|
Name |
Accession |
Description |
Interval |
E-value |
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
1-444 |
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: 823.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 1 MCSVVGIYGNENASKLCFYSLFAMQHRGQEAAGISSSDGIHIKTVKDRGLVTQIFKEEHFNILKGNMAIGHTRYSTAGDD 80
Cdd:COG0034 7 ECGVFGIYGHEDVAQLTYYGLYALQHRGQESAGIATSDGGRFHLHKGMGLVSDVFDEEDLERLKGNIAIGHVRYSTTGSS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 81 SILDAQPVFARYGLGEISIAHNGNLVNAKEIRDELIKIGAIFQSNMDTENLIHLIAKNHQKPTLKERIIDAVKKIKGAFS 160
Cdd:COG0034 87 SLENAQPFYVNSPFGSIALAHNGNLTNAEELREELEEEGAIFQTTSDTEVILHLIARELTKEDLEEAIKEALRRVKGAYS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 161 LVILSRTKMFAIRDPFGFRPLSLGKIKsGGYIVASETCAFELVGAEFIRDIKPGEMITFENGELKSEMIF-NPTPKQCIF 239
Cdd:COG0034 167 LVILTGDGLIAARDPNGIRPLVLGKLE-DGYVVASESCALDILGAEFVRDVEPGEIVVIDEDGLRSRQFAeKPRPAPCIF 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 240 EYIYFARPDSNIFGKNVYSIRKQMGRELAKEMPVEADMVVPVPDSGVAAALGYSEKSKIPFEMAIMRNHYVGRTFIEPTQ 319
Cdd:COG0034 246 EYVYFARPDSVIDGRSVYEARKRMGRELAREAPVDADVVIPVPDSGRPAAIGYAEESGIPYEEGLIKNRYVGRTFIQPTQ 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 320 EIRDLKVKMKLSPIKHKIEGKRLVVIDDSIVRGTTSRRIVRMLKEAGAKEVHMRIASPATTGPCYYGVDTPTKEELIASR 399
Cdd:COG0034 326 ELRELGVRLKLNPIREVVKGKRVVLVDDSIVRGTTSRRIVKMLREAGAKEVHFRIASPPIRYPCYYGIDTPTREELIAAN 405
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 494738241 400 LSTDEIAKYIEADSLAYLSIDGLVRAVKDKKENYCFACFDGNYPI 444
Cdd:COG0034 406 RSVEEIREYIGADSLGYLSLEGLIEAVGEPIEGFCTACFTGDYPT 450
|
|
| purF |
TIGR01134 |
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ... |
2-443 |
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: 669.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 2 CSVVGIYGNEN-ASKLCFYSLFAMQHRGQEAAGISSSDGIHIKTVKDRGLVTQIFKEEHFNILKGNMAIGHTRYSTAGDD 80
Cdd:TIGR01134 1 CGVVGIYGQEEvAASLTYYGLYALQHRGQESAGISVFDGNRFRLHKGNGLVSDVFNEEHLQRLKGNVGIGHVRYSTAGSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 81 SILDAQPVFARYGLGEISIAHNGNLVNAKEIRDELIKIGAIFQSNMDTENLIHLIAKNH-QKPTLKERIIDAVKKIKGAF 159
Cdd:TIGR01134 81 GLENAQPFVVNSPYGGLALAHNGNLVNADELRRELEEEGRHFNTTSDSEVLLHLLAHNDeSKDDLFDAVARVLERVRGAY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 160 SLVILSRTKMFAIRDPFGFRPLSLGKIKSGgYIVASETCAFELVGAEFIRDIKPGEMITFENGELKSEMIFNPTPKQCIF 239
Cdd:TIGR01134 161 ALVLMTEDGLVAVRDPHGIRPLVLGRRGDG-YVVASESCALDILGAEFVRDVEPGEVVVIFDGGLESRQCARRPRAPCVF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 240 EYIYFARPDSNIFGKNVYSIRKQMGRELAKEMPVEADMVVPVPDSGVAAALGYSEKSKIPFEMAIMRNHYVGRTFIEPTQ 319
Cdd:TIGR01134 240 EYVYFARPDSVIDGISVYYARKRMGKELARESPVEADVVVPVPDSGRSAALGFAQASGIPYREGLIKNRYVGRTFIMPTQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 320 EIRDLKVKMKLSPIKHKIEGKRLVVIDDSIVRGTTSRRIVRMLKEAGAKEVHMRIASPATTGPCYYGVDTPTKEELIASR 399
Cdd:TIGR01134 320 ELRELSVRLKLNPVRAVFEGKRVVLVDDSIVRGTTSRQIVEMLRDAGAKEVHVRIASPPIRYPCYYGIDMPTREELIAAR 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 494738241 400 LSTDEIAKyIEADSLAYLSIDGLVRAVKDKKENYCFACFDGNYP 443
Cdd:TIGR01134 400 RTVEEIRK-IGADSLAYLSLEGLKEAVGNPESDLCLACFTGEYP 442
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
1-445 |
0e+00 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 623.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 1 MCSVVGIYGNENASKLCFYSLFAMQHRGQEAAGISSSDGIHIKTVKDRGLVTQIFKEEHFNILKGNMAIGHTRYSTAGDD 80
Cdd:PLN02440 1 ECGVVGIFGDPEASRLCYLGLHALQHRGQEGAGIVTVDGNRLQSITGNGLVSDVFDESKLDQLPGDIAIGHVRYSTAGAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 81 SILDAQPVFARYGLGEISIAHNGNLVNAKEIRDELIKIGAIFQSNMDTENLIHLIAKNHQKPTLkERIIDAVKKIKGAFS 160
Cdd:PLN02440 81 SLKNVQPFVANYRFGSIGVAHNGNLVNYEELRAKLEENGSIFNTSSDTEVLLHLIAISKARPFF-SRIVDACEKLKGAYS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 161 LVILSRTKMFAIRDPFGFRPLSLGKIKSGGYIVASETCAFELVGAEFIRDIKPGEMITFENGELKSEMIFNPTP--KQCI 238
Cdd:PLN02440 160 MVFLTEDKLVAVRDPHGFRPLVMGRRSNGAVVFASETCALDLIGATYEREVNPGEVIVVDKDKGVSSQCLMPHPepKPCI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 239 FEYIYFARPDSNIFGKNVYSIRKQMGRELAKEMPVEADMVVPVPDSGVAAALGYSEKSKIPFEMAIMRNHYVGRTFIEPT 318
Cdd:PLN02440 240 FEHIYFARPNSIVFGRSVYESRLEFGEILATEIPVDCDVVIPVPDSGRVAALGYAAKLGVPFQQGLIRSHYVGRTFIEPS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 319 QEIRDLKVKMKLSPIKHKIEGKRLVVIDDSIVRGTTSRRIVRMLKEAGAKEVHMRIASPATTGPCYYGVDTPTKEELIAS 398
Cdd:PLN02440 320 QKIRDFSVKLKLNPVRSVLEGKRVVVVDDSIVRGTTSSKIVRMLREAGAKEVHMRIASPPIIASCYYGVDTPSREELISN 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 494738241 399 RLSTDEIAKYIEADSLAYLSIDGLVRAVKDKKENYCFACFDGNYPIL 445
Cdd:PLN02440 400 RMSVEEIRKFIGCDSLAFLPLEDLKKSLGEESPRFCYACFSGDYPVL 446
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
2-444 |
0e+00 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 618.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 2 CSVVGIYGNEN--ASKLCFYSLFAMQHRGQEAAGISSSDGIHIKTVKDRGLVTQIFKEEHFNILKGNMAIGHTRYSTAGD 79
Cdd:PRK05793 15 CGVFGVFSKNNidVASLTYYGLYALQHRGQESAGIAVSDGEKIKVHKGMGLVSEVFSKEKLKGLKGNSAIGHVRYSTTGA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 80 DSILDAQPVFARYGLGEISIAHNGNLVNAKEIRDELIKIGAIFQSNMDTENLIHLIAKNHQKpTLKERIIDAVKKIKGAF 159
Cdd:PRK05793 95 SDLDNAQPLVANYKLGSIAIAHNGNLVNADVIRELLEDGGRIFQTSIDSEVILNLIARSAKK-GLEKALVDAIQAIKGSY 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 160 SLVILSRTKMFAIRDPFGFRPLSLGKIkSGGYIVASETCAFELVGAEFIRDIKPGEMITFENGELKSEMIFNPTPKQ-CI 238
Cdd:PRK05793 174 ALVILTEDKLIGVRDPHGIRPLCLGKL-GDDYILSSESCALDTIGAEFIRDVEPGEIVIIDEDGIKSIKFAEKTKCQtCA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 239 FEYIYFARPDSNIFGKNVYSIRKQMGRELAKEMPVEADMVVPVPDSGVAAALGYSEKSKIPFEMAIMRNHYVGRTFIEPT 318
Cdd:PRK05793 253 FEYIYFARPDSVIDGISVYESRVRAGRQLYKEYPVDADIVIGVPDSGIPAAIGYAEASGIPYGIGFIKNKYVGRTFIAPS 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 319 QEIRDLKVKMKLSPIKHKIEGKRLVVIDDSIVRGTTSRRIVRMLKEAGAKEVHMRIASPATTGPCYYGVDTPTKEELIAS 398
Cdd:PRK05793 333 QELRERAVRVKLNPLKVNVEGKRVVLIDDSIVRGTTSKRLVELLRKAGAKEVHFRVSSPPVKYPCYFGIDTPYRKELIGA 412
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 494738241 399 RLSTDEIAKYIEADSLAYLSIDGLVRAVkDKKENYCFACFDGNYPI 444
Cdd:PRK05793 413 NMSVEEIREMIGADSLGYLSIEGLLESL-NGDKGFCLGCFNGVYPV 457
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
2-252 |
5.31e-152 |
|
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: 431.11 E-value: 5.31e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 2 CSVVGIYGNENASKLCFYSLFAMQHRGQEAAGISSSDGIHIKTVKDRGLVTQIFKEEHFNILKGNMAIGHTRYSTAGDDS 81
Cdd:cd00715 1 CGVFGIYGAEDAARLTYLGLYALQHRGQESAGIATSDGKRFHTHKGMGLVSDVFDEEKLRRLPGNIAIGHVRYSTAGSSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 82 ILDAQPVFARYGLGEISIAHNGNLVNAKEIRDELIKIGAIFQSNMDTENLIHLIAKNHQKPTLKERIIDAVKKIKGAFSL 161
Cdd:cd00715 81 LENAQPFVVNSPLGGIALAHNGNLVNAKELREELEEEGRIFQTTSDSEVILHLIARSLAKDDLFEAIIDALERVKGAYSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 162 VILSRTKMFAIRDPFGFRPLSLGKIKSGGYIVASETCAFELVGAEFIRDIKPGEMITFENGELKSEMIF-NPTPKQCIFE 240
Cdd:cd00715 161 VIMTADGLIAVRDPHGIRPLVLGKLEGDGYVVASESCALDIIGAEFVRDVEPGEIVVIDDDGLESSQRApKPKPAPCIFE 240
|
250
....*....|..
gi 494738241 241 YIYFARPDSNIF 252
Cdd:cd00715 241 YVYFARPDSVID 252
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
2-217 |
5.83e-65 |
|
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: 208.07 E-value: 5.83e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 2 CSVVGIYGNENASKLCFY----SLFAMQHRGQEAAGISSSDGIHIKTVKDRGLVTQIFKEEHFNILKGNMAIGHTRYSTA 77
Cdd:cd00352 1 CGIFGIVGADGAASLLLLlllrGLAALEHRGPDGAGIAVYDGDGLFVEKRAGPVSDVALDLLDEPLKSGVALGHVRLATN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 78 GDDSILDAQPVfaRYGLGEISIAHNGNLVNAKEIRDELIKIGAIFQSNMDTENLIHLIAKNHQKPTLKERIIDAVKKIKG 157
Cdd:cd00352 81 GLPSEANAQPF--RSEDGRIALVHNGEIYNYRELREELEARGYRFEGESDSEVILHLLERLGREGGLFEAVEDALKRLDG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494738241 158 AFSLVILSR--TKMFAIRDPFGFRPLSLGKIKSGGYIVASETCAFELVGAEFIRDIKPGEMI 217
Cdd:cd00352 159 PFAFALWDGkpDRLFAARDRFGIRPLYYGITKDGGLVFASEPKALLALPFKGVRRLPPGELL 220
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
2-200 |
7.57e-28 |
|
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: 109.84 E-value: 7.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 2 CSVVGIYGNENASKLCFYSLFAMQHRGQEAAGISSSDGIHIKTVKDRGLVTQIFKEEHFNILKGNMAIGHTRYSTAGDDS 81
Cdd:cd00714 1 CGIVGYIGKREAVDILLEGLKRLEYRGYDSAGIAVIGDGSLEVVKAVGKVANLEEKLAEKPLSGHVGIGHTRWATHGEPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 82 ILDAQPvfARYGLGEISIAHNGNLVNAKEIRDELIKIGAIFQSNMDTENLIHLIAKNHQK-PTLKERIIDAVKKIKGAFS 160
Cdd:cd00714 81 DVNAHP--HRSCDGEIAVVHNGIIENYAELKEELEAKGYKFESETDTEVIAHLIEYYYDGgLDLLEAVKKALKRLEGAYA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 494738241 161 LVILSRT---KMFAIRdpfgfR--PLSLGkIKSGGYIVASETCAF 200
Cdd:cd00714 159 LAVISKDepdEIVAAR-----NgsPLVIG-IGDGENFVASDAPAL 197
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
71-200 |
3.43e-25 |
|
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: 99.51 E-value: 3.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 71 HTRYSTagDDSILDAQPvFARYGLGEISIAHNGNLVNAKEIRDELIKIGAIFQSNMDTENLIHLIAknhqkptlKERIID 150
Cdd:pfam13537 1 HRRLSI--IDLEGGAQP-MVSSEDGRYVIVFNGEIYNYRELRAELEAKGYRFRTHSDTEVILHLYE--------AEWGED 69
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 494738241 151 AVKKIKGAFSLVILSRTK--MFAIRDPFGFRPLSLGKIKSGGYIVASETCAF 200
Cdd:pfam13537 70 CVDRLNGMFAFAIWDRRRqrLFLARDRFGIKPLYYGRDDGGRLLFASELKAL 121
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-208 |
1.58e-24 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 106.26 E-value: 1.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 1 MCSVVGIYGNENASKLCFYSLFAMQHRGQEAAGISS-SDGIHIKTVKDRGLVTqifKEEHFNILKGNMA---------IG 70
Cdd:PTZ00295 24 CCGIVGYLGNEDASKILLEGIEILQNRGYDSCGISTiSSGGELKTTKYASDGT---TSDSIEILKEKLLdshknstigIA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 71 HTRYSTAGDDSILDAQPVFaRYGlGEISIAHNGNLVNAKEIRDELIKIGAIFQSNMDTENLIHLIAKN-HQKPTLKERII 149
Cdd:PTZ00295 101 HTRWATHGGKTDENAHPHC-DYK-KRIALVHNGTIENYVELKSELIAKGIKFRSETDSEVIANLIGLElDQGEDFQEAVK 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494738241 150 DAVKKIKGAFSLVILSR---TKMFAIRDPfgfRPLSLGkIKSGGYIVASETCAFELVGAEFI 208
Cdd:PTZ00295 179 SAISRLQGTWGLCIIHKdnpDSLIVARNG---SPLLVG-IGDDSIYVASEPSAFAKYTNEYI 236
|
|
| glmS |
TIGR01135 |
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ... |
2-224 |
6.55e-23 |
|
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from Methanococcus jannaschii contains an intein. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Central intermediary metabolism, Amino sugars]
Pssm-ID: 273462 [Multi-domain] Cd Length: 607 Bit Score: 101.56 E-value: 6.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 2 CSVVGIYGNENASKLCFYSLFAMQHRGQEAAGISSSDGIHIKTVKDRGLVTQIFKEEHFNILKGNMAIGHTRYSTAGDDS 81
Cdd:TIGR01135 1 CGIVGYIGQRDAVPILLEGLKRLEYRGYDSAGIAVVDEGKLFVRKAVGKVAELANKLGEKPLPGGVGIGHTRWATHGKPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 82 ILDAQPVFARYGlgEISIAHNGNLVNAKEIRDELIKIGAIFQSNMDTENLIHLIAKNHQKP-TLKERIIDAVKKIKGAFS 160
Cdd:TIGR01135 81 DENAHPHTDEGG--RIAVVHNGIIENYAELREELEARGHVFSSDTDTEVIAHLIEEELREGgDLLEAVQKALKQLRGAYA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494738241 161 LVILS---RTKMFAIRDPfgfRPLSLGkIKSGGYIVASETCAFelvgAEFIRDIkpgemITFENGEL 224
Cdd:TIGR01135 159 LAVLHadhPETLVAARSG---SPLIVG-LGDGENFVASDVTAL----LPYTRRV-----IYLEDGDI 212
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
1-224 |
1.55e-22 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 100.12 E-value: 1.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 1 MCSVVGIYGNENASKLCFYSLFAMQHRGQEAAGISSSDGIHIKTVKDRGLVTQIFKEEHFNILKGNMAIGHTRYSTAGDD 80
Cdd:PRK00331 1 MCGIVGYVGQRNAAEILLEGLKRLEYRGYDSAGIAVLDDGGLEVRKAVGKVANLEAKLEEEPLPGTTGIGHTRWATHGKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 81 SILDAQPVFARYGlgEISIAHNGNLVNAKEIRDELIKIGAIFQSNMDTENLIHLIAKNHQK-PTLKERIIDAVKKIKGAF 159
Cdd:PRK00331 81 TERNAHPHTDCSG--RIAVVHNGIIENYAELKEELLAKGHVFKSETDTEVIAHLIEEELKEgGDLLEAVRKALKRLEGAY 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494738241 160 SLVILSRT---KMFAIR-DPfgfrPLSLGkIKSGGYIVASETCAFelvgAEFIRDIkpgemITFENGEL 224
Cdd:PRK00331 159 ALAVIDKDepdTIVAARnGS----PLVIG-LGEGENFLASDALAL----LPYTRRV-----IYLEDGEI 213
|
|
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
1-224 |
2.49e-21 |
|
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: 96.62 E-value: 2.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 1 MCSVVGIYGNENASKLCFYSLFAMQHRGQEAAGISSSDGIHIKTVKDRG----LVTQIFKEEhfniLKGNMAIGHTRYST 76
Cdd:COG0449 1 MCGIVGYIGKRDAAPILLEGLKRLEYRGYDSAGIAVLDDGGLEVRKAVGklanLEEKLAEEP----LSGTIGIGHTRWAT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 77 AGDDSILDAQPVFAryGLGEISIAHNGNLVNAKEIRDELIKIGAIFQSNMDTENLIHLIAKNHQK-PTLKERIIDAVKKI 155
Cdd:COG0449 77 HGAPSDENAHPHTS--CSGRIAVVHNGIIENYAELREELEAKGHTFKSETDTEVIAHLIEEYLKGgGDLLEAVRKALKRL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494738241 156 KGAFSLVILSRT---KMFAIR-DPfgfrPLSLGkIKSGGYIVASETCAFelvgAEFIRDIkpgemITFENGEL 224
Cdd:COG0449 155 EGAYALAVISADepdRIVAARkGS----PLVIG-LGEGENFLASDVPAL----LPYTRRV-----IYLEDGEI 213
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
68-196 |
1.19e-19 |
|
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: 84.66 E-value: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 68 AIGHTRYSTAGDDSILdAQPVFARYGlgEISIAHNGNLVNAKEIRDELIKIGAIFQSNMDTENLIHLIaknHQKPTlker 147
Cdd:pfam13522 13 ALGHVRLAIVDLPDAG-NQPMLSRDG--RLVLVHNGEIYNYGELREELADLGHAFRSRSDTEVLLALY---EEWGE---- 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 494738241 148 iiDAVKKIKGAFSLVILSRTK--MFAIRDPFGFRPLSLGkIKSGGYIVASE 196
Cdd:pfam13522 83 --DCLERLRGMFAFAIWDRRRrtLFLARDRLGIKPLYYG-ILGGGFVFASE 130
|
|
| PRTases_typeI |
cd06223 |
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ... |
263-384 |
1.75e-19 |
|
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: 83.98 E-value: 1.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 263 MGRELAKEMP---VEADMVVPVPDSGVAAALGYSEKSKIPFEMAIMRNHYVGRTFIEPTQeirdlkvkmKLSPIKHKIEG 339
Cdd:cd06223 1 AGRLLAEEIRedlLEPDVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSEPYG---------LELPLGGDVKG 71
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 494738241 340 KRLVVIDDSIVRGTTSRRIVRMLKEAGAKEVHMRIASPATTGPCY 384
Cdd:cd06223 72 KRVLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGGAR 116
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-196 |
2.59e-18 |
|
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: 83.38 E-value: 2.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 2 CSVVGIY---GNENASKLCFYSLFAMQHRGQEAAGISSSDGIhiktvkdrglvtqifkeehfnilkgnmAIGHTRYStag 78
Cdd:cd00712 1 CGIAGIIgldGASVDRATLERMLDALAHRGPDGSGIWIDEGV---------------------------ALGHRRLS--- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 79 ddsILD----AQPVfaRYGLGEISIAHNGNLVNAKEIRDELIKIGAIFQSNMDTENLIHLIaknhqkptlKERIIDAVKK 154
Cdd:cd00712 51 ---IIDlsggAQPM--VSEDGRLVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHLY---------EEWGEDCLER 116
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 494738241 155 IKGAFSLVILSRTK--MFAIRDPFGFRPLSLGkIKSGGYIVASE 196
Cdd:cd00712 117 LNGMFAFALWDKRKrrLFLARDRFGIKPLYYG-RDGGGLAFASE 159
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
2-217 |
6.58e-17 |
|
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: 80.00 E-value: 6.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 2 CSVVGIY---GNENASKLCFYSLFAMQHRG-QEAAG-----------ISSSDGIHIktVKDRGLVTQIFKEehFNI--LK 64
Cdd:cd01907 1 CGIFGIMskdGEPFVGALLVEMLDAMQERGpGDGAGfalygdpdafvYSSGKDMEV--FKGVGYPEDIARR--YDLeeYK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 65 GNMAIGHTRYSTAGDDSILDAQPvfarYGLGEISIAHNGNLVNAKEIRDELIKIGAIFQSNMDTENLIHLIAKNH----- 139
Cdd:cd01907 77 GYHWIAHTRQPTNSAVWWYGAHP----FSIGDIAVVHNGEISNYGSNREYLERFGYKFETETDTEVIAYYLDLLLrkggl 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 140 ---------------QKPTLKERIIDAVKKIKGAFSLVILSRTKMFAIRDPFGFRPLSLGKIKSGGYIvASETCAF-ELV 203
Cdd:cd01907 153 pleyykhiirmpeeeRELLLALRLTYRLADLDGPFTIIVGTPDGFIVIRDRIKLRPAVVAETDDYVAI-ASEECAIrEIP 231
|
250
....*....|....*.
gi 494738241 204 GAEFIRDI--KPGEMI 217
Cdd:cd01907 232 DRDNAKVWepRPGEYV 247
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-243 |
3.19e-16 |
|
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: 80.65 E-value: 3.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 1 MCSVVGIYGNENASKLcfySLF-----AMQHRGQEAAGISSSDGIhiktvkdrglvtqifkeehfnilkgnmAIGHTRys 75
Cdd:COG0367 1 MCGIAGIIDFDGGADR---EVLermldALAHRGPDGSGIWVDGGV---------------------------ALGHRR-- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 76 tagdDSILD-----AQPVFarYGLGEISIAHNGNLVNAKEIRDELIKIGAIFQSNMDTENLIHLIAknhqkptlkERIID 150
Cdd:COG0367 49 ----LSIIDlseggHQPMV--SEDGRYVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHAYE---------EWGED 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 151 AVKKIKGAFSLVILSRTK--MFAIRDPFGFRPLSLGKiKSGGYIVASETCAFeLVGAEFIRDIKPGEMITFengelkseM 228
Cdd:COG0367 114 CLERLNGMFAFAIWDRRErrLFLARDRFGIKPLYYAE-DGGGLAFASELKAL-LAHPGVDRELDPEALAEY--------L 183
|
250
....*....|....*.
gi 494738241 229 IFNPTPK-QCIFEYIY 243
Cdd:COG0367 184 TLGYVPApRTIFKGIR 199
|
|
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
1-225 |
7.51e-15 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 76.49 E-value: 7.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 1 MCSVVGIYG---NENASKLCFYSLF-AMQHRGQEAAGISSSDgihiktvkdrglvtqifkeehfnilkgNMAIGHTRYSt 76
Cdd:PRK09431 1 MCGIFGILDiktDADELRKKALEMSrLMRHRGPDWSGIYASD---------------------------NAILGHERLS- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 77 agddsILD----AQPVFARYGlgEISIAHNGNLVNAKEIRDELIKIGAiFQSNMDTENLIHLiaknhqkptLKERIIDAV 152
Cdd:PRK09431 53 -----IVDvnggAQPLYNEDG--THVLAVNGEIYNHQELRAELGDKYA-FQTGSDCEVILAL---------YQEKGPDFL 115
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494738241 153 KKIKGAFSLVILSRTK--MFAIRDPFGFRPLSLGKIKSGGYIVASETCAFELVgAEFIRDIKPGEMITFENGELK 225
Cdd:PRK09431 116 DDLDGMFAFALYDSEKdaYLIARDPIGIIPLYYGYDEHGNLYFASEMKALVPV-CKTIKEFPPGHYYWSKDGEFV 189
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
64-247 |
6.75e-14 |
|
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing asparagine synthase. A poorly conserved C-terminal extension was removed from the model. Bacterial members of the family tend to have a long, poorly conserved insert lacking from archaeal and eukaryotic sequences. Multiple isozymes have been demonstrated, such as in Bacillus subtilis. Long-branch members of the phylogenetic tree (which typically were also second or third candidate members from their genomes) were removed from the seed alignment and score below trusted cutoff. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 273676 [Multi-domain] Cd Length: 466 Bit Score: 73.14 E-value: 6.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 64 KGNMAIGHTRYSTAgdDSILDAQPVFARYGlgEISIAHNGNLVNAKEIRDELIKIGAIFQSNMDTENLIHLIAKnHQKpt 143
Cdd:TIGR01536 39 DGNAILGHRRLAII--DLSGGAQPMSNEGK--TYVIVFNGEIYNHEELREELEAKGYTFQTDSDTEVILHLYEE-WGE-- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 144 lkeriiDAVKKIKGAFSLVIL--SRTKMFAIRDPFGFRPLSLGKIkSGGYIVASETCAFELVGaefirDIKPgemitFEN 221
Cdd:TIGR01536 112 ------ECVDRLDGMFAFALWdsEKGELFLARDRFGIKPLYYAYD-GGQLYFASEIKALLAHP-----NIKP-----FPD 174
|
170 180
....*....|....*....|....*...
gi 494738241 222 GE-LKSEMIFNP-TPKQCIFEYIYFARP 247
Cdd:TIGR01536 175 GAaLAPGFGFVRvPPPSTFFRGVFELEP 202
|
|
| YafJ |
COG0121 |
Predicted glutamine amidotransferase YafJ [General function prediction only]; |
63-223 |
9.21e-11 |
|
Predicted glutamine amidotransferase YafJ [General function prediction only];
Pssm-ID: 439891 [Multi-domain] Cd Length: 248 Bit Score: 61.91 E-value: 9.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 63 LKGNMAIGHTRYSTAGDDSILDAQPvFARyglGEISIAHNGNLVNAKEIRDELIK-IGAIFQSNM----DTENLIHLIAK 137
Cdd:COG0121 74 IKSRLVIAHVRKATVGPVSLENTHP-FRG---GRWLFAHNGQLDGFDRLRRRLAEeLPDELYFQPvgttDSELAFALLLS 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 138 NHQK--PTLKERIIDAVKKIK------GAFSLVILSRTKMFAIRDPFGFRPLSL-----GKIKSGGYIVASETcafeLVG 204
Cdd:COG0121 150 RLRDggPDPAEALAEALRELAelarapGRLNLLLSDGERLYATRYTSDDPYPTLyyltrTTPDDRVVVVASEP----LTD 225
|
170
....*....|....*....
gi 494738241 205 AEFIRDIKPGEMITFENGE 223
Cdd:COG0121 226 DEGWTEVPPGELLVVRDGL 244
|
|
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
1-166 |
9.63e-10 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 60.53 E-value: 9.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 1 MCSVVGiYGNENASK-------LCFYSLFAMQHRGQEAAGISSSDGIHIKT-----VKDRG----LVTQIFKEEHFNILK 64
Cdd:PLN02981 1 MCGIFA-YLNYNVPRerrfileVLFNGLRRLEYRGYDSAGIAIDNDPSLESssplvFREEGkiesLVRSVYEEVAETDLN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 65 GNMA------IGHTRYSTAGDDSILDAQPVFARYGlGEISIAHNGNLVNAKEIRDELIKIGAIFQSNMDTEnLIHLIAK- 137
Cdd:PLN02981 80 LDLVfenhagIAHTRWATHGPPAPRNSHPQSSGPG-NEFLVVHNGIITNYEVLKETLLRHGFTFESDTDTE-VIPKLAKf 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 494738241 138 ----NHQKP---TLKERIIDAVKKIKGAFSLVILSR 166
Cdd:PLN02981 158 vfdkLNEEEgdvTFSQVVMEVMRQLEGAYALIFKSP 193
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
95-196 |
4.18e-09 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 58.57 E-value: 4.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 95 GEISIAHNGNLVNAKEIRDELIKIGAIFQSNMDTENLIHLIaKNHQKPtlkeriiDAVKKIKGAFSLVILSRTK--MFAI 172
Cdd:PTZ00077 73 ETVALMQNGEIYNHWEIRPELEKEGYKFSSNSDCEIIGHLY-KEYGPK-------DFWNHLDGMFATVIYDMKTntFFAA 144
|
90 100
....*....|....*....|....
gi 494738241 173 RDPFGFRPLSLGKIKSGGYIVASE 196
Cdd:PTZ00077 145 RDHIGIIPLYIGYAKDGSIWFSSE 168
|
|
| YafJ |
cd01908 |
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ... |
1-222 |
2.21e-08 |
|
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: 55.09 E-value: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 1 MCSVVGIYGNE---NASKLCFY-SLFAMQHRGQEAAGISSSDG-------------IHIKTVK----DRGLVTQIFKeeh 59
Cdd:cd01908 1 MCRLLGYSGAPiplEPLLIRPShSLLVQSGGPREMKGTVHADGwgigwyegkggrpFRYRSPLpawsDINLESLARP--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 60 fniLKGNMAIGHTRYSTAGDDSILDAQPvFARyglGEISIAHNGNLVNAKEIRDELI-KIGAIFQSNMDTENLIHLI--- 135
Cdd:cd01908 78 ---IKSPLVLAHVRAATVGPVSLENCHP-FTR---GRWLFAHNGQLDGFRLLRRRLLrLLPRLPVGTTDSELAFALLlsr 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 136 ---AKNHQKPTLKERIIDAVKKI-----KGAFSLVILSRTKMFAIR-------------DPFGFRPLSLGKIK---SGGY 191
Cdd:cd01908 151 lleRDPLDPAELLDAILQTLRELaalapPGRLNLLLSDGEYLIATRyasapslyyltrrAPFGCARLLFRSVTtpnDDGV 230
|
250 260 270
....*....|....*....|....*....|.
gi 494738241 192 IVASETcafeLVGAEFIRDIKPGEMITFENG 222
Cdd:cd01908 231 VVASEP----LTDDEGWTEVPPGELVVVSEG 257
|
|
| PRK07322 |
PRK07322 |
adenine phosphoribosyltransferase; Provisional |
264-370 |
1.53e-06 |
|
adenine phosphoribosyltransferase; Provisional
Pssm-ID: 180928 Cd Length: 178 Bit Score: 48.05 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 264 GRELAKEMPVEADMVVPVPDSGVAAALGYSEKSKIPFEMA-IMRNHYVGRTFIEPTQEIRdLKVKMKL---SPIKHKIEG 339
Cdd:PRK07322 42 AEALAKRLPTEVDVLVTPETKGIPLAHALSRRLGKPYVVArKSRKPYMQDPIIQEVVSIT-TGKPQLLvldGADAEKLKG 120
|
90 100 110
....*....|....*....|....*....|.
gi 494738241 340 KRLVVIDDSIVRGTTSRRIVRMLKEAGAKEV 370
Cdd:PRK07322 121 KRVAIVDDVVSTGGTLTALERLVERAGGQVV 151
|
|
| PLN02549 |
PLN02549 |
asparagine synthase (glutamine-hydrolyzing) |
1-196 |
4.30e-06 |
|
asparagine synthase (glutamine-hydrolyzing)
Pssm-ID: 178164 [Multi-domain] Cd Length: 578 Bit Score: 48.99 E-value: 4.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 1 MCSVVGIYG---NENASKLCFYSLFA-MQHRGQEaagissSDGIHIktVKDRGLVtqifkeehfnilkgnmaigHTRYS- 75
Cdd:PLN02549 1 MCGILAVLGcsdDSQAKRSRVLELSRrLRHRGPD------WSGLYG--NEDCYLA-------------------HERLAi 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 76 ---TAGDdsildaQPVFarYGLGEISIAHNGNLVNAKEIRDELIKIgaIFQSNMDTENLIHLIAKNHQkptlkeriiDAV 152
Cdd:PLN02549 54 mdpESGD------QPLY--NEDKTIVVTANGEIYNHKELREKLKLH--KFRTGSDCEVIAHLYEEHGE---------EFV 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 494738241 153 KKIKGAFSLVILSR--TKMFAIRDPFGFRPLSLGKIKSGGYIVASE 196
Cdd:PLN02549 115 DMLDGMFSFVLLDTrdNSFIAARDHIGITPLYIGWGLDGSVWFASE 160
|
|
| Pribosyltran |
pfam00156 |
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ... |
276-371 |
3.04e-05 |
|
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: 43.89 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 276 DMVVPVPDSGVAAALGYSEKSKIPFEMAIMRNHYvgrtfieptqeiRDLKVKMKLSPIKHKIEGKRLVVIDDSIVRGTTS 355
Cdd:pfam00156 31 DVVVGILRGGLPFAGILARRLDVPLAFVRKVSYN------------PDTSEVMKTSSALPDLKGKTVLIVDDILDTGGTL 98
|
90
....*....|....*.
gi 494738241 356 RRIVRMLKEAGAKEVH 371
Cdd:pfam00156 99 LKVLELLKNVGPKEVK 114
|
|
| ComFC |
COG1040 |
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General ... |
263-371 |
1.28e-04 |
|
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General function prediction only];
Pssm-ID: 440662 [Multi-domain] Cd Length: 196 Bit Score: 42.89 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 263 MGRELAKEMPVEADMVVPVPDSgvAAAL---GY----------SEKSKIPfemaiMRNHYVGRTFIEPTQE-------IR 322
Cdd:COG1040 67 LARALREALLPRPDLIVPVPLH--RRRLrrrGFnqaellaralARALGIP-----VLPDLLRRVRATPSQAglsraerRR 139
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 494738241 323 DLKVKMKLSPiKHKIEGKRLVVIDDsiVR--GTTSRRIVRMLKEAGAKEVH 371
Cdd:COG1040 140 NLRGAFAVRP-PARLAGKHVLLVDD--VLttGATLAEAARALKAAGAARVD 187
|
|
| PRK02277 |
PRK02277 |
orotate phosphoribosyltransferase-like protein; Provisional |
336-370 |
4.72e-04 |
|
orotate phosphoribosyltransferase-like protein; Provisional
Pssm-ID: 235023 [Multi-domain] Cd Length: 200 Bit Score: 41.01 E-value: 4.72e-04
10 20 30
....*....|....*....|....*....|....*
gi 494738241 336 KIEGKRLVVIDDSIVRGTTSRRIVRMLKEAGAKEV 370
Cdd:PRK02277 137 SVEGKRCVIVDDVITSGTTMKETIEYLKEHGGKPV 171
|
|
| Gn_AT_II_novel |
cd03766 |
Gn_AT_II_novel. This asparagine synthase-related domain is present in eukaryotes but its ... |
114-190 |
5.38e-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: 40.73 E-value: 5.38e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494738241 114 ELIKIGAIFQSNMDTENLIHLIAKNhqkPTLKERIIDAVKKIKGAFSLVI--LSRTKMFAIRDPFGFRPLSLGKIKSGG 190
Cdd:cd03766 81 ELYNIDGVEDEENDTEVIFELLANC---SSESQDILDVLSSIEGPFAFIYydASENKLYFGRDCLGRRSLLYKLDPNGF 156
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
69-165 |
7.85e-04 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 41.79 E-value: 7.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 69 IGHTRYSTAGDDSILDAQPvfARYGLGEISIAHNGNLVNAKEIRDELIKIGAIFQSNMDTENLI----HLIAKNHqKPTL 144
Cdd:PTZ00394 101 IAHTRWATHGGVCERNCHP--QQSNNGEFTIVHNGIVTNYMTLKELLKEEGYHFSSDTDTEVISvlseYLYTRKG-IHNF 177
|
90 100
....*....|....*....|.
gi 494738241 145 KERIIDAVKKIKGAFSLVILS 165
Cdd:PTZ00394 178 ADLALEVSRMVEGSYALLVKS 198
|
|
| ribP_PPkin |
TIGR01251 |
ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In ... |
276-432 |
9.54e-04 |
|
ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In some systems, close homologs lacking enzymatic activity exist and perform regulatory functions. The model is designated subfamily rather than equivalog for this reason. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273523 [Multi-domain] Cd Length: 308 Bit Score: 41.11 E-value: 9.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 276 DMVVPVPDSG-VAAALGYSEKSKIPFEMaimrnhyvgrtfIEPTQEIRDLKVKMKlsPIKHKIEGKRLVVIDDSIVRGTT 354
Cdd:TIGR01251 160 NPVVVSPDAGgVERAKKVADALGCPLAI------------IDKRRISATNEVEVM--NLVGDVEGKDVVIVDDIIDTGGT 225
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494738241 355 SRRIVRMLKEAGAKEVHMRIASPATTGPCYYGVDTPTKEELIasrlSTDEIAKYIEADSLAYLSIDGLV-RAVKDKKEN 432
Cdd:TIGR01251 226 IAKAAEILKSAGAKRVIAAATHGVFSGPAIERIANAGVEEVI----VTNTIPHEKHKPKVSVISVAPLIaEAIRRIHNN 300
|
|
| PRK02269 |
PRK02269 |
ribose-phosphate diphosphokinase; |
276-424 |
1.63e-03 |
|
ribose-phosphate diphosphokinase;
Pssm-ID: 167353 [Multi-domain] Cd Length: 320 Bit Score: 40.55 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 276 DMVVPVPD-SGVAAALGYSEKSKIPfeMAIMRNhyvgrtfieptqeiRDLKVKMKLSPIKH---KIEGKRLVVIDDSIVR 351
Cdd:PRK02269 166 DVVVVSPDhGGVTRARKLAQFLKTP--IAIIDK--------------RRSVDKMNTSEVMNiigNVKGKKCILIDDMIDT 229
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494738241 352 GTTSRRIVRMLKEAGAKEVHMRIASPATTGPCYYGVDTPTKEELIAS---RLSTDEIAKYIEADSLAYLSIDGLVR 424
Cdd:PRK02269 230 AGTICHAADALAEAGATEVYASCTHPVLSGPALDNIQKSAIEKLVVLdtiYLPEERLIDKIEQISIADLLGEAIIR 305
|
|
| Hpt1 |
COG2236 |
Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine ... |
330-391 |
2.86e-03 |
|
Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine phosphoribosyltransferase is part of the Pathway/BioSystem: Purine salvage
Pssm-ID: 441837 [Multi-domain] Cd Length: 153 Bit Score: 38.29 E-value: 2.86e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494738241 330 LSPIKHKIEGKRLVVIDDSIVRGTTSRRIVRMLKEAGAKEVhmRIASP-----ATTGPCYYGVDTPT 391
Cdd:COG2236 79 KGPLDEDLAGKRVLIVDDVADTGRTLEAVRDLLKEAGPAEV--RTAVLyykpsSKFKPDYYAEETDA 143
|
|
| PLN02369 |
PLN02369 |
ribose-phosphate pyrophosphokinase |
243-400 |
5.04e-03 |
|
ribose-phosphate pyrophosphokinase
Pssm-ID: 215209 [Multi-domain] Cd Length: 302 Bit Score: 38.91 E-value: 5.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 243 YFARPDSNIFGKNV---YsirkqmgreLAKEMPVEADMVVPVPD-SGVAAALGYSEK-SKIPFEMAIMRNHyvGRTFIEP 317
Cdd:PLN02369 125 YFDIPVDHVYGQPVildY---------LASKTISSPDLVVVSPDvGGVARARAFAKKlSDAPLAIVDKRRQ--GHNVAEV 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494738241 318 TQEIRDLKvkmklspikhkieGKRLVVIDDSIVRGTTSRRIVRMLKEAGAKEVHmriaspattGPCYYGVDTPTKEELIA 397
Cdd:PLN02369 194 MNLIGDVK-------------GKVAIMVDDMIDTAGTITKGAALLHQEGAREVY---------ACATHAVFSPPAIERLS 251
|
...
gi 494738241 398 SRL 400
Cdd:PLN02369 252 SGL 254
|
|
| PRK00934 |
PRK00934 |
ribose-phosphate pyrophosphokinase; Provisional |
309-371 |
7.34e-03 |
|
ribose-phosphate pyrophosphokinase; Provisional
Pssm-ID: 234868 [Multi-domain] Cd Length: 285 Bit Score: 38.36 E-value: 7.34e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494738241 309 YVGRTFIEPTqeirdlKVKMKLSPIKhkIEGKRLVVIDDSIVRGTTSRRIVRMLKEAGAKEVH 371
Cdd:PRK00934 182 YLEKTRISPT------EVEIAPKNLD--VKGKDVLIVDDIISTGGTMATAIKILKEQGAKKVY 236
|
|
| PyrE |
COG0461 |
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ... |
338-372 |
8.49e-03 |
|
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate phosphoribosyltransferase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 440229 Cd Length: 201 Bit Score: 37.44 E-value: 8.49e-03
10 20 30
....*....|....*....|....*....|....*
gi 494738241 338 EGKRLVVIDDSIVRGTTSRRIVRMLKEAGAKEVHM 372
Cdd:COG0461 111 PGERVLVVEDVITTGGSVLEAVEALREAGAEVVGV 145
|
|
| |
