|
Name |
Accession |
Description |
Interval |
E-value |
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
1-479 |
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: 585.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554892 1 MCGIFGIVAAgnyEHLNVLAANGLAALQHRGTESTGLVGSDGitrDHVEIIKGHGLVRDVITEDNISRMNGqSIIIGHNR 80
Cdd:COG0034 7 ECGVFGIYGH---EDVAQLTYYGLYALQHRGQESAGIATSDG---GRFHLHKGMGLVSDVFDEEDLERLKG-NIAIGHVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554892 81 YSTAGKkkSGINCVQPFVVYTAMGTVAIAHNGELVDAKQKRKEVLHEGVGLSTDTDSELIAQMIAKAIalnvkckygqEM 160
Cdd:COG0034 80 YSTTGS--SSLENAQPFYVNSPFGSIALAHNGNLTNAEELREELEEEGAIFQTTSDTEVILHLIAREL----------TK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554892 161 GDITRELAVTMSALNMSYSLLVMTFDRLYAIRDPFGNRPLCVGTvyskngNPEAFIASSESCAFPA-NAKLDFEVRPGEI 239
Cdd:COG0034 148 EDLEEAIKEALRRVKGAYSLVILTGDGLIAARDPNGIRPLVLGK------LEDGYVVASESCALDIlGAEFVRDVEPGEI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554892 240 VELSTGGIKSVwQMKPNTPLAMCIFEYVYFARNDSEIEGQQVQTVREECGKTMALEDDLEADIVGNVPDSSLSAAIGYAS 319
Cdd:COG0034 222 VVIDEDGLRSR-QFAEKPRPAPCIFEYVYFARPDSVIDGRSVYEARKRMGRELAREAPVDADVVIPVPDSGRPAAIGYAE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554892 320 QSGITYEPVLHRNSYVGRSFIEPNDEMRQNAIKMKFGVLKKKIHGQRIVLVDDSIVRGNTMRTLVKMLRDAGAKEVHLRI 399
Cdd:COG0034 301 ESGIPYEEGLIKNRYVGRTFIQPTQELRELGVRLKLNPIREVVKGKRVVLVDDSIVRGTTSRRIVKMLREAGAKEVHFRI 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554892 400 ASPPVKFPCFMGINIPTTKELIAAEKTIPEICQFVGADSVRYLSVDGLVSSVQKGIEraanfspGHCTACLTGKYPVAID 479
Cdd:COG0034 381 ASPPIRYPCYYGIDTPTREELIAANRSVEEIREYIGADSLGYLSLEGLIEAVGEPIE-------GFCTACFTGDYPTGIP 453
|
|
| purF |
TIGR01134 |
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ... |
2-475 |
6.42e-170 |
|
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: 485.67 E-value: 6.42e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554892 2 CGIFGIVaaGNYEHLNVLAANGLAALQHRGTESTGLVGSDGitrDHVEIIKGHGLVRDVITEDNISRMNGqSIIIGHNRY 81
Cdd:TIGR01134 1 CGVVGIY--GQEEVAASLTYYGLYALQHRGQESAGISVFDG---NRFRLHKGNGLVSDVFNEEHLQRLKG-NVGIGHVRY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554892 82 STAGKkkSGINCVQPFVVYTAMGTVAIAHNGELVDAKQKRKEVLHEGVGLSTDTDSELIAQMIAKAIALNvkckygqemG 161
Cdd:TIGR01134 75 STAGS--SGLENAQPFVVNSPYGGLALAHNGNLVNADELRRELEEEGRHFNTTSDSEVLLHLLAHNDESK---------D 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554892 162 DITRELAVTMSALNMSYSLLVMTFDRLYAIRDPFGNRPLCVGtvysknGNPEAFIASSESCAFPA-NAKLDFEVRPGEIV 240
Cdd:TIGR01134 144 DLFDAVARVLERVRGAYALVLMTEDGLVAVRDPHGIRPLVLG------RRGDGYVVASESCALDIlGAEFVRDVEPGEVV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554892 241 ELSTGGIKSvwQMKPNTPLAMCIFEYVYFARNDSEIEGQQVQTVREECGKTMALEDDLEADIVGNVPDSSLSAAIGYASQ 320
Cdd:TIGR01134 218 VIFDGGLES--RQCARRPRAPCVFEYVYFARPDSVIDGISVYYARKRMGKELARESPVEADVVVPVPDSGRSAALGFAQA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554892 321 SGITYEPVLHRNSYVGRSFIEPNDEMRQNAIKMKFGVLKKKIHGQRIVLVDDSIVRGNTMRTLVKMLRDAGAKEVHLRIA 400
Cdd:TIGR01134 296 SGIPYREGLIKNRYVGRTFIMPTQELRELSVRLKLNPVRAVFEGKRVVLVDDSIVRGTTSRQIVEMLRDAGAKEVHVRIA 375
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17554892 401 SPPVKFPCFMGINIPTTKELIAAEKTIPEICQFvGADSVRYLSVDGLVSSVQKGIEraanfspGHCTACLTGKYP 475
Cdd:TIGR01134 376 SPPIRYPCYYGIDMPTREELIAARRTVEEIRKI-GADSLAYLSLEGLKEAVGNPES-------DLCLACFTGEYP 442
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
2-478 |
7.90e-166 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 476.45 E-value: 7.90e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554892 2 CGIFGIVAAGNYEhLNVLAANGLAALQHRGTESTGLVGSDGitrDHVEIIKGHGLVRDVITEDNISRMNGqSIIIGHNRY 81
Cdd:PRK05793 15 CGVFGVFSKNNID-VASLTYYGLYALQHRGQESAGIAVSDG---EKIKVHKGMGLVSEVFSKEKLKGLKG-NSAIGHVRY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554892 82 STAGKkkSGINCVQPFVVYTAMGTVAIAHNGELVDAKQKRKEVLHEGVGLSTDTDSELIAQMIAKaialnvkckYGQemG 161
Cdd:PRK05793 90 STTGA--SDLDNAQPLVANYKLGSIAIAHNGNLVNADVIRELLEDGGRIFQTSIDSEVILNLIAR---------SAK--K 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554892 162 DITRELAVTMSALNMSYSLLVMTFDRLYAIRDPFGNRPLCVGtvysKNGnpEAFIASSESCAFPA-NAKLDFEVRPGEIV 240
Cdd:PRK05793 157 GLEKALVDAIQAIKGSYALVILTEDKLIGVRDPHGIRPLCLG----KLG--DDYILSSESCALDTiGAEFIRDVEPGEIV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554892 241 ELSTGGIKSVwQMKPNTPLAMCIFEYVYFARNDSEIEGQQVQTVREECGKTMALEDDLEADIVGNVPDSSLSAAIGYASQ 320
Cdd:PRK05793 231 IIDEDGIKSI-KFAEKTKCQTCAFEYIYFARPDSVIDGISVYESRVRAGRQLYKEYPVDADIVIGVPDSGIPAAIGYAEA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554892 321 SGITYEPVLHRNSYVGRSFIEPNDEMRQNAIKMKFGVLKKKIHGQRIVLVDDSIVRGNTMRTLVKMLRDAGAKEVHLRIA 400
Cdd:PRK05793 310 SGIPYGIGFIKNKYVGRTFIAPSQELRERAVRVKLNPLKVNVEGKRVVLIDDSIVRGTTSKRLVELLRKAGAKEVHFRVS 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17554892 401 SPPVKFPCFMGINIPTTKELIAAEKTIPEICQFVGADSVRYLSVDGLVSSVQKgieraanfSPGHCTACLTGKYPVAI 478
Cdd:PRK05793 390 SPPVKYPCYFGIDTPYRKELIGANMSVEEIREMIGADSLGYLSIEGLLESLNG--------DKGFCLGCFNGVYPVSA 459
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
1-476 |
3.66e-135 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 398.67 E-value: 3.66e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554892 1 MCGIFGIVAAGNYEHLNVLaanGLAALQHRGTESTGLVGSDGitrDHVEIIKGHGLVRDVITEDNISRMNGqSIIIGHNR 80
Cdd:PLN02440 1 ECGVVGIFGDPEASRLCYL---GLHALQHRGQEGAGIVTVDG---NRLQSITGNGLVSDVFDESKLDQLPG-DIAIGHVR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554892 81 YSTAGKkkSGINCVQPFVVYTAMGTVAIAHNGELVDAKQKRKEVLHEGVGLSTDTDSELIAQMIAKAIALNVkckygqem 160
Cdd:PLN02440 74 YSTAGA--SSLKNVQPFVANYRFGSIGVAHNGNLVNYEELRAKLEENGSIFNTSSDTEVLLHLIAISKARPF-------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554892 161 gdITReLAVTMSALNMSYSLLVMTFDRLYAIRDPFGNRPLCVGTvySKNGnpeAFIASSESCAF-PANAKLDFEVRPGEI 239
Cdd:PLN02440 144 --FSR-IVDACEKLKGAYSMVFLTEDKLVAVRDPHGFRPLVMGR--RSNG---AVVFASETCALdLIGATYEREVNPGEV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554892 240 VELSTGGIKSVWQMKPNTPLAMCIFEYVYFARNDSEIEGQQVQTVREECGKTMALEDDLEADIVGNVPDSSLSAAIGYAS 319
Cdd:PLN02440 216 IVVDKDKGVSSQCLMPHPEPKPCIFEHIYFARPNSIVFGRSVYESRLEFGEILATEIPVDCDVVIPVPDSGRVAALGYAA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554892 320 QSGITYEPVLHRNSYVGRSFIEPNDEMRQNAIKMKFGVLKKKIHGQRIVLVDDSIVRGNTMRTLVKMLRDAGAKEVHLRI 399
Cdd:PLN02440 296 KLGVPFQQGLIRSHYVGRTFIEPSQKIRDFSVKLKLNPVRSVLEGKRVVVVDDSIVRGTTSSKIVRMLREAGAKEVHMRI 375
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17554892 400 ASPPVKFPCFMGINIPTTKELIAAEKTIPEICQFVGADSVRYLSVDGLVSSVQKGieraanfSPGHCTACLTGKYPV 476
Cdd:PLN02440 376 ASPPIIASCYYGVDTPSREELISNRMSVEEIRKFIGCDSLAFLPLEDLKKSLGEE-------SPRFCYACFSGDYPV 445
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
2-277 |
3.79e-111 |
|
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: 328.65 E-value: 3.79e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554892 2 CGIFGIVAAgnyEHLNVLAANGLAALQHRGTESTGLVGSDGitrDHVEIIKGHGLVRDVITEDNISRMNGqSIIIGHNRY 81
Cdd:cd00715 1 CGVFGIYGA---EDAARLTYLGLYALQHRGQESAGIATSDG---KRFHTHKGMGLVSDVFDEEKLRRLPG-NIAIGHVRY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554892 82 STAGKkkSGINCVQPFVVYTAMGTVAIAHNGELVDAKQKRKEVLHEGVGLSTDTDSELIAQMIAKAIalnvkckygqEMG 161
Cdd:cd00715 74 STAGS--SSLENAQPFVVNSPLGGIALAHNGNLVNAKELREELEEEGRIFQTTSDSEVILHLIARSL----------AKD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554892 162 DITRELAVTMSALNMSYSLLVMTFDRLYAIRDPFGNRPLCVGTVyskngNPEAFIASSESCAFPA-NAKLDFEVRPGEIV 240
Cdd:cd00715 142 DLFEAIIDALERVKGAYSLVIMTADGLIAVRDPHGIRPLVLGKL-----EGDGYVVASESCALDIiGAEFVRDVEPGEIV 216
|
250 260 270
....*....|....*....|....*....|....*..
gi 17554892 241 ELSTGGIKSVwQMKPNTPLAMCIFEYVYFARNDSEIE 277
Cdd:cd00715 217 VIDDDGLESS-QRAPKPKPAPCIFEYVYFARPDSVID 252
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
2-240 |
1.67e-43 |
|
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: 152.99 E-value: 1.67e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554892 2 CGIFGIVAA-GNYEHLNVLAANGLAALQHRGTESTGLVGSDGitrDHVEIIKGHGLVRDVITEDNISRMNGqSIIIGHNR 80
Cdd:cd00352 1 CGIFGIVGAdGAASLLLLLLLRGLAALEHRGPDGAGIAVYDG---DGLFVEKRAGPVSDVALDLLDEPLKS-GVALGHVR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554892 81 YSTAGKKKSGiNCvQPFVVytAMGTVAIAHNGELVDAKQKRKEVLHEGVGLSTDTDSELIAQMIAkaialnvkcKYGQEm 160
Cdd:cd00352 77 LATNGLPSEA-NA-QPFRS--EDGRIALVHNGEIYNYRELREELEARGYRFEGESDSEVILHLLE---------RLGRE- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554892 161 GDITRELAVTMSALNMSYSLLVMT--FDRLYAIRDPFGNRPLCVGTvysknGNPEAFIASSESCAF-PANAKLDFEVRPG 237
Cdd:cd00352 143 GGLFEAVEDALKRLDGPFAFALWDgkPDRLFAARDRFGIRPLYYGI-----TKDGGLVFASEPKALlALPFKGVRRLPPG 217
|
...
gi 17554892 238 EIV 240
Cdd:cd00352 218 ELL 220
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
2-240 |
1.15e-23 |
|
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: 99.65 E-value: 1.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554892 2 CGIFGIVAAGNYEHLNVLAANGLAALQHRGTE-STG--LVGSDGITR----DHVEIIKGHGLVRDVITEDNISRMNGqSI 74
Cdd:cd01907 1 CGIFGIMSKDGEPFVGALLVEMLDAMQERGPGdGAGfaLYGDPDAFVyssgKDMEVFKGVGYPEDIARRYDLEEYKG-YH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554892 75 IIGHNRYSTagkkKSGINCVQ--PFVVYtamgTVAIAHNGELVDAKQKRKEVLHEGVGLSTDTDSELIAQMIA------- 145
Cdd:cd01907 80 WIAHTRQPT----NSAVWWYGahPFSIG----DIAVVHNGEISNYGSNREYLERFGYKFETETDTEVIAYYLDlllrkgg 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554892 146 -----KAIALNVKCKYGQEMGDITRELAVTMsaLNMSYSLLVMTFDRLYAIRDPFGNRPLCVGtvysknGNPEAFIASSE 220
Cdd:cd01907 152 lpleyYKHIIRMPEEERELLLALRLTYRLAD--LDGPFTIIVGTPDGFIVIRDRIKLRPAVVA------ETDDYVAIASE 223
|
250 260
....*....|....*....|....
gi 17554892 221 SCA----FPANAKLDFEVRPGEIV 240
Cdd:cd01907 224 ECAireiPDRDNAKVWEPRPGEYV 247
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
2-218 |
3.35e-17 |
|
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: 80.18 E-value: 3.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554892 2 CGIFGIVaaGNYEHLNVLAaNGLAALQHRGTESTGLVGsdgITRDHVEIIKGHGLVRDVITEDNISRMNGQsIIIGHNRY 81
Cdd:cd00714 1 CGIVGYI--GKREAVDILL-EGLKRLEYRGYDSAGIAV---IGDGSLEVVKAVGKVANLEEKLAEKPLSGH-VGIGHTRW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554892 82 STAGKKkSGINCvQPFVVYTamGTVAIAHNGELVDAKQKRKEVLHEGVGLSTDTDSELIAQMIAkaialnvkcKYGQEMG 161
Cdd:cd00714 74 ATHGEP-TDVNA-HPHRSCD--GEIAVVHNGIIENYAELKEELEAKGYKFESETDTEVIAHLIE---------YYYDGGL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17554892 162 DItreLAVTMSALNM---SYSLLVMTF---DRLYAIRDpfgNRPLCVGTvysknGNPEAFIAS 218
Cdd:cd00714 141 DL---LEAVKKALKRlegAYALAVISKdepDEIVAARN---GSPLVIGI-----GDGENFVAS 192
|
|
| PRTases_typeI |
cd06223 |
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ... |
293-415 |
6.63e-16 |
|
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: 73.97 E-value: 6.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554892 293 ALEDDLEADIVGNVPDSSLSAAIGYASQSGITYEPVLHRNSYVGRSFIEPNDemrqnaikmKFGVLKKKIHGQRIVLVDD 372
Cdd:cd06223 9 IREDLLEPDVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSEPYG---------LELPLGGDVKGKRVLLVDD 79
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 17554892 373 SIVRGNTMRTLVKMLRDAGAKEVHLrIASPPVKFPCFMGINIP 415
Cdd:cd06223 80 VIATGGTLLAAIELLKEAGAKVVGV-AVLLDKPEGGARELASP 121
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-249 |
1.65e-13 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 72.75 E-value: 1.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554892 1 MCGIFGIVaaGNYEHLNVLAaNGLAALQHRGTESTGL-------------VGSDGITRDHVEIIKGHGLvrdvitedniS 67
Cdd:PTZ00295 24 CCGIVGYL--GNEDASKILL-EGIEILQNRGYDSCGIstissggelkttkYASDGTTSDSIEILKEKLL----------D 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554892 68 RMNGQSIIIGHNRYSTAGKKkSGINcVQPFVVYTamGTVAIAHNGELVDAKQKRKEVLHEGVGLSTDTDSELIAQMIAka 147
Cdd:PTZ00295 91 SHKNSTIGIAHTRWATHGGK-TDEN-AHPHCDYK--KRIALVHNGTIENYVELKSELIAKGIKFRSETDSEVIANLIG-- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554892 148 ialnvkcKYGQEMGDITRELAVTMSALNMSYSLLVMTF---DRLYAIRDpfgNRPLCVGtvYSKNGnpeAFIAsSESCAF 224
Cdd:PTZ00295 165 -------LELDQGEDFQEAVKSAISRLQGTWGLCIIHKdnpDSLIVARN---GSPLLVG--IGDDS---IYVA-SEPSAF 228
|
250 260
....*....|....*....|....*
gi 17554892 225 PANAKLDFEVRPGEIVELSTGGIKS 249
Cdd:PTZ00295 229 AKYTNEYISLKDGEIAELSLENVND 253
|
|
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
1-248 |
2.74e-13 |
|
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: 71.97 E-value: 2.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554892 1 MCGIFGIVAAGNyehlnvlAA----NGLAALQHRGTESTGLVGSDGitrDHVEIIKGHGLVRDVITEDNISRMNGqSIII 76
Cdd:COG0449 1 MCGIVGYIGKRD-------AApillEGLKRLEYRGYDSAGIAVLDD---GGLEVRKAVGKLANLEEKLAEEPLSG-TIGI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554892 77 GHNRYSTAGKkksgincvqPFVV-----YTAMGTVAIAHNG------ELvdakqkRKEVLHEGVGLSTDTDSELIAQMIA 145
Cdd:COG0449 70 GHTRWATHGA---------PSDEnahphTSCSGRIAVVHNGiienyaEL------REELEAKGHTFKSETDTEVIAHLIE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554892 146 KAIalnvkckygQEMGDITRELAVTMSALNMSYSLLVMT---FDRLYAIRDpfgNRPLCVGtvYSKNGNpeaFIASSesc 222
Cdd:COG0449 135 EYL---------KGGGDLLEAVRKALKRLEGAYALAVISadePDRIVAARK---GSPLVIG--LGEGEN---FLASD--- 194
|
250 260 270
....*....|....*....|....*....|.
gi 17554892 223 afpANAKLDF-----EVRPGEIVELSTGGIK 248
Cdd:COG0449 195 ---VPALLPYtrrviYLEDGEIAVLTRDGVE 222
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
73-207 |
1.07e-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: 433279 [Multi-domain] Cd Length: 130 Bit Score: 65.02 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554892 73 SIIIGHNRYSTAGKKKSGincVQPFVVYTamGTVAIAHNGELVDAKQKRKEVLHEGVGLSTDTDSELIAQMIakaialnv 152
Cdd:pfam13522 11 GVALGHVRLAIVDLPDAG---NQPMLSRD--GRLVLVHNGEIYNYGELREELADLGHAFRSRSDTEVLLALY-------- 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 17554892 153 kckygQEMGDITRELAVTMSAlnmsYSLLVMTFDRLYAIRDPFGNRPLCVGTVYS 207
Cdd:pfam13522 78 -----EEWGEDCLERLRGMFA----FAIWDRRRRTLFLARDRLGIKPLYYGILGG 123
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
1-248 |
1.70e-12 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 69.69 E-value: 1.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554892 1 MCGIFGIVaaGNYEHLNVLAaNGLAALQHRGTESTGLVGSDGitrDHVEIIKGHGLVRDVITEDNISRMNGqSIIIGHNR 80
Cdd:PRK00331 1 MCGIVGYV--GQRNAAEILL-EGLKRLEYRGYDSAGIAVLDD---GGLEVRKAVGKVANLEAKLEEEPLPG-TTGIGHTR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554892 81 YSTAGKkksgincvqPFVV-----YTAMGTVAIAHNG------ELvdakqkRKEVLHEGVGLSTDTDSELIAQMIAkaia 149
Cdd:PRK00331 74 WATHGK---------PTERnahphTDCSGRIAVVHNGiienyaEL------KEELLAKGHVFKSETDTEVIAHLIE---- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554892 150 lnvkcKYGQEMGDITRELAVTMSALNMSYSLLVMTF---DRLYAIRDpfgNRPLCVGTvysknGNPEAFIASSescafpA 226
Cdd:PRK00331 135 -----EELKEGGDLLEAVRKALKRLEGAYALAVIDKdepDTIVAARN---GSPLVIGL-----GEGENFLASD------A 195
|
250 260
....*....|....*....|....*..
gi 17554892 227 NAKLDF-----EVRPGEIVELSTGGIK 248
Cdd:PRK00331 196 LALLPYtrrviYLEDGEIAVLTRDGVE 222
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-220 |
1.70e-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: 63.73 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554892 2 CGIFGIVAAGNYEHLNVLAANGLAALQHRGTESTGLVGSDGItrdhveiikghglvrdvitednisrmngqsiIIGHNRY 81
Cdd:cd00712 1 CGIAGIIGLDGASVDRATLERMLDALAHRGPDGSGIWIDEGV-------------------------------ALGHRRL 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554892 82 S----TAGKkksgincvQPFvvYTAMGTVAIAHNGELVDAKQKRKEVLHEGVGLSTDTDSELIAQMIAkaialnvkcKYG 157
Cdd:cd00712 50 SiidlSGGA--------QPM--VSEDGRLVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHLYE---------EWG 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17554892 158 qemgditrELAVTMsaLN-MsYSLLVmtFD----RLYAIRDPFGNRPLCVGTvyskngNPEAFIASSE 220
Cdd:cd00712 111 --------EDCLER--LNgM-FAFAL--WDkrkrRLFLARDRFGIKPLYYGR------DGGGLAFASE 159
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
95-226 |
1.15e-10 |
|
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: 59.07 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554892 95 QPFVvYTAMGTVAIAHNGELVDAKQKRKEVLHEGVGLSTDTDSELIAQMIAKAialnvkckYGQEMgditrelavtMSAL 174
Cdd:pfam13537 14 QPMV-SSEDGRYVIVFNGEIYNYRELRAELEAKGYRFRTHSDTEVILHLYEAE--------WGEDC----------VDRL 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 17554892 175 NMSYSLLVMTFD--RLYAIRDPFGNRPLCVGTvysKNGNpeAFIASSESCAFPA 226
Cdd:pfam13537 75 NGMFAFAIWDRRrqRLFLARDRFGIKPLYYGR---DDGG--RLLFASELKALLA 123
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-220 |
2.99e-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: 2.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554892 1 MCGIFGIVAAGNYEHLNVLAAnGLAALQHRGtestglvgsdgitRDhveiikGHGLVRDvitednisrmngQSIIIGHNR 80
Cdd:COG0367 1 MCGIAGIIDFDGGADREVLER-MLDALAHRG-------------PD------GSGIWVD------------GGVALGHRR 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554892 81 YSTAGKKKSGincVQPFVvyTAMGTVAIAHNGELVDAKQKRKEVLHEGVGLSTDTDSELIAQMIAkaialnvkcKYGQEM 160
Cdd:COG0367 49 LSIIDLSEGG---HQPMV--SEDGRYVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHAYE---------EWGEDC 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17554892 161 gditrelavtMSALN-MsYSLLVmtFD----RLYAIRDPFGNRPLCvgtvYSKNGNpeAFIASSE 220
Cdd:COG0367 115 ----------LERLNgM-FAFAI--WDrrerRLFLARDRFGIKPLY----YAEDGG--GLAFASE 160
|
|
| YafJ |
cd01908 |
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ... |
1-245 |
3.92e-09 |
|
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: 57.40 E-value: 3.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554892 1 MCGIFGIVAAGNY-EHLNVLAANGLAALQHRGTESTGLVGSDG-----ITRDHVEIikghGLVRDVI-TEDNIS--RMNG 71
Cdd:cd01908 1 MCRLLGYSGAPIPlEPLLIRPSHSLLVQSGGPREMKGTVHADGwgigwYEGKGGRP----FRYRSPLpAWSDINleSLAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554892 72 Q---SIIIGHNRYSTAGKKKSgINCvQPFVVytamGTVAIAHNGELVDAKQKRKEVLHEG----VGlstDTDSELIAqmi 144
Cdd:cd01908 77 PiksPLVLAHVRAATVGPVSL-ENC-HPFTR----GRWLFAHNGQLDGFRLLRRRLLRLLprlpVG---TTDSELAF--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554892 145 akAIALN-VKCKYGQEMGDITRELAVTMSALNMSYSLLVMTF-----DRLYAIRDPFGN-----------RPLCVGTVYS 207
Cdd:cd01908 145 --ALLLSrLLERDPLDPAELLDAILQTLRELAALAPPGRLNLllsdgEYLIATRYASAPslyyltrrapfGCARLLFRSV 222
|
250 260 270
....*....|....*....|....*....|....*....
gi 17554892 208 KNGNPEAFIASSEscafPANAKLDF-EVRPGEIVELSTG 245
Cdd:cd01908 223 TTPNDDGVVVASE----PLTDDEGWtEVPPGELVVVSEG 257
|
|
| YafJ |
COG0121 |
Predicted glutamine amidotransferase YafJ [General function prediction only]; |
74-246 |
4.73e-06 |
|
Predicted glutamine amidotransferase YafJ [General function prediction only];
Pssm-ID: 439891 [Multi-domain] Cd Length: 248 Bit Score: 48.04 E-value: 4.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554892 74 IIIGHNRYSTAGKKKSgINCvQPFVvytaMGTVAIAHNGELVDAKQKRKEVLHEG--------VGlstDTDSELIAQMIA 145
Cdd:COG0121 78 LVIAHVRKATVGPVSL-ENT-HPFR----GGRWLFAHNGQLDGFDRLRRRLAEELpdelyfqpVG---TTDSELAFALLL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554892 146 KAIAlNVKCKYGQEMGDITR---ELAVTMSALNMsyslLVMTFDRLYAIRDPFGNRPLCVGTVYSKNGNPEAFIASSEsc 222
Cdd:COG0121 149 SRLR-DGGPDPAEALAEALRelaELARAPGRLNL----LLSDGERLYATRYTSDDPYPTLYYLTRTTPDDRVVVVASE-- 221
|
170 180
....*....|....*....|....*....
gi 17554892 223 afpanaKLDF-----EVRPGEIVELSTGG 246
Cdd:COG0121 222 ------PLTDdegwtEVPPGELLVVRDGL 244
|
|
| ComFC |
COG1040 |
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General ... |
318-396 |
3.57e-05 |
|
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General function prediction only];
Pssm-ID: 440662 [Multi-domain] Cd Length: 196 Bit Score: 44.43 E-value: 3.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554892 318 ASQSGITYEP-VLHRNSY----VGRSFIEpndemRQNAIKMKFGVLKK-KIHGQRIVLVDDsiVR--GNTMRTLVKMLRD 389
Cdd:COG1040 108 ARALGIPVLPdLLRRVRAtpsqAGLSRAE-----RRRNLRGAFAVRPPaRLAGKHVLLVDD--VLttGATLAEAARALKA 180
|
....*..
gi 17554892 390 AGAKEVH 396
Cdd:COG1040 181 AGAARVD 187
|
|
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
1-182 |
1.18e-04 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 44.74 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554892 1 MCGIFGIVaagNY-------EHLNVLAaNGLAALQHRGTESTGLVGSDGITRDHVE--IIKGHG----LVRDVITEDNIS 67
Cdd:PLN02981 1 MCGIFAYL---NYnvprerrFILEVLF-NGLRRLEYRGYDSAGIAIDNDPSLESSSplVFREEGkiesLVRSVYEEVAET 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554892 68 RMNGQSII-----IGHNRYSTAGK--------KKSGINcvQPFVVytamgtvaiAHNGELVDAKQKRKEVLHEGVGLSTD 134
Cdd:PLN02981 77 DLNLDLVFenhagIAHTRWATHGPpaprnshpQSSGPG--NEFLV---------VHNGIITNYEVLKETLLRHGFTFESD 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 17554892 135 TDSELIAQMiakaiALNVKCKYGQEMGDIT-RELAV-TMSALNMSYSLLV 182
Cdd:PLN02981 146 TDTEVIPKL-----AKFVFDKLNEEEGDVTfSQVVMeVMRQLEGAYALIF 190
|
|
| PLN02238 |
PLN02238 |
hypoxanthine phosphoribosyltransferase |
352-395 |
7.68e-04 |
|
hypoxanthine phosphoribosyltransferase
Pssm-ID: 215132 Cd Length: 189 Bit Score: 40.41 E-value: 7.68e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 17554892 352 KMKFGVLKKKIHGQRIVLVDDSIVRGNTMRTLVKMLRDAGAKEV 395
Cdd:PLN02238 85 KVSGADLKIDVKGKHVLLVEDIVDTGNTLSALVAHLEAKGAASV 128
|
|
| PRK00934 |
PRK00934 |
ribose-phosphate pyrophosphokinase; Provisional |
364-397 |
1.35e-03 |
|
ribose-phosphate pyrophosphokinase; Provisional
Pssm-ID: 234868 [Multi-domain] Cd Length: 285 Bit Score: 40.67 E-value: 1.35e-03
10 20 30
....*....|....*....|....*....|....
gi 17554892 364 GQRIVLVDDSIVRGNTMRTLVKMLRDAGAKEVHL 397
Cdd:PRK00934 204 GKDVLIVDDIISTGGTMATAIKILKEQGAKKVYV 237
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-182 |
1.57e-03 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 41.02 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554892 1 MCGIFGIVaagNY-------EHLNVLAaNGLAALQHRGTESTGLVGSDGITRDHVEI------IKGHGLVRDViteDNIS 67
Cdd:PTZ00394 1 MCGIFGYA---NHnvprtveQILNVLL-DGIQKVEYRGYDSAGLAIDANIGSEKEDGtaasapTPRPCVVRSV---GNIS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554892 68 R----------------MNGQS---IIIGHNRYSTAGKKkSGINCvQPfvVYTAMGTVAIAHNGELVDAKQKRKEVLHEG 128
Cdd:PTZ00394 74 QlrekvfseavaatlppMDATTshhVGIAHTRWATHGGV-CERNC-HP--QQSNNGEFTIVHNGIVTNYMTLKELLKEEG 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 17554892 129 VGLSTDTDSELIAQMIAKAIALNVKCKYGQEMGDITRElavtmsaLNMSYSLLV 182
Cdd:PTZ00394 150 YHFSSDTDTEVISVLSEYLYTRKGIHNFADLALEVSRM-------VEGSYALLV 196
|
|
| PRK02277 |
PRK02277 |
orotate phosphoribosyltransferase-like protein; Provisional |
334-395 |
1.73e-03 |
|
orotate phosphoribosyltransferase-like protein; Provisional
Pssm-ID: 235023 [Multi-domain] Cd Length: 200 Bit Score: 39.47 E-value: 1.73e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17554892 334 YVGRSFIEPNDEMRQNAIKMKFGvlkkKIHGQRIVLVDDSIVRGNTMRTLVKMLRDAGAKEV 395
Cdd:PRK02277 114 YHPKKWDHGEGEKKTGSFSRNFA----SVEGKRCVIVDDVITSGTTMKETIEYLKEHGGKPV 171
|
|
| PRK02304 |
PRK02304 |
adenine phosphoribosyltransferase; Provisional |
345-393 |
1.98e-03 |
|
adenine phosphoribosyltransferase; Provisional
Pssm-ID: 235028 Cd Length: 175 Bit Score: 39.29 E-value: 1.98e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 17554892 345 EMRQNAIKmkfgvlkkkiHGQRIVLVDDSIVRGNTMRTLVKMLRDAGAK 393
Cdd:PRK02304 105 EIHKDAIK----------PGDRVLIVDDLLATGGTLEAAIKLLERLGAE 143
|
|
| PRK07322 |
PRK07322 |
adenine phosphoribosyltransferase; Provisional |
361-395 |
2.42e-03 |
|
adenine phosphoribosyltransferase; Provisional
Pssm-ID: 180928 Cd Length: 178 Bit Score: 38.81 E-value: 2.42e-03
10 20 30
....*....|....*....|....*....|....*
gi 17554892 361 KIHGQRIVLVDDSIVRGNTMRTLVKMLRDAGAKEV 395
Cdd:PRK07322 117 KLKGKRVAIVDDVVSTGGTLTALERLVERAGGQVV 151
|
|
| Pribosyltran |
pfam00156 |
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ... |
364-397 |
3.26e-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: 38.11 E-value: 3.26e-03
10 20 30
....*....|....*....|....*....|....
gi 17554892 364 GQRIVLVDDSIVRGNTMRTLVKMLRDAGAKEVHL 397
Cdd:pfam00156 82 GKTVLIVDDILDTGGTLLKVLELLKNVGPKEVKI 115
|
|
| COG1926 |
COG1926 |
Predicted phosphoribosyltransferase [General function prediction only]; |
362-395 |
5.38e-03 |
|
Predicted phosphoribosyltransferase [General function prediction only];
Pssm-ID: 441529 Cd Length: 209 Bit Score: 38.13 E-value: 5.38e-03
10 20 30
....*....|....*....|....*....|....
gi 17554892 362 IHGQRIVLVDDSIVRGNTMRTLVKMLRDAGAKEV 395
Cdd:COG1926 119 LKGRTVILVDDGIATGATMRAALRALRRQGPARI 152
|
|
| PrsA |
COG0462 |
Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; ... |
362-396 |
7.92e-03 |
|
Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; Phosphoribosylpyrophosphate synthetase is part of the Pathway/BioSystem: Histidine biosynthesis, Purine biosynthesis
Pssm-ID: 440230 [Multi-domain] Cd Length: 311 Bit Score: 38.12 E-value: 7.92e-03
10 20 30
....*....|....*....|....*....|....*
gi 17554892 362 IHGQRIVLVDDSIVRGNTMRTLVKMLRDAGAKEVH 396
Cdd:COG0462 209 VEGKTCIIVDDMIDTGGTLVEAAEALKEAGAKSVY 243
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