|
Name |
Accession |
Description |
Interval |
E-value |
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
16-483 |
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: 744.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 16 DTLHEECGVFGILGHEDAAALTALGLHALQHRGQEAAGIVSYHNRRFHSERHMGLVGDHFTDAaTLNRLPGNRAIGHVRY 95
Cdd:COG0034 2 DKLHEECGVFGIYGHEDVAQLTYYGLYALQHRGQESAGIATSDGGRFHLHKGMGLVSDVFDEE-DLERLKGNIAIGHVRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 96 STTGETILRNVQPLFAELEVGGIAIAHNGNFTNGITLRKQLIASGAIFQATSDTEVVLHMIARSRHSSS-TDRFVEAIRQ 174
Cdd:COG0034 81 STTGSSSLENAQPFYVNSPFGSIALAHNGNLTNAEELREELEEEGAIFQTTSDTEVILHLIARELTKEDlEEAIKEALRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 175 VEGGYAMLALTRTKLIAARDPIGIRPLVMGELDGKPIFCSETCALDIIGAKYIRDVENGEVVVceIQKDGsitTRSIKPE 254
Cdd:COG0034 161 VKGAYSLVILTGDGLIAARDPNGIRPLVLGKLEDGYVVASESCALDILGAEFVRDVEPGEIVV--IDEDG---LRSRQFA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 255 NPQPERLCLFEYVYFARPDSVVGGRSVYVARKNMGMNLAAEAGvdadvvvpvPDG---------GTPAALGFAQASGIPF 325
Cdd:COG0034 236 EKPRPAPCIFEYVYFARPDSVIDGRSVYEARKRMGRELAREAP---------VDAdvvipvpdsGRPAAIGYAEESGIPY 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 326 EYGIIRNHYVGRTFIEPTQQIRALGVKLKHSANRAMIEGKRVVLVDDSIVRGTTSVKIVQMIRDAGATEVHMRVASPMIF 405
Cdd:COG0034 307 EEGLIKNRYVGRTFIQPTQELRELGVRLKLNPIREVVKGKRVVLVDDSIVRGTTSRRIVKMLREAGAKEVHFRIASPPIR 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489057333 406 HPDFYGIDTPHADKLLANQHeSLESMCRYIGADSLAFLSIDGLYKAVGGKPRDpkaptFTDHYFTGEYPTRLLDQEGE 483
Cdd:COG0034 387 YPCYYGIDTPTREELIAANR-SVEEIREYIGADSLGYLSLEGLIEAVGEPIEG-----FCTACFTGDYPTGIPDEEKK 458
|
|
| purF |
TIGR01134 |
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ... |
22-474 |
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: 568.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 22 CGVFGILGH-EDAAALTALGLHALQHRGQEAAGIVSYHNRRFHSERHMGLVGDHFtDAATLNRLPGNRAIGHVRYSTTGE 100
Cdd:TIGR01134 1 CGVVGIYGQeEVAASLTYYGLYALQHRGQESAGISVFDGNRFRLHKGNGLVSDVF-NEEHLQRLKGNVGIGHVRYSTAGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 101 TILRNVQPLFAELEVGGIAIAHNGNFTNGITLRKQLIASGAIFQATSDTEVVLHMIARSRHSSST--DRFVEAIRQVEGG 178
Cdd:TIGR01134 80 SGLENAQPFVVNSPYGGLALAHNGNLVNADELRRELEEEGRHFNTTSDSEVLLHLLAHNDESKDDlfDAVARVLERVRGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 179 YAMLALTRTKLIAARDPIGIRPLVMGELDGKPIFCSETCALDIIGAKYIRDVENGEVVVCeiqKDGSITTRSIKPENPQP 258
Cdd:TIGR01134 160 YALVLMTEDGLVAVRDPHGIRPLVLGRRGDGYVVASESCALDILGAEFVRDVEPGEVVVI---FDGGLESRQCARRPRAP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 259 erlCLFEYVYFARPDSVVGGRSVYVARKNMGMNLAAEAGVDADVVVPVPDGGTPAALGFAQASGIPFEYGIIRNHYVGRT 338
Cdd:TIGR01134 237 ---CVFEYVYFARPDSVIDGISVYYARKRMGKELARESPVEADVVVPVPDSGRSAALGFAQASGIPYREGLIKNRYVGRT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 339 FIEPTQQIRALGVKLKHSANRAMIEGKRVVLVDDSIVRGTTSVKIVQMIRDAGATEVHMRVASPMIFHPDFYGIDTPHAD 418
Cdd:TIGR01134 314 FIMPTQELRELSVRLKLNPVRAVFEGKRVVLVDDSIVRGTTSRQIVEMLRDAGAKEVHVRIASPPIRYPCYYGIDMPTRE 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 489057333 419 KLLANQHESLESmcRYIGADSLAFLSIDGLYKAVGGKPRDpkaptFTDHYFTGEYP 474
Cdd:TIGR01134 394 ELIAARRTVEEI--RKIGADSLAYLSLEGLKEAVGNPESD-----LCLACFTGEYP 442
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
8-474 |
0e+00 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 551.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 8 NAPFMLDDDTLHEECGVFGILGHE--DAAALTALGLHALQHRGQEAAGIVSYHNRRFHSERHMGLVGDHFtDAATLNRLP 85
Cdd:PRK05793 1 NMMMDLEGDKFKEECGVFGVFSKNniDVASLTYYGLYALQHRGQESAGIAVSDGEKIKVHKGMGLVSEVF-SKEKLKGLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 86 GNRAIGHVRYSTTGETILRNVQPLFAELEVGGIAIAHNGNFTNGITLRKQLIASGAIFQATSDTEVVLHMIARSRHSSST 165
Cdd:PRK05793 80 GNSAIGHVRYSTTGASDLDNAQPLVANYKLGSIAIAHNGNLVNADVIRELLEDGGRIFQTSIDSEVILNLIARSAKKGLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 166 DRFVEAIRQVEGGYAMLALTRTKLIAARDPIGIRPLVMGELDGKPIFCSETCALDIIGAKYIRDVENGEVVVceIQKDGS 245
Cdd:PRK05793 160 KALVDAIQAIKGSYALVILTEDKLIGVRDPHGIRPLCLGKLGDDYILSSESCALDTIGAEFIRDVEPGEIVI--IDEDGI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 246 ittRSIKPENPQPERLCLFEYVYFARPDSVVGGRSVYVARKNMGMNLAAEAGVDADVVVPVPDGGTPAALGFAQASGIPF 325
Cdd:PRK05793 238 ---KSIKFAEKTKCQTCAFEYIYFARPDSVIDGISVYESRVRAGRQLYKEYPVDADIVIGVPDSGIPAAIGYAEASGIPY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 326 EYGIIRNHYVGRTFIEPTQQIRALGVKLKHSANRAMIEGKRVVLVDDSIVRGTTSVKIVQMIRDAGATEVHMRVASPMIF 405
Cdd:PRK05793 315 GIGFIKNKYVGRTFIAPSQELRERAVRVKLNPLKVNVEGKRVVLIDDSIVRGTTSKRLVELLRKAGAKEVHFRVSSPPVK 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489057333 406 HPDFYGIDTPHADKLLAnQHESLESMCRYIGADSLAFLSIDGLYKAVGGKprdpkaPTFTDHYFTGEYP 474
Cdd:PRK05793 395 YPCYFGIDTPYRKELIG-ANMSVEEIREMIGADSLGYLSIEGLLESLNGD------KGFCLGCFNGVYP 456
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
21-474 |
0e+00 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 548.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 21 ECGVFGILGHEDAAALTALGLHALQHRGQEAAGIVSYHNRRFHSERHMGLVGDHFTDAAtLNRLPGNRAIGHVRYSTTGE 100
Cdd:PLN02440 1 ECGVVGIFGDPEASRLCYLGLHALQHRGQEGAGIVTVDGNRLQSITGNGLVSDVFDESK-LDQLPGDIAIGHVRYSTAGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 101 TILRNVQPLFAELEVGGIAIAHNGNFTNGITLRKQLIASGAIFQATSDTEVVLHMIARSRHSSSTDRFVEAIRQVEGGYA 180
Cdd:PLN02440 80 SSLKNVQPFVANYRFGSIGVAHNGNLVNYEELRAKLEENGSIFNTSSDTEVLLHLIAISKARPFFSRIVDACEKLKGAYS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 181 MLALTRTKLIAARDPIGIRPLVMGEL-DGKPIFCSETCALDIIGAKYIRDVENGEVVVceIQKDGSITTRSIKPeNPQPe 259
Cdd:PLN02440 160 MVFLTEDKLVAVRDPHGFRPLVMGRRsNGAVVFASETCALDLIGATYEREVNPGEVIV--VDKDKGVSSQCLMP-HPEP- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 260 RLCLFEYVYFARPDSVVGGRSVYVARKNMGMNLAAEAGVDADVVVPVPDGGTPAALGFAQASGIPFEYGIIRNHYVGRTF 339
Cdd:PLN02440 236 KPCIFEHIYFARPNSIVFGRSVYESRLEFGEILATEIPVDCDVVIPVPDSGRVAALGYAAKLGVPFQQGLIRSHYVGRTF 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 340 IEPTQQIRALGVKLKHSANRAMIEGKRVVLVDDSIVRGTTSVKIVQMIRDAGATEVHMRVASPMIFHPDFYGIDTPHADK 419
Cdd:PLN02440 316 IEPSQKIRDFSVKLKLNPVRSVLEGKRVVVVDDSIVRGTTSSKIVRMLREAGAKEVHMRIASPPIIASCYYGVDTPSREE 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 489057333 420 LLANQhESLESMCRYIGADSLAFLSIDGLYKAVGGKPrdpkaPTFTDHYFTGEYP 474
Cdd:PLN02440 396 LISNR-MSVEEIRKFIGCDSLAFLPLEDLKKSLGEES-----PRFCYACFSGDYP 444
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
22-276 |
1.42e-138 |
|
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: 399.14 E-value: 1.42e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 22 CGVFGILGHEDAAALTALGLHALQHRGQEAAGIVSYHNRRFHSERHMGLVGDHFTDAaTLNRLPGNRAIGHVRYSTTGET 101
Cdd:cd00715 1 CGVFGIYGAEDAARLTYLGLYALQHRGQESAGIATSDGKRFHTHKGMGLVSDVFDEE-KLRRLPGNIAIGHVRYSTAGSS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 102 ILRNVQPLFAELEVGGIAIAHNGNFTNGITLRKQLIASGAIFQATSDTEVVLHMIARSRHSSS-TDRFVEAIRQVEGGYA 180
Cdd:cd00715 80 SLENAQPFVVNSPLGGIALAHNGNLVNAKELREELEEEGRIFQTTSDSEVILHLIARSLAKDDlFEAIIDALERVKGAYS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 181 MLALTRTKLIAARDPIGIRPLVMGELDGK-PIFCSETCALDIIGAKYIRDVENGEVVVceIQKDGsitTRSIKPENPQPE 259
Cdd:cd00715 160 LVIMTADGLIAVRDPHGIRPLVLGKLEGDgYVVASESCALDIIGAEFVRDVEPGEIVV--IDDDG---LESSQRAPKPKP 234
|
250
....*....|....*..
gi 489057333 260 RLCLFEYVYFARPDSVV 276
Cdd:cd00715 235 APCIFEYVYFARPDSVI 251
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
22-236 |
1.79e-59 |
|
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: 195.36 E-value: 1.79e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 22 CGVFGILGHEDAAALTAL----GLHALQHRGQEAAGIVSYHNRRFHSERHMGLVGDHFTDAAtLNRLPGNRAIGHVRYST 97
Cdd:cd00352 1 CGIFGIVGADGAASLLLLlllrGLAALEHRGPDGAGIAVYDGDGLFVEKRAGPVSDVALDLL-DEPLKSGVALGHVRLAT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 98 TGETILRNVQPLFAEleVGGIAIAHNGNFTNGITLRKQLIASGAIFQATSDTEVVLHMIARS-RHSSSTDRFVEAIRQVE 176
Cdd:cd00352 80 NGLPSEANAQPFRSE--DGRIALVHNGEIYNYRELREELEARGYRFEGESDSEVILHLLERLgREGGLFEAVEDALKRLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489057333 177 GGYAMLALTR--TKLIAARDPIGIRPLVMGEL-DGKPIFCSETCALDIIGAKYIRDVENGEVV 236
Cdd:cd00352 158 GPFAFALWDGkpDRLFAARDRFGIRPLYYGITkDGGLVFASEPKALLALPFKGVRRLPPGELL 220
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
22-237 |
2.60e-26 |
|
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: 106.38 E-value: 2.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 22 CGVFGILGHEDAAALTALGLHALQHRGQEAAGIVSYHNRRFHSERHMGLVGDhFTDAATLNRLPGNRAIGHVRYSTTGET 101
Cdd:cd00714 1 CGIVGYIGKREAVDILLEGLKRLEYRGYDSAGIAVIGDGSLEVVKAVGKVAN-LEEKLAEKPLSGHVGIGHTRWATHGEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 102 ILRNVQPLFAEleVGGIAIAHNGNFTNGITLRKQLIASGAIFQATSDTEVVLHMIARS--RHSSSTDRFVEAIRQVEGGY 179
Cdd:cd00714 80 TDVNAHPHRSC--DGEIAVVHNGIIENYAELKEELEAKGYKFESETDTEVIAHLIEYYydGGLDLLEAVKKALKRLEGAY 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489057333 180 AMLALTRT---KLIAARdpigiR--PLVMGELDGKPIFCSETCALdiigAKYIRDV---ENGEVVV 237
Cdd:cd00714 158 ALAVISKDepdEIVAAR-----NgsPLVIGIGDGENFVASDAPAL----LEHTRRViylEDGDIAV 214
|
|
| glmS |
TIGR01135 |
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ... |
22-244 |
2.12e-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: 103.49 E-value: 2.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 22 CGVFGILGHEDAAALTALGLHALQHRGQEAAGIVSYHNRRFHSERHMGLVGDhFTDAATLNRLPGNRAIGHVRYSTTGET 101
Cdd:TIGR01135 1 CGIVGYIGQRDAVPILLEGLKRLEYRGYDSAGIAVVDEGKLFVRKAVGKVAE-LANKLGEKPLPGGVGIGHTRWATHGKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 102 ILRNVQPLFAELevGGIAIAHNGNFTNGITLRKQLIASGAIFQATSDTEVVLHMIArsRHSSSTDRFVEA----IRQVEG 177
Cdd:TIGR01135 80 TDENAHPHTDEG--GRIAVVHNGIIENYAELREELEARGHVFSSDTDTEVIAHLIE--EELREGGDLLEAvqkaLKQLRG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489057333 178 GYAMLALT---RTKLIAARDPigiRPLVMGELDGKPIFCSETCALdiigAKYIRDV---ENGEVVVceIQKDG 244
Cdd:TIGR01135 156 AYALAVLHadhPETLVAARSG---SPLIVGLGDGENFVASDVTAL----LPYTRRViylEDGDIAI--LTKDG 219
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
22-258 |
6.29e-23 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 102.04 E-value: 6.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 22 CGVFGILGHEDAAALTALGLHALQHRGQEAAGIVSYHNRRFHSERHMGLVgDHFTDAATLNRLPGNRAIGHVRYSTTGET 101
Cdd:PRK00331 2 CGIVGYVGQRNAAEILLEGLKRLEYRGYDSAGIAVLDDGGLEVRKAVGKV-ANLEAKLEEEPLPGTTGIGHTRWATHGKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 102 ILRNVQPLFAEleVGGIAIAHNG---NFTngiTLRKQLIASGAIFQATSDTEVVLHMIAR--SRHSSSTDRFVEAIRQVE 176
Cdd:PRK00331 81 TERNAHPHTDC--SGRIAVVHNGiieNYA---ELKEELLAKGHVFKSETDTEVIAHLIEEelKEGGDLLEAVRKALKRLE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 177 GGYAMLALTRT---KLIAAR-DPigirPLVMGELDGKPIFCSETCALdiigAKYIRDV---ENGEVVVceIQKDG-SITT 248
Cdd:PRK00331 156 GAYALAVIDKDepdTIVAARnGS----PLVIGLGEGENFLASDALAL----LPYTRRViylEDGEIAV--LTRDGvEIFD 225
|
250
....*....|
gi 489057333 249 RSIKPENPQP 258
Cdd:PRK00331 226 FDGNPVEREV 235
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
22-219 |
7.73e-23 |
|
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: 96.47 E-value: 7.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 22 CGVFGILG----HEDAAALTALgLHALQHRGQEAAGIvsYHNRRFhserhmglvgdhftdaatlnrlpgnrAIGHVRYST 97
Cdd:cd00712 1 CGIAGIIGldgaSVDRATLERM-LDALAHRGPDGSGI--WIDEGV--------------------------ALGHRRLSI 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 98 TGETilRNVQPLFaeLEVGGIAIAHNGNFTNGITLRKQLIASGAIFQATSDTEVVLHMIARSRhssstDRFVEAIRqveG 177
Cdd:cd00712 52 IDLS--GGAQPMV--SEDGRLVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHLYEEWG-----EDCLERLN---G 119
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489057333 178 GYAmLAL--TRTK-LIAARDPIGIRPLVMGELDGKPIFCSETCAL 219
Cdd:cd00712 120 MFA-FALwdKRKRrLFLARDRFGIKPLYYGRDGGGLAFASELKAL 163
|
|
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
22-261 |
5.55e-22 |
|
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: 99.32 E-value: 5.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 22 CGVFGILGHEDAAALtaL--GLHALQHRGQEAAGIVSYHNRRFHSERHMGLVGDhFTDAATLNRLPGNRAIGHVRYSTTG 99
Cdd:COG0449 2 CGIVGYIGKRDAAPI--LleGLKRLEYRGYDSAGIAVLDDGGLEVRKAVGKLAN-LEEKLAEEPLSGTIGIGHTRWATHG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 100 ETILRNVQPLFAEleVGGIAIAHNG---NFTngiTLRKQLIASGAIFQATSDTEVVLHMIAR--SRHSSSTDRFVEAIRQ 174
Cdd:COG0449 79 APSDENAHPHTSC--SGRIAVVHNGiieNYA---ELREELEAKGHTFKSETDTEVIAHLIEEylKGGGDLLEAVRKALKR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 175 VEGGYAMLALTRT---KLIAAR-DPigirPLVMGELDGKPIFCSETCALdiigAKYIRDV---ENGEVVVceIQKDG-SI 246
Cdd:COG0449 154 LEGAYALAVISADepdRIVAARkGS----PLVIGLGEGENFLASDVPAL----LPYTRRViylEDGEIAV--LTRDGvEI 223
|
250
....*....|....*
gi 489057333 247 TTRSIKPENPQPERL 261
Cdd:COG0449 224 YDLDGEPVEREVKTV 238
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
22-238 |
2.72e-19 |
|
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: 87.32 E-value: 2.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 22 CGVFGIL---GHEDAAALTALGLHALQHRG-QEAAGIVSY---HNRRFHSERHMGL---VGDHfTDAATLNRLP---GNR 88
Cdd:cd01907 1 CGIFGIMskdGEPFVGALLVEMLDAMQERGpGDGAGFALYgdpDAFVYSSGKDMEVfkgVGYP-EDIARRYDLEeykGYH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 89 AIGHVRYSTTGETILRNVQPLFaeleVGGIAIAHNGNFTNGITLRKQLIASGAIFQATSDTEVVLHMIAR--SRHSSSTD 166
Cdd:cd01907 80 WIAHTRQPTNSAVWWYGAHPFS----IGDIAVVHNGEISNYGSNREYLERFGYKFETETDTEVIAYYLDLllRKGGLPLE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 167 RFVEAIRQVE-------------------GGYAMLALTRTKLIAARDPIGIRPLVMGELDGKPIFCSETCALD-IIGAKY 226
Cdd:cd01907 156 YYKHIIRMPEeerelllalrltyrladldGPFTIIVGTPDGFIVIRDRIKLRPAVVAETDDYVAIASEECAIReIPDRDN 235
|
250
....*....|....
gi 489057333 227 IRDVE--NGEVVVC 238
Cdd:cd01907 236 AKVWEprPGEYVIW 249
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
22-219 |
4.93e-19 |
|
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: 89.90 E-value: 4.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 22 CGVFGILGHEDAAALTALG--LHALQHRGQEAAGIvsyhnrrfHSERHMGLvgdhftdaatlnrlpgnraiGHVRYSTTG 99
Cdd:COG0367 2 CGIAGIIDFDGGADREVLErmLDALAHRGPDGSGI--------WVDGGVAL--------------------GHRRLSIID 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 100 ETIlRNVQPLFAELevGGIAIAHNGNFTNGITLRKQLIASGAIFQATSDTEVVLHMIARSRhssstdrfVEAIRQVEGGY 179
Cdd:COG0367 54 LSE-GGHQPMVSED--GRYVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHAYEEWG--------EDCLERLNGMF 122
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489057333 180 AmLAL---TRTKLIAARDPIGIRPLVMGELDGKPIFCSETCAL 219
Cdd:COG0367 123 A-FAIwdrRERRLFLARDRFGIKPLYYAEDGGGLAFASELKAL 164
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
107-219 |
6.48e-18 |
|
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: 79.48 E-value: 6.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 107 QPLFAElEVGGIAIAHNGNFTNGITLRKQLIASGAIFQATSDTEVVLHMIARsrhssstDRFVEAIRQVEGGYAmLAL-- 184
Cdd:pfam13537 14 QPMVSS-EDGRYVIVFNGEIYNYRELRAELEAKGYRFRTHSDTEVILHLYEA-------EWGEDCVDRLNGMFA-FAIwd 84
|
90 100 110
....*....|....*....|....*....|....*..
gi 489057333 185 -TRTKLIAARDPIGIRPLVMGELDGKP-IFCSETCAL 219
Cdd:pfam13537 85 rRRQRLFLARDRFGIKPLYYGRDDGGRlLFASELKAL 121
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
89-215 |
1.12e-16 |
|
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: 76.19 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 89 AIGHVRYSTTGETILRNvQPLFaeLEVGGIAIAHNGNFTNGITLRKQLIASGAIFQATSDTEVVLHMIArsRHSSST-DR 167
Cdd:pfam13522 13 ALGHVRLAIVDLPDAGN-QPML--SRDGRLVLVHNGEIYNYGELREELADLGHAFRSRSDTEVLLALYE--EWGEDClER 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 489057333 168 FVEAIRqveggYAMLALTRTKLIAARDPIGIRPLVMGELDGKPIFCSE 215
Cdd:pfam13522 88 LRGMFA-----FAIWDRRRRTLFLARDRLGIKPLYYGILGGGFVFASE 130
|
|
| PRTases_typeI |
cd06223 |
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ... |
309-415 |
1.19e-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: 76.28 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 309 GGTPAALGFAQASGIPFEYGIIRNHYVGRTFIEPTQqiralgvklKHSANRAMIEGKRVVLVDDSIVRGTTSVKIVQMIR 388
Cdd:cd06223 25 GGLPLAAALARALGLPLAFIRKERKGPGRTPSEPYG---------LELPLGGDVKGKRVLLVDDVIATGGTLLAAIELLK 95
|
90 100
....*....|....*....|....*..
gi 489057333 389 DAGATEVHMRVAsPMIFHPDFYGIDTP 415
Cdd:cd06223 96 EAGAKVVGVAVL-LDKPEGGARELASP 121
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
19-244 |
1.52e-15 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 79.30 E-value: 1.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 19 HEECGVFGILGHEDAAALTALGLHALQHRGQEAAGIVSYHNR------RFHSERHMGLVGDHFTDAATLNRLPGNRAIGH 92
Cdd:PTZ00295 22 DYCCGIVGYLGNEDASKILLEGIEILQNRGYDSCGISTISSGgelkttKYASDGTTSDSIEILKEKLLDSHKNSTIGIAH 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 93 VRYSTTGETILRNVQPLFAELEvgGIAIAHNGNFTNGITLRKQLIASGAIFQATSDTEVVLHMIArsRHSSSTDRFVEA- 171
Cdd:PTZ00295 102 TRWATHGGKTDENAHPHCDYKK--RIALVHNGTIENYVELKSELIAKGIKFRSETDSEVIANLIG--LELDQGEDFQEAv 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 172 ---IRQVEGGYAMLALTR---TKLIAARDPigiRPLVMGELDGKPIFCSETCALdiigAKYIRD---VENGEVVvcEIQK 242
Cdd:PTZ00295 178 ksaISRLQGTWGLCIIHKdnpDSLIVARNG---SPLLVGIGDDSIYVASEPSAF----AKYTNEyisLKDGEIA--ELSL 248
|
..
gi 489057333 243 DG 244
Cdd:PTZ00295 249 EN 250
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
24-219 |
8.28e-15 |
|
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: 76.60 E-value: 8.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 24 VFGILGHEDAAALTALGLHALQ----HRGQEAAGIVSYHnrrfhserhmglvgdhftdaatlnrlpGNRAIGHVRYSTTG 99
Cdd:TIGR01536 1 IAGFFDLDDKAVEEDEAIKRMSdtiaHRGPDASGIEYKD---------------------------GNAILGHRRLAIID 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 100 ETILRnvQPLFAEleVGGIAIAHNGNFTNGITLRKQLIASGAIFQATSDTEVVLHMIARSRhssstdrfVEAIRQVEGGY 179
Cdd:TIGR01536 54 LSGGA--QPMSNE--GKTYVIVFNGEIYNHEELREELEAKGYTFQTDSDTEVILHLYEEWG--------EECVDRLDGMF 121
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489057333 180 AmLALT---RTKLIAARDPIGIRPLVMGELDGKPIFCSETCAL 219
Cdd:TIGR01536 122 A-FALWdseKGELFLARDRFGIKPLYYAYDGGQLYFASEIKAL 163
|
|
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
22-219 |
2.00e-13 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 72.63 E-value: 2.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 22 CGVFGILG-HEDAAALTALGLHALQ---HRGQEAAGIVSyhnrrfhserhmglvgdhfTDAATLnrlpgnraiGHVRYS- 96
Cdd:PRK09431 2 CGIFGILDiKTDADELRKKALEMSRlmrHRGPDWSGIYA-------------------SDNAIL---------GHERLSi 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 97 ---TTGEtilrnvQPLFAEleVGGIAIAHNGNFTNGITLRKQLiASGAIFQATSDTEVVLHMIarsrhsssTDRFVEAIR 173
Cdd:PRK09431 54 vdvNGGA------QPLYNE--DGTHVLAVNGEIYNHQELRAEL-GDKYAFQTGSDCEVILALY--------QEKGPDFLD 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489057333 174 QVEGGYAMlALTRTK---LIAARDPIGIRPLVMGE-LDGKPIFCSETCAL 219
Cdd:PRK09431 117 DLDGMFAF-ALYDSEkdaYLIARDPIGIIPLYYGYdEHGNLYFASEMKAL 165
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
22-220 |
2.09e-11 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 66.28 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 22 CG---VFGILGHEDAAALTALGLHA-LQHRGQEAAGIVSYHNrrfhserhmglvGDHFTDAATLNRLpgnrAIGHVrysT 97
Cdd:PTZ00077 2 CGilaIFNSKGERHELRRKALELSKrLRHRGPDWSGIIVLEN------------SPGTYNILAHERL----AIVDL---S 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 98 TGEtilrnvQPLFAELEVggIAIAHNGNFTNGITLRKQLIASGAIFQATSDTEVVLHMIarSRHSSStdrfvEAIRQVEG 177
Cdd:PTZ00077 63 DGK------QPLLDDDET--VALMQNGEIYNHWEIRPELEKEGYKFSSNSDCEIIGHLY--KEYGPK-----DFWNHLDG 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489057333 178 GYAMLALTRTK--LIAARDPIGIRPLVMG-ELDGKPIFCSETCALD 220
Cdd:PTZ00077 128 MFATVIYDMKTntFFAARDHIGIIPLYIGyAKDGSIWFSSELKALH 173
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
22-213 |
1.60e-09 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 60.28 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 22 CGVFGILGH------EDAAALTALGLHALQHRGQEAAGIVSyhNRRFHSERHMGLVGDH--------------------- 74
Cdd:PTZ00394 2 CGIFGYANHnvprtvEQILNVLLDGIQKVEYRGYDSAGLAI--DANIGSEKEDGTAASAptprpcvvrsvgnisqlrekv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 75 FTDAATLNRLPGNR------AIGHVRYSTTGETILRNVQPlfAELEVGGIAIAHNGNFTNGITLRKQLIASGAIFQATSD 148
Cdd:PTZ00394 80 FSEAVAATLPPMDAttshhvGIAHTRWATHGGVCERNCHP--QQSNNGEFTIVHNGIVTNYMTLKELLKEEGYHFSSDTD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489057333 149 TEVVL----HMIARSRHSSSTDRFVEAIRQVEGGYAMLALT---RTKLIAARDPigiRPLVMGELDGKPIFC 213
Cdd:PTZ00394 158 TEVISvlseYLYTRKGIHNFADLALEVSRMVEGSYALLVKSvyfPGQLAASRKG---SPLMVGIRRTDDRGC 226
|
|
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
22-209 |
3.51e-09 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 59.38 E-value: 3.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 22 CGVFGILGH----EDAAALTAL--GLHALQHRGQEAAGIVSYHNRRFHSE-----RHMG----LVGDHFTDAATLNrLPG 86
Cdd:PLN02981 2 CGIFAYLNYnvprERRFILEVLfnGLRRLEYRGYDSAGIAIDNDPSLESSsplvfREEGkiesLVRSVYEEVAETD-LNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 87 NRA------IGHVRYSTTGETILRNVQPLFAELEvGGIAIAHNGNFTNGITLRKQLIASGAIFQATSDTEVVLHMiARSR 160
Cdd:PLN02981 81 DLVfenhagIAHTRWATHGPPAPRNSHPQSSGPG-NEFLVVHNGIITNYEVLKETLLRHGFTFESDTDTEVIPKL-AKFV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489057333 161 HSSSTDR---------FVEAIRQVEGGYAMLALTR---TKLIAARDPigiRPLVMG--ELDGK 209
Cdd:PLN02981 159 FDKLNEEegdvtfsqvVMEVMRQLEGAYALIFKSPhypNELVACKRG---SPLLLGvkELPEE 218
|
|
| PLN02549 |
PLN02549 |
asparagine synthase (glutamine-hydrolyzing) |
22-219 |
5.23e-08 |
|
asparagine synthase (glutamine-hydrolyzing)
Pssm-ID: 178164 [Multi-domain] Cd Length: 578 Bit Score: 55.54 E-value: 5.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 22 CGVFGILG-HEDAAALTA--LGLHA-LQHRGQEAAGIvsYHNRRFhserhmglvgdhftdaatlnrlpgnrAIGHVRYS- 96
Cdd:PLN02549 2 CGILAVLGcSDDSQAKRSrvLELSRrLRHRGPDWSGL--YGNEDC--------------------------YLAHERLAi 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 97 ---TTGEtilrnvQPLFAEleVGGIAIAHNGNFTNGITLRKQLiaSGAIFQATSDTEVVLHMIArsrhssstDRFVEAIR 173
Cdd:PLN02549 54 mdpESGD------QPLYNE--DKTIVVTANGEIYNHKELREKL--KLHKFRTGSDCEVIAHLYE--------EHGEEFVD 115
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489057333 174 QVEGGYAMLAL-TRTK-LIAARDPIGIRPLVMG-ELDGKPIFCSETCAL 219
Cdd:PLN02549 116 MLDGMFSFVLLdTRDNsFIAARDHIGITPLYIGwGLDGSVWFASEMKAL 164
|
|
| YafJ |
COG0121 |
Predicted glutamine amidotransferase YafJ [General function prediction only]; |
90-247 |
8.07e-08 |
|
Predicted glutamine amidotransferase YafJ [General function prediction only];
Pssm-ID: 439891 [Multi-domain] Cd Length: 248 Bit Score: 53.43 E-value: 8.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 90 IGHVRYSTTGETILRNVQPlFAElevGGIAIAHNGNFTNGITLRKQLIASGAIF-----QATSDTEVVLHMIA---RSRH 161
Cdd:COG0121 80 IAHVRKATVGPVSLENTHP-FRG---GRWLFAHNGQLDGFDRLRRRLAEELPDElyfqpVGTTDSELAFALLLsrlRDGG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 162 SSSTDRFVEAIRQVE------GGYAMLALTRTKLIAARDPIGIRPLVM------GELDGKPIFCSETcaLDiiGAKYIRD 229
Cdd:COG0121 156 PDPAEALAEALRELAelarapGRLNLLLSDGERLYATRYTSDDPYPTLyyltrtTPDDRVVVVASEP--LT--DDEGWTE 231
|
170
....*....|....*...
gi 489057333 230 VENGEVVVceIQKDGSIT 247
Cdd:COG0121 232 VPPGELLV--VRDGLEVE 247
|
|
| YafJ |
cd01908 |
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ... |
90-175 |
5.97e-06 |
|
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: 47.77 E-value: 5.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 90 IGHVRYSTTGETILRNVQPlFAElevGGIAIAHNGNFTNGITLRKQLIASGAIF-QATSDTEVVLHMI---ARSRHSSST 165
Cdd:cd01908 84 LAHVRAATVGPVSLENCHP-FTR---GRWLFAHNGQLDGFRLLRRRLLRLLPRLpVGTTDSELAFALLlsrLLERDPLDP 159
|
90
....*....|
gi 489057333 166 DRFVEAIRQV 175
Cdd:cd01908 160 AELLDAILQT 169
|
|
| Hpt1 |
COG2236 |
Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine ... |
360-415 |
1.65e-05 |
|
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: 44.84 E-value: 1.65e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489057333 360 AMIEGKRVVLVDDSIVRGTTSVKIVQMIRDAGATEVhmRVASP-----MIFHPDFYGIDTP 415
Cdd:COG2236 84 EDLAGKRVLIVDDVADTGRTLEAVRDLLKEAGPAEV--RTAVLyykpsSKFKPDYYAEETD 142
|
|
| PRK09162 |
PRK09162 |
hypoxanthine-guanine phosphoribosyltransferase; Provisional |
362-415 |
3.67e-05 |
|
hypoxanthine-guanine phosphoribosyltransferase; Provisional
Pssm-ID: 181675 Cd Length: 181 Bit Score: 44.47 E-value: 3.67e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489057333 362 IEGKRVVLVDDSIVRGTTSVKIVQMIRDAGATEV---------HMRVASPMifHPDFYGIDTP 415
Cdd:PRK09162 95 LKGRTVLVVDDILDEGHTLAAIRDRCLEMGAAEVysavlvdktHDRKAKPL--KADFVGLEVP 155
|
|
| PyrE |
COG0461 |
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ... |
359-397 |
1.96e-04 |
|
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate phosphoribosyltransferase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 440229 Cd Length: 201 Bit Score: 42.45 E-value: 1.96e-04
10 20 30
....*....|....*....|....*....|....*....
gi 489057333 359 RAMIEGKRVVLVDDSIVRGTTSVKIVQMIRDAGATEVHM 397
Cdd:COG0461 107 GGLLPGERVLVVEDVITTGGSVLEAVEALREAGAEVVGV 145
|
|
| PRK02277 |
PRK02277 |
orotate phosphoribosyltransferase-like protein; Provisional |
356-395 |
6.07e-04 |
|
orotate phosphoribosyltransferase-like protein; Provisional
Pssm-ID: 235023 [Multi-domain] Cd Length: 200 Bit Score: 41.01 E-value: 6.07e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 489057333 356 SANRAMIEGKRVVLVDDSIVRGTTSVKIVQMIRDAGATEV 395
Cdd:PRK02277 132 SRNFASVEGKRCVIVDDVITSGTTMKETIEYLKEHGGKPV 171
|
|
| pyrE |
PRK00455 |
orotate phosphoribosyltransferase; Validated |
360-397 |
6.81e-04 |
|
orotate phosphoribosyltransferase; Validated
Pssm-ID: 234771 Cd Length: 202 Bit Score: 40.91 E-value: 6.81e-04
10 20 30
....*....|....*....|....*....|....*...
gi 489057333 360 AMIEGKRVVLVDDSIVRGTTSVKIVQMIRDAGATEVHM 397
Cdd:PRK00455 109 RRLFGKRVLVVEDVITTGGSVLEAVEAIRAAGAEVVGV 146
|
|
| Pribosyltran |
pfam00156 |
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ... |
322-396 |
8.81e-04 |
|
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl transferase enzymes. This family includes: Adenine phosphoribosyl-transferase EC:2.4.2.7. Hypoxanthine-guanine-xanthine phosphoribosyl-transferase. Hypoxanthine phosphoribosyl-transferase EC:2.4.2.8. Ribose-phosphate pyrophosphokinase i EC:2.7.6.1. Amidophosphoribosyltransferase EC:2.4.2.14. Orotate phosphoribosyl-transferase EC:2.4.2.10. Uracil phosphoribosyl-transferase EC:2.4.2.9. Xanthine-guanine phosphoribosyl-transferase EC:2.4.2.22. In Arabidopsis, At the very N-terminus of this domain is the P-Loop NTPase domain.
Pssm-ID: 425489 [Multi-domain] Cd Length: 150 Bit Score: 39.66 E-value: 8.81e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489057333 322 GIPFEYGIIRNHYVGRTFIEPTQQIRALGVKLKHSANRAMIEGKRVVLVDDSIVRGTTSVKIVQMIRDAGATEVH 396
Cdd:pfam00156 40 GLPFAGILARRLDVPLAFVRKVSYNPDTSEVMKTSSALPDLKGKTVLIVDDILDTGGTLLKVLELLKNVGPKEVK 114
|
|
| HAND |
pfam09110 |
HAND; The HAND domain adopts a secondary structure consisting of four alpha helices, three of ... |
444-487 |
1.26e-03 |
|
HAND; The HAND domain adopts a secondary structure consisting of four alpha helices, three of which (H2, H3, H4) form an L-like configuration. Helix H2 runs antiparallel to helices H3 and H4, packing closely against helix H4, whilst helix H1 reposes in the concave surface formed by these three helices and runs perpendicular to them. The domain confers DNA and nucleosome binding properties to the protein.
Pssm-ID: 430414 Cd Length: 110 Bit Score: 38.31 E-value: 1.26e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 489057333 444 SIDGLYKAVGG-----------KPRDPKAPTFTDHYFtgeYPTRLLD-QEGESNVH 487
Cdd:pfam09110 1 SVDNYYKDVLGtggkksttkpkAPRAPKQINIQDHQF---FPPRLKElQEKEQLYY 53
|
|
| PrsA |
COG0462 |
Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; ... |
362-396 |
6.03e-03 |
|
Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; Phosphoribosylpyrophosphate synthetase is part of the Pathway/BioSystem: Histidine biosynthesis, Purine biosynthesis
Pssm-ID: 440230 [Multi-domain] Cd Length: 311 Bit Score: 38.89 E-value: 6.03e-03
10 20 30
....*....|....*....|....*....|....*
gi 489057333 362 IEGKRVVLVDDSIVRGTTSVKIVQMIRDAGATEVH 396
Cdd:COG0462 209 VEGKTCIIVDDMIDTGGTLVEAAEALKEAGAKSVY 243
|
|
| PRK07322 |
PRK07322 |
adenine phosphoribosyltransferase; Provisional |
310-395 |
8.52e-03 |
|
adenine phosphoribosyltransferase; Provisional
Pssm-ID: 180928 Cd Length: 178 Bit Score: 37.26 E-value: 8.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489057333 310 GTPAALGFAQASGIPfeYGIIRNH---YVGRTFIEPTQQIrALGVKLK---HSANRAMIEGKRVVLVDDSIVRGTTSVKI 383
Cdd:PRK07322 63 GIPLAHALSRRLGKP--YVVARKSrkpYMQDPIIQEVVSI-TTGKPQLlvlDGADAEKLKGKRVAIVDDVVSTGGTLTAL 139
|
90
....*....|..
gi 489057333 384 VQMIRDAGATEV 395
Cdd:PRK07322 140 ERLVERAGGQVV 151
|
|
| |
