|
Name |
Accession |
Description |
Interval |
E-value |
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
1-469 |
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: 721.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738648172 1 MCGIIGIHGCSPVNQLLYDGLLLLQHRGQDAAGIATYQNNQFHIFKAQGLVRDVFRTRNMRSLPGNSGIGQVRYPISGtP 80
Cdd:COG0034 7 ECGVFGIYGHEDVAQLTYYGLYALQHRGQESAGIATSDGGRFHLHKGMGLVSDVFDEEDLERLKGNIAIGHVRYSTTG-S 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738648172 81 SDTEEAQPFYVNAPYG-ICFTHNGNLTNSDELRESLFKHDRrHINTSSNSEVLLNVFAHELYEASkssslqvseIFDAVT 159
Cdd:COG0034 86 SSLENAQPFYVNSPFGsIALAHNGNLTNAEELREELEEEGA-IFQTTSDTEVILHLIARELTKED---------LEEAIK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738648172 160 AVHRRVKGAYAAIAQIaGYGLLAFRDPNGIRPLSLGTQETpqgvEWILASESVAVEGIGFEFVRDVAPGEAIFIDTEGkL 239
Cdd:COG0034 156 EALRRVKGAYSLVILT-GDGLIAARDPNGIRPLVLGKLED----GYVVASESCALDILGAEFVRDVEPGEIVVIDEDG-L 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738648172 240 HSRLCADNAQLSPCIFEYVYFARPDSTIDGVNVYNCRLRMGELLAQK--VarelrlsEVDVVMPIPDSSRPAGMELASTL 317
Cdd:COG0034 230 RSRQFAEKPRPAPCIFEYVYFARPDSVIDGRSVYEARKRMGRELAREapV-------DADVVIPVPDSGRPAAIGYAEES 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738648172 318 DLSYREGFIKNRYVGRTFIMPGQTVRKKSVRQKLNPMSIEFKGKNVLLVDDSIVRGTTSREIVSMARHAGANKVFFASAA 397
Cdd:COG0034 303 GIPYEEGLIKNRYVGRTFIQPTQELRELGVRLKLNPIREVVKGKRVVLVDDSIVRGTTSRRIVKMLREAGAKEVHFRIAS 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 738648172 398 PAVRYPNFYGIDMPDQSDLIAYGKSTEQIAQEIGADALVFQDLDDLKLAISElnpKIERFDASCFDGDYVTG 469
Cdd:COG0034 383 PPIRYPCYYGIDTPTREELIAANRSVEEIREYIGADSLGYLSLEGLIEAVGE---PIEGFCTACFTGDYPTG 451
|
|
| 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: 595.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738648172 2 CGIIGIHGCSPVNQLLYDGLLLL-QHRGQDAAGIATYQNNQFHIFKAQGLVRDVFRTRNMRSLPGNSGIGQVRYPISGTp 80
Cdd:TIGR01134 1 CGVVGIYGQEEVAASLTYYGLYAlQHRGQESAGISVFDGNRFRLHKGNGLVSDVFNEEHLQRLKGNVGIGHVRYSTAGS- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738648172 81 SDTEEAQPFYVNAPYG-ICFTHNGNLTNSDELRESLFKhDRRHINTSSNSEVLLNVFAHElyeaskssSLQVSEIFDAVT 159
Cdd:TIGR01134 80 SGLENAQPFVVNSPYGgLALAHNGNLVNADELRRELEE-EGRHFNTTSDSEVLLHLLAHN--------DESKDDLFDAVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738648172 160 AVHRRVKGAYAAIAqIAGYGLLAFRDPNGIRPLSLGTQETpqgvEWILASESVAVEGIGFEFVRDVAPGEAIFIDtEGKL 239
Cdd:TIGR01134 151 RVLERVRGAYALVL-MTEDGLVAVRDPHGIRPLVLGRRGD----GYVVASESCALDILGAEFVRDVEPGEVVVIF-DGGL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738648172 240 HSRLCADNAQlSPCIFEYVYFARPDSTIDGVNVYNCRLRMGELLAQKVArelrlSEVDVVMPIPDSSRPAGMELASTLDL 319
Cdd:TIGR01134 225 ESRQCARRPR-APCVFEYVYFARPDSVIDGISVYYARKRMGKELARESP-----VEADVVVPVPDSGRSAALGFAQASGI 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738648172 320 SYREGFIKNRYVGRTFIMPGQTVRKKSVRQKLNPMSIEFKGKNVLLVDDSIVRGTTSREIVSMARHAGANKVFFASAAPA 399
Cdd:TIGR01134 299 PYREGLIKNRYVGRTFIMPTQELRELSVRLKLNPVRAVFEGKRVVLVDDSIVRGTTSRQIVEMLRDAGAKEVHVRIASPP 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 738648172 400 VRYPNFYGIDMPDQSDLIAYGKSTEQIAQeIGADALVFQDLDDLKLAIselNPKIERFDASCFDGDYV 467
Cdd:TIGR01134 379 IRYPCYYGIDMPTREELIAARRTVEEIRK-IGADSLAYLSLEGLKEAV---GNPESDLCLACFTGEYP 442
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
1-467 |
0e+00 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 557.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738648172 1 MCGIIGIHGCSPVNQLLYDGLLLLQHRGQDAAGIATYQNNQFHIFKAQGLVRDVFRTRNMRSLPGNSGIGQVRYPISGTP 80
Cdd:PLN02440 1 ECGVVGIFGDPEASRLCYLGLHALQHRGQEGAGIVTVDGNRLQSITGNGLVSDVFDESKLDQLPGDIAIGHVRYSTAGAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738648172 81 SDTEeAQPFYVNAPYG-ICFTHNGNLTNSDELRESLfKHDRRHINTSSNSEVLLNVFAHELYEAskssslqvseIFDAVT 159
Cdd:PLN02440 81 SLKN-VQPFVANYRFGsIGVAHNGNLVNYEELRAKL-EENGSIFNTSSDTEVLLHLIAISKARP----------FFSRIV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738648172 160 AVHRRVKGAYAAIAQIAGYgLLAFRDPNGIRPLSLGTQetpQGVEWILASESVAVEGIGFEFVRDVAPGEAIFIDtEGKL 239
Cdd:PLN02440 149 DACEKLKGAYSMVFLTEDK-LVAVRDPHGFRPLVMGRR---SNGAVVFASETCALDLIGATYEREVNPGEVIVVD-KDKG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738648172 240 HSRLCA-DNAQLSPCIFEYVYFARPDSTIDGVNVYNCRLRMGELLAQKVARELrlsevDVVMPIPDSSRPAGMELASTLD 318
Cdd:PLN02440 224 VSSQCLmPHPEPKPCIFEHIYFARPNSIVFGRSVYESRLEFGEILATEIPVDC-----DVVIPVPDSGRVAALGYAAKLG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738648172 319 LSYREGFIKNRYVGRTFIMPGQTVRKKSVRQKLNPMSIEFKGKNVLLVDDSIVRGTTSREIVSMARHAGANKVFFASAAP 398
Cdd:PLN02440 299 VPFQQGLIRSHYVGRTFIEPSQKIRDFSVKLKLNPVRSVLEGKRVVVVDDSIVRGTTSSKIVRMLREAGAKEVHMRIASP 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 738648172 399 AVRYPNFYGIDMPDQSDLIAYGKSTEQIAQEIGADALVFQDLDDLKLAISElNPKieRFDASCFDGDYV 467
Cdd:PLN02440 379 PIIASCYYGVDTPSREELISNRMSVEEIRKFIGCDSLAFLPLEDLKKSLGE-ESP--RFCYACFSGDYP 444
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
2-466 |
4.81e-146 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 425.60 E-value: 4.81e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738648172 2 CGIIGIHGCSP--VNQLLYDGLLLLQHRGQDAAGIATYQNNQFHIFKAQGLVRDVFRTRNMRSLPGNSGIGQVRYPISGT 79
Cdd:PRK05793 15 CGVFGVFSKNNidVASLTYYGLYALQHRGQESAGIAVSDGEKIKVHKGMGLVSEVFSKEKLKGLKGNSAIGHVRYSTTGA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738648172 80 pSDTEEAQPFYVNAPYG-ICFTHNGNLTNSDELRESLFKhDRRHINTSSNSEVLLNVFAHELYeaskssslqvSEIFDAV 158
Cdd:PRK05793 95 -SDLDNAQPLVANYKLGsIAIAHNGNLVNADVIRELLED-GGRIFQTSIDSEVILNLIARSAK----------KGLEKAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738648172 159 TAVHRRVKGAYAaIAQIAGYGLLAFRDPNGIRPLSLGTQEtpqgVEWILASESVAVEGIGFEFVRDVAPGEAIFIDTEGk 238
Cdd:PRK05793 163 VDAIQAIKGSYA-LVILTEDKLIGVRDPHGIRPLCLGKLG----DDYILSSESCALDTIGAEFIRDVEPGEIVIIDEDG- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738648172 239 LHSRLCADNAQLSPCIFEYVYFARPDSTIDGVNVYNCRLRMGELLAqkvaRELRLsEVDVVMPIPDSSRPAGMELASTLD 318
Cdd:PRK05793 237 IKSIKFAEKTKCQTCAFEYIYFARPDSVIDGISVYESRVRAGRQLY----KEYPV-DADIVIGVPDSGIPAAIGYAEASG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738648172 319 LSYREGFIKNRYVGRTFIMPGQTVRKKSVRQKLNPMSIEFKGKNVLLVDDSIVRGTTSREIVSMARHAGANKVFFASAAP 398
Cdd:PRK05793 312 IPYGIGFIKNKYVGRTFIAPSQELRERAVRVKLNPLKVNVEGKRVVLIDDSIVRGTTSKRLVELLRKAGAKEVHFRVSSP 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 738648172 399 AVRYPNFYGIDMPDQSDLIAYGKSTEQIAQEIGADALVFQDLDDLKLAIselnPKIERFDASCFDGDY 466
Cdd:PRK05793 392 PVKYPCYFGIDTPYRKELIGANMSVEEIREMIGADSLGYLSIEGLLESL----NGDKGFCLGCFNGVY 455
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
2-268 |
2.37e-122 |
|
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: 357.16 E-value: 2.37e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738648172 2 CGIIGIHGCSPVNQLLYDGLLLLQHRGQDAAGIATYQNNQFHIFKAQGLVRDVFRTRNMRSLPGNSGIGQVRYPISGTpS 81
Cdd:cd00715 1 CGVFGIYGAEDAARLTYLGLYALQHRGQESAGIATSDGKRFHTHKGMGLVSDVFDEEKLRRLPGNIAIGHVRYSTAGS-S 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738648172 82 DTEEAQPFYVNAP-YGICFTHNGNLTNSDELRESLFKHDrRHINTSSNSEVLLNVFAHELYEASkssslqvseIFDAVTA 160
Cdd:cd00715 80 SLENAQPFVVNSPlGGIALAHNGNLVNAKELREELEEEG-RIFQTTSDSEVILHLIARSLAKDD---------LFEAIID 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738648172 161 VHRRVKGAYAAIAQIAgYGLLAFRDPNGIRPLSLGTQETPqgvEWILASESVAVEGIGFEFVRDVAPGEAIFIDTEGKLH 240
Cdd:cd00715 150 ALERVKGAYSLVIMTA-DGLIAVRDPHGIRPLVLGKLEGD---GYVVASESCALDIIGAEFVRDVEPGEIVVIDDDGLES 225
|
250 260
....*....|....*....|....*...
gi 738648172 241 SRlCADNAQLSPCIFEYVYFARPDSTID 268
Cdd:cd00715 226 SQ-RAPKPKPAPCIFEYVYFARPDSVID 252
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
2-231 |
8.51e-51 |
|
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: 171.86 E-value: 8.51e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738648172 2 CGIIGIHGCSPVNQLLYDGLLLL----QHRGQDAAGIATYQNNQFHIFKAQGLVRDVFRTRNMRSLPGNSGIGQVRYPIS 77
Cdd:cd00352 1 CGIFGIVGADGAASLLLLLLLRGlaalEHRGPDGAGIAVYDGDGLFVEKRAGPVSDVALDLLDEPLKSGVALGHVRLATN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738648172 78 GTPSDtEEAQPFYVNaPYGICFTHNGNLTNSDELRESLFKHdRRHINTSSNSEVLLNVFAHELYEaskssslqvSEIFDA 157
Cdd:cd00352 81 GLPSE-ANAQPFRSE-DGRIALVHNGEIYNYRELREELEAR-GYRFEGESDSEVILHLLERLGRE---------GGLFEA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 738648172 158 VTAVHRRVKGAYA-AIAQIAGYGLLAFRDPNGIRPLSLGTQEtpqGVEWILASESVAVEGIGFEFVRDVAPGEAI 231
Cdd:cd00352 149 VEDALKRLDGPFAfALWDGKPDRLFAARDRFGIRPLYYGITK---DGGLVFASEPKALLALPFKGVRRLPPGELL 220
|
|
| PRTases_typeI |
cd06223 |
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ... |
279-418 |
1.84e-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: 1.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738648172 279 MGELLAQKVARELRlsEVDVVMPIPDSSRPAGMELASTLDLSYREGFIKNRYVGRTFIMPgqtvrkksvRQKLNPMSIEF 358
Cdd:cd06223 1 AGRLLAEEIREDLL--EPDVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSEP---------YGLELPLGGDV 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 738648172 359 KGKNVLLVDDSIVRGTTSREIVSMARHAGANKVFFAsAAPAVRYPNFYGIDMPDQSDLIA 418
Cdd:cd06223 70 KGKRVLLVDDVIATGGTLLAAIELLKEAGAKVVGVA-VLLDKPEGGARELASPGDPVYSL 128
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
2-214 |
4.09e-15 |
|
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: 75.00 E-value: 4.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738648172 2 CGIIGIH---GCSPVNQLLYDGLLLLQHRG-QDAAGIATYQNNQ---------FHIFKAQGLVRDVFRTRNMRSLPGNSG 68
Cdd:cd01907 1 CGIFGIMskdGEPFVGALLVEMLDAMQERGpGDGAGFALYGDPDafvyssgkdMEVFKGVGYPEDIARRYDLEEYKGYHW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738648172 69 IGQVRYPiSGTPSDTEEAQPFYVnapYGICFTHNGNLTNSDELRESLfKHDRRHINTSSNSEVLLNVFAHEL------YE 142
Cdd:cd01907 81 IAHTRQP-TNSAVWWYGAHPFSI---GDIAVVHNGEISNYGSNREYL-ERFGYKFETETDTEVIAYYLDLLLrkgglpLE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 738648172 143 ASKSSSLQVSEIFDAVTAV-----HRRVKGAYAAIAQIAGyGLLAFRDPNGIRPLSLGtqETPQgvEWILASESVAV 214
Cdd:cd01907 156 YYKHIIRMPEEERELLLALrltyrLADLDGPFTIIVGTPD-GFIVIRDRIKLRPAVVA--ETDD--YVAIASEECAI 227
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
2-225 |
1.95e-13 |
|
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: 69.40 E-value: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738648172 2 CGIIGIHGCSPVNQLLYDGLLLLQHRGQDAAGIATYQNNQFHIFKAQGLVRDVFRTRNMRSLPGNSGIGQVRYPISGTPS 81
Cdd:cd00714 1 CGIVGYIGKREAVDILLEGLKRLEYRGYDSAGIAVIGDGSLEVVKAVGKVANLEEKLAEKPLSGHVGIGHTRWATHGEPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738648172 82 DtEEAQPfYVNAPYGICFTHNGNLTNSDELRESLFKHDrrHINTS-SNSEVLLNVFAHElYEASKSsslqvseIFDAVTA 160
Cdd:cd00714 81 D-VNAHP-HRSCDGEIAVVHNGIIENYAELKEELEAKG--YKFESeTDTEVIAHLIEYY-YDGGLD-------LLEAVKK 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 738648172 161 VHRRVKGAYAaiaqiagyglLAF---RDPNGI---R---PLSLGTQEtpqgVEWILASESVAVegigFEFVRDV 225
Cdd:cd00714 149 ALKRLEGAYA----------LAViskDEPDEIvaaRngsPLVIGIGD----GENFVASDAPAL----LEHTRRV 204
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
1-170 |
2.59e-10 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 62.75 E-value: 2.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738648172 1 MCGIIGIHGCSPVNQLLYDGLLLLQHRGQDAAGIATYQNNQFHIFKAQGLVRDVFRTRNMRSLPGNSGIGQVRYPISGTP 80
Cdd:PRK00331 1 MCGIVGYVGQRNAAEILLEGLKRLEYRGYDSAGIAVLDDGGLEVRKAVGKVANLEAKLEEEPLPGTTGIGHTRWATHGKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738648172 81 SDteeaqpfyVNA-PY-----GICFTHNGNLTNSDELRESLFKHDrrHINTS-SNSEVLLNVFAHELYEAskssslqvSE 153
Cdd:PRK00331 81 TE--------RNAhPHtdcsgRIAVVHNGIIENYAELKEELLAKG--HVFKSeTDTEVIAHLIEEELKEG--------GD 142
|
170
....*....|....*..
gi 738648172 154 IFDAVTAVHRRVKGAYA 170
Cdd:PRK00331 143 LLEAVRKALKRLEGAYA 159
|
|
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
1-170 |
5.66e-10 |
|
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: 61.57 E-value: 5.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738648172 1 MCGIIGIHGCSPVnqllydgllllQ-----------HRGQDAAGIATYQNNQFHIFKAQGLVRDVFRTRNMRSLPGNSGI 69
Cdd:COG0449 1 MCGIVGYIGKRDA-----------ApilleglkrleYRGYDSAGIAVLDDGGLEVRKAVGKLANLEEKLAEEPLSGTIGI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738648172 70 GQVRYPISGTPSDteeaqpfyVNA-PY-----GICFTHNGNLTNSDELRESLFKHDrrHINTS-SNSEVLlnvfAH---E 139
Cdd:COG0449 70 GHTRWATHGAPSD--------ENAhPHtscsgRIAVVHNGIIENYAELREELEAKG--HTFKSeTDTEVI----AHlieE 135
|
170 180 190
....*....|....*....|....*....|.
gi 738648172 140 LYEASKSsslqvseIFDAVTAVHRRVKGAYA 170
Cdd:COG0449 136 YLKGGGD-------LLEAVRKALKRLEGAYA 159
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
86-213 |
5.53e-09 |
|
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: 54.06 E-value: 5.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738648172 86 AQPFYVNAPYGICFTHNGNLTNSDELRESLFKHDRRHiNTSSNSEVLLNVFAHElyeaskssslqvsEIFDAVtavhRRV 165
Cdd:pfam13537 13 AQPMVSSEDGRYVIVFNGEIYNYRELRAELEAKGYRF-RTHSDTEVILHLYEAE-------------WGEDCV----DRL 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 738648172 166 KGAYA-AIAQIAGYGLLAFRDPNGIRPLSLGTQEtpqGVEWILASESVA 213
Cdd:pfam13537 75 NGMFAfAIWDRRRQRLFLARDRFGIKPLYYGRDD---GGRLLFASELKA 120
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
65-198 |
2.86e-08 |
|
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: 52.31 E-value: 2.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738648172 65 GNSGIGQVRYPISGTPSDTeeAQPFYVnaPYG-ICFTHNGNLTNSDELRESLfKHDRRHINTSSNSEVLLNVFaHELYEa 143
Cdd:pfam13522 10 GGVALGHVRLAIVDLPDAG--NQPMLS--RDGrLVLVHNGEIYNYGELREEL-ADLGHAFRSRSDTEVLLALY-EEWGE- 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 738648172 144 skssslqvseifDAVtavhRRVKGAYA-AIAQIAGYGLLAFRDPNGIRPLSLGTQE 198
Cdd:pfam13522 83 ------------DCL----ERLRGMFAfAIWDRRRRTLFLARDRLGIKPLYYGILG 122
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-170 |
1.49e-06 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 50.79 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738648172 1 MCGIIGIHGCSPVNQLLYDGLLLLQHRGQDAAGIATYQN-NQFHIFK-----AQGLVRDVFRTRNMRSLPGNS-GIGQVR 73
Cdd:PTZ00295 24 CCGIVGYLGNEDASKILLEGIEILQNRGYDSCGISTISSgGELKTTKyasdgTTSDSIEILKEKLLDSHKNSTiGIAHTR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738648172 74 YPISGTPSDtEEAQPfYVNAPYGICFTHNGNLTNSDELRESLFKhdrRHINTSSN--SEVLLNVFAHELYeaskssslQV 151
Cdd:PTZ00295 104 WATHGGKTD-ENAHP-HCDYKKRIALVHNGTIENYVELKSELIA---KGIKFRSEtdSEVIANLIGLELD--------QG 170
|
170
....*....|....*....
gi 738648172 152 SEIFDAVTAVHRRVKGAYA 170
Cdd:PTZ00295 171 EDFQEAVKSAISRLQGTWG 189
|
|
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
25-202 |
2.05e-06 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 50.13 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738648172 25 QHRGQDAAGIATYQNNQFH-----IFKAQG----LVRDVFRTRNMRSLPGN------SGIGQVRY-------PISGTPSD 82
Cdd:PLN02981 31 EYRGYDSAGIAIDNDPSLEsssplVFREEGkiesLVRSVYEEVAETDLNLDlvfenhAGIAHTRWathgppaPRNSHPQS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738648172 83 TEEAQPFYVnapygicfTHNGNLTNSDELRESLFKHDRRhINTSSNSEVL--LNVFAHELYeASKSSSLQVSEIfdaVTA 160
Cdd:PLN02981 111 SGPGNEFLV--------VHNGIITNYEVLKETLLRHGFT-FESDTDTEVIpkLAKFVFDKL-NEEEGDVTFSQV---VME 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 738648172 161 VHRRVKGAYAAIAQIAGYgllafrdPNGI------RPLSLGTQETPQG 202
Cdd:PLN02981 178 VMRQLEGAYALIFKSPHY-------PNELvackrgSPLLLGVKELPEE 218
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
1-210 |
2.19e-06 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 50.10 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738648172 1 MCGIIGIHGCS----PVNQLLYDGLLLLQHRGQDAAGIATYQNNQ--FHIfkaqglvrdvfrtrnmrslpgnsgIGQVRY 74
Cdd:PTZ00077 1 MCGILAIFNSKgerhELRRKALELSKRLRHRGPDWSGIIVLENSPgtYNI------------------------LAHERL 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738648172 75 PISGTPSDteeAQPFYVNApYGICFTHNGNLTNSDELREsLFKHDRRHINTSSNSEVLLNvfaheLYEASKSSSL--QVS 152
Cdd:PTZ00077 57 AIVDLSDG---KQPLLDDD-ETVALMQNGEIYNHWEIRP-ELEKEGYKFSSNSDCEIIGH-----LYKEYGPKDFwnHLD 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 738648172 153 EIFDAVtaVHRRVKGAYaaiaqiagyglLAFRDPNGIRPLSLGTQetPQGVEWiLASE 210
Cdd:PTZ00077 127 GMFATV--IYDMKTNTF-----------FAARDHIGIIPLYIGYA--KDGSIW-FSSE 168
|
|
| YafJ |
COG0121 |
Predicted glutamine amidotransferase YafJ [General function prediction only]; |
30-241 |
2.41e-06 |
|
Predicted glutamine amidotransferase YafJ [General function prediction only];
Pssm-ID: 439891 [Multi-domain] Cd Length: 248 Bit Score: 48.81 E-value: 2.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738648172 30 DAAGIATY-QNNQFHIFKAqglVRDVFRTRNMRSLPGNS----GIGQVRYPiSGTPSDTEEAQPFYVnapYGICFTHNGN 104
Cdd:COG0121 39 DGWGIGWYeGDGEPRLYRD---PLPAWSDPNLRLLARPIksrlVIAHVRKA-TVGPVSLENTHPFRG---GRWLFAHNGQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738648172 105 LTNSDELR----ESLFKHDRRHINTSSNSEVLLNVFAHELYEASKSSslqVSEIFDAVTAVH--RRVKGAYAAIAQIAGY 178
Cdd:COG0121 112 LDGFDRLRrrlaEELPDELYFQPVGTTDSELAFALLLSRLRDGGPDP---AEALAEALRELAelARAPGRLNLLLSDGER 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 738648172 179 gLLAFRDPNGIRPLSL--GTQETPQGVEWILASESVAVEGiGFefvRDVAPGEAIFIDTEGKLHS 241
Cdd:COG0121 189 -LYATRYTSDDPYPTLyyLTRTTPDDRVVVVASEPLTDDE-GW---TEVPPGELLVVRDGLEVEV 248
|
|
| ComFC |
COG1040 |
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General ... |
273-397 |
4.07e-06 |
|
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General function prediction only];
Pssm-ID: 440662 [Multi-domain] Cd Length: 196 Bit Score: 47.51 E-value: 4.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738648172 273 YNCRLRMGELLAQKVARELR---LSEVDVVMPIPdSSR---------PAGM---ELASTLDLSYR-EGFIKNRYVgrtfi 336
Cdd:COG1040 53 YRGRLDLARLLARLLARALRealLPRPDLIVPVP-LHRrrlrrrgfnQAELlarALARALGIPVLpDLLRRVRAT----- 126
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738648172 337 mPGQT-----VRKKSVRQ--KLNPmSIEFKGKNVLLVDDsiVR--GTTSREIVSMARHAGANKVFFASAA 397
Cdd:COG1040 127 -PSQAglsraERRRNLRGafAVRP-PARLAGKHVLLVDD--VLttGATLAEAARALKAAGAARVDVLVLA 192
|
|
| PRK08558 |
PRK08558 |
adenine phosphoribosyltransferase; Provisional |
281-391 |
4.24e-05 |
|
adenine phosphoribosyltransferase; Provisional
Pssm-ID: 181466 [Multi-domain] Cd Length: 238 Bit Score: 44.98 E-value: 4.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738648172 281 ELLAQKVARELRLSEVDVVMPIPDSSRPAGMELASTLDLS------YREGFIKNRYVGRTFIMPGqtvrkkSVRQKLNPM 354
Cdd:PRK08558 97 RLIAPVVAERFMGLRVDVVLTAATDGIPLAVAIASYFGADlvyakkSKETGVEKFYEEYQRLASG------IEVTLYLPA 170
|
90 100 110
....*....|....*....|....*....|....*..
gi 738648172 355 SIEFKGKNVLLVDDSIVRGTTSREIVSMARHAGANKV 391
Cdd:PRK08558 171 SALKKGDRVLIVDDIIRSGETQRALLDLARQAGADVV 207
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-210 |
7.83e-05 |
|
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: 43.70 E-value: 7.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738648172 2 CGIIGIHGCSPVNQLLYDGLLLLQ---HRGQDAAGIatYQNNQFhifkaqglvrdvfrtrnmrslpgnsGIGQVRYPISG 78
Cdd:cd00712 1 CGIAGIIGLDGASVDRATLERMLDalaHRGPDGSGI--WIDEGV-------------------------ALGHRRLSIID 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738648172 79 TpsdTEEAQPFYvNAPYGICFTHNGNLTNSDELRESLfKHDRRHINTSSNSEVLLnvfahELYEASKSSSLQvseifdav 158
Cdd:cd00712 54 L---SGGAQPMV-SEDGRLVLVFNGEIYNYRELRAEL-EALGHRFRTHSDTEVIL-----HLYEEWGEDCLE-------- 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 738648172 159 tavhrRVKGAYA-AI----AQIagygLLAFRDPNGIRPLSLGtqETPQGVewILASE 210
Cdd:cd00712 116 -----RLNGMFAfALwdkrKRR----LFLARDRFGIKPLYYG--RDGGGL--AFASE 159
|
|
| Pribosyltran |
pfam00156 |
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ... |
283-394 |
1.51e-04 |
|
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: 41.97 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738648172 283 LAQKVARELRLSEvDVVMPIPDSSRPAGMELASTLDLSYrEGFIKNRYVGRTfimpgqtvrkkSVRQKLNPMSIEFKGKN 362
Cdd:pfam00156 18 LAAQINEDYGGKP-DVVVGILRGGLPFAGILARRLDVPL-AFVRKVSYNPDT-----------SEVMKTSSALPDLKGKT 84
|
90 100 110
....*....|....*....|....*....|..
gi 738648172 363 VLLVDDSIVRGTTSREIVSMARHAGANKVFFA 394
Cdd:pfam00156 85 VLIVDDILDTGGTLLKVLELLKNVGPKEVKIA 116
|
|
| Hpt1 |
COG2236 |
Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine ... |
339-412 |
1.87e-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: 41.76 E-value: 1.87e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 738648172 339 GQTVRKKSVRQklnPMSIEFKGKNVLLVDDSIVRGTTSREIVSMARHAGANKVFFAS--AAPAVRY-PNFYGIDMPD 412
Cdd:COG2236 70 AKRLEEPVVKG---PLDEDLAGKRVLIVDDVADTGRTLEAVRDLLKEAGPAEVRTAVlyYKPSSKFkPDYYAEETDA 143
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-210 |
7.05e-04 |
|
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: 42.13 E-value: 7.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738648172 1 MCGIIGI-HGCSPVNQLLYDGLLLLQ-HRGQDAAGIatYQNnqfhifkaqglvrdvfrtrnmrslpGNSGIGQVRYPIsg 78
Cdd:COG0367 1 MCGIAGIiDFDGGADREVLERMLDALaHRGPDGSGI--WVD-------------------------GGVALGHRRLSI-- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738648172 79 TPSDTEEAQPFyVNAPYGICFTHNGNLTNSDELRESLFKHDRRHiNTSSNSEVLLnvfahELYEASKSSSLQvseifdav 158
Cdd:COG0367 52 IDLSEGGHQPM-VSEDGRYVLVFNGEIYNYRELRAELEALGHRF-RTHSDTEVIL-----HAYEEWGEDCLE-------- 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 738648172 159 tavhrRVKGAYA-AIAQIAGYGLLAFRDPNGIRPLSLGtqETPQGveWILASE 210
Cdd:COG0367 117 -----RLNGMFAfAIWDRRERRLFLARDRFGIKPLYYA--EDGGG--LAFASE 160
|
|
| PRK00934 |
PRK00934 |
ribose-phosphate pyrophosphokinase; Provisional |
350-394 |
1.22e-03 |
|
ribose-phosphate pyrophosphokinase; Provisional
Pssm-ID: 234868 [Multi-domain] Cd Length: 285 Bit Score: 40.67 E-value: 1.22e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 738648172 350 KLNPMSIEFKGKNVLLVDDSIVRGTTSREIVSMARHAGANKVFFA 394
Cdd:PRK00934 194 EIAPKNLDVKGKDVLIVDDIISTGGTMATAIKILKEQGAKKVYVA 238
|
|
| YafJ |
cd01908 |
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ... |
30-188 |
1.64e-03 |
|
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: 40.06 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738648172 30 DAAGIATYQNNQFHIFK------AQGLVRDVFRTRNMRSlpgNSGIGQVRypiSGTPSDTEEA--QPFYVNapyGICFTH 101
Cdd:cd01908 42 DGWGIGWYEGKGGRPFRyrsplpAWSDINLESLARPIKS---PLVLAHVR---AATVGPVSLEncHPFTRG---RWLFAH 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738648172 102 NGNLTNSDELRESLFKHDRRHINTSSNSEVllnVFAHELYEASKSSSLQVSEIFDAVTAVHRRvkgayaaIAQIAGYGLL 181
Cdd:cd01908 113 NGQLDGFRLLRRRLLRLLPRLPVGTTDSEL---AFALLLSRLLERDPLDPAELLDAILQTLRE-------LAALAPPGRL 182
|
....*..
gi 738648172 182 AFRDPNG 188
Cdd:cd01908 183 NLLLSDG 189
|
|
| PRK09162 |
PRK09162 |
hypoxanthine-guanine phosphoribosyltransferase; Provisional |
355-412 |
9.70e-03 |
|
hypoxanthine-guanine phosphoribosyltransferase; Provisional
Pssm-ID: 181675 Cd Length: 181 Bit Score: 37.15 E-value: 9.70e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 738648172 355 SIEFKGKNVLLVDDSIVRGTTSREIVSMARHAGANKVFFA--------SAAPAVRyPNFYGIDMPD 412
Cdd:PRK09162 92 RESLKGRTVLVVDDILDEGHTLAAIRDRCLEMGAAEVYSAvlvdkthdRKAKPLK-ADFVGLEVPD 156
|
|
| |
