|
Name |
Accession |
Description |
Interval |
E-value |
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
19-481 |
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: 789.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1968689742 19 PQDACGVFGVWAPgEEVAKLTYYGLYALQHRGQEAAGIATSDGHSLLVYKDVGLVSQVFDESSLASLRGHLAVGHCRYST 98
Cdd:COG0034 4 LHEECGVFGIYGH-EDVAQLTYYGLYALQHRGQESAGIATSDGGRFHLHKGMGLVSDVFDEEDLERLKGNIAIGHVRYST 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1968689742 99 TGRNTWENAQPTLGGTEDQTVALAHNGNLINTSELRDRLAEiYGGDLNNapgevrrgnTTDTALVTGLL-TADPDLSLEA 177
Cdd:COG0034 83 TGSSSLENAQPFYVNSPFGSIALAHNGNLTNAEELREELEE-EGAIFQT---------TSDTEVILHLIaRELTKEDLEE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1968689742 178 SALQVLPTLRGAFSLVFCDEQTLYAARDPQGVRPLVLGRLERGWVVSSETSGLDIVGASFVREIEPGELIAIDQNGLRTQ 257
Cdd:COG0034 153 AIKEALRRVKGAYSLVILTGDGLIAARDPNGIRPLVLGKLEDGYVVASESCALDILGAEFVRDVEPGEIVVIDEDGLRSR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1968689742 258 RFAE-ADRKGCVFEYVYLARPDTSLNGRGVYESRVEMGRTLAREHPVEADMVMPTPESGTPAAIGYAEQSGIPYGAGLVK 336
Cdd:COG0034 233 QFAEkPRPAPCIFEYVYFARPDSVIDGRSVYEARKRMGRELAREAPVDADVVIPVPDSGRPAAIGYAEESGIPYEEGLIK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1968689742 337 NAYVGRTFIAPSQTIRQLGIRLKLNPLRDVIRGKRLVVVDDSIVRGNTQRALVRMLREAGAAEVHVRISSPPVRWPCFYG 416
Cdd:COG0034 313 NRYVGRTFIQPTQELRELGVRLKLNPIREVVKGKRVVLVDDSIVRGTTSRRIVKMLREAGAKEVHFRIASPPIRYPCYYG 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1968689742 417 IDFATRAELIATGLGVEDIRQSIGADSLGYISEEGMVAATHQERDQLCTACFSGVYPIELPEAEK 481
Cdd:COG0034 393 IDTPTREELIAANRSVEEIREYIGADSLGYLSLEGLIEAVGEPIEGFCTACFTGDYPTGIPDEEK 457
|
|
| purF |
TIGR01134 |
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ... |
23-473 |
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: 629.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1968689742 23 CGVFGVWAPGEEVAKLTYYGLYALQHRGQEAAGIATSDGHSLLVYKDVGLVSQVFDESSLASLRGHLAVGHCRYSTTGRN 102
Cdd:TIGR01134 1 CGVVGIYGQEEVAASLTYYGLYALQHRGQESAGISVFDGNRFRLHKGNGLVSDVFNEEHLQRLKGNVGIGHVRYSTAGSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1968689742 103 TWENAQPTLGGTEDQTVALAHNGNLINTSELRDRLAEiyggdlnnapgEVRRGNTTDTALVTGLLTADPDLS---LEASA 179
Cdd:TIGR01134 81 GLENAQPFVVNSPYGGLALAHNGNLVNADELRRELEE-----------EGRHFNTTSDSEVLLHLLAHNDESkddLFDAV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1968689742 180 LQVLPTLRGAFSLVFCDEQTLYAARDPQGVRPLVLGRLERGWVVSSETSGLDIVGASFVREIEPGELIAIDQNGLRTQRF 259
Cdd:TIGR01134 150 ARVLERVRGAYALVLMTEDGLVAVRDPHGIRPLVLGRRGDGYVVASESCALDILGAEFVRDVEPGEVVVIFDGGLESRQC 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1968689742 260 AEADRKGCVFEYVYLARPDTSLNGRGVYESRVEMGRTLAREHPVEADMVMPTPESGTPAAIGYAEQSGIPYGAGLVKNAY 339
Cdd:TIGR01134 230 ARRPRAPCVFEYVYFARPDSVIDGISVYYARKRMGKELARESPVEADVVVPVPDSGRSAALGFAQASGIPYREGLIKNRY 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1968689742 340 VGRTFIAPSQTIRQLGIRLKLNPLRDVIRGKRLVVVDDSIVRGNTQRALVRMLREAGAAEVHVRISSPPVRWPCFYGIDF 419
Cdd:TIGR01134 310 VGRTFIMPTQELRELSVRLKLNPVRAVFEGKRVVLVDDSIVRGTTSRQIVEMLRDAGAKEVHVRIASPPIRYPCYYGIDM 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1968689742 420 ATRAELIATGLGVEDIRQsIGADSLGYISEEGMVAATHQERDQLCTACFSGVYP 473
Cdd:TIGR01134 390 PTREELIAARRTVEEIRK-IGADSLAYLSLEGLKEAVGNPESDLCLACFTGEYP 442
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
13-481 |
0e+00 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 607.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1968689742 13 MPDEKVPQDACGVFGVWAPGE-EVAKLTYYGLYALQHRGQEAAGIATSDGHSLLVYKDVGLVSQVFDESSLASLRGHLAV 91
Cdd:PRK05793 5 DLEGDKFKEECGVFGVFSKNNiDVASLTYYGLYALQHRGQESAGIAVSDGEKIKVHKGMGLVSEVFSKEKLKGLKGNSAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1968689742 92 GHCRYSTTGRNTWENAQPTLGGTEDQTVALAHNGNLINTSELRDRLAEiyGGDLNNApgevrrgnTTDTALVTGLLTADP 171
Cdd:PRK05793 85 GHVRYSTTGASDLDNAQPLVANYKLGSIAIAHNGNLVNADVIRELLED--GGRIFQT--------SIDSEVILNLIARSA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1968689742 172 DLSLEASALQVLPTLRGAFSLVFCDEQTLYAARDPQGVRPLVLGRLERGWVVSSETSGLDIVGASFVREIEPGELIAIDQ 251
Cdd:PRK05793 155 KKGLEKALVDAIQAIKGSYALVILTEDKLIGVRDPHGIRPLCLGKLGDDYILSSESCALDTIGAEFIRDVEPGEIVIIDE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1968689742 252 NGLRTQRFAEADR-KGCVFEYVYLARPDTSLNGRGVYESRVEMGRTLAREHPVEADMVMPTPESGTPAAIGYAEQSGIPY 330
Cdd:PRK05793 235 DGIKSIKFAEKTKcQTCAFEYIYFARPDSVIDGISVYESRVRAGRQLYKEYPVDADIVIGVPDSGIPAAIGYAEASGIPY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1968689742 331 GAGLVKNAYVGRTFIAPSQTIRQLGIRLKLNPLRDVIRGKRLVVVDDSIVRGNTQRALVRMLREAGAAEVHVRISSPPVR 410
Cdd:PRK05793 315 GIGFIKNKYVGRTFIAPSQELRERAVRVKLNPLKVNVEGKRVVLIDDSIVRGTTSKRLVELLRKAGAKEVHFRVSSPPVK 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1968689742 411 WPCFYGIDFATRAELIATGLGVEDIRQSIGADSLGYISEEGMVAAThQERDQLCTACFSGVYPIELP-EAEK 481
Cdd:PRK05793 395 YPCYFGIDTPYRKELIGANMSVEEIREMIGADSLGYLSIEGLLESL-NGDKGFCLGCFNGVYPVSAPkEGPK 465
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
23-486 |
4.43e-179 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 512.30 E-value: 4.43e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1968689742 23 CGVFGVWApGEEVAKLTYYGLYALQHRGQEAAGIATSDGHSLLVYKDVGLVSQVFDESSLASLRGHLAVGHCRYSTTGRN 102
Cdd:PLN02440 2 CGVVGIFG-DPEASRLCYLGLHALQHRGQEGAGIVTVDGNRLQSITGNGLVSDVFDESKLDQLPGDIAIGHVRYSTAGAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1968689742 103 TWENAQPTLGGTEDQTVALAHNGNLINTSELRDRLaEIYGGDLNNapgevrrgnTTDTALVTGLLTADPDLSLEASALQV 182
Cdd:PLN02440 81 SLKNVQPFVANYRFGSIGVAHNGNLVNYEELRAKL-EENGSIFNT---------SSDTEVLLHLIAISKARPFFSRIVDA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1968689742 183 LPTLRGAFSLVFCDEQTLYAARDPQGVRPLVLGRLERG-WVVSSETSGLDIVGASFVREIEPGELIAIDQNGLRTQRFA- 260
Cdd:PLN02440 151 CEKLKGAYSMVFLTEDKLVAVRDPHGFRPLVMGRRSNGaVVFASETCALDLIGATYEREVNPGEVIVVDKDKGVSSQCLm 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1968689742 261 -EADRKGCVFEYVYLARPDTSLNGRGVYESRVEMGRTLAREHPVEADMVMPTPESGTPAAIGYAEQSGIPYGAGLVKNAY 339
Cdd:PLN02440 231 pHPEPKPCIFEHIYFARPNSIVFGRSVYESRLEFGEILATEIPVDCDVVIPVPDSGRVAALGYAAKLGVPFQQGLIRSHY 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1968689742 340 VGRTFIAPSQTIRQLGIRLKLNPLRDVIRGKRLVVVDDSIVRGNTQRALVRMLREAGAAEVHVRISSPPVRWPCFYGIDF 419
Cdd:PLN02440 311 VGRTFIEPSQKIRDFSVKLKLNPVRSVLEGKRVVVVDDSIVRGTTSSKIVRMLREAGAKEVHMRIASPPIIASCYYGVDT 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1968689742 420 ATRAELIATGLGVEDIRQSIGADSLGYISEEGMVAATHQERDQLCTACFSGVYPIELPEaekLGKDV 486
Cdd:PLN02440 391 PSREELISNRMSVEEIRKFIGCDSLAFLPLEDLKKSLGEESPRFCYACFSGDYPVLPKR---VGGDI 454
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
23-282 |
8.71e-118 |
|
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: 347.53 E-value: 8.71e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1968689742 23 CGVFGVWAPgEEVAKLTYYGLYALQHRGQEAAGIATSDGHSLLVYKDVGLVSQVFDESSLASLRGHLAVGHCRYSTTGRN 102
Cdd:cd00715 1 CGVFGIYGA-EDAARLTYLGLYALQHRGQESAGIATSDGKRFHTHKGMGLVSDVFDEEKLRRLPGNIAIGHVRYSTAGSS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1968689742 103 TWENAQPTLGGTEDQTVALAHNGNLINTSELRDRLAEiyggdlnnapgEVRRGNTT-DTALVTGLL-TADPDLSLEASAL 180
Cdd:cd00715 80 SLENAQPFVVNSPLGGIALAHNGNLVNAKELREELEE-----------EGRIFQTTsDSEVILHLIaRSLAKDDLFEAII 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1968689742 181 QVLPTLRGAFSLVFCDEQTLYAARDPQGVRPLVLGRLER-GWVVSSETSGLDIVGASFVREIEPGELIAIDQNGLRT-QR 258
Cdd:cd00715 149 DALERVKGAYSLVIMTADGLIAVRDPHGIRPLVLGKLEGdGYVVASESCALDIIGAEFVRDVEPGEIVVIDDDGLESsQR 228
|
250 260
....*....|....*....|....
gi 1968689742 259 FAEADRKGCVFEYVYLARPDTSLN 282
Cdd:cd00715 229 APKPKPAPCIFEYVYFARPDSVID 252
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
23-247 |
5.73e-55 |
|
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: 184.19 E-value: 5.73e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1968689742 23 CGVFGVWAPGEEVAKLTY---YGLYALQHRGQEAAGIATSDGHSLLVYKDVGLVSQVFDESSLASLRGHLAVGHCRYSTT 99
Cdd:cd00352 1 CGIFGIVGADGAASLLLLlllRGLAALEHRGPDGAGIAVYDGDGLFVEKRAGPVSDVALDLLDEPLKSGVALGHVRLATN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1968689742 100 GRNTWENAQPTLGgtEDQTVALAHNGNLINTSELRDRLAEIYggdlnnapgeVRRGNTTDTALVTGLLTADPDLS-LEAS 178
Cdd:cd00352 81 GLPSEANAQPFRS--EDGRIALVHNGEIYNYRELREELEARG----------YRFEGESDSEVILHLLERLGREGgLFEA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1968689742 179 ALQVLPTLRGAFSLVFCD--EQTLYAARDPQGVRPLVLGRLERG-WVVSSETSGLDIVGASFVREIEPGELI 247
Cdd:cd00352 149 VEDALKRLDGPFAFALWDgkPDRLFAARDRFGIRPLYYGITKDGgLVFASEPKALLALPFKGVRRLPPGELL 220
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
23-230 |
1.72e-20 |
|
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: 89.81 E-value: 1.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1968689742 23 CGVFGVWAPGEeVAKLTYYGLYALQHRGQEAAGIATSDGHSLLVYKDVGLVSQVFDESSLASLRGHLAVGHCRYSTTGRN 102
Cdd:cd00714 1 CGIVGYIGKRE-AVDILLEGLKRLEYRGYDSAGIAVIGDGSLEVVKAVGKVANLEEKLAEKPLSGHVGIGHTRWATHGEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1968689742 103 TWENAQPTLggTEDQTVALAHNGNLINTSELRDRLAEiyggdlnnapgevrRGNT----TDTA----LVTGLLTADPDls 174
Cdd:cd00714 80 TDVNAHPHR--SCDGEIAVVHNGIIENYAELKEELEA--------------KGYKfeseTDTEviahLIEYYYDGGLD-- 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1968689742 175 LEASALQVLPTLRGAFSLVF---CDEQTLYAARdpQGvRPLVLGRLERGWVVSSETSGL 230
Cdd:cd00714 142 LLEAVKKALKRLEGAYALAViskDEPDEIVAAR--NG-SPLVIGIGDGENFVASDAPAL 197
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
23-247 |
1.34e-18 |
|
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: 85.40 E-value: 1.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1968689742 23 CGVFGVWAPGEE--VAKLTYYGLYALQHRG-QEAAGIAT---------SDGHSLLVYKDVGLVSQVFDESSLASLRGHLA 90
Cdd:cd01907 1 CGIFGIMSKDGEpfVGALLVEMLDAMQERGpGDGAGFALygdpdafvySSGKDMEVFKGVGYPEDIARRYDLEEYKGYHW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1968689742 91 VGHCRYSTTGRNTWENAQP-TLGGtedqtVALAHNGNLINTSELRDRLaEIYGGdlnnapgevRRGNTTDTALVTGLLT- 168
Cdd:cd01907 81 IAHTRQPTNSAVWWYGAHPfSIGD-----IAVVHNGEISNYGSNREYL-ERFGY---------KFETETDTEVIAYYLDl 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1968689742 169 --ADPDLSLEASALQVLPT------------------LRGAFSLVFCDEQTLYAARDPQGVRPLVLGRLERGWVVSSETS 228
Cdd:cd01907 146 llRKGGLPLEYYKHIIRMPeeerelllalrltyrladLDGPFTIIVGTPDGFIVIRDRIKLRPAVVAETDDYVAIASEEC 225
|
250 260
....*....|....*....|..
gi 1968689742 229 GLDIVGAS---FVREIEPGELI 247
Cdd:cd01907 226 AIREIPDRdnaKVWEPRPGEYV 247
|
|
| PRTases_typeI |
cd06223 |
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ... |
293-419 |
7.98e-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: 79.75 E-value: 7.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1968689742 293 MGRTLAREHP---VEADMVMPTPESGTPAAIGYAEQSGIPYGAGLVKNAYVGRTFIAPSQtirqlgirlKLNPLRDVIRG 369
Cdd:cd06223 1 AGRLLAEEIRedlLEPDVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSEPYG---------LELPLGGDVKG 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1968689742 370 KRLVVVDDSIVRGNTQRALVRMLREAGAAEVHVrISSPPVRWPCFYGIDF 419
Cdd:cd06223 72 KRVLLVDDVIATGGTLLAAIELLKEAGAKVVGV-AVLLDKPEGGARELAS 120
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
23-255 |
2.47e-16 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 82.01 E-value: 2.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1968689742 23 CGVFGVWAPgEEVAKLTYYGLYALQHRGQEAAGIATSDGHSLLVYKDVGLVSQVFDESSLASLRGHLAVGHCRYSTTGRN 102
Cdd:PRK00331 2 CGIVGYVGQ-RNAAEILLEGLKRLEYRGYDSAGIAVLDDGGLEVRKAVGKVANLEAKLEEEPLPGTTGIGHTRWATHGKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1968689742 103 TWENAQPTLGGTEDqtVALAHNGNLINTSELRDRLAEiyggdlnnapgevrRGNT----TDTALVTGLLT--ADPDLSLE 176
Cdd:PRK00331 81 TERNAHPHTDCSGR--IAVVHNGIIENYAELKEELLA--------------KGHVfkseTDTEVIAHLIEeeLKEGGDLL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1968689742 177 ASALQVLPTLRGAFSLVFCDEQ---TLYAARdpQGVrPLVLGRLERGWVVSSETSGLdivgASFVREI---EPGELIAID 250
Cdd:PRK00331 145 EAVRKALKRLEGAYALAVIDKDepdTIVAAR--NGS-PLVIGLGEGENFLASDALAL----LPYTRRViylEDGEIAVLT 217
|
....*
gi 1968689742 251 QNGLR 255
Cdd:PRK00331 218 RDGVE 222
|
|
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
23-260 |
2.65e-16 |
|
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: 81.98 E-value: 2.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1968689742 23 CGVFGVWAPgEEVAKLTYYGLYALQHRGQEAAGIATSDGHSLLVYKDVGLVSQVFDESSLASLRGHLAVGHCRYSTTGRN 102
Cdd:COG0449 2 CGIVGYIGK-RDAAPILLEGLKRLEYRGYDSAGIAVLDDGGLEVRKAVGKLANLEEKLAEEPLSGTIGIGHTRWATHGAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1968689742 103 TWENAQPTLGGTEDqtVALAHNGnlI--NTSELRDRLAEiyggdlnnapgevrRGNT----TDT----ALVTGLLTADPD 172
Cdd:COG0449 81 SDENAHPHTSCSGR--IAVVHNG--IieNYAELREELEA--------------KGHTfkseTDTeviaHLIEEYLKGGGD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1968689742 173 lsLEASALQVLPTLRGAFSLVFCDEQ---TLYAARdpQGVrPLVLGRLERGWVVSSETSGLdivgASFVREI---EPGEL 246
Cdd:COG0449 143 --LLEAVRKALKRLEGAYALAVISADepdRIVAAR--KGS-PLVIGLGEGENFLASDVPAL----LPYTRRViylEDGEI 213
|
250
....*....|....
gi 1968689742 247 IAIDQNGLRTQRFA 260
Cdd:COG0449 214 AVLTRDGVEIYDLD 227
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
23-259 |
5.69e-13 |
|
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: 68.35 E-value: 5.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1968689742 23 CGVFGVWAPG------EEVAKLtyygLYALQHRGQEAAGIATSDGhsllvykdVGLvsqvfdesslaslrghlavGHCRY 96
Cdd:cd00712 1 CGIAGIIGLDgasvdrATLERM----LDALAHRGPDGSGIWIDEG--------VAL-------------------GHRRL 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1968689742 97 STTGRNTWenAQPTLGgtEDQTVALAHNGNLINTSELRDRLAeiyggdlnnAPGEVRRGNTtDTALvtgLLTAdpdlsLE 176
Cdd:cd00712 50 SIIDLSGG--AQPMVS--EDGRLVLVFNGEIYNYRELRAELE---------ALGHRFRTHS-DTEV---ILHL-----YE 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1968689742 177 ASALQVLPTLRGAFSLVFCD--EQTLYAARDPQGVRPLVLGRLERGWVVSSETSGL----------DIVGASF------- 237
Cdd:cd00712 108 EWGEDCLERLNGMFAFALWDkrKRRLFLARDRFGIKPLYYGRDGGGLAFASELKALlalpgvprelDEAALAEylafqyv 187
|
250 260 270
....*....|....*....|....*....|.
gi 1968689742 238 ---------VREIEPGELIAIDQNGLRTQRF 259
Cdd:cd00712 188 paprtifkgIRKLPPGHYLTVDPGGVEIRRY 218
|
|
| YafJ |
COG0121 |
Predicted glutamine amidotransferase YafJ [General function prediction only]; |
55-253 |
6.87e-13 |
|
Predicted glutamine amidotransferase YafJ [General function prediction only];
Pssm-ID: 439891 [Multi-domain] Cd Length: 248 Bit Score: 68.45 E-value: 6.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1968689742 55 GIAT-SDGHSLLVYKDVGLVsqvFDESSLASL----RGHLAVGHCRYSTTGRNTWENAQPTLGGTedqtVALAHNGNLIN 129
Cdd:COG0121 42 GIGWyEGDGEPRLYRDPLPA---WSDPNLRLLarpiKSRLVIAHVRKATVGPVSLENTHPFRGGR----WLFAHNGQLDG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1968689742 130 TSELRDRLAEiyggDLNNAPGEVRRGnTTDT----ALVTGLLTADPDLSLEA-----SALQVLPTLRGAFSLVFCDEQTL 200
Cdd:COG0121 115 FDRLRRRLAE----ELPDELYFQPVG-TTDSelafALLLSRLRDGGPDPAEAlaealRELAELARAPGRLNLLLSDGERL 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1968689742 201 YAARDPQGVRPLVLGRLER------GWVVSSETsgLDIvGASFvREIEPGELIAIDQNG 253
Cdd:COG0121 190 YATRYTSDDPYPTLYYLTRttpddrVVVVASEP--LTD-DEGW-TEVPPGELLVVRDGL 244
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
86-226 |
2.41e-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: 64.25 E-value: 2.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1968689742 86 RGHLAVGHCRYSTTGRNTwENAQPTLggTEDQTVALAHNGNLINTSELRDRLAeiyggdlnnAPGEVRRGNTtDTALvtg 165
Cdd:pfam13522 9 EGGVALGHVRLAIVDLPD-AGNQPML--SRDGRLVLVHNGEIYNYGELREELA---------DLGHAFRSRS-DTEV--- 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1968689742 166 LLTADPDLsleasALQVLPTLRGAFSLVF--CDEQTLYAARDPQGVRPLVLGRLERGWVVSSE 226
Cdd:pfam13522 73 LLALYEEW-----GEDCLERLRGMFAFAIwdRRRRTLFLARDRLGIKPLYYGILGGGFVFASE 130
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
23-230 |
2.62e-12 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 69.28 E-value: 2.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1968689742 23 CGVFGVWApGEEVAKLTYYGLYALQHRGQEAAGIAT-SDGHSLLV--YKDVGLVSQVFD---ESSLASLRG-HLAVGHCR 95
Cdd:PTZ00295 25 CGIVGYLG-NEDASKILLEGIEILQNRGYDSCGISTiSSGGELKTtkYASDGTTSDSIEilkEKLLDSHKNsTIGIAHTR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1968689742 96 YSTTGRNTWENAQPTLggTEDQTVALAHNGNLINTSELRDRLAEiyggdlnnaPGEVRRGNtTDTALVTGL--LTADPDL 173
Cdd:PTZ00295 104 WATHGGKTDENAHPHC--DYKKRIALVHNGTIENYVELKSELIA---------KGIKFRSE-TDSEVIANLigLELDQGE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1968689742 174 SLEASALQVLPTLRGAFSLVF---CDEQTLYAARdpQGvRPLVLGRLERGWVVSSETSGL 230
Cdd:PTZ00295 172 DFQEAVKSAISRLQGTWGLCIihkDNPDSLIVAR--NG-SPLLVGIGDDSIYVASEPSAF 228
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
107-226 |
2.91e-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: 433289 [Multi-domain] Cd Length: 123 Bit Score: 60.61 E-value: 2.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1968689742 107 AQPtLGGTEDQTVALAHNGNLINTSELRDRLAeiyggdlnnAPGEVRRGnTTDTALVTGLLTadpdlslEASALQVLPTL 186
Cdd:pfam13537 13 AQP-MVSSEDGRYVIVFNGEIYNYRELRAELE---------AKGYRFRT-HSDTEVILHLYE-------AEWGEDCVDRL 74
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1968689742 187 RG--AFSLVFCDEQTLYAARDPQGVRPLVLGRLE-RGWVVSSE 226
Cdd:pfam13537 75 NGmfAFAIWDRRRQRLFLARDRFGIKPLYYGRDDgGRLLFASE 117
|
|
| YafJ |
cd01908 |
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ... |
55-252 |
8.53e-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: 62.41 E-value: 8.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1968689742 55 GIA--TSDGHSLLVYKDVGLV-SQVFDESSLASLRGHLAVGHCRYSTTGRNTWENAQPTlggTEDQtVALAHNGNLINTS 131
Cdd:cd01908 45 GIGwyEGKGGRPFRYRSPLPAwSDINLESLARPIKSPLVLAHVRAATVGPVSLENCHPF---TRGR-WLFAHNGQLDGFR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1968689742 132 ELRDRLAEIYGGdlnnapgevRRGNTTDT----ALVTGLLTADPDLSLEASALQVLPTLR--------GAFSLVFCDEQT 199
Cdd:cd01908 121 LLRRRLLRLLPR---------LPVGTTDSelafALLLSRLLERDPLDPAELLDAILQTLRelaalappGRLNLLLSDGEY 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1968689742 200 LYAAR-------------DPQGVRPLVLGRL----ERGWVVSSETSGLDIVgasfVREIEPGELIAIDQN 252
Cdd:cd01908 192 LIATRyasapslyyltrrAPFGCARLLFRSVttpnDDGVVVASEPLTDDEG----WTEVPPGELVVVSEG 257
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
23-259 |
2.03e-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: 59.85 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1968689742 23 CGVFGVWAPG-----EEVAKLTYyglyALQHRGQEAAGIATSdghsllvykdvglvsqvfdesslaslrGHLAVGHCRYS 97
Cdd:COG0367 2 CGIAGIIDFDggadrEVLERMLD----ALAHRGPDGSGIWVD---------------------------GGVALGHRRLS 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1968689742 98 TTGrntwenaqPTLGG-----TEDQTVALAHNGNLINTSELRDRLAeiyggdlnnAPGEVRRGNTtDTALvtgLLTAdpd 172
Cdd:COG0367 51 IID--------LSEGGhqpmvSEDGRYVLVFNGEIYNYRELRAELE---------ALGHRFRTHS-DTEV---ILHA--- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1968689742 173 lsLEASALQVLPTLRGAFSLVFCD--EQTLYAARDPQGVRPLVLGRLERGWVVSSE----------TSGLDIVG------ 234
Cdd:COG0367 107 --YEEWGEDCLERLNGMFAFAIWDrrERRLFLARDRFGIKPLYYAEDGGGLAFASElkallahpgvDRELDPEAlaeylt 184
|
250 260 270
....*....|....*....|....*....|....*.
gi 1968689742 235 -------ASF---VREIEPGELIAIDQNG-LRTQRF 259
Cdd:COG0367 185 lgyvpapRTIfkgIRKLPPGHYLTVDAGGeLEIRRY 220
|
|
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
23-194 |
7.06e-08 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 55.14 E-value: 7.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1968689742 23 CGVFGVW---APGE--EVAKLTYYGLYALQHRGQEAAGIATSDGHSL-----LVYKDVG----LVSQVFDESSLASL--- 85
Cdd:PLN02981 2 CGIFAYLnynVPRErrFILEVLFNGLRRLEYRGYDSAGIAIDNDPSLessspLVFREEGkiesLVRSVYEEVAETDLnld 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1968689742 86 ---RGHLAVGHCRYSTTGRNTWENAQPTLGGTEDQTVaLAHNGNLINTSELRDRLaeiyggdlnnapgeVRRGNT----T 158
Cdd:PLN02981 82 lvfENHAGIAHTRWATHGPPAPRNSHPQSSGPGNEFL-VVHNGIITNYEVLKETL--------------LRHGFTfesdT 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1968689742 159 DTALVTGLLT--------ADPDLSLEASALQVLPTLRGAFSLVF 194
Cdd:PLN02981 147 DTEVIPKLAKfvfdklneEEGDVTFSQVVMEVMRQLEGAYALIF 190
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
107-231 |
1.32e-07 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 54.33 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1968689742 107 AQPTLggTEDQTVALAHNGNLINTSELRDRL-AEIYggdlnnapgevRRGNTTDTALVtglltadPDLSLEASALQVLPT 185
Cdd:PTZ00077 65 KQPLL--DDDETVALMQNGEIYNHWEIRPELeKEGY-----------KFSSNSDCEII-------GHLYKEYGPKDFWNH 124
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1968689742 186 LRGAFSLVFCD--EQTLYAARDPQGVRPLVLGRLERGWV-VSSETSGLD 231
Cdd:PTZ00077 125 LDGMFATVIYDmkTNTFFAARDHIGIIPLYIGYAKDGSIwFSSELKALH 173
|
|
| PRK07322 |
PRK07322 |
adenine phosphoribosyltransferase; Provisional |
294-397 |
1.77e-04 |
|
adenine phosphoribosyltransferase; Provisional
Pssm-ID: 180928 Cd Length: 178 Bit Score: 42.27 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1968689742 294 GRTLAREHPVEADMVMpTPE-SGTPAAIGYAEQSGIPYgagLV--KN--AYVGRTFIAPSQTI----RQLgirLKLNPlR 364
Cdd:PRK07322 42 AEALAKRLPTEVDVLV-TPEtKGIPLAHALSRRLGKPY---VVarKSrkPYMQDPIIQEVVSIttgkPQL---LVLDG-A 113
|
90 100 110
....*....|....*....|....*....|....*
gi 1968689742 365 DV--IRGKRLVVVDDSIVRGNTQRALVRMLREAGA 397
Cdd:PRK07322 114 DAekLKGKRVAIVDDVVSTGGTLTALERLVERAGG 148
|
|
| Hpt1 |
COG2236 |
Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine ... |
362-402 |
3.10e-04 |
|
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: 41.37 E-value: 3.10e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1968689742 362 PLRDVIRGKRLVVVDDSIVRGNTQRALVRMLREAGAAEVHV 402
Cdd:COG2236 81 PLDEDLAGKRVLIVDDVADTGRTLEAVRDLLKEAGPAEVRT 121
|
|
| PLN02238 |
PLN02238 |
hypoxanthine phosphoribosyltransferase |
357-402 |
5.80e-04 |
|
hypoxanthine phosphoribosyltransferase
Pssm-ID: 215132 Cd Length: 189 Bit Score: 41.18 E-value: 5.80e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1968689742 357 RLKLNPLRDVIRGKRLVVVDDSIVRGNTQRALVRMLREAGAAEVHV 402
Cdd:PLN02238 85 KVSGADLKIDVKGKHVLLVEDIVDTGNTLSALVAHLEAKGAASVSV 130
|
|
| Gn_AT_II_novel |
cd03766 |
Gn_AT_II_novel. This asparagine synthase-related domain is present in eukaryotes but its ... |
139-244 |
8.50e-04 |
|
Gn_AT_II_novel. This asparagine synthase-related domain is present in eukaryotes but its function has not yet been determined. 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: 239735 [Multi-domain] Cd Length: 181 Bit Score: 40.35 E-value: 8.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1968689742 139 EIYGGDlnnapGEVRRGNttDTALVTGLLTADPdlSLEASALQVLPTLRGAFSLVF--CDEQTLYAARDPQGVRPLVLGR 216
Cdd:cd03766 81 ELYNID-----GVEDEEN--DTEVIFELLANCS--SESQDILDVLSSIEGPFAFIYydASENKLYFGRDCLGRRSLLYKL 151
|
90 100 110
....*....|....*....|....*....|
gi 1968689742 217 LERG--WVVSSETSGLDIVGAsfvREIEPG 244
Cdd:cd03766 152 DPNGfeLSISSVSGSSSGSGF---QEVLAG 178
|
|
| ComFC |
COG1040 |
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General ... |
293-402 |
1.95e-03 |
|
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General function prediction only];
Pssm-ID: 440662 [Multi-domain] Cd Length: 196 Bit Score: 39.42 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1968689742 293 MGRTLAREHPVEADMVMPTPesGTPAAI---GY----------AEQSGIPYGAGLVKnayvgRTFIAPSQTirQLGIRLK 359
Cdd:COG1040 67 LARALREALLPRPDLIVPVP--LHRRRLrrrGFnqaellaralARALGIPVLPDLLR-----RVRATPSQA--GLSRAER 137
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1968689742 360 LNPLRDV--------IRGKRLVVVDDsiVR--GNTQRALVRMLREAGAAEVHV 402
Cdd:COG1040 138 RRNLRGAfavrpparLAGKHVLLVDD--VLttGATLAEAARALKAAGAARVDV 188
|
|
| PRK08558 |
PRK08558 |
adenine phosphoribosyltransferase; Provisional |
368-397 |
4.47e-03 |
|
adenine phosphoribosyltransferase; Provisional
Pssm-ID: 181466 [Multi-domain] Cd Length: 238 Bit Score: 38.82 E-value: 4.47e-03
10 20 30
....*....|....*....|....*....|
gi 1968689742 368 RGKRLVVVDDSIVRGNTQRALVRMLREAGA 397
Cdd:PRK08558 175 KGDRVLIVDDIIRSGETQRALLDLARQAGA 204
|
|
| Pribosyltran |
pfam00156 |
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ... |
327-401 |
4.62e-03 |
|
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl transferase enzymes. This family includes: Adenine phosphoribosyl-transferase EC:2.4.2.7. Hypoxanthine-guanine-xanthine phosphoribosyl-transferase. Hypoxanthine phosphoribosyl-transferase EC:2.4.2.8. Ribose-phosphate pyrophosphokinase i EC:2.7.6.1. Amidophosphoribosyltransferase EC:2.4.2.14. Orotate phosphoribosyl-transferase EC:2.4.2.10. Uracil phosphoribosyl-transferase EC:2.4.2.9. Xanthine-guanine phosphoribosyl-transferase EC:2.4.2.22. In Arabidopsis, At the very N-terminus of this domain is the P-Loop NTPase domain.
Pssm-ID: 425489 [Multi-domain] Cd Length: 150 Bit Score: 37.73 E-value: 4.62e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1968689742 327 GIPYGAGLVKNAYVGRTFIAPSQTIRQLGIRLKLNPLRDVIRGKRLVVVDDSIVRGNTQRALVRMLREAGAAEVH 401
Cdd:pfam00156 40 GLPFAGILARRLDVPLAFVRKVSYNPDTSEVMKTSSALPDLKGKTVLIVDDILDTGGTLLKVLELLKNVGPKEVK 114
|
|
| PRK00934 |
PRK00934 |
ribose-phosphate pyrophosphokinase; Provisional |
367-402 |
7.67e-03 |
|
ribose-phosphate pyrophosphokinase; Provisional
Pssm-ID: 234868 [Multi-domain] Cd Length: 285 Bit Score: 38.36 E-value: 7.67e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1968689742 367 IRGKRLVVVDDSIVRGNTQRALVRMLREAGAAEVHV 402
Cdd:PRK00934 202 VKGKDVLIVDDIISTGGTMATAIKILKEQGAKKVYV 237
|
|
| |
