|
Name |
Accession |
Description |
Interval |
E-value |
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
40-529 |
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: 682.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511205 40 MCGIIGILGHPltQVASSIYDGMLVLQHRGQDAAGIVTSDSENIYHRRANGLVRDVFRAKHMSNLLGHMGMGHVRYPTAG 119
Cdd:COG0034 7 ECGVFGIYGHE--DVAQLTYYGLYALQHRGQESAGIATSDGGRFHLHKGMGLVSDVFDEEDLERLKGNIAIGHVRYSTTG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511205 120 SSSVAEAQPFYTNTPFG-VSLAHNGNLNNTTDIINGLLEYDHRrINTSSDSEALLNLFAAEiqrsvngrpggldaLSEDD 198
Cdd:COG0034 85 SSSLENAQPFYVNSPFGsIALAHNGNLTNAEELREELEEEGAI-FQTTSDTEVILHLIARE--------------LTKED 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511205 199 IFRAVERTHLRVEGSYSVIAMITGwGLVAFRDPHGIRPLFMGVcENEGFterMFTSESVACAALGFTPERDIAPGEAVIA 278
Cdd:COG0034 150 LEEAIKEALRRVKGAYSLVILTGD-GLIAARDPNGIRPLVLGK-LEDGY---VVASESCALDILGAEFVRDVEPGEIVVI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511205 279 RVDGAFSaKQCHSEPAYTPCIFEHVYFARPDSTIDGISVHGARLRMGAALAsrvlkERPGHGIDAIIPVPDSGRIAAMEM 358
Cdd:COG0034 225 DEDGLRS-RQFAEKPRPAPCIFEYVYFARPDSVIDGRSVYEARKRMGRELA-----REAPVDADVVIPVPDSGRPAAIGY 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511205 359 ARTLGVDYREGFVKNRYIGRTFIMPGQSMRKDSVKKKLNTIDWEFAGKTVMIVDDSIVRGNTSRRIIEMAKEAGAKQVFF 438
Cdd:COG0034 299 AEESGIPYEEGLIKNRYVGRTFIQPTQELRELGVRLKLNPIREVVKGKRVVLVDDSIVRGTTSRRIVKMLREAGAKEVHF 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511205 439 ASSAPPIIHPNVYGIDMPARAEYVAHDRSIKEIAEAIGADWLIYQELDDLVEAcLGDGKDkpaNFDCSCFDGVYVTgGIT 518
Cdd:COG0034 379 RIASPPIRYPCYYGIDTPTREELIAANRSVEEIREYIGADSLGYLSLEGLIEA-VGEPIE---GFCTACFTGDYPT-GIP 453
|
490
....*....|.
gi 663511205 519 EEYLSRVERVR 529
Cdd:COG0034 454 DEEKKRLELLR 464
|
|
| purF |
TIGR01134 |
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ... |
41-513 |
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: 575.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511205 41 CGIIGILGHPlTQVASSIYDGMLVLQHRGQDAAGIVTSDSENIYHRRANGLVRDVFRAKHMSNLLGHMGMGHVRYPTAGS 120
Cdd:TIGR01134 1 CGVVGIYGQE-EVAASLTYYGLYALQHRGQESAGISVFDGNRFRLHKGNGLVSDVFNEEHLQRLKGNVGIGHVRYSTAGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511205 121 SSVAEAQPFYTNTPFG-VSLAHNGNLNNTTDIINgLLEYDHRRINTSSDSEALLNLFAAEIqrsvngrpggldaLSEDDI 199
Cdd:TIGR01134 80 SGLENAQPFVVNSPYGgLALAHNGNLVNADELRR-ELEEEGRHFNTTSDSEVLLHLLAHND-------------ESKDDL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511205 200 FRAVERTHLRVEGSYSVIAMiTGWGLVAFRDPHGIRPLFMGVCENEGfterMFTSESVACAALGFTPERDIAPGEAVIAR 279
Cdd:TIGR01134 146 FDAVARVLERVRGAYALVLM-TEDGLVAVRDPHGIRPLVLGRRGDGY----VVASESCALDILGAEFVRDVEPGEVVVIF 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511205 280 VDGAFSAKqcHSEPAYTPCIFEHVYFARPDSTIDGISVHGARLRMGAALAsrvlKERPGHGiDAIIPVPDSGRIAAMEMA 359
Cdd:TIGR01134 221 DGGLESRQ--CARRPRAPCVFEYVYFARPDSVIDGISVYYARKRMGKELA----RESPVEA-DVVVPVPDSGRSAALGFA 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511205 360 RTLGVDYREGFVKNRYIGRTFIMPGQSMRKDSVKKKLNTIDWEFAGKTVMIVDDSIVRGNTSRRIIEMAKEAGAKQVFFA 439
Cdd:TIGR01134 294 QASGIPYREGLIKNRYVGRTFIMPTQELRELSVRLKLNPVRAVFEGKRVVLVDDSIVRGTTSRQIVEMLRDAGAKEVHVR 373
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663511205 440 SSAPPIIHPNVYGIDMPARAEYVAHDRSIKEIAEaIGADWLIYQELDDLVEAclgdGKDKPANFDCSCFDGVYV 513
Cdd:TIGR01134 374 IASPPIRYPCYYGIDMPTREELIAARRTVEEIRK-IGADSLAYLSLEGLKEA----VGNPESDLCLACFTGEYP 442
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
40-534 |
0e+00 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 565.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511205 40 MCGIIGILGHPltQVASSIYDGMLVLQHRGQDAAGIVTSDSENIYHRRANGLVRDVFRAKHMSNLLGHMGMGHVRYPTAG 119
Cdd:PLN02440 1 ECGVVGIFGDP--EASRLCYLGLHALQHRGQEGAGIVTVDGNRLQSITGNGLVSDVFDESKLDQLPGDIAIGHVRYSTAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511205 120 SSSVAEAQPFYTNTPFG-VSLAHNGNLNNTTDIINgLLEYDHRRINTSSDSEALLNLFAAEIQRSvngrpggldalsedd 198
Cdd:PLN02440 79 ASSLKNVQPFVANYRFGsIGVAHNGNLVNYEELRA-KLEENGSIFNTSSDTEVLLHLIAISKARP--------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511205 199 IFRAVERTHLRVEGSYSVIAMITGwGLVAFRDPHGIRPLFMGVCENEGFterMFTSESVACAALGFTPERDIAPGEAVIA 278
Cdd:PLN02440 143 FFSRIVDACEKLKGAYSMVFLTED-KLVAVRDPHGFRPLVMGRRSNGAV---VFASETCALDLIGATYEREVNPGEVIVV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511205 279 RVDGAFSAKQCHSEPAYTPCIFEHVYFARPDSTIDGISVHGARLRMGAALASRVLKErpghgIDAIIPVPDSGRIAAMEM 358
Cdd:PLN02440 219 DKDKGVSSQCLMPHPEPKPCIFEHIYFARPNSIVFGRSVYESRLEFGEILATEIPVD-----CDVVIPVPDSGRVAALGY 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511205 359 ARTLGVDYREGFVKNRYIGRTFIMPGQSMRKDSVKKKLNTIDWEFAGKTVMIVDDSIVRGNTSRRIIEMAKEAGAKQVFF 438
Cdd:PLN02440 294 AAKLGVPFQQGLIRSHYVGRTFIEPSQKIRDFSVKLKLNPVRSVLEGKRVVVVDDSIVRGTTSSKIVRMLREAGAKEVHM 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511205 439 ASSAPPIIHPNVYGIDMPARAEYVAHDRSIKEIAEAIGADWLIYQELDDLVEAclgdGKDKPANFDCSCFDGVY------ 512
Cdd:PLN02440 374 RIASPPIIASCYYGVDTPSREELISNRMSVEEIRKFIGCDSLAFLPLEDLKKS----LGEESPRFCYACFSGDYpvlpkr 449
|
490 500
....*....|....*....|..
gi 663511205 513 VTGGITEEYLSRVERVRNDAAK 534
Cdd:PLN02440 450 VGGDIDDGYLESLEEAGRGWGR 471
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
41-512 |
3.27e-144 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 423.29 E-value: 3.27e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511205 41 CGIIGILGHPLTQVASSIYDGMLVLQHRGQDAAGIVTSDSENIYHRRANGLVRDVFRAKHMSNLLGHMGMGHVRYPTAGS 120
Cdd:PRK05793 15 CGVFGVFSKNNIDVASLTYYGLYALQHRGQESAGIAVSDGEKIKVHKGMGLVSEVFSKEKLKGLKGNSAIGHVRYSTTGA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511205 121 SSVAEAQPFYTNTPFG-VSLAHNGNLNNTtDIINGLLEYDHRRINTSSDSEALLNLFAAEIQRsvngrpggldalsedDI 199
Cdd:PRK05793 95 SDLDNAQPLVANYKLGsIAIAHNGNLVNA-DVIRELLEDGGRIFQTSIDSEVILNLIARSAKK---------------GL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511205 200 FRAVERTHLRVEGSYSvIAMITGWGLVAFRDPHGIRPLFMGVCEnEGFterMFTSESVACAALGFTPERDIAPGEAVIAR 279
Cdd:PRK05793 159 EKALVDAIQAIKGSYA-LVILTEDKLIGVRDPHGIRPLCLGKLG-DDY---ILSSESCALDTIGAEFIRDVEPGEIVIID 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511205 280 VDGAFSAKqCHSEPAYTPCIFEHVYFARPDSTIDGISVHGARLRMGAALAsrvlKERPghgIDA--IIPVPDSGRIAAME 357
Cdd:PRK05793 234 EDGIKSIK-FAEKTKCQTCAFEYIYFARPDSVIDGISVYESRVRAGRQLY----KEYP---VDAdiVIGVPDSGIPAAIG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511205 358 MARTLGVDYREGFVKNRYIGRTFIMPGQSMRKDSVKKKLNTIDWEFAGKTVMIVDDSIVRGNTSRRIIEMAKEAGAKQVF 437
Cdd:PRK05793 306 YAEASGIPYGIGFIKNKYVGRTFIAPSQELRERAVRVKLNPLKVNVEGKRVVLIDDSIVRGTTSKRLVELLRKAGAKEVH 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663511205 438 FASSAPPIIHPNVYGIDMPARAEYVAHDRSIKEIAEAIGADWLIYQELDDLVEACLGDgkdkpANFDCSCFDGVY 512
Cdd:PRK05793 386 FRVSSPPVKYPCYFGIDTPYRKELIGANMSVEEIREMIGADSLGYLSIEGLLESLNGD-----KGFCLGCFNGVY 455
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
41-313 |
1.31e-113 |
|
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: 337.13 E-value: 1.31e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511205 41 CGIIGILGHPltQVASSIYDGMLVLQHRGQDAAGIVTSDSENIYHRRANGLVRDVFRAKHMSNLLGHMGMGHVRYPTAGS 120
Cdd:cd00715 1 CGVFGIYGAE--DAARLTYLGLYALQHRGQESAGIATSDGKRFHTHKGMGLVSDVFDEEKLRRLPGNIAIGHVRYSTAGS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511205 121 SSVAEAQPFYTNTPFG-VSLAHNGNLNNTTDIINGLLEyDHRRINTSSDSEALLNLFAAEIQRsvngrpggldalseDDI 199
Cdd:cd00715 79 SSLENAQPFVVNSPLGgIALAHNGNLVNAKELREELEE-EGRIFQTTSDSEVILHLIARSLAK--------------DDL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511205 200 FRAVERTHLRVEGSYSVIAMITGwGLVAFRDPHGIRPLFMGVCENEGFterMFTSESVACAALGFTPERDIAPGEAVIAR 279
Cdd:cd00715 144 FEAIIDALERVKGAYSLVIMTAD-GLIAVRDPHGIRPLVLGKLEGDGY---VVASESCALDIIGAEFVRDVEPGEIVVID 219
|
250 260 270
....*....|....*....|....*....|....
gi 663511205 280 VDGAFSaKQCHSEPAYTPCIFEHVYFARPDSTID 313
Cdd:cd00715 220 DDGLES-SQRAPKPKPAPCIFEYVYFARPDSVID 252
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
41-276 |
5.19e-49 |
|
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: 168.78 E-value: 5.19e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511205 41 CGIIGILGH--PLTQVASSIYDGMLVLQHRGQDAAGIVTSDSENIYHRRANGLVRDVFRAKHMSNLLGHMGMGHVRYPTA 118
Cdd:cd00352 1 CGIFGIVGAdgAASLLLLLLLRGLAALEHRGPDGAGIAVYDGDGLFVEKRAGPVSDVALDLLDEPLKSGVALGHVRLATN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511205 119 GSSSVAEAQPFYTNTPfGVSLAHNGNLNNTTDIINGLLEYDHrRINTSSDSEALLNLFAAEIQrsvngrpggldalsEDD 198
Cdd:cd00352 81 GLPSEANAQPFRSEDG-RIALVHNGEIYNYRELREELEARGY-RFEGESDSEVILHLLERLGR--------------EGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 663511205 199 IFRAVERTHLRVEGSYSVIAMITGWG-LVAFRDPHGIRPLFMGVCENEGFterMFTSESVACAALGFTPERDIAPGEAV 276
Cdd:cd00352 145 LFEAVEDALKRLDGPFAFALWDGKPDrLFAARDRFGIRPLYYGITKDGGL---VFASEPKALLALPFKGVRRLPPGELL 220
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
41-247 |
1.36e-16 |
|
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: 78.64 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511205 41 CGIIGILGHplTQVASSIYDGMLVLQHRGQDAAGIVTSDSENIYHRRANGLVRDVFRAKHMSNLLGHMGMGHVRYPTAGS 120
Cdd:cd00714 1 CGIVGYIGK--REAVDILLEGLKRLEYRGYDSAGIAVIGDGSLEVVKAVGKVANLEEKLAEKPLSGHVGIGHTRWATHGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511205 121 SSVAEAQPfYTNTPFGVSLAHNGNLNNTTDIINGLLEYDHrRINTSSDSEALLNLFAAEIQRSvngrpggldalseDDIF 200
Cdd:cd00714 79 PTDVNAHP-HRSCDGEIAVVHNGIIENYAELKEELEAKGY-KFESETDTEVIAHLIEYYYDGG-------------LDLL 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 663511205 201 RAVERTHLRVEGSYSVIAMITGwglvafrDPHGI---R---PLFMGVCENEGF 247
Cdd:cd00714 144 EAVKKALKRLEGAYALAVISKD-------EPDEIvaaRngsPLVIGIGDGENF 189
|
|
| PRTases_typeI |
cd06223 |
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ... |
324-463 |
2.75e-16 |
|
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The type I PRTases are identified by a conserved PRPP binding motif which features two adjacent acidic residues surrounded by one or more hydrophobic residue. PRTases catalyze the displacement of the alpha-1'-pyrophosphate of 5-phosphoribosyl-alpha1-pyrophosphate (PRPP) by a nitrogen-containing nucleophile. The reaction products are an alpha-1 substituted ribose-5'-phosphate and a free pyrophosphate (PP). PRPP, an activated form of ribose-5-phosphate, is a key metabolite connecting nucleotide synthesis and salvage pathways. The type I PRTase family includes a range of diverse phosphoribosyl transferase enzymes and regulatory proteins of the nucleotide synthesis and salvage pathways, including adenine phosphoribosyltransferase EC:2.4.2.7., hypoxanthine-guanine-xanthine phosphoribosyltransferase, hypoxanthine phosphoribosyltransferase EC:2.4.2.8., ribose-phosphate pyrophosphokinase EC:2.7.6.1., amidophosphoribosyltransferase EC:2.4.2.14., orotate phosphoribosyltransferase EC:2.4.2.10., uracil phosphoribosyltransferase EC:2.4.2.9., and xanthine-guanine phosphoribosyltransferase EC:2.4.2.22.
Pssm-ID: 206754 [Multi-domain] Cd Length: 130 Bit Score: 75.51 E-value: 2.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511205 324 MGAALASRVLKErpGHGIDAIIPVPDSGRIAAMEMARTLGVDYREGFVKNRYIGRTFIMPGQSMRKDSVKKKlntidwef 403
Cdd:cd06223 1 AGRLLAEEIRED--LLEPDVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSEPYGLELPLGGDVK-------- 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511205 404 aGKTVMIVDDSIVRGNTSRRIIEMAKEAGAKQVFFAsSAPPIIHPNVYGIDMPARAEYVA 463
Cdd:cd06223 71 -GKRVLLVDDVIATGGTLLAAIELLKEAGAKVVGVA-VLLDKPEGGARELASPGDPVYSL 128
|
|
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
40-247 |
9.70e-15 |
|
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: 76.98 E-value: 9.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511205 40 MCGIIGILGHplTQVASSIYDGMLVLQHRGQDAAGIVTSDSENIYHRRANGLVRDVFRAKHMSNLLGHMGMGHVRYPTAG 119
Cdd:COG0449 1 MCGIVGYIGK--RDAAPILLEGLKRLEYRGYDSAGIAVLDDGGLEVRKAVGKLANLEEKLAEEPLSGTIGIGHTRWATHG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511205 120 SSSVAEAQPFYTNTPfGVSLAHNGnlnnttdII-------NGLLEYDHrRINTSSDSEALLNLFAAEIQRsvngrpggld 192
Cdd:COG0449 79 APSDENAHPHTSCSG-RIAVVHNG-------IIenyaelrEELEAKGH-TFKSETDTEVIAHLIEEYLKG---------- 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663511205 193 alsEDDIFRAVERTHLRVEGSYSVIAMITGwglvafrDPHGI---R---PLFMGVCENEGF 247
Cdd:COG0449 140 ---GGDLLEAVRKALKRLEGAYALAVISAD-------EPDRIvaaRkgsPLVIGLGEGENF 190
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
40-221 |
2.41e-14 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 75.83 E-value: 2.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511205 40 MCGIIGILGhplTQVASSI-YDGMLVLQHRGQDAAGIVTSDSENI--------YHRRANGLVR--DVFRAKHMSNllgHM 108
Cdd:PTZ00295 24 CCGIVGYLG---NEDASKIlLEGIEILQNRGYDSCGISTISSGGElkttkyasDGTTSDSIEIlkEKLLDSHKNS---TI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511205 109 GMGHVRYPTAGSSSVAEAQPF--YTNTpfgVSLAHNGNLNNTTDIINgllEYDHRRINTSS--DSEALLNLFAAEIQrsv 184
Cdd:PTZ00295 98 GIAHTRWATHGGKTDENAHPHcdYKKR---IALVHNGTIENYVELKS---ELIAKGIKFRSetDSEVIANLIGLELD--- 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 663511205 185 ngrpggldalSEDDIFRAVERTHLRVEGSYSvIAMIT 221
Cdd:PTZ00295 169 ----------QGEDFQEAVKSAISRLQGTWG-LCIIH 194
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
41-278 |
1.86e-13 |
|
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: 70.37 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511205 41 CGIIGIL---GHPltQVASSIYDGMLVLQHRG-QDAAG---------IVTSDSENIYHRRANGLVRDVFRAKHMSNLLGH 107
Cdd:cd01907 1 CGIFGIMskdGEP--FVGALLVEMLDAMQERGpGDGAGfalygdpdaFVYSSGKDMEVFKGVGYPEDIARRYDLEEYKGY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511205 108 MGMGHVRYPTAGSSSVAEAQPFYTntpFGVSLAHNGNLNNtTDIINGLLEYDHRRINTSSDSEALLNLFAAEIQRSVNGR 187
Cdd:cd01907 79 HWIAHTRQPTNSAVWWYGAHPFSI---GDIAVVHNGEISN-YGSNREYLERFGYKFETETDTEVIAYYLDLLLRKGGLPL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511205 188 PGGLDALSEDDIFR------AVERTHLRVEGSYSVIaMITGWGLVAFRDPHGIRPLFMgvceneGFTERMF--TSESVAC 259
Cdd:cd01907 155 EYYKHIIRMPEEERelllalRLTYRLADLDGPFTII-VGTPDGFIVIRDRIKLRPAVV------AETDDYVaiASEECAI 227
|
250 260
....*....|....*....|..
gi 663511205 260 AAL-GFTPERDIAP--GEAVIA 278
Cdd:cd01907 228 REIpDRDNAKVWEPrpGEYVIW 249
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
40-282 |
3.85e-12 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 68.92 E-value: 3.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511205 40 MCGIIGILGHplTQVASSIYDGMLVLQHRGQDAAGIVTSDSENIYHRRANGLVRDVFRAKHMSNLLGHMGMGHVRYPTAG 119
Cdd:PRK00331 1 MCGIVGYVGQ--RNAAEILLEGLKRLEYRGYDSAGIAVLDDGGLEVRKAVGKVANLEAKLEEEPLPGTTGIGHTRWATHG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511205 120 SSSVAEAQPFYTNTpfG-VSLAHNGNLNNTTDIINGLLEYDHrRINTSSDSEALLNLFAAEIQRSvngrpggldalseDD 198
Cdd:PRK00331 79 KPTERNAHPHTDCS--GrIAVVHNGIIENYAELKEELLAKGH-VFKSETDTEVIAHLIEEELKEG-------------GD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511205 199 IFRAVERTHLRVEGSYSvIAMITGwglvafRDPHGI---R---PLFMGVCENEgfterMFTSESVAcAALGFTpeRDIAP 272
Cdd:PRK00331 143 LLEAVRKALKRLEGAYA-LAVIDK------DEPDTIvaaRngsPLVIGLGEGE-----NFLASDAL-ALLPYT--RRVIY 207
|
250
....*....|...
gi 663511205 273 ---GEAVIARVDG 282
Cdd:PRK00331 208 ledGEIAVLTRDG 220
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
41-255 |
7.25e-11 |
|
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine synthetase B catalyses the ATP-dependent conversion of aspartate to asparagine. This enzyme is a homodimer, with each monomer composed of a glutaminase domain and a synthetase domain. The N-terminal glutaminase domain hydrolyzes glutamine to glutamic acid and ammonia.
Pssm-ID: 238364 [Multi-domain] Cd Length: 220 Bit Score: 62.19 E-value: 7.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511205 41 CGIIGILGHPLTQVASSIYDGML-VLQHRGQDAAGIVTSdseniyhrranglvrdvfrakhmsnllGHMGMGHVRyptag 119
Cdd:cd00712 1 CGIAGIIGLDGASVDRATLERMLdALAHRGPDGSGIWID---------------------------EGVALGHRR----- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511205 120 sSSV----AEAQPFYTNTPfGVSLAHNGNLNNTTDIINGLLEYDHRRiNTSSDSEALLNLFAAEiqrsvngrpgGLDALS 195
Cdd:cd00712 49 -LSIidlsGGAQPMVSEDG-RLVLVFNGEIYNYRELRAELEALGHRF-RTHSDTEVILHLYEEW----------GEDCLE 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 663511205 196 EDD------IFRAVERThlrvegsysviamitgwgLVAFRDPHGIRPLFMGVCENeGFterMFTSE 255
Cdd:cd00712 116 RLNgmfafaLWDKRKRR------------------LFLARDRFGIKPLYYGRDGG-GL---AFASE 159
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
40-255 |
1.45e-09 |
|
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; Asparagine synthetase B (glutamine-hydrolyzing) is part of the Pathway/BioSystem: Asparagine biosynthesis
Pssm-ID: 440136 [Multi-domain] Cd Length: 558 Bit Score: 60.62 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511205 40 MCGIIGILGHPLTQVASSIYDGMLVLQHRGQDAAGIVTSdseniyhrranglvrdvfrakhmsnllGHMGMGHVRyptag 119
Cdd:COG0367 1 MCGIAGIIDFDGGADREVLERMLDALAHRGPDGSGIWVD---------------------------GGVALGHRR----- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511205 120 SS----SVAEAQPFYtNTPFGVSLAHNGNLNNTTDIINGLLEYDHRrINTSSDSEALLNLFAAEiqrsvngrpgGLDALS 195
Cdd:COG0367 49 LSiidlSEGGHQPMV-SEDGRYVLVFNGEIYNYRELRAELEALGHR-FRTHSDTEVILHAYEEW----------GEDCLE 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 663511205 196 EDD------IFRAVERThlrvegsysviamitgwgLVAFRDPHGIRPLFMGVcENEGFterMFTSE 255
Cdd:COG0367 117 RLNgmfafaIWDRRERR------------------LFLARDRFGIKPLYYAE-DGGGL---AFASE 160
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
122-258 |
2.45e-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: 55.22 E-value: 2.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511205 122 SVAEAQPFYTNTPFGVSLAHNGNLNNTTDIINGLLEYDHRrINTSSDSEALLNLFAAEiqrsvngrpGGLDALSeddifr 201
Cdd:pfam13537 9 LEGGAQPMVSSEDGRYVIVFNGEIYNYRELRAELEAKGYR-FRTHSDTEVILHLYEAE---------WGEDCVD------ 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663511205 202 avertHLRveGSYSVIAmitgWG-----LVAFRDPHGIRPLFMGVCENEGFterMFTSESVA 258
Cdd:pfam13537 73 -----RLN--GMFAFAI----WDrrrqrLFLARDRFGIKPLYYGRDDGGRL---LFASELKA 120
|
|
| YafJ |
cd01908 |
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ... |
40-281 |
6.16e-09 |
|
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine amidotransferase-like protein of unknown function found in prokaryotes, eukaryotes and archaea. YafJ has a conserved structural fold similar to those of other class II glutamine amidotransferases including glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). The YafJ fold is also somewhat similar to the Ntn (N-terminal nucleophile) hydrolase fold of the proteasomal alpha and beta subunits.
Pssm-ID: 238889 [Multi-domain] Cd Length: 257 Bit Score: 57.01 E-value: 6.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511205 40 MCGIIGILGHPLTQ------------VASSIYDGMLVLQHRgqDAAGIV--TSDSENIYHRR----ANGLVRDVFRAKHm 101
Cdd:cd01908 1 MCRLLGYSGAPIPLepllirpshsllVQSGGPREMKGTVHA--DGWGIGwyEGKGGRPFRYRsplpAWSDINLESLARP- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511205 102 snLLGHMGMGHVRYPTAGSSSVAEAQPFYTNtpfGVSLAHNGNLNNTTDIINGLLEYDHRRINTSSDSEALLNLFAAEIq 181
Cdd:cd01908 78 --IKSPLVLAHVRAATVGPVSLENCHPFTRG---RWLFAHNGQLDGFRLLRRRLLRLLPRLPVGTTDSELAFALLLSRL- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511205 182 rsvngrpGGLDALSEDDIFRAVERT--HLRVEGSYSVIAMI--TGWGLVAFRDPhGIRPLF------MGVCENEGFTERM 251
Cdd:cd01908 152 -------LERDPLDPAELLDAILQTlrELAALAPPGRLNLLlsDGEYLIATRYA-SAPSLYyltrraPFGCARLLFRSVT 223
|
250 260 270
....*....|....*....|....*....|....
gi 663511205 252 FTSESVACAA---LGF-TPERDIAPGEAVIARVD 281
Cdd:cd01908 224 TPNDDGVVVAsepLTDdEGWTEVPPGELVVVSEG 257
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
40-255 |
2.39e-08 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 56.65 E-value: 2.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511205 40 MCGIIGILGHPLT--QVASSIYDGMLVLQHRGQDAAGIVTSDSEniyhrranglvrdvfraKHMSNLLGHMGMGHVRyPT 117
Cdd:PTZ00077 1 MCGILAIFNSKGErhELRRKALELSKRLRHRGPDWSGIIVLENS-----------------PGTYNILAHERLAIVD-LS 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511205 118 AGsssvaeAQPFYtNTPFGVSLAHNGNLNNTTDIiNGLLEYDHRRINTSSDSEALLNLFAaeiqrsvngRPGGLDALSE- 196
Cdd:PTZ00077 63 DG------KQPLL-DDDETVALMQNGEIYNHWEI-RPELEKEGYKFSSNSDCEIIGHLYK---------EYGPKDFWNHl 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 663511205 197 DDIFRAVerthlrvegsysVIAMITGwGLVAFRDPHGIRPLFMGVCENEgftERMFTSE 255
Cdd:PTZ00077 126 DGMFATV------------IYDMKTN-TFFAARDHIGIIPLYIGYAKDG---SIWFSSE 168
|
|
| Pribosyltran |
pfam00156 |
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ... |
318-465 |
7.31e-07 |
|
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: 48.90 E-value: 7.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511205 318 HGARLRMGAALASRVLKERPGHgIDAIIPVPDSGRIAAMEMARTLGVDYrEGFVKNRYIGRTFImpgqsmrkdSVKKKLN 397
Cdd:pfam00156 8 NPAILKAVARLAAQINEDYGGK-PDVVVGILRGGLPFAGILARRLDVPL-AFVRKVSYNPDTSE---------VMKTSSA 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663511205 398 TIDweFAGKTVMIVDDSIVRGNTSRRIIEMAKEAGAKQVFFA------SSAPPIIHPNVYGIDMPARAEYVAHD 465
Cdd:pfam00156 77 LPD--LKGKTVLIVDDILDTGGTLLKVLELLKNVGPKEVKIAvlidkpAGTEPKDKYDKRVDDWIVFVVGFGLD 148
|
|
| YafJ |
COG0121 |
Predicted glutamine amidotransferase YafJ [General function prediction only]; |
107-282 |
1.00e-06 |
|
Predicted glutamine amidotransferase YafJ [General function prediction only];
Pssm-ID: 439891 [Multi-domain] Cd Length: 248 Bit Score: 49.96 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511205 107 HMGMGHVRYPTAGSSSVAEAQPFYTntpFGVSLAHNGNLNN----TTDIINGLLEYDHRRINTSSDSEALLNLFAAEIQR 182
Cdd:COG0121 77 RLVIAHVRKATVGPVSLENTHPFRG---GRWLFAHNGQLDGfdrlRRRLAEELPDELYFQPVGTTDSELAFALLLSRLRD 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511205 183 SvngrpgglDALSEDDIFRAVERTHlRVEGSYSV--IAMITGWGLVAFRDPHGIRP--LFMGVCENEGFTERMFTSESVA 258
Cdd:COG0121 154 G--------GPDPAEALAEALRELA-ELARAPGRlnLLLSDGERLYATRYTSDDPYptLYYLTRTTPDDRVVVVASEPLT 224
|
170 180
....*....|....*....|....
gi 663511205 259 CAAlGFTPerdIAPGEAVIARVDG 282
Cdd:COG0121 225 DDE-GWTE---VPPGELLVVRDGL 244
|
|
| PRK02277 |
PRK02277 |
orotate phosphoribosyltransferase-like protein; Provisional |
315-436 |
1.76e-06 |
|
orotate phosphoribosyltransferase-like protein; Provisional
Pssm-ID: 235023 [Multi-domain] Cd Length: 200 Bit Score: 48.71 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511205 315 ISVHGARLR-MGAALASRVLKErpGHGIDAIIPVPDSG-RIAAMeMARTLGVDYregfvknryigrTFIMPGQSMRKDSV 392
Cdd:PRK02277 61 IGSSSSRLRyIASAMADMLEKE--DEEVDVVVGIAKSGvPLATL-VADELGKDL------------AIYHPKKWDHGEGE 125
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 663511205 393 KKKlNTIDWEFA---GKTVMIVDDSIVRGNTSRRIIEMAKEAGAKQV 436
Cdd:PRK02277 126 KKT-GSFSRNFAsveGKRCVIVDDVITSGTTMKETIEYLKEHGGKPV 171
|
|
| PRK00934 |
PRK00934 |
ribose-phosphate pyrophosphokinase; Provisional |
329-448 |
6.95e-06 |
|
ribose-phosphate pyrophosphokinase; Provisional
Pssm-ID: 234868 [Multi-domain] Cd Length: 285 Bit Score: 47.99 E-value: 6.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511205 329 ASRVLKERPGHGI-DAIIPVPDSGriaAMEMART----LGVDYRegfvknrYIGRTFIMPgqsmrkDSVKKKLNTIDWEf 403
Cdd:PRK00934 141 AAPLIAEYIGDKLdDPLVLAPDKG---ALELAKEaaeiLGCEYD-------YLEKTRISP------TEVEIAPKNLDVK- 203
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 663511205 404 aGKTVMIVDDSIVRGNTSRRIIEMAKEAGAKQVFFASsappiIHP 448
Cdd:PRK00934 204 -GKDVLIVDDIISTGGTMATAIKILKEQGAKKVYVAC-----VHP 242
|
|
| PRK08558 |
PRK08558 |
adenine phosphoribosyltransferase; Provisional |
327-436 |
4.00e-05 |
|
adenine phosphoribosyltransferase; Provisional
Pssm-ID: 181466 [Multi-domain] Cd Length: 238 Bit Score: 44.98 E-value: 4.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511205 327 ALASRVLKER-PGHGIDAIIPVPDSGRIAAMEMARTLGVD------YREGFVKNRYIGRTFIMPGQSMR----KDSVKKk 395
Cdd:PRK08558 97 RLIAPVVAERfMGLRVDVVLTAATDGIPLAVAIASYFGADlvyakkSKETGVEKFYEEYQRLASGIEVTlylpASALKK- 175
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 663511205 396 lntidwefaGKTVMIVDDSIVRGNTSRRIIEMAKEAGAKQV 436
Cdd:PRK08558 176 ---------GDRVLIVDDIIRSGETQRALLDLARQAGADVV 207
|
|
| Apt |
COG0503 |
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ... |
323-434 |
2.61e-04 |
|
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide transport and metabolism]; Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein is part of the Pathway/BioSystem: Purine salvage
Pssm-ID: 440269 Cd Length: 171 Bit Score: 41.98 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511205 323 RMGAALASRVlkerPGHGIDAIIPVPDSGRIAAMEMARTLGVdyreGFV----KNRYIGRTFIMPGQS---------MRK 389
Cdd:COG0503 35 AAGDELAERF----ADKGIDKVVGIEARGFILAAALAYALGV----PFVparkPGKLPGETVSEEYDLeygtgdtleLHK 106
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 663511205 390 DSVKKklntidwefaGKTVMIVDDSIVRGNTSRRIIEMAKEAGAK 434
Cdd:COG0503 107 DALKP----------GDRVLIVDDLLATGGTAKAAIKLVEEAGAE 141
|
|
| ribP_PPkin |
TIGR01251 |
ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In ... |
329-443 |
4.95e-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: 42.27 E-value: 4.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663511205 329 ASRVLKE--RPGHGIDAIIPVPDSGRIA-AMEMARTLGVDYregfvknryigrtFIMPGQSMRKDSVKKKLNtIDWEFAG 405
Cdd:TIGR01251 145 ASPVLAEylKKKILDNPVVVSPDAGGVErAKKVADALGCPL-------------AIIDKRRISATNEVEVMN-LVGDVEG 210
|
90 100 110
....*....|....*....|....*....|....*...
gi 663511205 406 KTVMIVDDSIVRGNTSRRIIEMAKEAGAKQVFFASSAP 443
Cdd:TIGR01251 211 KDVVIVDDIIDTGGTIAKAAEILKSAGAKRVIAAATHG 248
|
|
| PRK06827 |
PRK06827 |
phosphoribosylpyrophosphate synthetase; Provisional |
405-443 |
7.34e-03 |
|
phosphoribosylpyrophosphate synthetase; Provisional
Pssm-ID: 180714 [Multi-domain] Cd Length: 382 Bit Score: 38.78 E-value: 7.34e-03
10 20 30
....*....|....*....|....*....|....*....
gi 663511205 405 GKTVMIVDDSIVRGNTSRRIIEMAKEAGAKQVFFASSAP 443
Cdd:PRK06827 264 GKDVLIVDDMIASGGSMIDAAKELKSRGAKKIIVAATFG 302
|
|
| |
