|
Name |
Accession |
Description |
Interval |
E-value |
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
1-476 |
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: 768.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 1 MCGIVGIVGKTPVAQSLYDGLTVIQHRGQDAAGIMTIDQNMFNLRKANGLVRDVFHTRHMKRLSGNMGIGHVRYPTAGTS 80
Cdd:COG0034 7 ECGVFGIYGHEDVAQLTYYGLYALQHRGQESAGIATSDGGRFHLHKGMGLVSDVFDEEDLERLKGNIAIGHVRYSTTGSS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 81 SSAEAQPFYVNSPFG-IAFAHNGNLTNAHDLQEEVFRIARrHINTTSDSELLLNILAHELqqvaglsvTAEHIFEVVTKV 159
Cdd:COG0034 87 SLENAQPFYVNSPFGsIALAHNGNLTNAEELREELEEEGA-IFQTTSDTEVILHLIAREL--------TKEDLEEAIKEA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 160 HKKIRGAYAVVAaIIGQGIVAFRDPHGIRPLALGKRmtelGEEWMVASESVALDAVGFQFIRDVSPGEAVYITENGeLHT 239
Cdd:COG0034 158 LRRVKGAYSLVI-LTGDGLIAARDPNGIRPLVLGKL----EDGYVVASESCALDILGAEFVRDVEPGEIVVIDEDG-LRS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 240 RQCAENPITSPCIFEFVYFARPDSFIDGISVYASRVNMGRRLgekiAREwSDLDIDVVIPIPETSMDVALQIANTLELPY 319
Cdd:COG0034 232 RQFAEKPRPAPCIFEYVYFARPDSVIDGRSVYEARKRMGREL----ARE-APVDADVVIPVPDSGRPAAIGYAEESGIPY 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 320 RQGFVKNRYIGRTFIMPGQTMRKKSVRRKLNAISSEFKGKNVLLVDDSIVRGTTSGQIIEMARESGAKKVYFASAAPEIR 399
Cdd:COG0034 307 EEGLIKNRYVGRTFIQPTQELRELGVRLKLNPIREVVKGKRVVLVDDSIVRGTTSRRIVKMLREAGAKEVHFRIASPPIR 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1023065406 400 FPNVYGIDMPSANELIAYGREIDQIADLIQADGLIFQDITDLVEAVREEndsIQRFETSVFDGNYITG--DVDQDYLER 476
Cdd:COG0034 387 YPCYYGIDTPTREELIAANRSVEEIREYIGADSLGYLSLEGLIEAVGEP---IEGFCTACFTGDYPTGipDEEKKRLEL 462
|
|
| purF |
TIGR01134 |
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ... |
2-464 |
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: 654.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 2 CGIVGIVGKTPVAQSL-YDGLTVIQHRGQDAAGIMTIDQNMFNLRKANGLVRDVFHTRHMKRLSGNMGIGHVRYPTAGTS 80
Cdd:TIGR01134 1 CGVVGIYGQEEVAASLtYYGLYALQHRGQESAGISVFDGNRFRLHKGNGLVSDVFNEEHLQRLKGNVGIGHVRYSTAGSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 81 SSAEAQPFYVNSPFG-IAFAHNGNLTNAHDLQEEVFRiARRHINTTSDSELLLNILAHELQQVAGLsvtaehiFEVVTKV 159
Cdd:TIGR01134 81 GLENAQPFVVNSPYGgLALAHNGNLVNADELRRELEE-EGRHFNTTSDSEVLLHLLAHNDESKDDL-------FDAVARV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 160 HKKIRGAYAVVAaIIGQGIVAFRDPHGIRPLALGKRmtelGEEWMVASESVALDAVGFQFIRDVSPGEAVYITEnGELHT 239
Cdd:TIGR01134 153 LERVRGAYALVL-MTEDGLVAVRDPHGIRPLVLGRR----GDGYVVASESCALDILGAEFVRDVEPGEVVVIFD-GGLES 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 240 RQCAENPiTSPCIFEFVYFARPDSFIDGISVYASRVNMGRRLGEKiarewSDLDIDVVIPIPETSMDVALQIANTLELPY 319
Cdd:TIGR01134 227 RQCARRP-RAPCVFEYVYFARPDSVIDGISVYYARKRMGKELARE-----SPVEADVVVPVPDSGRSAALGFAQASGIPY 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 320 RQGFVKNRYIGRTFIMPGQTMRKKSVRRKLNAISSEFKGKNVLLVDDSIVRGTTSGQIIEMARESGAKKVYFASAAPEIR 399
Cdd:TIGR01134 301 REGLIKNRYVGRTFIMPTQELRELSVRLKLNPVRAVFEGKRVVLVDDSIVRGTTSRQIVEMLRDAGAKEVHVRIASPPIR 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1023065406 400 FPNVYGIDMPSANELIAYGREIDQIADlIQADGLIFQDITDLVEAVREendSIQRFETSVFDGNY 464
Cdd:TIGR01134 381 YPCYYGIDMPTREELIAARRTVEEIRK-IGADSLAYLSLEGLKEAVGN---PESDLCLACFTGEY 441
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
1-488 |
0e+00 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 617.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 1 MCGIVGIVGKTPVAQSLYDGLTVIQHRGQDAAGIMTIDQNMFNLRKANGLVRDVFHTRHMKRLSGNMGIGHVRYPTAGTS 80
Cdd:PLN02440 1 ECGVVGIFGDPEASRLCYLGLHALQHRGQEGAGIVTVDGNRLQSITGNGLVSDVFDESKLDQLPGDIAIGHVRYSTAGAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 81 SSAEAQPFYVNSPFG-IAFAHNGNLTNAHDLQEEVfRIARRHINTTSDSELLLNILAHELqqvaglsvtAEHIFEVVTKV 159
Cdd:PLN02440 81 SLKNVQPFVANYRFGsIGVAHNGNLVNYEELRAKL-EENGSIFNTSSDTEVLLHLIAISK---------ARPFFSRIVDA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 160 HKKIRGAYAVVAAIIGQgIVAFRDPHGIRPLALGKRMTElgeEWMVASESVALDAVGFQFIRDVSPGEAVYITEnGELHT 239
Cdd:PLN02440 151 CEKLKGAYSMVFLTEDK-LVAVRDPHGFRPLVMGRRSNG---AVVFASETCALDLIGATYEREVNPGEVIVVDK-DKGVS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 240 RQCAE-NPITSPCIFEFVYFARPDSFIDGISVYASRVNMGRRLGEKIARewsdlDIDVVIPIPETSMDVALQIANTLELP 318
Cdd:PLN02440 226 SQCLMpHPEPKPCIFEHIYFARPNSIVFGRSVYESRLEFGEILATEIPV-----DCDVVIPVPDSGRVAALGYAAKLGVP 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 319 YRQGFVKNRYIGRTFIMPGQTMRKKSVRRKLNAISSEFKGKNVLLVDDSIVRGTTSGQIIEMARESGAKKVYFASAAPEI 398
Cdd:PLN02440 301 FQQGLIRSHYVGRTFIEPSQKIRDFSVKLKLNPVRSVLEGKRVVVVDDSIVRGTTSSKIVRMLREAGAKEVHMRIASPPI 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 399 RFPNVYGIDMPSANELIAYGREIDQIADLIQADGLIFQDITDLVEAVREENdsiQRFETSVFDGNY------ITGDVDQD 472
Cdd:PLN02440 381 IASCYYGVDTPSREELISNRMSVEEIRKFIGCDSLAFLPLEDLKKSLGEES---PRFCYACFSGDYpvlpkrVGGDIDDG 457
|
490
....*....|....*.
gi 1023065406 473 YLERIDISRGEKSREA 488
Cdd:PLN02440 458 YLESLEEAGRGWGRKG 473
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
2-475 |
3.99e-157 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 455.26 E-value: 3.99e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 2 CGIVGIVGKTP--VAQSLYDGLTVIQHRGQDAAGIMTIDQNMFNLRKANGLVRDVFHTRHMKRLSGNMGIGHVRYPTAGT 79
Cdd:PRK05793 15 CGVFGVFSKNNidVASLTYYGLYALQHRGQESAGIAVSDGEKIKVHKGMGLVSEVFSKEKLKGLKGNSAIGHVRYSTTGA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 80 SSSAEAQPFYVNSPFG-IAFAHNGNLTNAHDLQEEVfRIARRHINTTSDSELLLNILAHELQQvaglsvtaeHIFEVVTK 158
Cdd:PRK05793 95 SDLDNAQPLVANYKLGsIAIAHNGNLVNADVIRELL-EDGGRIFQTSIDSEVILNLIARSAKK---------GLEKALVD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 159 VHKKIRGAYAVVaaIIGQG-IVAFRDPHGIRPLALGKrmteLGEEWMVASESVALDAVGFQFIRDVSPGEAVYITENGeL 237
Cdd:PRK05793 165 AIQAIKGSYALV--ILTEDkLIGVRDPHGIRPLCLGK----LGDDYILSSESCALDTIGAEFIRDVEPGEIVIIDEDG-I 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 238 HTRQCAENPITSPCIFEFVYFARPDSFIDGISVYASRVNMGRRLgekiAREwSDLDIDVVIPIPETSMDVALQIANTLEL 317
Cdd:PRK05793 238 KSIKFAEKTKCQTCAFEYIYFARPDSVIDGISVYESRVRAGRQL----YKE-YPVDADIVIGVPDSGIPAAIGYAEASGI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 318 PYRQGFVKNRYIGRTFIMPGQTMRKKSVRRKLNAISSEFKGKNVLLVDDSIVRGTTSGQIIEMARESGAKKVYFASAAPE 397
Cdd:PRK05793 313 PYGIGFIKNKYVGRTFIAPSQELRERAVRVKLNPLKVNVEGKRVVLIDDSIVRGTTSKRLVELLRKAGAKEVHFRVSSPP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 398 IRFPNVYGIDMPSANELIAYGREIDQIADLIQADGLIFQDITDLVEAVREENDsiqrFETSVFDGNY---ITGDVDQDYL 474
Cdd:PRK05793 393 VKYPCYFGIDTPYRKELIGANMSVEEIREMIGADSLGYLSIEGLLESLNGDKG----FCLGCFNGVYpvsAPKEGPKYLL 468
|
.
gi 1023065406 475 E 475
Cdd:PRK05793 469 E 469
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
2-266 |
9.99e-135 |
|
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: 389.90 E-value: 9.99e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 2 CGIVGIVGKTPVAQSLYDGLTVIQHRGQDAAGIMTIDQNMFNLRKANGLVRDVFHTRHMKRLSGNMGIGHVRYPTAGTSS 81
Cdd:cd00715 1 CGVFGIYGAEDAARLTYLGLYALQHRGQESAGIATSDGKRFHTHKGMGLVSDVFDEEKLRRLPGNIAIGHVRYSTAGSSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 82 SAEAQPFYVNSPFG-IAFAHNGNLTNAHDLQEEVFRIArRHINTTSDSELLLNILAHELQQvaglsvtaEHIFEVVTKVH 160
Cdd:cd00715 81 LENAQPFVVNSPLGgIALAHNGNLVNAKELREELEEEG-RIFQTTSDSEVILHLIARSLAK--------DDLFEAIIDAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 161 KKIRGAYAVVaAIIGQGIVAFRDPHGIRPLALGKRMtelGEEWMVASESVALDAVGFQFIRDVSPGEAVYITENGeLHTR 240
Cdd:cd00715 152 ERVKGAYSLV-IMTADGLIAVRDPHGIRPLVLGKLE---GDGYVVASESCALDIIGAEFVRDVEPGEIVVIDDDG-LESS 226
|
250 260
....*....|....*....|....*.
gi 1023065406 241 QCAENPITSPCIFEFVYFARPDSFID 266
Cdd:cd00715 227 QRAPKPKPAPCIFEYVYFARPDSVID 252
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
2-229 |
1.11e-57 |
|
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. This domain is related to members of the Ntn (N-terminal nucleophile) hydrolase superfamily and is found at the N-terminus of enzymes such as glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). GLMS catalyzes the formation of glucosamine 6-phosphate from fructose 6-phosphate and glutamine in amino sugar synthesis. GPATase catalyzes the first step in purine biosynthesis, an amide transfer from glutamine to PRPP, resulting in phosphoribosylamine, pyrophosphate and glutamate. Asparagine synthetase B synthesizes asparagine from aspartate and glutamine. Beta-LS catalyzes the formation of the beta-lactam ring in the beta-lactamase inhibitor clavulanic acid. GltS synthesizes L-glutamate from 2-oxoglutarate and L-glutamine. These enzymes are generally dimers, but GPATase also exists as a homotetramer.
Pssm-ID: 238212 [Multi-domain] Cd Length: 220 Bit Score: 190.74 E-value: 1.11e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 2 CGIVGIVGKTPVAQSLYD----GLTVIQHRGQDAAGIMTIDQNMFNLRKANGLVRDVFHTRHMKRLSGNMGIGHVRYPTA 77
Cdd:cd00352 1 CGIFGIVGADGAASLLLLlllrGLAALEHRGPDGAGIAVYDGDGLFVEKRAGPVSDVALDLLDEPLKSGVALGHVRLATN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 78 GTSSSAEAQPFYVNSPfGIAFAHNGNLTNAHDLQEEVFRiARRHINTTSDSELLLNILAHELQQvaglsvtaEHIFEVVT 157
Cdd:cd00352 81 GLPSEANAQPFRSEDG-RIALVHNGEIYNYRELREELEA-RGYRFEGESDSEVILHLLERLGRE--------GGLFEAVE 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1023065406 158 KVHKKIRGAYAVVAAIIGQG-IVAFRDPHGIRPLALGKRMtelGEEWMVASESVALDAVGFQFIRDVSPGEAV 229
Cdd:cd00352 151 DALKRLDGPFAFALWDGKPDrLFAARDRFGIRPLYYGITK---DGGLVFASEPKALLALPFKGVRRLPPGELL 220
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
2-212 |
3.70e-23 |
|
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus of glucosamine-6P synthase (GlmS, or GFAT in humans). The glutaminase domain catalyzes amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. In humans, GFAT catalyzes the first and rate-limiting step of hexosamine metabolism, the conversion of D-fructose-6P (Fru6P) into D-glucosamine-6P using L-glutamine as a nitrogen source. The end product of this pathway, UDP-N-acetyl glucosamine, is a major building block of the bacterial peptidoglycan and fungal chitin.
Pssm-ID: 238366 [Multi-domain] Cd Length: 215 Bit Score: 97.52 E-value: 3.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 2 CGIVGIVGKTPVAQSLYDGLTVIQHRGQDAAGIMTIDQNMFNLRKANGLVRDVFHTRHMKRLSGNMGIGHVRYPTAGTSS 81
Cdd:cd00714 1 CGIVGYIGKREAVDILLEGLKRLEYRGYDSAGIAVIGDGSLEVVKAVGKVANLEEKLAEKPLSGHVGIGHTRWATHGEPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 82 SAEAQPfYVNSPFGIAFAHNGNLTNAHDLQEEVfrIARRHI-NTTSDSELLLNILAHELQQvaglsvtAEHIFEVVTKVH 160
Cdd:cd00714 81 DVNAHP-HRSCDGEIAVVHNGIIENYAELKEEL--EAKGYKfESETDTEVIAHLIEYYYDG-------GLDLLEAVKKAL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1023065406 161 KKIRGAYAVVAAIIGQG--IVAFRdpHGiRPLALGkrmteLGEEWM-VASESVAL 212
Cdd:cd00714 151 KRLEGAYALAVISKDEPdeIVAAR--NG-SPLVIG-----IGDGENfVASDAPAL 197
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
1-235 |
4.53e-21 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 96.65 E-value: 4.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 1 MCGIVGIVGKTPVAQSLYDGLTVIQHRGQDAAGIMTIDQNMFNLRKANGLVRDVFHTRHMKRLSGNMGIGHVRYPTAGTS 80
Cdd:PRK00331 1 MCGIVGYVGQRNAAEILLEGLKRLEYRGYDSAGIAVLDDGGLEVRKAVGKVANLEAKLEEEPLPGTTGIGHTRWATHGKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 81 SSAEAQPFYVNSpfG-IAFAHNGNLTNAHDLQEEVfrIARRHI-NTTSDSELLLNILAHELQQvaGLSVtaehiFEVVTK 158
Cdd:PRK00331 81 TERNAHPHTDCS--GrIAVVHNGIIENYAELKEEL--LAKGHVfKSETDTEVIAHLIEEELKE--GGDL-----LEAVRK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 159 VHKKIRGAYAVvaAIIGQG-----IVAFRDPhgirPLALGkrmteLGE-EWMVASesvalDAVGF-QFIRDVSP---GEA 228
Cdd:PRK00331 150 ALKRLEGAYAL--AVIDKDepdtiVAARNGS----PLVIG-----LGEgENFLAS-----DALALlPYTRRVIYledGEI 213
|
....*..
gi 1023065406 229 VYITENG 235
Cdd:PRK00331 214 AVLTRDG 220
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
2-215 |
1.23e-20 |
|
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: 91.18 E-value: 1.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 2 CGIVGIVGKTP---VAQSLYDGLTVIQHRG-QDAAG----------IMTIDQNMfNLRKANGLVRDVFHTRHMKRLSGNM 67
Cdd:cd01907 1 CGIFGIMSKDGepfVGALLVEMLDAMQERGpGDGAGfalygdpdafVYSSGKDM-EVFKGVGYPEDIARRYDLEEYKGYH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 68 GIGHVRYPT--AGTSSSaeAQPFyvnSPFGIAFAHNGNLTNAHDLQEEVfRIARRHINTTSDSELLLNILAHELQQVAGL 145
Cdd:cd01907 80 WIAHTRQPTnsAVWWYG--AHPF---SIGDIAVVHNGEISNYGSNREYL-ERFGYKFETETDTEVIAYYLDLLLRKGGLP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 146 SVTAEHIFEVVTKV------------HKKIRGAYAVVAAiIGQGIVAFRDPHGIRPLALGKRmtelGEEWMVASESVALD 213
Cdd:cd01907 154 LEYYKHIIRMPEEErelllalrltyrLADLDGPFTIIVG-TPDGFIVIRDRIKLRPAVVAET----DDYVAIASEECAIR 228
|
..
gi 1023065406 214 AV 215
Cdd:cd01907 229 EI 230
|
|
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
1-235 |
6.34e-20 |
|
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: 93.15 E-value: 6.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 1 MCGIVGIVGKTPVAQSLYDGLTVIQHRGQDAAGIMTIDQNMFNLRKANGLVRDVFHTRHMKRLSGNMGIGHVRYPTAGTS 80
Cdd:COG0449 1 MCGIVGYIGKRDAAPILLEGLKRLEYRGYDSAGIAVLDDGGLEVRKAVGKLANLEEKLAEEPLSGTIGIGHTRWATHGAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 81 SSAEAQPFYVNSPfGIAFAHNGNLTNAHDLQEEVfrIARRHI-NTTSDSELLLNILAHELQQVAGLsvtaehiFEVVTKV 159
Cdd:COG0449 81 SDENAHPHTSCSG-RIAVVHNGIIENYAELREEL--EAKGHTfKSETDTEVIAHLIEEYLKGGGDL-------LEAVRKA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 160 HKKIRGAYAVVAAIIGQ--GIVAFRdpHGiRPLALGkrmteLGE-EWMVASESVALdavgFQFIRDVSP---GEAVYITE 233
Cdd:COG0449 151 LKRLEGAYALAVISADEpdRIVAAR--KG-SPLVIG-----LGEgENFLASDVPAL----LPYTRRVIYledGEIAVLTR 218
|
..
gi 1023065406 234 NG 235
Cdd:COG0449 219 DG 220
|
|
| PRTases_typeI |
cd06223 |
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ... |
277-396 |
5.38e-17 |
|
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: 77.44 E-value: 5.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 277 MGRRLGEKIAREWsdLDIDVVIPIPETSMDVALQIANTLELPYRQGFVKNRYIGRTFIMPGQtmrkksvrrKLNAISSEF 356
Cdd:cd06223 1 AGRLLAEEIREDL--LEPDVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSEPYG---------LELPLGGDV 69
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1023065406 357 KGKNVLLVDDSIVRGTTSGQIIEMARESGAKKVYFASAAP 396
Cdd:cd06223 70 KGKRVLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVLLD 109
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-212 |
8.53e-16 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 80.07 E-value: 8.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 1 MCGIVGIVGKTPVAQSLYDGLTVIQHRGQDAAGIMTI-DQNMFNLRK-------ANGLV--RDVFHTRHmkrLSGNMGIG 70
Cdd:PTZ00295 24 CCGIVGYLGNEDASKILLEGIEILQNRGYDSCGISTIsSGGELKTTKyasdgttSDSIEilKEKLLDSH---KNSTIGIA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 71 HVRYPTAGTSSSAEAQPfYVNSPFGIAFAHNGNLTNAHDLQEEVfrIARR-HINTTSDSELLLNILAHELQQvaglsvtA 149
Cdd:PTZ00295 101 HTRWATHGGKTDENAHP-HCDYKKRIALVHNGTIENYVELKSEL--IAKGiKFRSETDSEVIANLIGLELDQ-------G 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1023065406 150 EHIFEVVTKVHKKIRGAYAVvaAIIGQG-----IVAfrdPHGiRPLALGKRmtelGEEWMVASESVAL 212
Cdd:PTZ00295 171 EDFQEAVKSAISRLQGTWGL--CIIHKDnpdslIVA---RNG-SPLLVGIG----DDSIYVASEPSAF 228
|
|
| YafJ |
COG0121 |
Predicted glutamine amidotransferase YafJ [General function prediction only]; |
61-238 |
4.66e-13 |
|
Predicted glutamine amidotransferase YafJ [General function prediction only];
Pssm-ID: 439891 [Multi-domain] Cd Length: 248 Bit Score: 68.84 E-value: 4.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 61 KRLSGNMGIGHVRYPTAGTSSSAEAQPFYVnspFGIAFAHNGNLTN----AHDLQEEVFRIARRHINTTSDSELLLNILA 136
Cdd:COG0121 72 RPIKSRLVIAHVRKATVGPVSLENTHPFRG---GRWLFAHNGQLDGfdrlRRRLAEELPDELYFQPVGTTDSELAFALLL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 137 HELQQVAGLSVTAehIFEVVTKVhKKIRGAYAVVAAII--GQGIVAFRDPHGIRPLAL--GKRMTELGEEWMVASESVAL 212
Cdd:COG0121 149 SRLRDGGPDPAEA--LAEALREL-AELARAPGRLNLLLsdGERLYATRYTSDDPYPTLyyLTRTTPDDRVVVVASEPLTD 225
|
170 180
....*....|....*....|....*.
gi 1023065406 213 DAVgfqfIRDVSPGEAVYITENGELH 238
Cdd:COG0121 226 DEG----WTEVPPGELLVVRDGLEVE 247
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
64-208 |
5.08e-13 |
|
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain found in a variety of enzymes, such as asparagine synthetase and glutamine--fructose-6-phosphate transaminase.
Pssm-ID: 433279 [Multi-domain] Cd Length: 130 Bit Score: 65.79 E-value: 5.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 64 SGNMGIGHVRYPTAGTSSSAeAQPFYVNSPfGIAFAHNGNLTNAHDLQEEvFRIARRHINTTSDSELLLNILAHelqqva 143
Cdd:pfam13522 9 EGGVALGHVRLAIVDLPDAG-NQPMLSRDG-RLVLVHNGEIYNYGELREE-LADLGHAFRSRSDTEVLLALYEE------ 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1023065406 144 glsvTAEHIFEvvtkvhkKIRGAYAVVA--AIIGQGIVAfRDPHGIRPLALGkrmtELGEEWMVASE 208
Cdd:pfam13522 80 ----WGEDCLE-------RLRGMFAFAIwdRRRRTLFLA-RDRLGIKPLYYG----ILGGGFVFASE 130
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
81-214 |
1.01e-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: 62.15 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 81 SSAEAQPFyVNSPFG-IAFAHNGNLTNAHDLQEEVfrIARRHI-NTTSDSELLLNILAHelqqvaglsvtaEHIFEVVtk 158
Cdd:pfam13537 9 LEGGAQPM-VSSEDGrYVIVFNGEIYNYRELRAEL--EAKGYRfRTHSDTEVILHLYEA------------EWGEDCV-- 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1023065406 159 vhKKIRGAYAVvaAII---GQGIVAFRDPHGIRPLALGKRmteLGEEWMVASESVALDA 214
Cdd:pfam13537 72 --DRLNGMFAF--AIWdrrRQRLFLARDRFGIKPLYYGRD---DGGRLLFASELKALLA 123
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-241 |
6.37e-11 |
|
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: 64.47 E-value: 6.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 1 MCGIVGIVGKTPVAQS--LYDGLTVIQHRGQDAAGImtidqnmfnlrkanglvrdvfhtrhmkRLSGNMGIGHVRyptag 78
Cdd:COG0367 1 MCGIAGIIDFDGGADRevLERMLDALAHRGPDGSGI---------------------------WVDGGVALGHRR----- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 79 TS----SSAEAQPFyVNSPFGIAFAHNGNLTNAHDLQEEVfrIARRHI-NTTSDSELLLNilAHELQQVAGLsvtaehif 153
Cdd:COG0367 49 LSiidlSEGGHQPM-VSEDGRYVLVFNGEIYNYRELRAEL--EALGHRfRTHSDTEVILH--AYEEWGEDCL-------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 154 evvtkvhKKIRGAYAVvaAI---IGQGIVAFRDPHGIRPLAlgkrMTELGEEWMVASE----------SVALDAVG---- 216
Cdd:COG0367 116 -------ERLNGMFAF--AIwdrRERRLFLARDRFGIKPLY----YAEDGGGLAFASElkallahpgvDRELDPEAlaey 182
|
250 260 270
....*....|....*....|....*....|....*..
gi 1023065406 217 --FQF----------IRDVSPGEAVYITENGELHTRQ 241
Cdd:COG0367 183 ltLGYvpaprtifkgIRKLPPGHYLTVDAGGELEIRR 219
|
|
| YafJ |
cd01908 |
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ... |
69-182 |
2.19e-09 |
|
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine amidotransferase-like protein of unknown function found in prokaryotes, eukaryotes and archaea. YafJ has a conserved structural fold similar to those of other class II glutamine amidotransferases including glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). The YafJ fold is also somewhat similar to the Ntn (N-terminal nucleophile) hydrolase fold of the proteasomal alpha and beta subunits.
Pssm-ID: 238889 [Multi-domain] Cd Length: 257 Bit Score: 58.17 E-value: 2.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 69 IGHVRYPTAGTSSSAEAQPFYVNSpfgIAFAHNGNLTNAHDLQEEVFRIARRHINTTSDSELLLNILAHELQQVAGLSVT 148
Cdd:cd01908 84 LAHVRAATVGPVSLENCHPFTRGR---WLFAHNGQLDGFRLLRRRLLRLLPRLPVGTTDSELAFALLLSRLLERDPLDPA 160
|
90 100 110
....*....|....*....|....*....|....*...
gi 1023065406 149 AehIFEVVTKVHKKIRGAYAVVAAII----GQGIVAFR 182
Cdd:cd01908 161 E--LLDAILQTLRELAALAPPGRLNLllsdGEYLIATR 196
|
|
| ComFC |
COG1040 |
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General ... |
271-395 |
7.46e-07 |
|
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General function prediction only];
Pssm-ID: 440662 [Multi-domain] Cd Length: 196 Bit Score: 49.82 E-value: 7.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 271 YASRVNMGRRLGEKIAREWSDL---DIDVVIPIP-----------ETSMDVALQIANTLELPYR-QGFVKNRyigRTfim 335
Cdd:COG1040 53 YRGRLDLARLLARLLARALREAllpRPDLIVPVPlhrrrlrrrgfNQAELLARALARALGIPVLpDLLRRVR---AT--- 126
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 336 PGQTMRKKSVRRKL--NAI----SSEFKGKNVLLVDDsIVrgtTSGQ-IIEMAR---ESGAKKVYFASAA 395
Cdd:COG1040 127 PSQAGLSRAERRRNlrGAFavrpPARLAGKHVLLVDD-VL---TTGAtLAEAARalkAAGAARVDVLVLA 192
|
|
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
1-185 |
1.79e-06 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 50.52 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 1 MCGIVGIVG------KTPVAQSLYDGLTVIQHRGQDAAGImTIDQNMFNLR----------KANGLVRDVFHTRHMKRLS 64
Cdd:PLN02981 1 MCGIFAYLNynvpreRRFILEVLFNGLRRLEYRGYDSAGI-AIDNDPSLESssplvfreegKIESLVRSVYEEVAETDLN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 65 GNM------GIGHVRYPTAGTSSSAEAQPfyVNSPFGIAF--AHNGNLTNAHDLQEEVFriarRH---INTTSDSELLLN 133
Cdd:PLN02981 80 LDLvfenhaGIAHTRWATHGPPAPRNSHP--QSSGPGNEFlvVHNGIITNYEVLKETLL----RHgftFESDTDTEVIPK 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1023065406 134 iLAHELQQVAGLSVTAEHIFEVVTKVHKKIRGAYAVVaaiigqgivaFRDPH 185
Cdd:PLN02981 154 -LAKFVFDKLNEEEGDVTFSQVVMEVMRQLEGAYALI----------FKSPH 194
|
|
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
1-239 |
7.02e-06 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 48.75 E-value: 7.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 1 MCGIVGIVGKTPVAQSL----YDGLTVIQHRGQDAAGIMTidqnmfnlrkanglvrdvfhtrhmkrlSGNMGIGHVRYPT 76
Cdd:PRK09431 1 MCGIFGILDIKTDADELrkkaLEMSRLMRHRGPDWSGIYA---------------------------SDNAILGHERLSI 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 77 AGTSSSaeAQPFYvNSPFGIAFAHNGNLTNAHDLQEEvfrIARRH-INTTSDSELLLnilahELQQVAGLsvtaehifEV 155
Cdd:PRK09431 54 VDVNGG--AQPLY-NEDGTHVLAVNGEIYNHQELRAE---LGDKYaFQTGSDCEVIL-----ALYQEKGP--------DF 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 156 VtkvhKKIRG--AYAVVAAIIGQGIVAfRDPHGIRPLALGKRmtELGeEWMVASESVALdaVGF-QFIRDVSPGEaVYIT 232
Cdd:PRK09431 115 L----DDLDGmfAFALYDSEKDAYLIA-RDPIGIIPLYYGYD--EHG-NLYFASEMKAL--VPVcKTIKEFPPGH-YYWS 183
|
....*..
gi 1023065406 233 ENGELHT 239
Cdd:PRK09431 184 KDGEFVR 190
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
1-214 |
8.85e-05 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 45.09 E-value: 8.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 1 MCGIVGIVGKTPVAQSL----YDGLTVIQHRGQDAAGIMTIDQNmfnlrkanglvRDVFHTrhmkrlsgnmgIGHVRYPT 76
Cdd:PTZ00077 1 MCGILAIFNSKGERHELrrkaLELSKRLRHRGPDWSGIIVLENS-----------PGTYNI-----------LAHERLAI 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 77 AGTSSSAeaQPFYVNSPfGIAFAHNGNLTNAHDLQEEVFRIARRhINTTSDSELLLNilaheLQQVAGLSVTAEH---IF 153
Cdd:PTZ00077 59 VDLSDGK--QPLLDDDE-TVALMQNGEIYNHWEIRPELEKEGYK-FSSNSDCEIIGH-----LYKEYGPKDFWNHldgMF 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1023065406 154 EVVTKVHKKirgayavvaaiigQGIVAFRDPHGIRPLALGkrMTELGEEWmVASESVALDA 214
Cdd:PTZ00077 130 ATVIYDMKT-------------NTFFAARDHIGIIPLYIG--YAKDGSIW-FSSELKALHD 174
|
|
| PRK00934 |
PRK00934 |
ribose-phosphate pyrophosphokinase; Provisional |
265-392 |
1.96e-04 |
|
ribose-phosphate pyrophosphokinase; Provisional
Pssm-ID: 234868 [Multi-domain] Cd Length: 285 Bit Score: 43.36 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 265 IDGISVYASRVnmgrrLGEKIArewSDLDIDVVIPIPETSMDVALQIANTLELPYRQgFVKNRYIGRTFimpgqTMRKKS 344
Cdd:PRK00934 134 IPFINLDAAPL-----IAEYIG---DKLDDPLVLAPDKGALELAKEAAEILGCEYDY-LEKTRISPTEV-----EIAPKN 199
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1023065406 345 VrrklnaissEFKGKNVLLVDDSIVRGTTSGQIIEMARESGAKKVYFA 392
Cdd:PRK00934 200 L---------DVKGKDVLIVDDIISTGGTMATAIKILKEQGAKKVYVA 238
|
|
| PLN02549 |
PLN02549 |
asparagine synthase (glutamine-hydrolyzing) |
1-193 |
6.71e-04 |
|
asparagine synthase (glutamine-hydrolyzing)
Pssm-ID: 178164 [Multi-domain] Cd Length: 578 Bit Score: 42.44 E-value: 6.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 1 MCGIVGIVGKTPVAQS----LYDGLTVIQHRGQDAAGImtiDQNmfnlrKANGLVrdvfhtrHmKRLSgnmgighVRYPT 76
Cdd:PLN02549 1 MCGILAVLGCSDDSQAkrsrVLELSRRLRHRGPDWSGL---YGN-----EDCYLA-------H-ERLA-------IMDPE 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 77 AGTsssaeaQPFYvNSPFGIAFAHNGNLTNAHDLQEEVFRIARRhinTTSDSElllnILAHelqqvaglsVTAEHIFEVV 156
Cdd:PLN02549 58 SGD------QPLY-NEDKTIVVTANGEIYNHKELREKLKLHKFR---TGSDCE----VIAH---------LYEEHGEEFV 114
|
170 180 190
....*....|....*....|....*....|....*...
gi 1023065406 157 tkvhKKIRGAYA-VVAAIIGQGIVAFRDPHGIRPLALG 193
Cdd:PLN02549 115 ----DMLDGMFSfVLLDTRDNSFIAARDHIGITPLYIG 148
|
|
| PRK08558 |
PRK08558 |
adenine phosphoribosyltransferase; Provisional |
262-389 |
7.34e-04 |
|
adenine phosphoribosyltransferase; Provisional
Pssm-ID: 181466 [Multi-domain] Cd Length: 238 Bit Score: 41.13 E-value: 7.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 262 DSFIDGISVyASRVNMGRRLGEKIAREWSDLDIDVVIPIPETSMDVALQIANTLELP------YRQGFVKNRYIGRTFIM 335
Cdd:PRK08558 81 EGYVDNSSV-VFDPSFLRLIAPVVAERFMGLRVDVVLTAATDGIPLAVAIASYFGADlvyakkSKETGVEKFYEEYQRLA 159
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 336 PGqtmrkksvrRKLN------AISsefKGKNVLLVDDSIVRGTTSGQIIEMARESGAKKV 389
Cdd:PRK08558 160 SG---------IEVTlylpasALK---KGDRVLIVDDIIRSGETQRALLDLARQAGADVV 207
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-198 |
8.88e-04 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 41.79 E-value: 8.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 1 MCGIVG-IVGKTP-----VAQSLYDGLTVIQHRGQDAAGiMTIDQNMFNLRKANG----------LVRDVFHTRHMKR-- 62
Cdd:PTZ00394 1 MCGIFGyANHNVPrtveqILNVLLDGIQKVEYRGYDSAG-LAIDANIGSEKEDGTaasaptprpcVVRSVGNISQLREkv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 63 ---------------LSGNMGIGHVRYPTAGTSSSAEAQPFYVNSpFGIAFAHNGNLTNAHDLQeEVFRIARRHINTTSD 127
Cdd:PTZ00394 80 fseavaatlppmdatTSHHVGIAHTRWATHGGVCERNCHPQQSNN-GEFTIVHNGIVTNYMTLK-ELLKEEGYHFSSDTD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023065406 128 SELllnilahelqqvagLSVTAEHIF---------EVVTKVHKKIRGAYAVVAAII---GQgIVAFRDPhgiRPLALGKR 195
Cdd:PTZ00394 158 TEV--------------ISVLSEYLYtrkgihnfaDLALEVSRMVEGSYALLVKSVyfpGQ-LAASRKG---SPLMVGIR 219
|
...
gi 1023065406 196 MTE 198
Cdd:PTZ00394 220 RTD 222
|
|
| Hpt1 |
COG2236 |
Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine ... |
337-392 |
6.60e-03 |
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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: 37.13 E-value: 6.60e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1023065406 337 GQTMRKKSVRRKLNaisSEFKGKNVLLVDDSIVRGTTSGQIIEMARESGAKKVYFA 392
Cdd:COG2236 70 AKRLEEPVVKGPLD---EDLAGKRVLIVDDVADTGRTLEAVRDLLKEAGPAEVRTA 122
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