|
Name |
Accession |
Description |
Interval |
E-value |
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
1-483 |
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: 771.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 1 MCGIVGIAGVMPVNQSIYDALTVLQHRGQDAAGIITIDaNNCFRLRKANGLVNDVFEARHMQRLQGNMGIGHVRYPTAGS 80
Cdd:COG0034 7 ECGVFGIYGHEDVAQLTYYGLYALQHRGQESAGIATSD-GGRFHLHKGMGLVSDVFDEEDLERLKGNIAIGHVRYSTTGS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 81 SSASEAQPFYVNSPYG-ITLAHNGNLTNAHELRKMLFEEKRrHINTTSDSEILLNIFASELdnfrhyplEADNIFAAIAA 159
Cdd:COG0034 86 SSLENAQPFYVNSPFGsIALAHNGNLTNAEELREELEEEGA-IFQTTSDTEVILHLIAREL--------TKEDLEEAIKE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 160 MNRLIRGAYACVAMIiGHGMVAFRDPNGIRPLVLGKRDAGngraeYMVASESVALDTLGFEFLRDVAPGEAVYISEKGqL 239
Cdd:COG0034 157 ALRRVKGAYSLVILT-GDGLIAARDPNGIRPLVLGKLEDG-----YVVASESCALDILGAEFVRDVEPGEIVVIDEDG-L 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 240 FTRQCADNPVSNPCLFEYVYFARPDSFIDKISVYSARVEMGKKLgekiAREwEDLDIDVVIPIPETSCDIALEIARILNK 319
Cdd:COG0034 230 RSRQFAEKPRPAPCIFEYVYFARPDSVIDGRSVYEARKRMGREL----ARE-APVDADVVIPVPDSGRPAAIGYAEESGI 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 320 PYRQGFVKNRYVGRTFIMPGQHLRRKSVRRKLNANRAEFRDKNVLLVDDSIVRGTTSEQIIEMAREAGAKKVYLASAAPE 399
Cdd:COG0034 305 PYEEGLIKNRYVGRTFIQPTQELRELGVRLKLNPIREVVKGKRVVLVDDSIVRGTTSRRIVKMLREAGAKEVHFRIASPP 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 400 IRFPNVYGIDMPSANELIAHGREVDEIRQIIGADGLIFQDLDDLIEAVRAenpDIQQFECSVFNGVYVTkDVDHQYLEYL 479
Cdd:COG0034 385 IRYPCYYGIDTPTREELIAANRSVEEIREYIGADSLGYLSLEGLIEAVGE---PIEGFCTACFTGDYPT-GIPDEEKKRL 460
|
....
gi 1758370708 480 ESLR 483
Cdd:COG0034 461 ELLR 464
|
|
| 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: 696.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 2 CGIVGIAGVMPVNQS-IYDALTVLQHRGQDAAGIITIDaNNCFRLRKANGLVNDVFEARHMQRLQGNMGIGHVRYPTAGS 80
Cdd:TIGR01134 1 CGVVGIYGQEEVAASlTYYGLYALQHRGQESAGISVFD-GNRFRLHKGNGLVSDVFNEEHLQRLKGNVGIGHVRYSTAGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 81 SSASEAQPFYVNSPYG-ITLAHNGNLTNAHELRKMLfEEKRRHINTTSDSEILLNIFAseldnfrHYPLEADNIFAAIAA 159
Cdd:TIGR01134 80 SGLENAQPFVVNSPYGgLALAHNGNLVNADELRREL-EEEGRHFNTTSDSEVLLHLLA-------HNDESKDDLFDAVAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 160 MNRLIRGAYACVAMIiGHGMVAFRDPNGIRPLVLGKRDAGngraeYMVASESVALDTLGFEFLRDVAPGEAVYISEkGQL 239
Cdd:TIGR01134 152 VLERVRGAYALVLMT-EDGLVAVRDPHGIRPLVLGRRGDG-----YVVASESCALDILGAEFVRDVEPGEVVVIFD-GGL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 240 FTRQCADNPVsNPCLFEYVYFARPDSFIDKISVYSARVEMGKKLGEKiarewEDLDIDVVIPIPETSCDIALEIARILNK 319
Cdd:TIGR01134 225 ESRQCARRPR-APCVFEYVYFARPDSVIDGISVYYARKRMGKELARE-----SPVEADVVVPVPDSGRSAALGFAQASGI 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 320 PYRQGFVKNRYVGRTFIMPGQHLRRKSVRRKLNANRAEFRDKNVLLVDDSIVRGTTSEQIIEMAREAGAKKVYLASAAPE 399
Cdd:TIGR01134 299 PYREGLIKNRYVGRTFIMPTQELRELSVRLKLNPVRAVFEGKRVVLVDDSIVRGTTSRQIVEMLRDAGAKEVHVRIASPP 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1758370708 400 IRFPNVYGIDMPSANELIAHGREVDEIRQiIGADGLIFQDLDDLIEAVRAenpDIQQFECSVFNGVYV 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: 620.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 1 MCGIVGIAGVMPVNQSIYDALTVLQHRGQDAAGIITIDANNcFRLRKANGLVNDVFEARHMQRLQGNMGIGHVRYPTAGS 80
Cdd:PLN02440 1 ECGVVGIFGDPEASRLCYLGLHALQHRGQEGAGIVTVDGNR-LQSITGNGLVSDVFDESKLDQLPGDIAIGHVRYSTAGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 81 SSASEAQPFYVNSPYG-ITLAHNGNLTNAHELRKMLfEEKRRHINTTSDSEILLNIFASELdnfrhypleADNIFAAIAA 159
Cdd:PLN02440 80 SSLKNVQPFVANYRFGsIGVAHNGNLVNYEELRAKL-EENGSIFNTSSDTEVLLHLIAISK---------ARPFFSRIVD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 160 MNRLIRGAYACVAMIIGHgMVAFRDPNGIRPLVLGKRDAGngraEYMVASESVALDTLGFEFLRDVAPGEAVYIsEKGQL 239
Cdd:PLN02440 150 ACEKLKGAYSMVFLTEDK-LVAVRDPHGFRPLVMGRRSNG----AVVFASETCALDLIGATYEREVNPGEVIVV-DKDKG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 240 FTRQCA-DNPVSNPCLFEYVYFARPDSFIDKISVYSARVEMGKKLGEKIARewedlDIDVVIPIPETSCDIALEIARILN 318
Cdd:PLN02440 224 VSSQCLmPHPEPKPCIFEHIYFARPNSIVFGRSVYESRLEFGEILATEIPV-----DCDVVIPVPDSGRVAALGYAAKLG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 319 KPYRQGFVKNRYVGRTFIMPGQHLRRKSVRRKLNANRAEFRDKNVLLVDDSIVRGTTSEQIIEMAREAGAKKVYLASAAP 398
Cdd:PLN02440 299 VPFQQGLIRSHYVGRTFIEPSQKIRDFSVKLKLNPVRSVLEGKRVVVVDDSIVRGTTSSKIVRMLREAGAKEVHMRIASP 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 399 EIRFPNVYGIDMPSANELIAHGREVDEIRQIIGADGLIFQDLDDLIEAVRAENPdiqQFECSVFNGVY------VTKDVD 472
Cdd:PLN02440 379 PIIASCYYGVDTPSREELISNRMSVEEIRKFIGCDSLAFLPLEDLKKSLGEESP---RFCYACFSGDYpvlpkrVGGDID 455
|
490 500
....*....|....*....|...
gi 1758370708 473 HQYLEYLESLRNDDAKAVMRQNE 495
Cdd:PLN02440 456 DGYLESLEEAGRGWGRKGRRQEA 478
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
2-477 |
5.61e-151 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 439.47 E-value: 5.61e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 2 CGIVGIAGVMPVNQS--IYDALTVLQHRGQDAAGIITIDANNcFRLRKANGLVNDVFEARHMQRLQGNMGIGHVRYPTAG 79
Cdd:PRK05793 15 CGVFGVFSKNNIDVAslTYYGLYALQHRGQESAGIAVSDGEK-IKVHKGMGLVSEVFSKEKLKGLKGNSAIGHVRYSTTG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 80 SSSASEAQPFYVNSPYG-ITLAHNGNLTNAHELRKMLfEEKRRHINTTSDSEILLNIFASELdnfrHYPLEAdnifAAIA 158
Cdd:PRK05793 94 ASDLDNAQPLVANYKLGsIAIAHNGNLVNADVIRELL-EDGGRIFQTSIDSEVILNLIARSA----KKGLEK----ALVD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 159 AMNRlIRGAYACVAM----IIGhgmvaFRDPNGIRPLVLGKRDAGngraeYMVASESVALDTLGFEFLRDVAPGEAVYIS 234
Cdd:PRK05793 165 AIQA-IKGSYALVILtedkLIG-----VRDPHGIRPLCLGKLGDD-----YILSSESCALDTIGAEFIRDVEPGEIVIID 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 235 EKGqLFTRQCADNPVSNPCLFEYVYFARPDSFIDKISVYSARVEMGKKLgekiAREWEdLDIDVVIPIPETSCDIALEIA 314
Cdd:PRK05793 234 EDG-IKSIKFAEKTKCQTCAFEYIYFARPDSVIDGISVYESRVRAGRQL----YKEYP-VDADIVIGVPDSGIPAAIGYA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 315 RILNKPYRQGFVKNRYVGRTFIMPGQHLRRKSVRRKLNANRAEFRDKNVLLVDDSIVRGTTSEQIIEMAREAGAKKVYLA 394
Cdd:PRK05793 308 EASGIPYGIGFIKNKYVGRTFIAPSQELRERAVRVKLNPLKVNVEGKRVVLIDDSIVRGTTSKRLVELLRKAGAKEVHFR 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 395 SAAPEIRFPNVYGIDMPSANELIAHGREVDEIRQIIGADGLIFQDLDDLIEAVRAENpdiqQFECSVFNGVY---VTKDV 471
Cdd:PRK05793 388 VSSPPVKYPCYFGIDTPYRKELIGANMSVEEIREMIGADSLGYLSIEGLLESLNGDK----GFCLGCFNGVYpvsAPKEG 463
|
....*.
gi 1758370708 472 DHQYLE 477
Cdd:PRK05793 464 PKYLLE 469
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
2-268 |
2.31e-142 |
|
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: 409.16 E-value: 2.31e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 2 CGIVGIAGVMPVNQSIYDALTVLQHRGQDAAGIITIDaNNCFRLRKANGLVNDVFEARHMQRLQGNMGIGHVRYPTAGSS 81
Cdd:cd00715 1 CGVFGIYGAEDAARLTYLGLYALQHRGQESAGIATSD-GKRFHTHKGMGLVSDVFDEEKLRRLPGNIAIGHVRYSTAGSS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 82 SASEAQPFYVNSP-YGITLAHNGNLTNAHELRKMLFEEKrRHINTTSDSEILLNIFASELDNfrhypleaDNIFAAIAAM 160
Cdd:cd00715 80 SLENAQPFVVNSPlGGIALAHNGNLVNAKELREELEEEG-RIFQTTSDSEVILHLIARSLAK--------DDLFEAIIDA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 161 NRLIRGAYACVAMIIgHGMVAFRDPNGIRPLVLGKRDAGngraEYMVASESVALDTLGFEFLRDVAPGEAVYISEKGqLF 240
Cdd:cd00715 151 LERVKGAYSLVIMTA-DGLIAVRDPHGIRPLVLGKLEGD----GYVVASESCALDIIGAEFVRDVEPGEIVVIDDDG-LE 224
|
250 260
....*....|....*....|....*...
gi 1758370708 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 |
1.33e-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: 190.74 E-value: 1.33e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 2 CGIVGIAGVMPVNQSIYDA----LTVLQHRGQDAAGIITIDANNCFRLRKAnGLVNDVFEARHMQRLQGNMGIGHVRYPT 77
Cdd:cd00352 1 CGIFGIVGADGAASLLLLLllrgLAALEHRGPDGAGIAVYDGDGLFVEKRA-GPVSDVALDLLDEPLKSGVALGHVRLAT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 78 AGSSSASEAQPFYVNSpYGITLAHNGNLTNAHELRKMLfEEKRRHINTTSDSEILLNIFASELDNFRhypleadnIFAAI 157
Cdd:cd00352 80 NGLPSEANAQPFRSED-GRIALVHNGEIYNYRELREEL-EARGYRFEGESDSEVILHLLERLGREGG--------LFEAV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1758370708 158 AAMNRLIRGAYACVAMIIG-HGMVAFRDPNGIRPLVLGKRDAGngraEYMVASESVALDTLGFEFLRDVAPGEAV 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 ... |
2-214 |
1.94e-23 |
|
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: 98.29 E-value: 1.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 2 CGIVGIAGVMPVNQSIYDALTVLQHRGQDAAGiITIDANNCFRLRKANGLVNDVFEARHMQRLQGNMGIGHVRYPTAGSS 81
Cdd:cd00714 1 CGIVGYIGKREAVDILLEGLKRLEYRGYDSAG-IAVIGDGSLEVVKAVGKVANLEEKLAEKPLSGHVGIGHTRWATHGEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 82 SASEAQPfYVNSPYGITLAHNGNLTNAHELRKMLfeEKRRHI-NTTSDSEILLNIFASELDnfrhyplEADNIFAAI-AA 159
Cdd:cd00714 80 TDVNAHP-HRSCDGEIAVVHNGIIENYAELKEEL--EAKGYKfESETDTEVIAHLIEYYYD-------GGLDLLEAVkKA 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1758370708 160 MNRLiRGAYACVAMIIGHG--MVAFRdpNGiRPLVLGKrdagnGRAEYMVASESVAL 214
Cdd:cd00714 150 LKRL-EGAYALAVISKDEPdeIVAAR--NG-SPLVIGI-----GDGENFVASDAPAL 197
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
2-215 |
5.88e-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: 95.03 E-value: 5.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 2 CGIVGIA---GVMPVNQSIYDALTVLQHRG-QDAAGIITIDANNCFRLR--------KANGLVNDVFEARHMQRLQGNMG 69
Cdd:cd01907 1 CGIFGIMskdGEPFVGALLVEMLDAMQERGpGDGAGFALYGDPDAFVYSsgkdmevfKGVGYPEDIARRYDLEEYKGYHW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 70 IGHVRYPTAGSSSASEAQPFyvnSPYGITLAHNGNLTNAHELRKMLfEEKRRHINTTSDSEILLNIFA---SELDNFRHY 146
Cdd:cd01907 81 IAHTRQPTNSAVWWYGAHPF---SIGDIAVVHNGEISNYGSNREYL-ERFGYKFETETDTEVIAYYLDlllRKGGLPLEY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 147 -------PLEADNIFAAIAAMNRLIR--GAYAcvaMIIGH--GMVAFRDPNGIRPLVLGKRDagngrAEYMVASESVALD 215
Cdd:cd01907 157 ykhiirmPEEERELLLALRLTYRLADldGPFT---IIVGTpdGFIVIRDRIKLRPAVVAETD-----DYVAIASEECAIR 228
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
1-237 |
1.34e-20 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 95.11 E-value: 1.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 1 MCGIVGIAGVMPVNQSIYDALTVLQHRGQDAAGIITIDaNNCFRLRKANGLVNDVFEARHMQRLQGNMGIGHVRYPTAGS 80
Cdd:PRK00331 1 MCGIVGYVGQRNAAEILLEGLKRLEYRGYDSAGIAVLD-DGGLEVRKAVGKVANLEAKLEEEPLPGTTGIGHTRWATHGK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 81 SSASEAQPFYVNSPYgITLAHNGNLTNAHELRKMLfEEKRRHINTTSDSEILLNIFASELDnfrhyplEADNIFAAIAAM 160
Cdd:PRK00331 80 PTERNAHPHTDCSGR-IAVVHNGIIENYAELKEEL-LAKGHVFKSETDTEVIAHLIEEELK-------EGGDLLEAVRKA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 161 NRLIRGAYACVAMIIGH--GMVAFRdpNGiRPLVLGKrdaGNGraEYMVASesvalDTLGF-EFLRDVAP---GEAVYIS 234
Cdd:PRK00331 151 LKRLEGAYALAVIDKDEpdTIVAAR--NG-SPLVIGL---GEG--ENFLAS-----DALALlPYTRRVIYledGEIAVLT 217
|
...
gi 1758370708 235 EKG 237
Cdd:PRK00331 218 RDG 220
|
|
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
1-237 |
2.08e-19 |
|
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: 91.23 E-value: 2.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 1 MCGIVGIAGVMPVNQSIYDALTVLQHRGQDAAGIITIDANNcFRLRKANGLVNDVFEARHMQRLQGNMGIGHVRYPTAGS 80
Cdd:COG0449 1 MCGIVGYIGKRDAAPILLEGLKRLEYRGYDSAGIAVLDDGG-LEVRKAVGKLANLEEKLAEEPLSGTIGIGHTRWATHGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 81 SSASEAQPFYVNSPyGITLAHNGNLTNAHELRKMLfEEKRRHINTTSDSEILLNIFASELDnfrhyplEADNIFAAIAAM 160
Cdd:COG0449 80 PSDENAHPHTSCSG-RIAVVHNGIIENYAELREEL-EAKGHTFKSETDTEVIAHLIEEYLK-------GGGDLLEAVRKA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 161 NRLIRGAYACVAMIIGH--GMVAFRdpNGiRPLVLGKrdaGNGraEYMVASESVALdtlgFEFLRDVAP---GEAVYISE 235
Cdd:COG0449 151 LKRLEGAYALAVISADEpdRIVAAR--KG-SPLVIGL---GEG--ENFLASDVPAL----LPYTRRVIYledGEIAVLTR 218
|
..
gi 1758370708 236 KG 237
Cdd:COG0449 219 DG 220
|
|
| PRTases_typeI |
cd06223 |
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ... |
279-398 |
2.29e-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: 81.29 E-value: 2.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 279 MGKKLGEKIAREWedLDIDVVIPIPETSCDIALEIARILNKPYRQGFVKNRYVGRTFIMPGQhlrrksvrrKLNANRAEF 358
Cdd:cd06223 1 AGRLLAEEIREDL--LEPDVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSEPYG---------LELPLGGDV 69
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1758370708 359 RDKNVLLVDDSIVRGTTSEQIIEMAREAGAKKVYLASAAP 398
Cdd:cd06223 70 KGKRVLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVLLD 109
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-214 |
1.01e-17 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 86.23 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 1 MCGIVGIAGVMPVNQSIYDALTVLQHRGQDAAGIITIDANNCFRLRK-------ANGLV--NDVFEARHmqrLQGNMGIG 71
Cdd:PTZ00295 24 CCGIVGYLGNEDASKILLEGIEILQNRGYDSCGISTISSGGELKTTKyasdgttSDSIEilKEKLLDSH---KNSTIGIA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 72 HVRYPTAGSSSASEAQPfYVNSPYGITLAHNGNLTNAHELRKMLFEEKRRHINTTsDSEILLNIFASELDNfrhypleAD 151
Cdd:PTZ00295 101 HTRWATHGGKTDENAHP-HCDYKKRIALVHNGTIENYVELKSELIAKGIKFRSET-DSEVIANLIGLELDQ-------GE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1758370708 152 NIFAAI-AAMNRLiRGAYACVAMIIGH--GMVAFRdpNGiRPLVLGKRDAGngraeYMVASESVAL 214
Cdd:PTZ00295 172 DFQEAVkSAISRL-QGTWGLCIIHKDNpdSLIVAR--NG-SPLLVGIGDDS-----IYVASEPSAF 228
|
|
| YafJ |
COG0121 |
Predicted glutamine amidotransferase YafJ [General function prediction only]; |
62-231 |
3.30e-13 |
|
Predicted glutamine amidotransferase YafJ [General function prediction only];
Pssm-ID: 439891 [Multi-domain] Cd Length: 248 Bit Score: 69.22 E-value: 3.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 62 QRLQGNMGIGHVRYPTAGSSSASEAQPFYVnspYGITLAHNGNLTN----AHELRKMLFEEKRRHINTTSDSEILLNIFA 137
Cdd:COG0121 72 RPIKSRLVIAHVRKATVGPVSLENTHPFRG---GRWLFAHNGQLDGfdrlRRRLAEELPDELYFQPVGTTDSELAFALLL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 138 SELDNFRHYPLEAdnIFAAIAAMNRLIRGAYAC-VAMIIGHGMVAFRDPNGIRP--LVLGKRDAGNGRAeYMVASESVAL 214
Cdd:COG0121 149 SRLRDGGPDPAEA--LAEALRELAELARAPGRLnLLLSDGERLYATRYTSDDPYptLYYLTRTTPDDRV-VVVASEPLTD 225
|
170
....*....|....*..
gi 1758370708 215 DtlgfEFLRDVAPGEAV 231
Cdd:COG0121 226 D----EGWTEVPPGELL 238
|
|
| YafJ |
cd01908 |
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ... |
70-235 |
6.79e-12 |
|
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: 65.49 E-value: 6.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 70 IGHVRYPTAGSSSASEAQPFYVNSpygITLAHNGNLTNAHELRKMLFEEKRRHINTTSDSEILLNIFASELDNfrHYPLE 149
Cdd:cd01908 84 LAHVRAATVGPVSLENCHPFTRGR---WLFAHNGQLDGFRLLRRRLLRLLPRLPVGTTDSELAFALLLSRLLE--RDPLD 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 150 ADNIFAAIAA----MNRLIRGAYACVAMIIGHGMVAFRDPNgIRPLVLGKRDAGNGRAE-------------YMVASEsv 212
Cdd:cd01908 159 PAELLDAILQtlreLAALAPPGRLNLLLSDGEYLIATRYAS-APSLYYLTRRAPFGCARllfrsvttpnddgVVVASE-- 235
|
170 180
....*....|....*....|....
gi 1758370708 213 aldTLGFEF-LRDVAPGEAVYISE 235
Cdd:cd01908 236 ---PLTDDEgWTEVPPGELVVVSE 256
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
69-210 |
1.91e-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: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 69 GIGHVRYPTAGSSSASeAQPFYvnSPYG-ITLAHNGNLTNAHELRKMLfEEKRRHINTTSDSEILLNIfaseldnFRHYP 147
Cdd:pfam13522 13 ALGHVRLAIVDLPDAG-NQPML--SRDGrLVLVHNGEIYNYGELREEL-ADLGHAFRSRSDTEVLLAL-------YEEWG 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1758370708 148 LEadnifaaiaAMNRLiRGAYA-CVAMIIGHGMVAFRDPNGIRPLVLGKRDAGngraeYMVASE 210
Cdd:pfam13522 82 ED---------CLERL-RGMFAfAIWDRRRRTLFLARDRLGIKPLYYGILGGG-----FVFASE 130
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
82-214 |
2.51e-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: 60.99 E-value: 2.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 82 SASEAQPFYVNSPYGITLAHNGNLTNAHELRKMLfEEKRRHINTTSDSEILLNIFASEldnfrhypleadnifaaiaamn 161
Cdd:pfam13537 9 LEGGAQPMVSSEDGRYVIVFNGEIYNYRELRAEL-EAKGYRFRTHSDTEVILHLYEAE---------------------- 65
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1758370708 162 rlirGAYACVAMIigHGMVAF-------------RDPNGIRPLVLGKRDaGNGraeYMVASESVAL 214
Cdd:pfam13537 66 ----WGEDCVDRL--NGMFAFaiwdrrrqrlflaRDRFGIKPLYYGRDD-GGR---LLFASELKAL 121
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-210 |
3.70e-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: 62.96 E-value: 3.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 2 CGIVGI---AGVMPVNQSIYDALTVLQHRGQDAAGIitidanncfrlrkanglvndvfearhmqRLQGNMGIGHVRY--- 75
Cdd:cd00712 1 CGIAGIiglDGASVDRATLERMLDALAHRGPDGSGI----------------------------WIDEGVALGHRRLsii 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 76 -PTAGsssaseAQPFYVNSPyGITLAHNGNLTNAHELRKMLfEEKRRHINTTSDSEILLnifasELdnFRHYpleadnif 154
Cdd:cd00712 53 dLSGG------AQPMVSEDG-RLVLVFNGEIYNYRELRAEL-EALGHRFRTHSDTEVIL-----HL--YEEW-------- 109
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1758370708 155 aaiaamnrlirGAyACVAMIigHGMVAF-------------RDPNGIRPLVLGKRDAGngraeYMVASE 210
Cdd:cd00712 110 -----------GE-DCLERL--NGMFAFalwdkrkrrlflaRDRFGIKPLYYGRDGGG-----LAFASE 159
|
|
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
1-214 |
4.32e-10 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 61.85 E-value: 4.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 1 MCGIVGIAGV----MPVNQSIYDALTVLQHRGQDAAGIITIDanncfrlrkanglvndvfearhmqrlqgNMGIGHVRYP 76
Cdd:PRK09431 1 MCGIFGILDIktdaDELRKKALEMSRLMRHRGPDWSGIYASD----------------------------NAILGHERLS 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 77 TAGSSSAseAQPFYvNSPYGITLAHNGNLTNAHELRKMLfeEKRRHINTTSDSEILLNI-------FASELDN---FRHY 146
Cdd:PRK09431 53 IVDVNGG--AQPLY-NEDGTHVLAVNGEIYNHQELRAEL--GDKYAFQTGSDCEVILALyqekgpdFLDDLDGmfaFALY 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1758370708 147 PLEADNIFAAiaamnrlirgayacvamiighgmvafRDPNGIRPLVLGKRDAGNgraeYMVASESVAL 214
Cdd:PRK09431 128 DSEKDAYLIA--------------------------RDPIGIIPLYYGYDEHGN----LYFASEMKAL 165
|
|
| ComFC |
COG1040 |
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General ... |
273-397 |
2.01e-09 |
|
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General function prediction only];
Pssm-ID: 440662 [Multi-domain] Cd Length: 196 Bit Score: 57.14 E-value: 2.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 273 YSARVEMGKKLGEKIAREWEDL---DIDVVIPIP-----------ETSCDIALEIARILNKPYR-QGFVKNRYVgrtfim 337
Cdd:COG1040 53 YRGRLDLARLLARLLARALREAllpRPDLIVPVPlhrrrlrrrgfNQAELLARALARALGIPVLpDLLRRVRAT------ 126
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1758370708 338 PGQHLRRKSVRRKLNAN------RAEFRDKNVLLVDDsiVR--GTTSEQIIEMAREAGAKKVYLASAA 397
Cdd:COG1040 127 PSQAGLSRAERRRNLRGafavrpPARLAGKHVLLVDD--VLttGATLAEAARALKAAGAARVDVLVLA 192
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-210 |
6.59e-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: 58.31 E-value: 6.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 1 MCGIVGIAG-VMPVNQSIYDALT-VLQHRGQDAAGIItidanncfrlrkanglvndvfearhmqrLQGNMGIGHVRypta 78
Cdd:COG0367 1 MCGIAGIIDfDGGADREVLERMLdALAHRGPDGSGIW----------------------------VDGGVALGHRR---- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 79 gSS----SASEAQPFyVNSPYGITLAHNGNLTNAHELRKMLfEEKRRHINTTSDSEILLnifaseldnfrhypleadnif 154
Cdd:COG0367 49 -LSiidlSEGGHQPM-VSEDGRYVLVFNGEIYNYRELRAEL-EALGHRFRTHSDTEVIL--------------------- 104
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1758370708 155 AAIAAMnrlirGAyACVAMIigHGMVAF-------------RDPNGIRPLVLGKRDAGngraeYMVASE 210
Cdd:COG0367 105 HAYEEW-----GE-DCLERL--NGMFAFaiwdrrerrlflaRDRFGIKPLYYAEDGGG-----LAFASE 160
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
1-215 |
2.19e-08 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 56.65 E-value: 2.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 1 MCGIVGIAGVM----PVNQSIYDALTVLQHRGQDAAGIITIDAnncfrlrkANGLVNdvfearhmqrlqgnmGIGHVRYP 76
Cdd:PTZ00077 1 MCGILAIFNSKgerhELRRKALELSKRLRHRGPDWSGIIVLEN--------SPGTYN---------------ILAHERLA 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 77 TAGSSSAseAQPFYVNSpYGITLAHNGNLTNAHELRKmLFEEKRRHINTTSDSEILLNIFASELDNfrHYPLEADNIFAA 156
Cdd:PTZ00077 58 IVDLSDG--KQPLLDDD-ETVALMQNGEIYNHWEIRP-ELEKEGYKFSSNSDCEIIGHLYKEYGPK--DFWNHLDGMFAT 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1758370708 157 I---AAMNRLirgayacvamiighgmVAFRDPNGIRPLVLGKRDAGngraEYMVASESVALD 215
Cdd:PTZ00077 132 ViydMKTNTF----------------FAARDHIGIIPLYIGYAKDG----SIWFSSELKALH 173
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-200 |
1.11e-05 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 47.95 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 1 MCGIVGIAGvMPVNQSIYDALTVL-------QHRGQDAAGIiTIDANncFRLRKANGLVNDVFEARH-MQRLQGNM---- 68
Cdd:PTZ00394 1 MCGIFGYAN-HNVPRTVEQILNVLldgiqkvEYRGYDSAGL-AIDAN--IGSEKEDGTAASAPTPRPcVVRSVGNIsqlr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 69 -----------------------GIGHVRYPTAGSSSASEAQPFYVNSpYGITLAHNGNLTNAHELRKMLFEEKrRHINT 125
Cdd:PTZ00394 77 ekvfseavaatlppmdattshhvGIAHTRWATHGGVCERNCHPQQSNN-GEFTIVHNGIVTNYMTLKELLKEEG-YHFSS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1758370708 126 TSDSEIlLNIFASELdnfrhYPLEADNIFAAIAA-MNRLIRGAYACV--AMIIGHGMVAFRDPNgirPLVLGKRDAGN 200
Cdd:PTZ00394 155 DTDTEV-ISVLSEYL-----YTRKGIHNFADLALeVSRMVEGSYALLvkSVYFPGQLAASRKGS---PLMVGIRRTDD 223
|
|
| PLN02549 |
PLN02549 |
asparagine synthase (glutamine-hydrolyzing) |
1-194 |
1.75e-05 |
|
asparagine synthase (glutamine-hydrolyzing)
Pssm-ID: 178164 [Multi-domain] Cd Length: 578 Bit Score: 47.45 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 1 MCGI---VGIAGVMPVNQS-IYDALTVLQHRGQDAAGIitidanncfRLRKANGLVNdvfearhmQRLQgnmgighVRYP 76
Cdd:PLN02549 1 MCGIlavLGCSDDSQAKRSrVLELSRRLRHRGPDWSGL---------YGNEDCYLAH--------ERLA-------IMDP 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 77 TAGSssaseaQPFYvNSPYGITLAHNGNLTNAHELRKMLFEEKRRhinTTSDSEILLNIFASELDNFrhyPLEADNIFAA 156
Cdd:PLN02549 57 ESGD------QPLY-NEDKTIVVTANGEIYNHKELREKLKLHKFR---TGSDCEVIAHLYEEHGEEF---VDMLDGMFSF 123
|
170 180 190
....*....|....*....|....*....|....*...
gi 1758370708 157 IAAMNRlirgayacvamiiGHGMVAFRDPNGIRPLVLG 194
Cdd:PLN02549 124 VLLDTR-------------DNSFIAARDHIGITPLYIG 148
|
|
| PyrE |
COG0461 |
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ... |
266-389 |
1.65e-04 |
|
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate phosphoribosyltransferase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 440229 Cd Length: 201 Bit Score: 42.83 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 266 FIDK---ISVYSARVEMGKKLGEKIAREweDLDIDVV-------IPIpetscdiALEIARILNKPYRqgfvknrYVGRTf 335
Cdd:COG0461 33 YIDCrlvLSYPEALELLGEALAELIKEL--GPEFDAVagpatggIPL-------AAAVARALGLPAI-------FVRKE- 95
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1758370708 336 imPGQHLRRKSVRRKLNANraefrdKNVLLVDDSIVRGTTSEQIIEMAREAGAK 389
Cdd:COG0461 96 --AKDHGTGGQIEGGLLPG------ERVLVVEDVITTGGSVLEAVEALREAGAE 141
|
|
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
1-132 |
1.74e-04 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 44.36 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 1 MCGIVGIA--GVMPVNQSIYD----ALTVLQHRGQDAAGIiTIDANNCFR------LR---KANGLVNDVFEARHMQRLQ 65
Cdd:PLN02981 1 MCGIFAYLnyNVPRERRFILEvlfnGLRRLEYRGYDSAGI-AIDNDPSLEsssplvFReegKIESLVRSVYEEVAETDLN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1758370708 66 GNM------GIGHVRYPTAGSSSASEAQPFYVNSPYGITLAHNGNLTNAHELRKMLFeekrRH---INTTSDSEIL 132
Cdd:PLN02981 80 LDLvfenhaGIAHTRWATHGPPAPRNSHPQSSGPGNEFLVVHNGIITNYEVLKETLL----RHgftFESDTDTEVI 151
|
|
| PRK00934 |
PRK00934 |
ribose-phosphate pyrophosphokinase; Provisional |
281-394 |
3.02e-04 |
|
ribose-phosphate pyrophosphokinase; Provisional
Pssm-ID: 234868 [Multi-domain] Cd Length: 285 Bit Score: 42.59 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 281 KKLGEKIArewEDLDIDVVIPIPETSCDIALEIARILNKPYRQgFVKNRYVGRTFIMpgqhlRRKSVrrklnanraEFRD 360
Cdd:PRK00934 143 PLIAEYIG---DKLDDPLVLAPDKGALELAKEAAEILGCEYDY-LEKTRISPTEVEI-----APKNL---------DVKG 204
|
90 100 110
....*....|....*....|....*....|....
gi 1758370708 361 KNVLLVDDSIVRGTTSEQIIEMAREAGAKKVYLA 394
Cdd:PRK00934 205 KDVLIVDDIISTGGTMATAIKILKEQGAKKVYVA 238
|
|
| PRK08558 |
PRK08558 |
adenine phosphoribosyltransferase; Provisional |
264-391 |
8.76e-04 |
|
adenine phosphoribosyltransferase; Provisional
Pssm-ID: 181466 [Multi-domain] Cd Length: 238 Bit Score: 41.13 E-value: 8.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 264 DSFIDKISVYSARVEMgKKLGEKIAREWEDLDIDVVIPIPETSCDIALEIARILN------KPYRQGFVKNRYVGRTFIM 337
Cdd:PRK08558 81 EGYVDNSSVVFDPSFL-RLIAPVVAERFMGLRVDVVLTAATDGIPLAVAIASYFGadlvyaKKSKETGVEKFYEEYQRLA 159
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1758370708 338 PGQ----HLRRKSVRRklnanraefrDKNVLLVDDSIVRGTTSEQIIEMAREAGAKKV 391
Cdd:PRK08558 160 SGIevtlYLPASALKK----------GDRVLIVDDIIRSGETQRALLDLARQAGADVV 207
|
|
| Pribosyltran |
pfam00156 |
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ... |
278-414 |
2.24e-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: 38.50 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 278 EMGKKLGEKIAREWEDLD--IDVVIPIPETSCDIALEIARILNKPYrQGFVKNRYVGRTfimPGQHlrrksvrrKLNANR 355
Cdd:pfam00156 10 AILKAVARLAAQINEDYGgkPDVVVGILRGGLPFAGILARRLDVPL-AFVRKVSYNPDT---SEVM--------KTSSAL 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1758370708 356 AEFRDKNVLLVDDSIVRGTTSEQIIEMAREAGAKKVYLA------SAAPEIRFPNVYGIDMPSAN 414
Cdd:pfam00156 78 PDLKGKTVLIVDDILDTGGTLLKVLELLKNVGPKEVKIAvlidkpAGTEPKDKYDKRVDDWIVFV 142
|
|
| RlhA |
COG0826 |
23S rRNA C2501 and tRNA U34 5'-hydroxylation protein RlhA/YrrN/YrrO, U32 peptidase family ... |
377-454 |
2.28e-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: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 377 EQIIEMAREAGaKKVYLASaapeirfpNVygidmpsanelIAHGREVDEIRQII------GADGLIFQDLdDLIEAVRAE 450
Cdd:COG0826 49 AEAVEYAHERG-KKVYVTL--------NT-----------LLHDEELEELEEYLdflaeaGVDAIIVQDL-GVLELAREI 107
|
....
gi 1758370708 451 NPDI 454
Cdd:COG0826 108 APDL 111
|
|
| Hpt1 |
COG2236 |
Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine ... |
339-394 |
2.86e-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: 38.29 E-value: 2.86e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1758370708 339 GQHLRRKSVRRKLNANraeFRDKNVLLVDDSIVRGTTSEQIIEMAREAGAKKVYLA 394
Cdd:COG2236 70 AKRLEEPVVKGPLDED---LAGKRVLIVDDVADTGRTLEAVRDLLKEAGPAEVRTA 122
|
|
| pyrE |
PRK00455 |
orotate phosphoribosyltransferase; Validated |
266-389 |
4.56e-03 |
|
orotate phosphoribosyltransferase; Validated
Pssm-ID: 234771 Cd Length: 202 Bit Score: 38.60 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 266 FIDK---ISVYSARVEMGKKLGEKIAREweDLDIDVVI-P----IPetscdIALEIARILNKPYrqGFV----KNRYVGR 333
Cdd:PRK00455 34 YFDCrklLSYPEALALLGRFLAEAIKDS--GIEFDVVAgPatggIP-----LAAAVARALDLPA--IFVrkeaKDHGEGG 104
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1758370708 334 TFImpgqhLRRKSvrrklnanraefrDKNVLLVDDSIVRGTTSEQIIEMAREAGAK 389
Cdd:PRK00455 105 QIE-----GRRLF-------------GKRVLVVEDVITTGGSVLEAVEAIRAAGAE 142
|
|
| ribP_PPkin |
TIGR01251 |
ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In ... |
292-394 |
4.85e-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: 4.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758370708 292 EDLDIDVVIPIPET-SCDIALEIARILNKPYrqgfvknryvgrtFIMpgqhlrRKsvRRKLNANRAEFR-------DKNV 363
Cdd:TIGR01251 155 KKILDNPVVVSPDAgGVERAKKVADALGCPL-------------AII------DK--RRISATNEVEVMnlvgdveGKDV 213
|
90 100 110
....*....|....*....|....*....|.
gi 1758370708 364 LLVDDSIVRGTTSEQIIEMAREAGAKKVYLA 394
Cdd:TIGR01251 214 VIVDDIIDTGGTIAKAAEILKSAGAKRVIAA 244
|
|
| |
