|
Name |
Accession |
Description |
Interval |
E-value |
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
1-475 |
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: 772.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 1 MCGIVGIVGSTPVNQSIYDALTVLQHRGQDAAGICTIESNRFRLRKANGLVKDVFEAKHMQRLQGEVGIGHVRYPTAGSS 80
Cdd:COG0034 7 ECGVFGIYGHEDVAQLTYYGLYALQHRGQESAGIATSDGGRFHLHKGMGLVSDVFDEEDLERLKGNIAIGHVRYSTTGSS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 81 SASEAQPFYVNSPFG-ITLAHNGNLTNANEVREKLFEKDRrHVNTTSDSEVLLNVLAHEIdtvkgnvTSDDVFRAVANVH 159
Cdd:COG0034 87 SLENAQPFYVNSPFGsIALAHNGNLTNAEELREELEEEGA-IFQTTSDTEVILHLIAREL-------TKEDLEEAIKEAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 160 RTIRGAYAVTAMIiGHGMIAFRDPHGIRPLCLGKREvqgkTEYMVASESVALDAVGFDFMRDVAPGEAIYATFDGeLFTK 239
Cdd:COG0034 159 RRVKGAYSLVILT-GDGLIAARDPNGIRPLVLGKLE----DGYVVASESCALDILGAEFVRDVEPGEIVVIDEDG-LRSR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 240 QCADNPQLNPCIFEFVYFARPDSFIDKISVYSARVEMGEMLGKRikeeyADLDIDVVIPIPETSNDIALRIAQAINKPYR 319
Cdd:COG0034 233 QFAEKPRPAPCIFEYVYFARPDSVIDGRSVYEARKRMGRELARE-----APVDADVVIPVPDSGRPAAIGYAEESGIPYE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 320 QGFVKNRYVGRTFIMPGQQQRKKSVRRKLNAIRSEFKGKNVLLVDDSIVRGTTSEQIIEMARDSGANKVFMVSAAPEVRF 399
Cdd:COG0034 308 EGLIKNRYVGRTFIQPTQELRELGVRLKLNPIREVVKGKRVVLVDDSIVRGTTSRRIVKMLREAGAKEVHFRIASPPIRY 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515634076 400 PNVYGIDMPSATELIAHGRDNETICKQIGADALIFQTLPDLISAVGmgnQDISRFDTSVFNGEYVTGDIDQAYLDF 475
Cdd:COG0034 388 PCYYGIDTPTREELIAANRSVEEIREYIGADSLGYLSLEGLIEAVG---EPIEGFCTACFTGDYPTGIPDEEKKRL 460
|
|
| purF |
TIGR01134 |
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ... |
2-464 |
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: 697.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 2 CGIVGIVGSTPVNQS-IYDALTVLQHRGQDAAGICTIESNRFRLRKANGLVKDVFEAKHMQRLQGEVGIGHVRYPTAGSS 80
Cdd:TIGR01134 1 CGVVGIYGQEEVAASlTYYGLYALQHRGQESAGISVFDGNRFRLHKGNGLVSDVFNEEHLQRLKGNVGIGHVRYSTAGSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 81 SASEAQPFYVNSPFG-ITLAHNGNLTNANEVREKLFEkDRRHVNTTSDSEVLLNVLAHEIDTVkgnvtsDDVFRAVANVH 159
Cdd:TIGR01134 81 GLENAQPFVVNSPYGgLALAHNGNLVNADELRRELEE-EGRHFNTTSDSEVLLHLLAHNDESK------DDLFDAVARVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 160 RTIRGAYAVTAMIiGHGMIAFRDPHGIRPLCLGKREvqgkTEYMVASESVALDAVGFDFMRDVAPGEAIYaTFDGELFTK 239
Cdd:TIGR01134 154 ERVRGAYALVLMT-EDGLVAVRDPHGIRPLVLGRRG----DGYVVASESCALDILGAEFVRDVEPGEVVV-IFDGGLESR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 240 QCADNPQlNPCIFEFVYFARPDSFIDKISVYSARVEMGEMLGKRIkeeyaDLDIDVVIPIPETSNDIALRIAQAINKPYR 319
Cdd:TIGR01134 228 QCARRPR-APCVFEYVYFARPDSVIDGISVYYARKRMGKELARES-----PVEADVVVPVPDSGRSAALGFAQASGIPYR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 320 QGFVKNRYVGRTFIMPGQQQRKKSVRRKLNAIRSEFKGKNVLLVDDSIVRGTTSEQIIEMARDSGANKVFMVSAAPEVRF 399
Cdd:TIGR01134 302 EGLIKNRYVGRTFIMPTQELRELSVRLKLNPVRAVFEGKRVVLVDDSIVRGTTSRQIVEMLRDAGAKEVHVRIASPPIRY 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515634076 400 PNVYGIDMPSATELIAHGRDNETICKqIGADALIFQTLPDLISAVGMGNQDisrFDTSVFNGEYV 464
Cdd:TIGR01134 382 PCYYGIDMPTREELIAARRTVEEIRK-IGADSLAYLSLEGLKEAVGNPESD---LCLACFTGEYP 442
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
1-492 |
0e+00 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 607.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 1 MCGIVGIVGSTPVNQSIYDALTVLQHRGQDAAGICTIESNRFRLRKANGLVKDVFEAKHMQRLQGEVGIGHVRYPTAGSS 80
Cdd:PLN02440 1 ECGVVGIFGDPEASRLCYLGLHALQHRGQEGAGIVTVDGNRLQSITGNGLVSDVFDESKLDQLPGDIAIGHVRYSTAGAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 81 SASEAQPFYVNSPFG-ITLAHNGNLTNANEVREKLfEKDRRHVNTTSDSEVLLNVLAHEIdtvkgnvtSDDVFRAVANVH 159
Cdd:PLN02440 81 SLKNVQPFVANYRFGsIGVAHNGNLVNYEELRAKL-EENGSIFNTSSDTEVLLHLIAISK--------ARPFFSRIVDAC 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 160 RTIRGAYAVTAMIIGHgMIAFRDPHGIRPLCLGKREvqgKTEYMVASESVALDAVGFDFMRDVAPGEAIYATfDGELFTK 239
Cdd:PLN02440 152 EKLKGAYSMVFLTEDK-LVAVRDPHGFRPLVMGRRS---NGAVVFASETCALDLIGATYEREVNPGEVIVVD-KDKGVSS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 240 QCA-DNPQLNPCIFEFVYFARPDSFIDKISVYSARVEMGEMLGKRIKEeyadlDIDVVIPIPETSNDIALRIAQAINKPY 318
Cdd:PLN02440 227 QCLmPHPEPKPCIFEHIYFARPNSIVFGRSVYESRLEFGEILATEIPV-----DCDVVIPVPDSGRVAALGYAAKLGVPF 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 319 RQGFVKNRYVGRTFIMPGQQQRKKSVRRKLNAIRSEFKGKNVLLVDDSIVRGTTSEQIIEMARDSGANKVFMVSAAPEVR 398
Cdd:PLN02440 302 QQGLIRSHYVGRTFIEPSQKIRDFSVKLKLNPVRSVLEGKRVVVVDDSIVRGTTSSKIVRMLREAGAKEVHMRIASPPII 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 399 FPNVYGIDMPSATELIAHGRDNETICKQIGADALIFQTLPDLIsavGMGNQDISRFDTSVFNGEY------VTGDIDQAY 472
Cdd:PLN02440 382 ASCYYGVDTPSREELISNRMSVEEIRKFIGCDSLAFLPLEDLK---KSLGEESPRFCYACFSGDYpvlpkrVGGDIDDGY 458
|
490 500
....*....|....*....|
gi 515634076 473 LDFLDSLRNDdsKVQREIQQ 492
Cdd:PLN02440 459 LESLEEAGRG--WGRKGRRQ 476
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
2-463 |
4.35e-147 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 429.45 E-value: 4.35e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 2 CGIVGIVGSTPVNQS--IYDALTVLQHRGQDAAGICTIESNRFRLRKANGLVKDVFEAKHMQRLQGEVGIGHVRYPTAGS 79
Cdd:PRK05793 15 CGVFGVFSKNNIDVAslTYYGLYALQHRGQESAGIAVSDGEKIKVHKGMGLVSEVFSKEKLKGLKGNSAIGHVRYSTTGA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 80 SSASEAQPFYVNSPFG-ITLAHNGNLTNANEVREKLfEKDRRHVNTTSDSEVLLNVLAHEidtvkgnvTSDDVFRAVANV 158
Cdd:PRK05793 95 SDLDNAQPLVANYKLGsIAIAHNGNLVNADVIRELL-EDGGRIFQTSIDSEVILNLIARS--------AKKGLEKALVDA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 159 HRTIRGAYAVTaMIIGHGMIAFRDPHGIRPLCLGKREVqgktEYMVASESVALDAVGFDFMRDVAPGEAIYATFDGeLFT 238
Cdd:PRK05793 166 IQAIKGSYALV-ILTEDKLIGVRDPHGIRPLCLGKLGD----DYILSSESCALDTIGAEFIRDVEPGEIVIIDEDG-IKS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 239 KQCADNPQLNPCIFEFVYFARPDSFIDKISVYSARVEMGEMLGKRikeeyADLDIDVVIPIPETSNDIALRIAQAINKPY 318
Cdd:PRK05793 240 IKFAEKTKCQTCAFEYIYFARPDSVIDGISVYESRVRAGRQLYKE-----YPVDADIVIGVPDSGIPAAIGYAEASGIPY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 319 RQGFVKNRYVGRTFIMPGQQQRKKSVRRKLNAIRSEFKGKNVLLVDDSIVRGTTSEQIIEMARDSGANKVFMVSAAPEVR 398
Cdd:PRK05793 315 GIGFIKNKYVGRTFIAPSQELRERAVRVKLNPLKVNVEGKRVVLIDDSIVRGTTSKRLVELLRKAGAKEVHFRVSSPPVK 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515634076 399 FPNVYGIDMPSATELIAHGRDNETICKQIGADALIFQTLPDLISAVGmgnqDISRFDTSVFNGEY 463
Cdd:PRK05793 395 YPCYFGIDTPYRKELIGANMSVEEIREMIGADSLGYLSIEGLLESLN----GDKGFCLGCFNGVY 455
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
2-265 |
1.52e-145 |
|
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: 417.25 E-value: 1.52e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 2 CGIVGIVGSTPVNQSIYDALTVLQHRGQDAAGICTIESNRFRLRKANGLVKDVFEAKHMQRLQGEVGIGHVRYPTAGSSS 81
Cdd:cd00715 1 CGVFGIYGAEDAARLTYLGLYALQHRGQESAGIATSDGKRFHTHKGMGLVSDVFDEEKLRRLPGNIAIGHVRYSTAGSSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 82 ASEAQPFYVNSPFG-ITLAHNGNLTNANEVREKLFEKDrRHVNTTSDSEVLLNVLAHEIDtvkgnvtSDDVFRAVANVHR 160
Cdd:cd00715 81 LENAQPFVVNSPLGgIALAHNGNLVNAKELREELEEEG-RIFQTTSDSEVILHLIARSLA-------KDDLFEAIIDALE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 161 TIRGAYAVTAMIIgHGMIAFRDPHGIRPLCLGKREvqgKTEYMVASESVALDAVGFDFMRDVAPGEAIYATFDGeLFTKQ 240
Cdd:cd00715 153 RVKGAYSLVIMTA-DGLIAVRDPHGIRPLVLGKLE---GDGYVVASESCALDIIGAEFVRDVEPGEIVVIDDDG-LESSQ 227
|
250 260
....*....|....*....|....*
gi 515634076 241 CADNPQLNPCIFEFVYFARPDSFID 265
Cdd:cd00715 228 RAPKPKPAPCIFEYVYFARPDSVID 252
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
2-228 |
8.68e-60 |
|
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: 196.13 E-value: 8.68e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 2 CGIVGIVGSTPVNQSIYDA----LTVLQHRGQDAAGICTIESNRFRLRKANGLVKDVFEAKHMQRLQGEVGIGHVRYPTA 77
Cdd:cd00352 1 CGIFGIVGADGAASLLLLLllrgLAALEHRGPDGAGIAVYDGDGLFVEKRAGPVSDVALDLLDEPLKSGVALGHVRLATN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 78 GSSSASEAQPFYVNSPfGITLAHNGNLTNANEVREKLfEKDRRHVNTTSDSEVLLNVLAHEIDtvkgnvtSDDVFRAVAN 157
Cdd:cd00352 81 GLPSEANAQPFRSEDG-RIALVHNGEIYNYRELREEL-EARGYRFEGESDSEVILHLLERLGR-------EGGLFEAVED 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515634076 158 VHRTIRGAYAVTAMIIG-HGMIAFRDPHGIRPLCLGKREvqgKTEYMVASESVALDAVGFDFMRDVAPGEAI 228
Cdd:cd00352 152 ALKRLDGPFAFALWDGKpDRLFAARDRFGIRPLYYGITK---DGGLVFASEPKALLALPFKGVRRLPPGELL 220
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
2-211 |
1.25e-26 |
|
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: 107.15 E-value: 1.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 2 CGIVGIVGSTPVNQSIYDALTVLQHRGQDAAGICTIESNRFRLRKANGLVKDVFEAKHMQRLQGEVGIGHVRYPTAGSSS 81
Cdd:cd00714 1 CGIVGYIGKREAVDILLEGLKRLEYRGYDSAGIAVIGDGSLEVVKAVGKVANLEEKLAEKPLSGHVGIGHTRWATHGEPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 82 ASEAQPfYVNSPFGITLAHNGNLTNANEVREKLFEKDRRHVNTTsDSEVLLNVLAHEIDtvkgnvTSDDVFRAVANVHRT 161
Cdd:cd00714 81 DVNAHP-HRSCDGEIAVVHNGIIENYAELKEELEAKGYKFESET-DTEVIAHLIEYYYD------GGLDLLEAVKKALKR 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515634076 162 IRGAYAVTAMIIGHG--MIAFRdpHGiRPLCLGKrevqGKTEYMVASESVAL 211
Cdd:cd00714 153 LEGAYALAVISKDEPdeIVAAR--NG-SPLVIGI----GDGENFVASDAPAL 197
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
1-211 |
3.54e-22 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 99.73 E-value: 3.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 1 MCGIVGIVGSTPVNQSIYDALTVLQHRGQDAAGICTIESNRFRLRKANGLVKDVFEAKHMQRLQGEVGIGHVRYPTAGSS 80
Cdd:PRK00331 1 MCGIVGYVGQRNAAEILLEGLKRLEYRGYDSAGIAVLDDGGLEVRKAVGKVANLEAKLEEEPLPGTTGIGHTRWATHGKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 81 SASEAQPFYVNSpfG-ITLAHNGNLTNANEVREKLFEKDRRHVNTTsDSEVLLNVLAHEIDtvkgnvTSDDVFRAVANVH 159
Cdd:PRK00331 81 TERNAHPHTDCS--GrIAVVHNGIIENYAELKEELLAKGHVFKSET-DTEVIAHLIEEELK------EGGDLLEAVRKAL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515634076 160 RTIRGAYAVtamiighGMIAFRDPHGI---R---PLCLGKrevqGKTEYMVASESVAL 211
Cdd:PRK00331 152 KRLEGAYAL-------AVIDKDEPDTIvaaRngsPLVIGL----GEGENFLASDALAL 198
|
|
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
1-211 |
3.81e-22 |
|
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: 99.70 E-value: 3.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 1 MCGIVGIVGSTPVNQSIYDALTVLQHRGQDAAGICTIESNRFRLRKANGLVKDVFEAKHMQRLQGEVGIGHVRYPTAGSS 80
Cdd:COG0449 1 MCGIVGYIGKRDAAPILLEGLKRLEYRGYDSAGIAVLDDGGLEVRKAVGKLANLEEKLAEEPLSGTIGIGHTRWATHGAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 81 SASEAQPFYVNSPfGITLAHNGNLTNANEVREKLFEKDRRHVNTTsDSEVLLNVLAHEIDtvkgnvTSDDVFRAVANVHR 160
Cdd:COG0449 81 SDENAHPHTSCSG-RIAVVHNGIIENYAELREELEAKGHTFKSET-DTEVIAHLIEEYLK------GGGDLLEAVRKALK 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 515634076 161 TIRGAYAVTAMIIGH--GMIAFRdpHGiRPLCLGKrevqGKTEYMVASESVAL 211
Cdd:COG0449 153 RLEGAYALAVISADEpdRIVAAR--KG-SPLVIGL----GEGENFLASDVPAL 198
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
2-214 |
2.64e-21 |
|
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: 93.10 E-value: 2.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 2 CGIVGIV---GSTPVNQSIYDALTVLQHRGQD------AAGICTIE----SNRFRLRKANGLVKDVFEAKHMQRLQGEVG 68
Cdd:cd01907 1 CGIFGIMskdGEPFVGALLVEMLDAMQERGPGdgagfaLYGDPDAFvyssGKDMEVFKGVGYPEDIARRYDLEEYKGYHW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 69 IGHVRYPTAGSSSASEAQPFyvnSPFGITLAHNGNLTNANEVREKLfEKDRRHVNTTSDSEVLLNVLAheiDTVKGNVTS 148
Cdd:cd01907 81 IAHTRQPTNSAVWWYGAHPF---SIGDIAVVHNGEISNYGSNREYL-ERFGYKFETETDTEVIAYYLD---LLLRKGGLP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 149 DDVFRAVANVHRTIRGAYAVTAMIIGH---------------GMIAFRDPHGIRPLCLGKREvqgkTEYMVASESVALDA 213
Cdd:cd01907 154 LEYYKHIIRMPEEERELLLALRLTYRLadldgpftiivgtpdGFIVIRDRIKLRPAVVAETD----DYVAIASEECAIRE 229
|
.
gi 515634076 214 V 214
Cdd:cd01907 230 I 230
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-211 |
4.50e-20 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 93.55 E-value: 4.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 1 MCGIVGIVGSTPVNQSIYDALTVLQHRGQDAAGICTIESN------RFRLRKANG----LVKDVFEAKHmqrLQGEVGIG 70
Cdd:PTZ00295 24 CCGIVGYLGNEDASKILLEGIEILQNRGYDSCGISTISSGgelkttKYASDGTTSdsieILKEKLLDSH---KNSTIGIA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 71 HVRYPTAGSSSASEAQPfYVNSPFGITLAHNGNLTNANEVREKLFEKDRRHVNTTsDSEVLLNVLAHEIDtvkgnvTSDD 150
Cdd:PTZ00295 101 HTRWATHGGKTDENAHP-HCDYKKRIALVHNGTIENYVELKSELIAKGIKFRSET-DSEVIANLIGLELD------QGED 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515634076 151 VFRAVANVHRTIRGAYAVTAMIIGH--GMIAFRdpHGiRPLCLGKrevqGKTEYMVASESVAL 211
Cdd:PTZ00295 173 FQEAVKSAISRLQGTWGLCIIHKDNpdSLIVAR--NG-SPLLVGI----GDDSIYVASEPSAF 228
|
|
| PRTases_typeI |
cd06223 |
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ... |
276-395 |
7.50e-17 |
|
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: 77.05 E-value: 7.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 276 MGEMLGKRIKEEYadLDIDVVIPIPETSNDIALRIAQAINKPYRQGFVKNRYVGRTFIMPGQqqrkksvrrKLNAIRSEF 355
Cdd:cd06223 1 AGRLLAEEIREDL--LEPDVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSEPYG---------LELPLGGDV 69
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 515634076 356 KGKNVLLVDDSIVRGTTSEQIIEMARDSGANKVFMVSAAP 395
Cdd:cd06223 70 KGKRVLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVLLD 109
|
|
| YafJ |
COG0121 |
Predicted glutamine amidotransferase YafJ [General function prediction only]; |
2-236 |
1.66e-14 |
|
Predicted glutamine amidotransferase YafJ [General function prediction only];
Pssm-ID: 439891 [Multi-domain] Cd Length: 248 Bit Score: 73.08 E-value: 1.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 2 CGIVGIVGSTPV--NQSIYDALTVLQHRGQ--------DAAGICTIESNR--FRLRKANGLVKDVFEAKHMQRLQGEVGI 69
Cdd:COG0121 1 CRLLGYSGNVPTdlEFLLLDPEHSLVRQSGatregphaDGWGIGWYEGDGepRLYRDPLPAWSDPNLRLLARPIKSRLVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 70 GHVRYPTAGSSSASEAQPFYVnspFGITLAHNGNLTNANEVREKLFEK----DRRHVNTTSDSEVLLNVLAHEIDTVKGN 145
Cdd:COG0121 81 AHVRKATVGPVSLENTHPFRG---GRWLFAHNGQLDGFDRLRRRLAEElpdeLYFQPVGTTDSELAFALLLSRLRDGGPD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 146 VTsDDVFRAVANVHRTIRGAYAVTAMII-GHGMIAFRDPHGIRP--LCLGKREVQGKTEYMVASESVALDAVgfdfMRDV 222
Cdd:COG0121 158 PA-EALAEALRELAELARAPGRLNLLLSdGERLYATRYTSDDPYptLYYLTRTTPDDRVVVVASEPLTDDEG----WTEV 232
|
250
....*....|....
gi 515634076 223 APGEAIYATFDGEL 236
Cdd:COG0121 233 PPGELLVVRDGLEV 246
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
65-207 |
5.19e-13 |
|
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: 65.79 E-value: 5.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 65 GEVGIGHVRYPTAGSSSASeAQPFYVNSPfGITLAHNGNLTNANEVREKLfEKDRRHVNTTSDSEVLLNVLAHeidtvkg 144
Cdd:pfam13522 10 GGVALGHVRLAIVDLPDAG-NQPMLSRDG-RLVLVHNGEIYNYGELREEL-ADLGHAFRSRSDTEVLLALYEE------- 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515634076 145 nvTSDDVFRAvanvhrtIRGAYAVTAM--IIGHGMIAfRDPHGIRPLCLGkreVQGKTeYMVASE 207
Cdd:pfam13522 80 --WGEDCLER-------LRGMFAFAIWdrRRRTLFLA-RDRLGIKPLYYG---ILGGG-FVFASE 130
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-232 |
8.73e-12 |
|
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: 64.50 E-value: 8.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 2 CGIVGIV---GSTPVNQSIYDALTVLQHRGQDAAGIctiesnrfrlrkanglvkdvfeakhmqRLQGEVGIGHVRY---- 74
Cdd:cd00712 1 CGIAGIIgldGASVDRATLERMLDALAHRGPDGSGI---------------------------WIDEGVALGHRRLsiid 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 75 PTAGsssaseAQPFYVNSPfGITLAHNGNLTNANEVREKLfEKDRRHVNTTSDSEVLLNVLAHeidtvkgnvtsddvfra 154
Cdd:cd00712 54 LSGG------AQPMVSEDG-RLVLVFNGEIYNYRELRAEL-EALGHRFRTHSDTEVILHLYEE----------------- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 155 vanvhrtiRGAYAVTAMiigHGMIAF-------------RDPHGIRPLCLGkrevQGKTEYMVASESVALDAVGFDFMRD 221
Cdd:cd00712 109 --------WGEDCLERL---NGMFAFalwdkrkrrlflaRDRFGIKPLYYG----RDGGGLAFASELKALLALPGVPREL 173
|
250
....*....|.
gi 515634076 222 VAPGEAIYATF 232
Cdd:cd00712 174 DEAALAEYLAF 184
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
81-213 |
9.96e-12 |
|
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: 62.15 E-value: 9.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 81 SASEAQPFyVNSPFG-ITLAHNGNLTNANEVREKLFEKDRRHvNTTSDSEVLLNVLAHE--IDTVKgnvtsddvfravan 157
Cdd:pfam13537 9 LEGGAQPM-VSSEDGrYVIVFNGEIYNYRELRAELEAKGYRF-RTHSDTEVILHLYEAEwgEDCVD-------------- 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 158 vHrtIRGAYAVtamII----GHGMIAFRDPHGIRPLCLGKREvqGKTeYMVASESVALDA 213
Cdd:pfam13537 73 -R--LNGMFAF---AIwdrrRQRLFLARDRFGIKPLYYGRDD--GGR-LLFASELKALLA 123
|
|
| YafJ |
cd01908 |
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ... |
1-207 |
5.14e-11 |
|
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: 63.18 E-value: 5.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 1 MCGIVGIVGSTPVN-------------QSIY-DALTVLQHRgqDAAGICTIESNR---FRLRKANGLVKDVFEAKHMQRL 63
Cdd:cd01908 1 MCRLLGYSGAPIPLepllirpshsllvQSGGpREMKGTVHA--DGWGIGWYEGKGgrpFRYRSPLPAWSDINLESLARPI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 64 QGEVGIGHVRYPTAGSSSASEAQPFYVNSpfgITLAHNGNLTNANEVREKLFEKDRRHVNTTSDSEVLLNVLAHEIDTVK 143
Cdd:cd01908 79 KSPLVLAHVRAATVGPVSLENCHPFTRGR---WLFAHNGQLDGFRLLRRRLLRLLPRLPVGTTDSELAFALLLSRLLERD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 144 GNvTSDDVFRAVANVHRTIRGAYAVTA--MII--GHGMIAFRDPH-----------GIRPLCLGKREVQGKTE--YMVAS 206
Cdd:cd01908 156 PL-DPAELLDAILQTLRELAALAPPGRlnLLLsdGEYLIATRYASapslyyltrraPFGCARLLFRSVTTPNDdgVVVAS 234
|
.
gi 515634076 207 E 207
Cdd:cd01908 235 E 235
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-253 |
2.51e-10 |
|
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: 62.55 E-value: 2.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 1 MCGIVGIVG-STPVNQSIYDALT-VLQHRGQDAAGIctiesnrfrlrkanglvkdvfeakhmqRLQGEVGIGHVRyptag 78
Cdd:COG0367 1 MCGIAGIIDfDGGADREVLERMLdALAHRGPDGSGI---------------------------WVDGGVALGHRR----- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 79 SS----SASEAQPFyVNSPFGITLAHNGNLTNANEVREKLFEKDRRHvNTTSDSEVLLNVLAHeidtvKGnvtsddvfra 154
Cdd:COG0367 49 LSiidlSEGGHQPM-VSEDGRYVLVFNGEIYNYRELRAELEALGHRF-RTHSDTEVILHAYEE-----WG---------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 155 VANVHRtIRGAYAVtamIIGHG----MIAFRDPHGIRPLCLGkrevQGKTEYMVASESVALDAVGfDFMRDVAPgEAIYa 230
Cdd:COG0367 112 EDCLER-LNGMFAF---AIWDRrerrLFLARDRFGIKPLYYA----EDGGGLAFASELKALLAHP-GVDRELDP-EALA- 180
|
250 260
....*....|....*....|...
gi 515634076 231 tfdgELFTKQCADNPQlnpCIFE 253
Cdd:COG0367 181 ----EYLTLGYVPAPR---TIFK 196
|
|
| ComFC |
COG1040 |
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General ... |
270-394 |
2.02e-07 |
|
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General function prediction only];
Pssm-ID: 440662 [Multi-domain] Cd Length: 196 Bit Score: 51.36 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 270 YSARVEMGEMLGKRIKEEYADL---DIDVVIPIP-----------ETSNDIALRIAQAINKPYR-QGFVKNRYVgrtfim 334
Cdd:COG1040 53 YRGRLDLARLLARLLARALREAllpRPDLIVPVPlhrrrlrrrgfNQAELLARALARALGIPVLpDLLRRVRAT------ 126
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515634076 335 PGQQQRKKSVRRKL--NAIR----SEFKGKNVLLVDDsiVR--GTTSEQIIEMARDSGANKVFMVSAA 394
Cdd:COG1040 127 PSQAGLSRAERRRNlrGAFAvrppARLAGKHVLLVDD--VLttGATLAEAARALKAAGAARVDVLVLA 192
|
|
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
1-217 |
3.03e-07 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 53.22 E-value: 3.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 1 MCGIVGIVGSTpVNQS-------IYDALTVLQHRGQDAAGIcTIESNR---------FRLR-KANGLVKDVFEAKHMQRL 63
Cdd:PLN02981 1 MCGIFAYLNYN-VPRErrfilevLFNGLRRLEYRGYDSAGI-AIDNDPslesssplvFREEgKIESLVRSVYEEVAETDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 64 QGE------VGIGHVRYPTAGSSSA--SEAQPFYVNSPFgiTLAHNGNLTNANEVREKLFekdrRH---VNTTSDSEVLL 132
Cdd:PLN02981 79 NLDlvfenhAGIAHTRWATHGPPAPrnSHPQSSGPGNEF--LVVHNGIITNYEVLKETLL----RHgftFESDTDTEVIP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 133 NVLAHEIDTVkGNVTSDDVFRA-VANVHRTIRGAYAVtamiighgmiAFRDPH----------GiRPLCLGKREVQGKTE 201
Cdd:PLN02981 153 KLAKFVFDKL-NEEEGDVTFSQvVMEVMRQLEGAYAL----------IFKSPHypnelvackrG-SPLLLGVKELPEEKN 220
|
250
....*....|....*.
gi 515634076 202 YMVASESVALDAVGFD 217
Cdd:PLN02981 221 SSAVFTSEGFLTKNRD 236
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-194 |
1.01e-06 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 51.42 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 1 MCGIVGIVGSTpVNQSIYDALTVL-------QHRGQDAAGICtIESNrFRLRKANGLVKDVFEAKHM------------- 60
Cdd:PTZ00394 1 MCGIFGYANHN-VPRTVEQILNVLldgiqkvEYRGYDSAGLA-IDAN-IGSEKEDGTAASAPTPRPCvvrsvgnisqlre 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 61 ---------------QRLQGEVGIGHVRYPTAGSSSASEAQPFYVNSpFGITLAHNGNLTNANEVREKLFEKDrRHVNTT 125
Cdd:PTZ00394 78 kvfseavaatlppmdATTSHHVGIAHTRWATHGGVCERNCHPQQSNN-GEFTIVHNGIVTNYMTLKELLKEEG-YHFSSD 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515634076 126 SDSEVlLNVLAHEIDTVKGNVTSDDVfraVANVHRTIRGAYA--VTAMIIGHGMIAFRDPhgiRPLCLGKR 194
Cdd:PTZ00394 156 TDTEV-ISVLSEYLYTRKGIHNFADL---ALEVSRMVEGSYAllVKSVYFPGQLAASRKG---SPLMVGIR 219
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
1-192 |
1.06e-06 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 51.25 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 1 MCGIVGIVGST----PVNQSIYDALTVLQHRGQDAAGICTIEsnrfrlrkaNGLVKDVFeakhmqrlqgevgIGHVRYPT 76
Cdd:PTZ00077 1 MCGILAIFNSKgerhELRRKALELSKRLRHRGPDWSGIIVLE---------NSPGTYNI-------------LAHERLAI 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 77 AGSSSAseAQPFYVNSPfGITLAHNGNLTNANEVREKLfEKDRRHVNTTSDSEVLLNV--------LAHEIDTVKGNVTS 148
Cdd:PTZ00077 59 VDLSDG--KQPLLDDDE-TVALMQNGEIYNHWEIRPEL-EKEGYKFSSNSDCEIIGHLykeygpkdFWNHLDGMFATVIY 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 515634076 149 DdvfrAVANVhrtirgayavtamiighgMIAFRDPHGIRPLCLG 192
Cdd:PTZ00077 135 D----MKTNT------------------FFAARDHIGIIPLYIG 156
|
|
| PRK00934 |
PRK00934 |
ribose-phosphate pyrophosphokinase; Provisional |
356-389 |
2.86e-03 |
|
ribose-phosphate pyrophosphokinase; Provisional
Pssm-ID: 234868 [Multi-domain] Cd Length: 285 Bit Score: 39.51 E-value: 2.86e-03
10 20 30
....*....|....*....|....*....|....
gi 515634076 356 KGKNVLLVDDSIVRGTTSEQIIEMARDSGANKVF 389
Cdd:PRK00934 203 KGKDVLIVDDIISTGGTMATAIKILKEQGAKKVY 236
|
|
| Hpt1 |
COG2236 |
Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine ... |
336-388 |
3.72e-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: 37.90 E-value: 3.72e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 515634076 336 GQQQRKKSVRRKLNairSEFKGKNVLLVDDSIVRGTTSEQIIEMARDSGANKV 388
Cdd:COG2236 70 AKRLEEPVVKGPLD---EDLAGKRVLIVDDVADTGRTLEAVRDLLKEAGPAEV 119
|
|
| PyrE |
COG0461 |
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ... |
263-393 |
4.77e-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: 38.21 E-value: 4.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 263 FIDK---ISVYSARVEMGEMLGKRIKEEYadLDIDVV-------IPIpetsndiALRIAQAINKPYRqgfvknrYVGRTf 332
Cdd:COG0461 33 YIDCrlvLSYPEALELLGEALAELIKELG--PEFDAVagpatggIPL-------AAAVARALGLPAI-------FVRKE- 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515634076 333 imPGQQQRKKSVRRKLNairsefKGKNVLLVDDSIVRGTTSEQIIEMARDSGANKVFMVSA 393
Cdd:COG0461 96 --AKDHGTGGQIEGGLL------PGERVLVVEDVITTGGSVLEAVEALREAGAEVVGVAVI 148
|
|
| PRK08558 |
PRK08558 |
adenine phosphoribosyltransferase; Provisional |
261-393 |
5.62e-03 |
|
adenine phosphoribosyltransferase; Provisional
Pssm-ID: 181466 [Multi-domain] Cd Length: 238 Bit Score: 38.43 E-value: 5.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634076 261 DSFIDKISVYSARVEMgEMLGKRIKEEYADLDIDVVIPIPETSNDIALRIAQ------AINKPYRQGFVKNRYVGRTFIM 334
Cdd:PRK08558 81 EGYVDNSSVVFDPSFL-RLIAPVVAERFMGLRVDVVLTAATDGIPLAVAIASyfgadlVYAKKSKETGVEKFYEEYQRLA 159
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515634076 335 PGqqqrkksvrRKLN------AIRsefKGKNVLLVDDSIVRGTTSEQIIEMARDSGANKV---FMVSA 393
Cdd:PRK08558 160 SG---------IEVTlylpasALK---KGDRVLIVDDIIRSGETQRALLDLARQAGADVVgvfFLIAV 215
|
|
| |
