGA----VVFASETCALDLIGATYEREVNPGEVIVVDK-DKG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 240 FTRQCA-DNPVSNPCLFEYVYFARPDSFIDKISVYSARVNMGTKLGEKIARewedlDIDVVIPIPETSCDIALEIARILG 318
Cdd:PLN02440 224 VSSQCLmPHPEPKPCIFEHIYFARPNSIVFGRSVYESRLEFGEILATEIPV-----DCDVVIPVPDSGRVAALGYAAKLG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 319 KPYRQGFVKNRYVGRTFIMPGQQLRRKSVRRKLNANRAEFRDKNVLLVDDSIVRGTTSEQIIEMAREAGAKKVYLASAAP 398
Cdd:PLN02440 299 VPFQQGLIRSHYVGRTFIEPSQKIRDFSVKLKLNPVRSVLEGKRVVVVDDSIVRGTTSSKIVRMLREAGAKEVHMRIASP 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 399 EIRFPNVYGIDMPSATELIAHGREVDEIRQIIGADGLIFQDLNDLIDAVRAENPdiqQFECSVFNGVY------VTKDVD 472
Cdd:PLN02440 379 PIIASCYYGVDTPSREELISNRMSVEEIRKFIGCDSLAFLPLEDLKKSLGEESP---RFCYACFSGDYpvlpkrVGGDID 455
|
490 500
....*....|....*....|...
gi 16130247 473 QGYLDFLDTLRNDDAKAVQRQNE 495
Cdd:PLN02440 456 DGYLESLEEAGRGWGRKGRRQEA 478
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
2-466 |
1.97e-148 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 432.92 E-value: 1.97e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 2 CGIVGIAGVMPVNQS--IYDALTVLQHRGQDAAGIITIDANNcFRLRKANGLVSDVFEARHMQRLQGNMGIGHVRYPTAG 79
Cdd:PRK05793 15 CGVFGVFSKNNIDVAslTYYGLYALQHRGQESAGIAVSDGEK-IKVHKGMGLVSEVFSKEKLKGLKGNSAIGHVRYSTTG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 80 SSSASEAQPFYVNSPYG-ITLAHNGNLTNAHELRKKLfEEKRRHINTTSDSEILLNIFASELdnfrHYPLEaDNIFAAIA 158
Cdd:PRK05793 94 ASDLDNAQPLVANYKLGsIAIAHNGNLVNADVIRELL-EDGGRIFQTSIDSEVILNLIARSA----KKGLE-KALVDAIQ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 159 AtnrlIRGAYACVAM----IIGhgmvaFRDPNGIRPLVLGKRDIDenrteYMVASESVALDTLGFDFLRDVAPGEAIYIT 234
Cdd:PRK05793 168 A----IKGSYALVILtedkLIG-----VRDPHGIRPLCLGKLGDD-----YILSSESCALDTIGAEFIRDVEPGEIVIID 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 235 EEGqLFTRQCADNPVSNPCLFEYVYFARPDSFIDKISVYSARVNMGtklgEKIAREWEdLDIDVVIPIPETSCDIALEIA 314
Cdd:PRK05793 234 EDG-IKSIKFAEKTKCQTCAFEYIYFARPDSVIDGISVYESRVRAG----RQLYKEYP-VDADIVIGVPDSGIPAAIGYA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 315 RILGKPYRQGFVKNRYVGRTFIMPGQQLRRKSVRRKLNANRAEFRDKNVLLVDDSIVRGTTSEQIIEMAREAGAKKVYLA 394
Cdd:PRK05793 308 EASGIPYGIGFIKNKYVGRTFIAPSQELRERAVRVKLNPLKVNVEGKRVVLIDDSIVRGTTSKRLVELLRKAGAKEVHFR 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130247 395 SAAPEIRFPNVYGIDMPSATELIAHGREVDEIRQIIGADGLIFQDLNDLIDAVRAENpdiqQFECSVFNGVY 466
Cdd:PRK05793 388 VSSPPVKYPCYFGIDTPYRKELIGANMSVEEIREMIGADSLGYLSIEGLLESLNGDK----GFCLGCFNGVY 455
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
2-268 |
1.25e-143 |
|
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: 412.24 E-value: 1.25e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 2 CGIVGIAGVMPVNQSIYDALTVLQHRGQDAAGIITIDaNNCFRLRKANGLVSDVFEARHMQRLQGNMGIGHVRYPTAGSS 81
Cdd:cd00715 1 CGVFGIYGAEDAARLTYLGLYALQHRGQESAGIATSD-GKRFHTHKGMGLVSDVFDEEKLRRLPGNIAIGHVRYSTAGSS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 82 SASEAQPFYVNSP-YGITLAHNGNLTNAHELRKKLFEEKrRHINTTSDSEILLNIFASELDNfrhypleaDNIFAAIAAT 160
Cdd:cd00715 80 SLENAQPFVVNSPlGGIALAHNGNLVNAKELREELEEEG-RIFQTTSDSEVILHLIARSLAK--------DDLFEAIIDA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 161 NRLIRGAYACVAMIIgHGMVAFRDPNGIRPLVLGKRDIDenrtEYMVASESVALDTLGFDFLRDVAPGEAIYITEEGqLF 240
Cdd:cd00715 151 LERVKGAYSLVIMTA-DGLIAVRDPHGIRPLVLGKLEGD----GYVVASESCALDIIGAEFVRDVEPGEIVVIDDDG-LE 224
|
250 260
....*....|....*....|....*...
gi 16130247 241 TRQCADNPVSNPCLFEYVYFARPDSFID 268
Cdd:cd00715 225 SSQRAPKPKPAPCIFEYVYFARPDSVID 252
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
2-231 |
4.04e-57 |
|
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: 189.20 E-value: 4.04e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 2 CGIVGIAGVMPVNQSIYDA----LTVLQHRGQDAAGIITIDANNCFRlRKANGLVSDVFEARHMQRLQGNMGIGHVRYPT 77
Cdd:cd00352 1 CGIFGIVGADGAASLLLLLllrgLAALEHRGPDGAGIAVYDGDGLFV-EKRAGPVSDVALDLLDEPLKSGVALGHVRLAT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 78 AGSSSASEAQPFYVNSpYGITLAHNGNLTNAHELRKKLfEEKRRHINTTSDSEILLNIFASELDNFRhypleadnIFAAI 157
Cdd:cd00352 80 NGLPSEANAQPFRSED-GRIALVHNGEIYNYRELREEL-EARGYRFEGESDSEVILHLLERLGREGG--------LFEAV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130247 158 AATNRLIRGAYACVAMIIG-HGMVAFRDPNGIRPLVLGKRDIDenrtEYMVASESVALDTLGFDFLRDVAPGEAI 231
Cdd:cd00352 150 EDALKRLDGPFAFALWDGKpDRLFAARDRFGIRPLYYGITKDG----GLVFASEPKALLALPFKGVRRLPPGELL 220
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
2-239 |
9.15e-25 |
|
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: 101.75 E-value: 9.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 2 CGIVGIAGVMPVNQSIYDALTVLQHRGQDAAGiITIDANNCFRLRKANGLVSDVFEARHMQRLQGNMGIGHVRYPTAGSS 81
Cdd:cd00714 1 CGIVGYIGKREAVDILLEGLKRLEYRGYDSAG-IAVIGDGSLEVVKAVGKVANLEEKLAEKPLSGHVGIGHTRWATHGEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 82 SASEAQPfYVNSPYGITLAHNGNLTNAHELRKKLfeEKRRHI-NTTSDSEILLNIFASELDnfrhyplEADNIFAAIAAT 160
Cdd:cd00714 80 TDVNAHP-HRSCDGEIAVVHNGIIENYAELKEEL--EAKGYKfESETDTEVIAHLIEYYYD-------GGLDLLEAVKKA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 161 NRLIRGAYACVAMIIGHG--MVAFRdpNGiRPLVLGKRDIdenrtEYMVASESVALdtlgFDFLRDVapgeaIYItEEGQ 238
Cdd:cd00714 150 LKRLEGAYALAVISKDEPdeIVAAR--NG-SPLVIGIGDG-----ENFVASDAPAL----LEHTRRV-----IYL-EDGD 211
|
.
gi 16130247 239 L 239
Cdd:cd00714 212 I 212
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
2-215 |
1.05e-22 |
|
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: 96.95 E-value: 1.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 2 CGIVGIA---GVMPVNQSIYDALTVLQHRG-QDAAGIITIDANNCFRLR--------KANGLVSDVFEARHMQRLQGNMG 69
Cdd:cd01907 1 CGIFGIMskdGEPFVGALLVEMLDAMQERGpGDGAGFALYGDPDAFVYSsgkdmevfKGVGYPEDIARRYDLEEYKGYHW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 70 IGHVRYPTAGSSSASEAQPFyvnSPYGITLAHNGNLTNAHELRKKLfEEKRRHINTTSDSEILLNIFA---SELDNFRHY 146
Cdd:cd01907 81 IAHTRQPTNSAVWWYGAHPF---SIGDIAVVHNGEISNYGSNREYL-ERFGYKFETETDTEVIAYYLDlllRKGGLPLEY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 147 -------PLEADNIFAAIAATNRLIR--GAYAcvaMIIGH--GMVAFRDPNGIRPLVLGKRDidenrTEYMVASESVALD 215
Cdd:cd01907 157 ykhiirmPEEERELLLALRLTYRLADldGPFT---IIVGTpdGFIVIRDRIKLRPAVVAETD-----DYVAIASEECAIR 228
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
1-237 |
4.62e-20 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 93.57 E-value: 4.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 1 MCGIVGIAGVMPVNQSIYDALTVLQHRGQDAAGIITIDaNNCFRLRKANGLVSDVFEARHMQRLQGNMGIGHVRYPTAGS 80
Cdd:PRK00331 1 MCGIVGYVGQRNAAEILLEGLKRLEYRGYDSAGIAVLD-DGGLEVRKAVGKVANLEAKLEEEPLPGTTGIGHTRWATHGK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 81 SSASEAQPFYVNSPYgITLAHNGNLTNAHELRKKLfEEKRRHINTTSDSEILLNIFASELDnfrhyplEADNIFAAIAAT 160
Cdd:PRK00331 80 PTERNAHPHTDCSGR-IAVVHNGIIENYAELKEEL-LAKGHVFKSETDTEVIAHLIEEELK-------EGGDLLEAVRKA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 161 NRLIRGAYACVAMIIGH--GMVAFRdpNGiRPLVLGKRDidenrTEYMVASesvalDTLGF-DFLRDVAP---GEAIYIT 234
Cdd:PRK00331 151 LKRLEGAYALAVIDKDEpdTIVAAR--NG-SPLVIGLGE-----GENFLAS-----DALALlPYTRRVIYledGEIAVLT 217
|
...
gi 16130247 235 EEG 237
Cdd:PRK00331 218 RDG 220
|
|
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
1-237 |
6.36e-20 |
|
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase domains [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440218 [Multi-domain] Cd Length: 610 Bit Score: 93.15 E-value: 6.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 1 MCGIVGIAGVMPVNQSIYDALTVLQHRGQDAAGIITIDANNcFRLRKANGLVSDVFEARHMQRLQGNMGIGHVRYPTAGS 80
Cdd:COG0449 1 MCGIVGYIGKRDAAPILLEGLKRLEYRGYDSAGIAVLDDGG-LEVRKAVGKLANLEEKLAEEPLSGTIGIGHTRWATHGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 81 SSASEAQPFYVNSPyGITLAHNGNLTNAHELRKKLfEEKRRHINTTSDSEILLNIFASELDnfrhyplEADNIFAAIAAT 160
Cdd:COG0449 80 PSDENAHPHTSCSG-RIAVVHNGIIENYAELREEL-EAKGHTFKSETDTEVIAHLIEEYLK-------GGGDLLEAVRKA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 161 NRLIRGAYACVAMIIGH--GMVAFRdpNGiRPLVLGkrdIDENrtEYMVASESVALdtlgFDFLRDVAP---GEAIYITE 235
Cdd:COG0449 151 LKRLEGAYALAVISADEpdRIVAAR--KG-SPLVIG---LGEG--ENFLASDVPAL----LPYTRRVIYledGEIAVLTR 218
|
..
gi 16130247 236 EG 237
Cdd:COG0449 219 DG 220
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-214 |
6.49e-19 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 90.08 E-value: 6.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 1 MCGIVGIAGVMPVNQSIYDALTVLQHRGQDAAGIITIDANNCFRLRK--ANGLVSDVFE-------ARHmqrLQGNMGIG 71
Cdd:PTZ00295 24 CCGIVGYLGNEDASKILLEGIEILQNRGYDSCGISTISSGGELKTTKyaSDGTTSDSIEilkekllDSH---KNSTIGIA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 72 HVRYPTAGSSSASEAQPfYVNSPYGITLAHNGNLTNAHELRKKLFEEKRRHINTTsDSEILLNIFASELDNfrhypleAD 151
Cdd:PTZ00295 101 HTRWATHGGKTDENAHP-HCDYKKRIALVHNGTIENYVELKSELIAKGIKFRSET-DSEVIANLIGLELDQ-------GE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130247 152 NIFAAIAATNRLIRGAYACVAMIIGH--GMVAFRdpNGiRPLVLGKRDidenrTEYMVASESVAL 214
Cdd:PTZ00295 172 DFQEAVKSAISRLQGTWGLCIIHKDNpdSLIVAR--NG-SPLLVGIGD-----DSIYVASEPSAF 228
|
|
| PRTases_typeI |
cd06223 |
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ... |
283-398 |
2.95e-18 |
|
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: 80.90 E-value: 2.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 283 LGEKIAREWED--LDIDVVIPIPETSCDIALEIARILGKPYRQGFVKNRYVGRTFIMPGQqlrrksvrrKLNANRAEFRD 360
Cdd:cd06223 1 AGRLLAEEIREdlLEPDVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSEPYG---------LELPLGGDVKG 71
|
90 100 110
....*....|....*....|....*....|....*...
gi 16130247 361 KNVLLVDDSIVRGTTSEQIIEMAREAGAKKVYLASAAP 398
Cdd:cd06223 72 KRVLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVLLD 109
|
|
| YafJ |
cd01908 |
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ... |
70-235 |
7.87e-13 |
|
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: 68.57 E-value: 7.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 70 IGHVRYPTAGSSSASEAQPFYVNSpygITLAHNGNLTNAHELRKKLFEEKRRHINTTSDSEILLNIFASELDNfrHYPLE 149
Cdd:cd01908 84 LAHVRAATVGPVSLENCHPFTRGR---WLFAHNGQLDGFRLLRRRLLRLLPRLPVGTTDSELAFALLLSRLLE--RDPLD 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 150 ADNIFAAIAAT----NRLIRGAYACVAMIIGHGMVAFR-------------DPNGIRPLVLGKRDIDENRTeYMVASEsv 212
Cdd:cd01908 159 PAELLDAILQTlrelAALAPPGRLNLLLSDGEYLIATRyasapslyyltrrAPFGCARLLFRSVTTPNDDG-VVVASE-- 235
|
170 180
....*....|....*....|....
gi 16130247 213 aldTLGFDF-LRDVAPGEAIYITE 235
Cdd:cd01908 236 ---PLTDDEgWTEVPPGELVVVSE 256
|
|
| YafJ |
COG0121 |
Predicted glutamine amidotransferase YafJ [General function prediction only]; |
2-239 |
8.66e-12 |
|
Predicted glutamine amidotransferase YafJ [General function prediction only];
Pssm-ID: 439891 [Multi-domain] Cd Length: 248 Bit Score: 65.37 E-value: 8.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 2 CGIVGIAGVMPV--NQSIYDALTVLQHRGQ--------DAAGIITIDANN-CFRLRKANGLVSDVFEARHMQRLQGNMGI 70
Cdd:COG0121 1 CRLLGYSGNVPTdlEFLLLDPEHSLVRQSGatregphaDGWGIGWYEGDGePRLYRDPLPAWSDPNLRLLARPIKSRLVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 71 GHVRYPTAGSSSASEAQPFYVnspYGITLAHNGNLTNAHELRKKLFEEK----RRHINTTSDSEILLNIFASELDNFRHY 146
Cdd:COG0121 81 AHVRKATVGPVSLENTHPFRG---GRWLFAHNGQLDGFDRLRRRLAEELpdelYFQPVGTTDSELAFALLLSRLRDGGPD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 147 PLEAdnIFAAIAATNRLIRGAYAC-VAMIIGHGMVAFRDPNGIRP--LVLGKRDIDENRTeYMVASESVALDTlGFdflR 223
Cdd:COG0121 158 PAEA--LAEALRELAELARAPGRLnLLLSDGERLYATRYTSDDPYptLYYLTRTTPDDRV-VVVASEPLTDDE-GW---T 230
|
250
....*....|....*.
gi 16130247 224 DVAPGEAIYITEEGQL 239
Cdd:COG0121 231 EVPPGELLVVRDGLEV 246
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
82-214 |
1.18e-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: 61.77 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 82 SASEAQPFYVNSPYGITLAHNGNLTNAHELRKKLfEEKRRHINTTSDSEILLNIFASE--LDNFRHypleADNIFA-AI- 157
Cdd:pfam13537 9 LEGGAQPMVSSEDGRYVIVFNGEIYNYRELRAEL-EAKGYRFRTHSDTEVILHLYEAEwgEDCVDR----LNGMFAfAIw 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 16130247 158 -AATNRLIrgayacvamiighgmvAFRDPNGIRPLVLGKRDidenRTEYMVASESVAL 214
Cdd:pfam13537 84 dRRRQRLF----------------LARDRFGIKPLYYGRDD----GGRLLFASELKAL 121
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
69-210 |
2.03e-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: 433279 [Multi-domain] Cd Length: 130 Bit Score: 61.55 E-value: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 69 GIGHVRYPTAGSSSASeAQPFYvnSPYG-ITLAHNGNLTNAHELRKKLfEEKRRHINTTSDSEILLNIfaseldnFRHYP 147
Cdd:pfam13522 13 ALGHVRLAIVDLPDAG-NQPML--SRDGrLVLVHNGEIYNYGELREEL-ADLGHAFRSRSDTEVLLAL-------YEEWG 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130247 148 LEadnifaaiaATNRLiRGAYA-CVAMIIGHGMVAFRDPNGIRPLVLGkrdIDENRteYMVASE 210
Cdd:pfam13522 82 ED---------CLERL-RGMFAfAIWDRRRRTLFLARDRLGIKPLYYG---ILGGG--FVFASE 130
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-197 |
2.06e-11 |
|
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: 63.73 E-value: 2.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 2 CGIVGI---AGVMPVNQSIYDALTVLQHRGQDAAGIitidanncfrlrkanglvsdvfearhmqRLQGNMGIGHVRY--- 75
Cdd:cd00712 1 CGIAGIiglDGASVDRATLERMLDALAHRGPDGSGI----------------------------WIDEGVALGHRRLsii 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 76 -PTAGsssaseAQPFYVNSPyGITLAHNGNLTNAHELRKKLfEEKRRHINTTSDSEILLnifasELdnFRHYPLEA---- 150
Cdd:cd00712 53 dLSGG------AQPMVSEDG-RLVLVFNGEIYNYRELRAEL-EALGHRFRTHSDTEVIL-----HL--YEEWGEDClerl 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16130247 151 DNIFA-AI--AATNRLIrgayacvamiighgmvAFRDPNGIRPLVLGKRD 197
Cdd:cd00712 118 NGMFAfALwdKRKRRLF----------------LARDRFGIKPLYYGRDG 151
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-191 |
1.66e-09 |
|
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: 60.24 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 1 MCGIVGIAG-VMPVNQSIYDALT-VLQHRGQDAAGIItidanncfrlrkanglvsdvfearhmqrLQGNMGIGHVRypta 78
Cdd:COG0367 1 MCGIAGIIDfDGGADREVLERMLdALAHRGPDGSGIW----------------------------VDGGVALGHRR---- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 79 gSS----SASEAQPFyVNSPYGITLAHNGNLTNAHELRKKLfEEKRRHINTTSDSEILLnifaseldnfrhypleadnif 154
Cdd:COG0367 49 -LSiidlSEGGHQPM-VSEDGRYVLVFNGEIYNYRELRAEL-EALGHRFRTHSDTEVIL--------------------- 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16130247 155 AAIAAtnrliRGAyACVAMIigHGMVAF-------------RDPNGIRPL 191
Cdd:COG0367 105 HAYEE-----WGE-DCLERL--NGMFAFaiwdrrerrlflaRDRFGIKPL 146
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
1-194 |
2.39e-09 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 59.73 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 1 MCGIVGIAGVM----PVNQSIYDALTVLQHRGQDAAGIITIDanncfrlrkaNGLVSDVFearhmqrlqgnmgIGHVRYP 76
Cdd:PTZ00077 1 MCGILAIFNSKgerhELRRKALELSKRLRHRGPDWSGIIVLE----------NSPGTYNI-------------LAHERLA 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 77 TAGSSSAseAQPFYVNSpYGITLAHNGNLTNAHELRKKLfEEKRRHINTTSDSEILLNIFASELDNfrHYPLEADNIFAA 156
Cdd:PTZ00077 58 IVDLSDG--KQPLLDDD-ETVALMQNGEIYNHWEIRPEL-EKEGYKFSSNSDCEIIGHLYKEYGPK--DFWNHLDGMFAT 131
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 16130247 157 I---AATNRLirgayacvamiighgmVAFRDPNGIRPLVLG 194
Cdd:PTZ00077 132 ViydMKTNTF----------------FAARDHIGIIPLYIG 156
|
|
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
1-214 |
3.86e-09 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 59.15 E-value: 3.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 1 MCGIVGIAGV----MPVNQSIYDALTVLQHRGQDAAGIITIDanncfrlrkanglvsdvfearhmqrlqgNMGIGHVRYP 76
Cdd:PRK09431 1 MCGIFGILDIktdaDELRKKALEMSRLMRHRGPDWSGIYASD----------------------------NAILGHERLS 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 77 TAGSSSAseAQPFYvNSPYGITLAHNGNLTNAHELRKKLfeEKRRHINTTSDSEILLNIFaseldnfRHYPLEA----DN 152
Cdd:PRK09431 53 IVDVNGG--AQPLY-NEDGTHVLAVNGEIYNHQELRAEL--GDKYAFQTGSDCEVILALY-------QEKGPDFlddlDG 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130247 153 IFA-AIAATNRlirGAYacvamIIGhgmvafRDPNGIRPLVLGKRDidenRTEYMVASESVAL 214
Cdd:PRK09431 121 MFAfALYDSEK---DAY-----LIA------RDPIGIIPLYYGYDE----HGNLYFASEMKAL 165
|
|
| ComFC |
COG1040 |
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General ... |
273-397 |
3.98e-08 |
|
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General function prediction only];
Pssm-ID: 440662 [Multi-domain] Cd Length: 196 Bit Score: 53.29 E-value: 3.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 273 YSARVNMGTKLGEKIAREWEDL---DIDVVIPIP-----------ETSCDIALEIARILGKPYR-QGFVKNRY----VGR 333
Cdd:COG1040 53 YRGRLDLARLLARLLARALREAllpRPDLIVPVPlhrrrlrrrgfNQAELLARALARALGIPVLpDLLRRVRAtpsqAGL 132
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130247 334 TfimpgQQLRRKSVRRKLNANR-AEFRDKNVLLVDDsiVR--GTTSEQIIEMAREAGAKKVYLASAA 397
Cdd:COG1040 133 S-----RAERRRNLRGAFAVRPpARLAGKHVLLVDD--VLttGATLAEAARALKAAGAARVDVLVLA 192
|
|
| PLN02549 |
PLN02549 |
asparagine synthase (glutamine-hydrolyzing) |
1-194 |
1.08e-06 |
|
asparagine synthase (glutamine-hydrolyzing)
Pssm-ID: 178164 [Multi-domain] Cd Length: 578 Bit Score: 51.30 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 1 MCGI---VGIAGVMPVNQS-IYDALTVLQHRGQDAAGIitidanncfRLRKANGLVsdvfearHmQRLQgnmgighVRYP 76
Cdd:PLN02549 1 MCGIlavLGCSDDSQAKRSrVLELSRRLRHRGPDWSGL---------YGNEDCYLA-------H-ERLA-------IMDP 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 77 TAGSssaseaQPFYvNSPYGITLAHNGNLTNAHELRKKLFEEKRRhinTTSDSEILLNIFASELDNFrhyPLEADNIFAA 156
Cdd:PLN02549 57 ESGD------QPLY-NEDKTIVVTANGEIYNHKELREKLKLHKFR---TGSDCEVIAHLYEEHGEEF---VDMLDGMFSF 123
|
170 180 190
....*....|....*....|....*....|....*...
gi 16130247 157 IAATNRlirgayacvamiiGHGMVAFRDPNGIRPLVLG 194
Cdd:PLN02549 124 VLLDTR-------------DNSFIAARDHIGITPLYIG 148
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-212 |
3.79e-05 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 46.41 E-value: 3.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 1 MCGIVGIAGvMPVNQSIYDALTVL-------QHRGQDAAGIiTIDANncFRLRKANGLVSDVFEARH-MQRLQGNM---- 68
Cdd:PTZ00394 1 MCGIFGYAN-HNVPRTVEQILNVLldgiqkvEYRGYDSAGL-AIDAN--IGSEKEDGTAASAPTPRPcVVRSVGNIsqlr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 69 -----------------------GIGHVRYPTAGSSSASEAQPFYVNSpYGITLAHNGNLTNAHELrKKLFEEKRRHINT 125
Cdd:PTZ00394 77 ekvfseavaatlppmdattshhvGIAHTRWATHGGVCERNCHPQQSNN-GEFTIVHNGIVTNYMTL-KELLKEEGYHFSS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 126 TSDSEIlLNIFASELdnfrhYPLEADNIFAAIAA-TNRLIRGAYACV--AMIIGHGMVAFRDPNgirPLVLGKRDIDENR 202
Cdd:PTZ00394 155 DTDTEV-ISVLSEYL-----YTRKGIHNFADLALeVSRMVEGSYALLvkSVYFPGQLAASRKGS---PLMVGIRRTDDRG 225
|
250
....*....|
gi 16130247 203 TEYMVASESV 212
Cdd:PTZ00394 226 CVMKLQTYDL 235
|
|
| PRK00934 |
PRK00934 |
ribose-phosphate pyrophosphokinase; Provisional |
310-394 |
2.29e-04 |
|
ribose-phosphate pyrophosphokinase; Provisional
Pssm-ID: 234868 [Multi-domain] Cd Length: 285 Bit Score: 42.98 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 310 ALEIARILGKPYRQgFVKNRYVGRTFIMpgqqlRRKSVrrklnanraEFRDKNVLLVDDSIVRGTTSEQIIEMAREAGAK 389
Cdd:PRK00934 169 AKEAAEILGCEYDY-LEKTRISPTEVEI-----APKNL---------DVKGKDVLIVDDIISTGGTMATAIKILKEQGAK 233
|
....*
gi 16130247 390 KVYLA 394
Cdd:PRK00934 234 KVYVA 238
|
|
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
1-132 |
4.38e-04 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 42.82 E-value: 4.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 1 MCGIVGIA--GVMPVNQSIYD----ALTVLQHRGQDAAGIiTIDANNCFR------LR---KANGLVSDVFEARHMQRLQ 65
Cdd:PLN02981 1 MCGIFAYLnyNVPRERRFILEvlfnGLRRLEYRGYDSAGI-AIDNDPSLEsssplvFReegKIESLVRSVYEEVAETDLN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130247 66 GNM------GIGHVRYPTAGSSSASEAQPFYVNSPYGITLAHNGNLTNaHELRKKLFEEKRRHINTTSDSEIL 132
Cdd:PLN02981 80 LDLvfenhaGIAHTRWATHGPPAPRNSHPQSSGPGNEFLVVHNGIITN-YEVLKETLLRHGFTFESDTDTEVI 151
|
|
| PRK08558 |
PRK08558 |
adenine phosphoribosyltransferase; Provisional |
283-391 |
6.67e-04 |
|
adenine phosphoribosyltransferase; Provisional
Pssm-ID: 181466 [Multi-domain] Cd Length: 238 Bit Score: 41.52 E-value: 6.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 283 LGEKIAREWEDLDIDVVIPIPETSCDIALEIARILG------KPYRQGFVKNRYVGRTFIMPGqqlrrksvrRKLN---A 353
Cdd:PRK08558 99 IAPVVAERFMGLRVDVVLTAATDGIPLAVAIASYFGadlvyaKKSKETGVEKFYEEYQRLASG---------IEVTlylP 169
|
90 100 110
....*....|....*....|....*....|....*...
gi 16130247 354 NRAEFRDKNVLLVDDSIVRGTTSEQIIEMAREAGAKKV 391
Cdd:PRK08558 170 ASALKKGDRVLIVDDIIRSGETQRALLDLARQAGADVV 207
|
|
| Hpt1 |
COG2236 |
Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine ... |
339-394 |
1.07e-03 |
|
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: 39.44 E-value: 1.07e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 16130247 339 GQQLRRKSVRRKLNANraeFRDKNVLLVDDSIVRGTTSEQIIEMAREAGAKKVYLA 394
Cdd:COG2236 70 AKRLEEPVVKGPLDED---LAGKRVLIVDDVADTGRTLEAVRDLLKEAGPAEVRTA 122
|
|
| RlhA |
COG0826 |
23S rRNA C2501 and tRNA U34 5'-hydroxylation protein RlhA/YrrN/YrrO, U32 peptidase family ... |
377-454 |
2.39e-03 |
|
23S rRNA C2501 and tRNA U34 5'-hydroxylation protein RlhA/YrrN/YrrO, U32 peptidase family [Translation, ribosomal structure and biogenesis]; 23S rRNA C2501 and tRNA U34 5'-hydroxylation protein RlhA/YrrN/YrrO, U32 peptidase family is part of the Pathway/BioSystem: 23S rRNA modification
Pssm-ID: 440588 Cd Length: 311 Bit Score: 40.13 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 377 EQIIEMAREAGaKKVYLASaapeirfpNVygidmpsatelIAHGREVDEIRQII------GADGLIFQDLNdLIDAVRAE 450
Cdd:COG0826 49 AEAVEYAHERG-KKVYVTL--------NT-----------LLHDEELEELEEYLdflaeaGVDAIIVQDLG-VLELAREI 107
|
....
gi 16130247 451 NPDI 454
Cdd:COG0826 108 APDL 111
|
|
| Pribosyltran |
pfam00156 |
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ... |
278-394 |
4.18e-03 |
|
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl transferase enzymes. This family includes: Adenine phosphoribosyl-transferase EC:2.4.2.7. Hypoxanthine-guanine-xanthine phosphoribosyl-transferase. Hypoxanthine phosphoribosyl-transferase EC:2.4.2.8. Ribose-phosphate pyrophosphokinase i EC:2.7.6.1. Amidophosphoribosyltransferase EC:2.4.2.14. Orotate phosphoribosyl-transferase EC:2.4.2.10. Uracil phosphoribosyl-transferase EC:2.4.2.9. Xanthine-guanine phosphoribosyl-transferase EC:2.4.2.22. In Arabidopsis, At the very N-terminus of this domain is the P-Loop NTPase domain.
Pssm-ID: 425489 [Multi-domain] Cd Length: 150 Bit Score: 37.73 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 278 NMGTKLGEKIAREWEDLD--IDVVIPIPETSCDIALEIARILGKPYrQGFVKNRYVGRTfimPGQQlrrksvrrKLNANR 355
Cdd:pfam00156 10 AILKAVARLAAQINEDYGgkPDVVVGILRGGLPFAGILARRLDVPL-AFVRKVSYNPDT---SEVM--------KTSSAL 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 16130247 356 AEFRDKNVLLVDDSIVRGTTSEQIIEMAREAGAKKVYLA 394
Cdd:pfam00156 78 PDLKGKTVLIVDDILDTGGTLLKVLELLKNVGPKEVKIA 116
|
|
| ribP_PPkin |
TIGR01251 |
ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In ... |
292-394 |
4.48e-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: 39.18 E-value: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 292 EDLDIDVVIPIPET-SCDIALEIARILGKPYrqgfvknryvgrtFIMpgqqlrRKsvRRKLNANRAEFR-------DKNV 363
Cdd:TIGR01251 155 KKILDNPVVVSPDAgGVERAKKVADALGCPL-------------AII------DK--RRISATNEVEVMnlvgdveGKDV 213
|
90 100 110
....*....|....*....|....*....|.
gi 16130247 364 LLVDDSIVRGTTSEQIIEMAREAGAKKVYLA 394
Cdd:TIGR01251 214 VIVDDIIDTGGTIAKAAEILKSAGAKRVIAA 244
|
|
| PyrE |
COG0461 |
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ... |
282-389 |
4.57e-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: 38.60 E-value: 4.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 282 KLGEKIAREWEDL--DIDVV-------IPIpetscdiALEIARILGKPYrqGFV----KNRyvGRtfimpGQQLRRKSVR 348
Cdd:COG0461 48 LLGEALAELIKELgpEFDAVagpatggIPL-------AAAVARALGLPA--IFVrkeaKDH--GT-----GGQIEGGLLP 111
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 16130247 349 rklnanraefrDKNVLLVDDSIVRGTTSEQIIEMAREAGAK 389
Cdd:COG0461 112 -----------GERVLVVEDVITTGGSVLEAVEALREAGAE 141
|
|
| pyrE |
PRK00455 |
orotate phosphoribosyltransferase; Validated |
282-389 |
8.74e-03 |
|
orotate phosphoribosyltransferase; Validated
Pssm-ID: 234771 Cd Length: 202 Bit Score: 37.44 E-value: 8.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130247 282 KLGEKIAREWED--LDIDVVI-P----IPetscdIALEIARILGKPYrqGFV----KNRYVGRTFImpgqqLRRKSvrrk 350
Cdd:PRK00455 49 LLGRFLAEAIKDsgIEFDVVAgPatggIP-----LAAAVARALDLPA--IFVrkeaKDHGEGGQIE-----GRRLF---- 112
|
90 100 110
....*....|....*....|....*....|....*....
gi 16130247 351 lnanraefrDKNVLLVDDSIVRGTTSEQIIEMAREAGAK 389
Cdd:PRK00455 113 ---------GKRVLVVEDVITTGGSVLEAVEAIRAAGAE 142
|
|
| |
