|
Name |
Accession |
Description |
Interval |
E-value |
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
6-468 |
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: 763.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 6 GLNEECGVFGIWNHSEATQLTYMGLHSLQHRGQEGAGIVVSDGEVLKGERGLGLLTEAIKGDQMDQLKdGHNAIGHVRYA 85
Cdd:COG0034 3 KLHEECGVFGIYGHEDVAQLTYYGLYALQHRGQESAGIATSDGGRFHLHKGMGLVSDVFDEEDLERLK-GNIAIGHVRYS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 86 TSGNKGIENIQPFLYHFYDMSVAICHNGNLINAQTLRQYLEKHGAIFHSSSDTEVIMHLIRRS-KAPTFEEALKESLRQI 164
Cdd:COG0034 82 TTGSSSLENAQPFYVNSPFGSIALAHNGNLTNAEELREELEEEGAIFQTTSDTEVILHLIARElTKEDLEEAIKEALRRV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 165 KGGFTFAILTKDALYGAVDPNAIRPLVVGKMqDDTYILASETCAIDVLGAEYVQDIHAGEYVVINNEGIEVKSYTSHTNT 244
Cdd:COG0034 162 KGAYSLVILTGDGLIAARDPNGIRPLVLGKL-EDGYVVASESCALDILGAEFVRDVEPGEIVVIDEDGLRSRQFAEKPRP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 245 AISAMEYIYFARPDSTIAGKNVHAVRKASGKKLAQESPANADMVIGVPNSSLSAASGYAEESHLPYEMGLVKNQYVARTF 324
Cdd:COG0034 241 APCIFEYVYFARPDSVIDGRSVYEARKRMGRELAREAPVDADVVIPVPDSGRPAAIGYAEESGIPYEEGLIKNRYVGRTF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 325 IQPTQELREQGVRVKLSAVKDIVEGKRIVLVDDSIVRGTTSKRIVRMLKDSGAKEVHVRIASPEFMFPSFYGIDVSTTAE 404
Cdd:COG0034 321 IQPTQELRELGVRLKLNPIREVVKGKRVVLVDDSIVRGTTSRRIVKMLREAGAKEVHFRIASPPIRYPCYYGIDTPTREE 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 739694894 405 LISASKSPKEICDYIGADSLSYLSVDGLIESIGLnydaPYSGLCVESFTGDYPAGLFDYEDKYY 468
Cdd:COG0034 401 LIAANRSVEEIREYIGADSLGYLSLEGLIEAVGE----PIEGFCTACFTGDYPTGIPDEEKKRL 460
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
1-468 |
0e+00 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 611.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 1 MFNYSG--LNEECGVFGIW--NHSEATQLTYMGLHSLQHRGQEGAGIVVSDGEVLKGERGLGLLTEAIKGDQMDQLKdGH 76
Cdd:PRK05793 3 MMDLEGdkFKEECGVFGVFskNNIDVASLTYYGLYALQHRGQESAGIAVSDGEKIKVHKGMGLVSEVFSKEKLKGLK-GN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 77 NAIGHVRYATSGNKGIENIQPFLYHFYDMSVAICHNGNLINAQTLRQYLEKHGAIFHSSSDTEVIMHLIRRSKAPTFEEA 156
Cdd:PRK05793 82 SAIGHVRYSTTGASDLDNAQPLVANYKLGSIAIAHNGNLVNADVIRELLEDGGRIFQTSIDSEVILNLIARSAKKGLEKA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 157 LKESLRQIKGGFTFAILTKDALYGAVDPNAIRPLVVGKMqDDTYILASETCAIDVLGAEYVQDIHAGEYVVINNEGIEVK 236
Cdd:PRK05793 162 LVDAIQAIKGSYALVILTEDKLIGVRDPHGIRPLCLGKL-GDDYILSSESCALDTIGAEFIRDVEPGEIVIIDEDGIKSI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 237 SYTSHTNTAISAMEYIYFARPDSTIAGKNVHAVRKASGKKLAQESPANADMVIGVPNSSLSAASGYAEESHLPYEMGLVK 316
Cdd:PRK05793 241 KFAEKTKCQTCAFEYIYFARPDSVIDGISVYESRVRAGRQLYKEYPVDADIVIGVPDSGIPAAIGYAEASGIPYGIGFIK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 317 NQYVARTFIQPTQELREQGVRVKLSAVKDIVEGKRIVLVDDSIVRGTTSKRIVRMLKDSGAKEVHVRIASPEFMFPSFYG 396
Cdd:PRK05793 321 NKYVGRTFIAPSQELRERAVRVKLNPLKVNVEGKRVVLIDDSIVRGTTSKRLVELLRKAGAKEVHFRVSSPPVKYPCYFG 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 739694894 397 IDVSTTAELISASKSPKEICDYIGADSLSYLSVDGLIESIGLNydapySGLCVESFTGDYPAGLFDYEDKYY 468
Cdd:PRK05793 401 IDTPYRKELIGANMSVEEIREMIGADSLGYLSIEGLLESLNGD-----KGFCLGCFNGVYPVSAPKEGPKYL 467
|
|
| purF |
TIGR01134 |
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ... |
11-457 |
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: 578.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 11 CGVFGIWNHSE-ATQLTYMGLHSLQHRGQEGAGIVVSDGEVLKGERGLGLLTEAIKGDQMDQLKdGHNAIGHVRYATSGN 89
Cdd:TIGR01134 1 CGVVGIYGQEEvAASLTYYGLYALQHRGQESAGISVFDGNRFRLHKGNGLVSDVFNEEHLQRLK-GNVGIGHVRYSTAGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 90 KGIENIQPFLYHFYDMSVAICHNGNLINAQTLRQYLEKHGAIFHSSSDTEVIMHLIRRSKAP--TFEEALKESLRQIKGG 167
Cdd:TIGR01134 80 SGLENAQPFVVNSPYGGLALAHNGNLVNADELRRELEEEGRHFNTTSDSEVLLHLLAHNDESkdDLFDAVARVLERVRGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 168 FTFAILTKDALYGAVDPNAIRPLVVGKMqDDTYILASETCAIDVLGAEYVQDIHAGEYVVINNEGIEVKSYtSHTNTAIS 247
Cdd:TIGR01134 160 YALVLMTEDGLVAVRDPHGIRPLVLGRR-GDGYVVASESCALDILGAEFVRDVEPGEVVVIFDGGLESRQC-ARRPRAPC 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 248 AMEYIYFARPDSTIAGKNVHAVRKASGKKLAQESPANADMVIGVPNSSLSAASGYAEESHLPYEMGLVKNQYVARTFIQP 327
Cdd:TIGR01134 238 VFEYVYFARPDSVIDGISVYYARKRMGKELARESPVEADVVVPVPDSGRSAALGFAQASGIPYREGLIKNRYVGRTFIMP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 328 TQELREQGVRVKLSAVKDIVEGKRIVLVDDSIVRGTTSKRIVRMLKDSGAKEVHVRIASPEFMFPSFYGIDVSTTAELIS 407
Cdd:TIGR01134 318 TQELRELSVRLKLNPVRAVFEGKRVVLVDDSIVRGTTSRQIVEMLRDAGAKEVHVRIASPPIRYPCYYGIDMPTREELIA 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 739694894 408 ASKSPKEICdYIGADSLSYLSVDGLIESIGlnydAPYSGLCVESFTGDYP 457
Cdd:TIGR01134 398 ARRTVEEIR-KIGADSLAYLSLEGLKEAVG----NPESDLCLACFTGEYP 442
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
10-472 |
8.94e-180 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 512.69 E-value: 8.94e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 10 ECGVFGIWNHSEATQLTYMGLHSLQHRGQEGAGIVVSDGEVLKGERGLGLLTEAIKGDQMDQLKdGHNAIGHVRYATSGN 89
Cdd:PLN02440 1 ECGVVGIFGDPEASRLCYLGLHALQHRGQEGAGIVTVDGNRLQSITGNGLVSDVFDESKLDQLP-GDIAIGHVRYSTAGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 90 KGIENIQPFLYHFYDMSVAICHNGNLINAQTLRQYLEKHGAIFHSSSDTEVIMHLIRRSKAPTFEEALKESLRQIKGGFT 169
Cdd:PLN02440 80 SSLKNVQPFVANYRFGSIGVAHNGNLVNYEELRAKLEENGSIFNTSSDTEVLLHLIAISKARPFFSRIVDACEKLKGAYS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 170 FAILTKDALYGAVDPNAIRPLVVGKMQDDTYILASETCAIDVLGAEYVQDIHAGEYVVIN-NEGIEVKSYTSHTNTAISA 248
Cdd:PLN02440 160 MVFLTEDKLVAVRDPHGFRPLVMGRRSNGAVVFASETCALDLIGATYEREVNPGEVIVVDkDKGVSSQCLMPHPEPKPCI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 249 MEYIYFARPDSTIAGKNVHAVRKASGKKLAQESPANADMVIGVPNSSLSAASGYAEESHLPYEMGLVKNQYVARTFIQPT 328
Cdd:PLN02440 240 FEHIYFARPNSIVFGRSVYESRLEFGEILATEIPVDCDVVIPVPDSGRVAALGYAAKLGVPFQQGLIRSHYVGRTFIEPS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 329 QELREQGVRVKLSAVKDIVEGKRIVLVDDSIVRGTTSKRIVRMLKDSGAKEVHVRIASPEFMFPSFYGIDVSTTAELISA 408
Cdd:PLN02440 320 QKIRDFSVKLKLNPVRSVLEGKRVVVVDDSIVRGTTSSKIVRMLREAGAKEVHMRIASPPIIASCYYGVDTPSREELISN 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 739694894 409 SKSPKEICDYIGADSLSYLSVDGLIESIGLNydAPysGLCVESFTGDYPAGLF----DYEDKYYKNLS 472
Cdd:PLN02440 400 RMSVEEIRKFIGCDSLAFLPLEDLKKSLGEE--SP--RFCYACFSGDYPVLPKrvggDIDDGYLESLE 463
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
11-261 |
1.70e-134 |
|
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: 388.74 E-value: 1.70e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 11 CGVFGIWNHSEATQLTYMGLHSLQHRGQEGAGIVVSDGEVLKGERGLGLLTEAIKGDQMDQLKdGHNAIGHVRYATSGNK 90
Cdd:cd00715 1 CGVFGIYGAEDAARLTYLGLYALQHRGQESAGIATSDGKRFHTHKGMGLVSDVFDEEKLRRLP-GNIAIGHVRYSTAGSS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 91 GIENIQPFLYHFYDMSVAICHNGNLINAQTLRQYLEKHGAIFHSSSDTEVIMHLIRRSKA-PTFEEALKESLRQIKGGFT 169
Cdd:cd00715 80 SLENAQPFVVNSPLGGIALAHNGNLVNAKELREELEEEGRIFQTTSDSEVILHLIARSLAkDDLFEAIIDALERVKGAYS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 170 FAILTKDALYGAVDPNAIRPLVVGKMQDDTYILASETCAIDVLGAEYVQDIHAGEYVVINNEGIEVKSYTSHTNTAISAM 249
Cdd:cd00715 160 LVIMTADGLIAVRDPHGIRPLVLGKLEGDGYVVASESCALDIIGAEFVRDVEPGEIVVIDDDGLESSQRAPKPKPAPCIF 239
|
250
....*....|..
gi 739694894 250 EYIYFARPDSTI 261
Cdd:cd00715 240 EYVYFARPDSVI 251
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
11-226 |
6.97e-63 |
|
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: 204.22 E-value: 6.97e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 11 CGVFGIWNHSEATQLTY----MGLHSLQHRGQEGAGIVVSDGEVLKGERGLGLLTEAIKGDQMDQLKdGHNAIGHVRYAT 86
Cdd:cd00352 1 CGIFGIVGADGAASLLLllllRGLAALEHRGPDGAGIAVYDGDGLFVEKRAGPVSDVALDLLDEPLK-SGVALGHVRLAT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 87 SGNKGIENIQPFLYHFYDmsVAICHNGNLINAQTLRQYLEKHGAIFHSSSDTEVIMHLIRRS-KAPTFEEALKESLRQIK 165
Cdd:cd00352 80 NGLPSEANAQPFRSEDGR--IALVHNGEIYNYRELREELEARGYRFEGESDSEVILHLLERLgREGGLFEAVEDALKRLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739694894 166 GGFTFAILTK--DALYGAVDPNAIRPLVVGKMQDDTYILASETCAIDVLGAEYVQDIHAGEYV 226
Cdd:cd00352 158 GPFAFALWDGkpDRLFAARDRFGIRPLYYGITKDGGLVFASEPKALLALPFKGVRRLPPGELL 220
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
11-228 |
2.64e-34 |
|
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: 128.33 E-value: 2.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 11 CGVFGIWNHSEATQLTYMGLHSLQHRGQEGAGI-VVSDGE--VLKGERGLGLLTEAIKGDQMDqlkdGHNAIGHVRYATS 87
Cdd:cd00714 1 CGIVGYIGKREAVDILLEGLKRLEYRGYDSAGIaVIGDGSleVVKAVGKVANLEEKLAEKPLS----GHVGIGHTRWATH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 88 GNKGIENIQPflyHF-YDMSVAICHNGNLINAQTLRQYLEKHGAIFHSSSDTEVIMHLIRRS--KAPTFEEALKESLRQI 164
Cdd:cd00714 77 GEPTDVNAHP---HRsCDGEIAVVHNGIIENYAELKEELEAKGYKFESETDTEVIAHLIEYYydGGLDLLEAVKKALKRL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739694894 165 KGGFTFAILTKDalygavDPN---AIR---PLVVGKmQDDTYILASETCAIdvlgAEYVQDI---HAGEYVVI 228
Cdd:cd00714 154 EGAYALAVISKD------EPDeivAARngsPLVIGI-GDGENFVASDAPAL----LEHTRRViylEDGDIAVI 215
|
|
| glmS |
TIGR01135 |
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ... |
11-236 |
4.55e-27 |
|
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: 114.66 E-value: 4.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 11 CGVFGIWNHSEATQLTYMGLHSLQHRGQEGAGIVVSDGEVLKGERGLGLLTEAIKG-DQMDQlkDGHNAIGHVRYATSGN 89
Cdd:TIGR01135 1 CGIVGYIGQRDAVPILLEGLKRLEYRGYDSAGIAVVDEGKLFVRKAVGKVAELANKlGEKPL--PGGVGIGHTRWATHGK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 90 KGIENIQPflyHF-YDMSVAICHNGNLINAQTLRQYLEKHGAIFHSSSDTEVIMHLIRRSKAPT--FEEALKESLRQIKG 166
Cdd:TIGR01135 79 PTDENAHP---HTdEGGRIAVVHNGIIENYAELREELEARGHVFSSDTDTEVIAHLIEEELREGgdLLEAVQKALKQLRG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739694894 167 GFTFAILTKDalygavDPNAI------RPLVVGKMQDDTYIlASETCAIdvlgAEYVQDI---HAGEYVVINNEGIEVK 236
Cdd:TIGR01135 156 AYALAVLHAD------HPETLvaarsgSPLIVGLGDGENFV-ASDVTAL----LPYTRRViylEDGDIAILTKDGVEIY 223
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
11-236 |
6.85e-27 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 113.99 E-value: 6.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 11 CGVFGIWNHSEATQLTYMGLHSLQHRGQEGAGIVVSDGEVLKGERGLG---LLTEAIKGDQMDqlkdGHNAIGHVRYATS 87
Cdd:PRK00331 2 CGIVGYVGQRNAAEILLEGLKRLEYRGYDSAGIAVLDDGGLEVRKAVGkvaNLEAKLEEEPLP----GTTGIGHTRWATH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 88 GNKGIENIQPflyHFyDMS--VAICHNGNLINAQTLRQYLEKHGAIFHSSSDTEVIMHLI--RRSKAPTFEEALKESLRQ 163
Cdd:PRK00331 78 GKPTERNAHP---HT-DCSgrIAVVHNGIIENYAELKEELLAKGHVFKSETDTEVIAHLIeeELKEGGDLLEAVRKALKR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 164 IKGGFTFAILTKDalygavDPNAI---R---PLVVGKmQDDTYILASETCAIdvlgAEYVQDI---HAGEYVVINNEGIE 234
Cdd:PRK00331 154 LEGAYALAVIDKD------EPDTIvaaRngsPLVIGL-GEGENFLASDALAL----LPYTRRViylEDGEIAVLTRDGVE 222
|
..
gi 739694894 235 VK 236
Cdd:PRK00331 223 IF 224
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
11-228 |
7.93e-27 |
|
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: 108.51 E-value: 7.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 11 CGVFGIWNHSEATQLTYM---GLHSLQHRG-QEGAG---------IVVSDG---EVLKGergLGLLTEAIKGDQMDQLKd 74
Cdd:cd01907 1 CGIFGIMSKDGEPFVGALlveMLDAMQERGpGDGAGfalygdpdaFVYSSGkdmEVFKG---VGYPEDIARRYDLEEYK- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 75 GHNAIGHVRYATsgNKGIeniqpFLYH---FYDMSVAICHNGNLINAQTLRQYLEKHGAIFHSSSDTEVIMH----LIRR 147
Cdd:cd01907 77 GYHWIAHTRQPT--NSAV-----WWYGahpFSIGDIAVVHNGEISNYGSNREYLERFGYKFETETDTEVIAYyldlLLRK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 148 SKAPTF-----------------EEALKESLRQIKGGFTFAILTKDALYGAVDPNAIRPLVVGKmQDDTYILASETCAID 210
Cdd:cd01907 150 GGLPLEyykhiirmpeeerelllALRLTYRLADLDGPFTIIVGTPDGFIVIRDRIKLRPAVVAE-TDDYVAIASEECAIR 228
|
250 260
....*....|....*....|.
gi 739694894 211 VLG---AEYVQDIHAGEYVVI 228
Cdd:cd01907 229 EIPdrdNAKVWEPRPGEYVIW 249
|
|
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
11-235 |
8.69e-26 |
|
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: 110.87 E-value: 8.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 11 CGVFGIWNHSEATQLTYMGLHSLQHRGQEGAGIVVSDGEVLKGERGLG-L--LTEAIKGDQMDqlkdGHNAIGHVRYATS 87
Cdd:COG0449 2 CGIVGYIGKRDAAPILLEGLKRLEYRGYDSAGIAVLDDGGLEVRKAVGkLanLEEKLAEEPLS----GTIGIGHTRWATH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 88 GNKGIENIQPflyHF-YDMSVAICHNGnlI--NAQTLRQYLEKHGAIFHSSSDTEVIMHLIRR--SKAPTFEEALKESLR 162
Cdd:COG0449 78 GAPSDENAHP---HTsCSGRIAVVHNG--IieNYAELREELEAKGHTFKSETDTEVIAHLIEEylKGGGDLLEAVRKALK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 163 QIKGGFTFAILTKDalygavDPN---AIR---PLVVGkMQDDTYILASetcaiDVLG-AEYVQDI---HAGEYVVINNEG 232
Cdd:COG0449 153 RLEGAYALAVISAD------EPDrivAARkgsPLVIG-LGEGENFLAS-----DVPAlLPYTRRViylEDGEIAVLTRDG 220
|
...
gi 739694894 233 IEV 235
Cdd:COG0449 221 VEI 223
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
11-234 |
6.10e-24 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 105.49 E-value: 6.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 11 CGVFGIWNHSEATQLTYMGLHSLQHRGQEGAGI-VVSDGEVLKGERglgLLTEAIKGDQMDQLKD-------GHN-AIGH 81
Cdd:PTZ00295 25 CGIVGYLGNEDASKILLEGIEILQNRGYDSCGIsTISSGGELKTTK---YASDGTTSDSIEILKEklldshkNSTiGIAH 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 82 VRYATSGNKGIENIQPflyHF-YDMSVAICHNGNLINAQTLRQYLEKHGAIFHSSSDTEVIMHLI--RRSKAPTFEEALK 158
Cdd:PTZ00295 102 TRWATHGGKTDENAHP---HCdYKKRIALVHNGTIENYVELKSELIAKGIKFRSETDSEVIANLIglELDQGEDFQEAVK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 159 ESLRQIKGGFTFAILTKDalygavDPNAI------RPLVVGKMQDDTYIlASETCAIDVLGAEYV--QDihaGEYVVINN 230
Cdd:PTZ00295 179 SAISRLQGTWGLCIIHKD------NPDSLivarngSPLLVGIGDDSIYV-ASEPSAFAKYTNEYIslKD---GEIAELSL 248
|
....
gi 739694894 231 EGIE 234
Cdd:PTZ00295 249 ENVN 252
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
11-238 |
1.28e-20 |
|
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: 90.31 E-value: 1.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 11 CGVFGIWN----HSEATQLTYMgLHSLQHRGQEGAGIVVsdgevlkgerglgllteaikgdqmdqlkDGHNAIGHVRYA- 85
Cdd:cd00712 1 CGIAGIIGldgaSVDRATLERM-LDALAHRGPDGSGIWI----------------------------DEGVALGHRRLSi 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 86 ---TSGNkgieniQPFLYHfyDMSVAICHNGNLINAQTLRQYLEKHGAIFHSSSDTEVIMHLIRRSKaptfEEALKEsLR 162
Cdd:cd00712 52 idlSGGA------QPMVSE--DGRLVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHLYEEWG----EDCLER-LN 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 163 qikGGFTFAILTKDA--LYGAVDPNAIRPLVVGKmQDDTYILASETCAI----------------DVLGAEYV------- 217
Cdd:cd00712 119 ---GMFAFALWDKRKrrLFLARDRFGIKPLYYGR-DGGGLAFASELKALlalpgvpreldeaalaEYLAFQYVpaprtif 194
|
250 260
....*....|....*....|....
gi 739694894 218 QDIH---AGEYVVINNEGIEVKSY 238
Cdd:cd00712 195 KGIRklpPGHYLTVDPGGVEIRRY 218
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
96-209 |
1.42e-19 |
|
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain found in a variety of enzymes such as asparagine synthetase and glutamine-fructose-6-phosphate transaminase.
Pssm-ID: 433289 [Multi-domain] Cd Length: 123 Bit Score: 84.49 E-value: 1.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 96 QPFLYHfYDMSVAICHNGNLINAQTLRQYLEKHGAIFHSSSDTEVIMHLIRrskaptfEEALKESLRQIKGGFTFAILTK 175
Cdd:pfam13537 14 QPMVSS-EDGRYVIVFNGEIYNYRELRAELEAKGYRFRTHSDTEVILHLYE-------AEWGEDCVDRLNGMFAFAIWDR 85
|
90 100 110
....*....|....*....|....*....|....*.
gi 739694894 176 DA--LYGAVDPNAIRPLVVGKMQDDTYILASETCAI 209
Cdd:pfam13537 86 RRqrLFLARDRFGIKPLYYGRDDGGRLLFASELKAL 121
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
74-205 |
4.26e-19 |
|
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain found in a variety of enzymes, such as asparagine synthetase and glutamine--fructose-6-phosphate transaminase.
Pssm-ID: 433279 [Multi-domain] Cd Length: 130 Bit Score: 83.12 E-value: 4.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 74 DGHNAIGHVRYATSGNKGIENiQPFLyhFYDMSVAICHNGNLINAQTLRQYLEKHGAIFHSSSDTEVIMHLirrskaptF 153
Cdd:pfam13522 9 EGGVALGHVRLAIVDLPDAGN-QPML--SRDGRLVLVHNGEIYNYGELREELADLGHAFRSRSDTEVLLAL--------Y 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 739694894 154 EEALKESLRQIKGGFTFAI--LTKDALYGAVDPNAIRPLVVGKMqDDTYILASE 205
Cdd:pfam13522 78 EEWGEDCLERLRGMFAFAIwdRRRRTLFLARDRLGIKPLYYGIL-GGGFVFASE 130
|
|
| PRTases_typeI |
cd06223 |
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ... |
274-385 |
2.41e-18 |
|
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The type I PRTases are identified by a conserved PRPP binding motif which features two adjacent acidic residues surrounded by one or more hydrophobic residue. PRTases catalyze the displacement of the alpha-1'-pyrophosphate of 5-phosphoribosyl-alpha1-pyrophosphate (PRPP) by a nitrogen-containing nucleophile. The reaction products are an alpha-1 substituted ribose-5'-phosphate and a free pyrophosphate (PP). PRPP, an activated form of ribose-5-phosphate, is a key metabolite connecting nucleotide synthesis and salvage pathways. The type I PRTase family includes a range of diverse phosphoribosyl transferase enzymes and regulatory proteins of the nucleotide synthesis and salvage pathways, including adenine phosphoribosyltransferase EC:2.4.2.7., hypoxanthine-guanine-xanthine phosphoribosyltransferase, hypoxanthine phosphoribosyltransferase EC:2.4.2.8., ribose-phosphate pyrophosphokinase EC:2.7.6.1., amidophosphoribosyltransferase EC:2.4.2.14., orotate phosphoribosyltransferase EC:2.4.2.10., uracil phosphoribosyltransferase EC:2.4.2.9., and xanthine-guanine phosphoribosyltransferase EC:2.4.2.22.
Pssm-ID: 206754 [Multi-domain] Cd Length: 130 Bit Score: 81.29 E-value: 2.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 274 GKKLAQE---SPANADMVIGVPNSSLSAASGYAEESHLPYEMGLVKNQYVARTFIQPTQelreqgvrvKLSAVKDIVEGK 350
Cdd:cd06223 2 GRLLAEEireDLLEPDVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSEPYG---------LELPLGGDVKGK 72
|
90 100 110
....*....|....*....|....*....|....*
gi 739694894 351 RIVLVDDSIVRGTTSKRIVRMLKDSGAKEVHVRIA 385
Cdd:cd06223 73 RVLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVL 107
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
11-238 |
3.10e-18 |
|
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: 87.58 E-value: 3.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 11 CGVFGIWNHS---EATQLTYMgLHSLQHRGQEGAGIVVsdgevlkgerglgllteaikgdqmdqlkDGHNAIGHVRYA-- 85
Cdd:COG0367 2 CGIAGIIDFDggaDREVLERM-LDALAHRGPDGSGIWV----------------------------DGGVALGHRRLSii 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 86 ---TSGNkgieniQPFLYHfyDMSVAICHNGNLINAQTLRQYLEKHGAIFHSSSDTEVIMHLIRRSKAptfeealkESLR 162
Cdd:COG0367 53 dlsEGGH------QPMVSE--DGRYVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHAYEEWGE--------DCLE 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 163 QIKGGFTFAI--LTKDALYGAVDPNAIRPLVVGkMQDDTYILASETCAI----------------DVLGAEYV------- 217
Cdd:COG0367 117 RLNGMFAFAIwdRRERRLFLARDRFGIKPLYYA-EDGGGLAFASELKALlahpgvdreldpealaEYLTLGYVpaprtif 195
|
250 260
....*....|....*....|....*
gi 739694894 218 QDIH---AGEYVVINNEG-IEVKSY 238
Cdd:COG0367 196 KGIRklpPGHYLTVDAGGeLEIRRY 220
|
|
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
11-179 |
8.88e-16 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 80.18 E-value: 8.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 11 CGVFGIWNHSEATQLTYM------GLHSLQHRGQEGAGIVVSDGEVLKG-------ERG-----LGLLTEAIKGDQM--D 70
Cdd:PLN02981 2 CGIFAYLNYNVPRERRFIlevlfnGLRRLEYRGYDSAGIAIDNDPSLESssplvfrEEGkieslVRSVYEEVAETDLnlD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 71 QLKDGHNAIGHVRYATSGNKGIENIQP--------FLyhfydmsvaICHNGNLINAQTLRQYLEKHGAIFHSSSDTEVIM 142
Cdd:PLN02981 82 LVFENHAGIAHTRWATHGPPAPRNSHPqssgpgneFL---------VVHNGIITNYEVLKETLLRHGFTFESDTDTEVIP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 739694894 143 HLIR--------RSKAPTFEEALKESLRQIKGGftFAILTKDALY 179
Cdd:PLN02981 153 KLAKfvfdklneEEGDVTFSQVVMEVMRQLEGA--YALIFKSPHY 195
|
|
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
11-205 |
1.78e-15 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 78.80 E-value: 1.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 11 CGVFGIWN-HSEATQLTYMGLHSLQ---HRGQEGAGIVVSDGEVLKGERglglLteAIkgdqMDqLKDGHnaighvryat 86
Cdd:PRK09431 2 CGIFGILDiKTDADELRKKALEMSRlmrHRGPDWSGIYASDNAILGHER----L--SI----VD-VNGGA---------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 87 sgnkgieniQPFLYHfyDMSVAICHNGNLINAQTLRQYLEKHGAiFHSSSDTEVIMHLirrskaptFEEALKESLRQIKG 166
Cdd:PRK09431 61 ---------QPLYNE--DGTHVLAVNGEIYNHQELRAELGDKYA-FQTGSDCEVILAL--------YQEKGPDFLDDLDG 120
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 739694894 167 GFTFAIL--TKDALYGAVDPNAIRPLVVGKMQDDTYILASE 205
Cdd:PRK09431 121 MFAFALYdsEKDAYLIARDPIGIIPLYYGYDEHGNLYFASE 161
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
73-227 |
4.72e-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: 77.37 E-value: 4.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 73 KDGHNAIGHVRYATSGNKGieNIQPFLYHFYdmSVAICHNGNLINAQTLRQYLEKHGAIFHSSSDTEVIMHLirrskapt 152
Cdd:TIGR01536 38 KDGNAILGHRRLAIIDLSG--GAQPMSNEGK--TYVIVFNGEIYNHEELREELEAKGYTFQTDSDTEVILHL-------- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 153 FEEALKESLRQIKGGFTFAIL--TKDALYGAVDPNAIRPLVVGkMQDDTYILASE------TCAIDV-LGAEYVQDIHAG 223
Cdd:TIGR01536 106 YEEWGEECVDRLDGMFAFALWdsEKGELFLARDRFGIKPLYYA-YDGGQLYFASEikallaHPNIKPfPDGAALAPGFGF 184
|
....
gi 739694894 224 EYVV 227
Cdd:TIGR01536 185 VRVP 188
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
11-238 |
3.79e-13 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 71.67 E-value: 3.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 11 CGVFGIWNHS----EATQLTYMGLHSLQHRGQEGAGIVVSDGEvlkgerglgllteaikgdqmdqlKDGHNAIGHVRYA- 85
Cdd:PTZ00077 2 CGILAIFNSKgerhELRRKALELSKRLRHRGPDWSGIIVLENS-----------------------PGTYNILAHERLAi 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 86 ---TSGNkgieniQPFLYHfyDMSVAICHNGNLINAQTLRQYLEKHGAIFHSSSDTEVIMHLIRRSKAPTFeealkesLR 162
Cdd:PTZ00077 59 vdlSDGK------QPLLDD--DETVALMQNGEIYNHWEIRPELEKEGYKFSSNSDCEIIGHLYKEYGPKDF-------WN 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 739694894 163 QIKGGFTFAIL--TKDALYGAVDPNAIRPLVVGKMQDDTYILASETCAIDVLGAEYVQdIHAGEYVVINNEGIEVKSY 238
Cdd:PTZ00077 124 HLDGMFATVIYdmKTNTFFAARDHIGIIPLYIGYAKDGSIWFSSELKALHDQCVEVKQ-FPPGHYYDQTKEKGEFVRY 200
|
|
| YafJ |
COG0121 |
Predicted glutamine amidotransferase YafJ [General function prediction only]; |
76-206 |
8.63e-11 |
|
Predicted glutamine amidotransferase YafJ [General function prediction only];
Pssm-ID: 439891 [Multi-domain] Cd Length: 248 Bit Score: 62.29 E-value: 8.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 76 HNAIGHVRYATSGNKGIENIQPFLY-HFYdmsvaICHNGNLINAQTLRQYLEKHGAIFH-----SSSDTEVIMHLIR--- 146
Cdd:COG0121 77 RLVIAHVRKATVGPVSLENTHPFRGgRWL-----FAHNGQLDGFDRLRRRLAEELPDELyfqpvGTTDSELAFALLLsrl 151
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739694894 147 RSKAPTFEEALKESLRQIK------GGFTFAILTKDALYGAVDPNAIRP-----LVVGKMQDDTYILASET 206
Cdd:COG0121 152 RDGGPDPAEALAEALRELAelarapGRLNLLLSDGERLYATRYTSDDPYptlyyLTRTTPDDRVVVVASEP 222
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
11-211 |
1.39e-10 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 63.74 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 11 CGVFGIWNHS------EATQLTYMGLHSLQHRGQEGAGIVVSDGEVLKGERG------------------LGLLTEAIKG 66
Cdd:PTZ00394 2 CGIFGYANHNvprtveQILNVLLDGIQKVEYRGYDSAGLAIDANIGSEKEDGtaasaptprpcvvrsvgnISQLREKVFS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 67 DQ-------MDQLKDGHNAIGHVRYATSGNKGIENIQPFLYHfyDMSVAICHNGNLINAQTLRQYLEKHGAIFHSSSDTE 139
Cdd:PTZ00394 82 EAvaatlppMDATTSHHVGIAHTRWATHGGVCERNCHPQQSN--NGEFTIVHNGIVTNYMTLKELLKEEGYHFSSDTDTE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 140 VIM----HLIRRSKAPTFEEALKESLRQIKGgfTFAILTKDALYgavdPNAI------RPLVVGKMQDDTYILASETCAI 209
Cdd:PTZ00394 160 VISvlseYLYTRKGIHNFADLALEVSRMVEG--SYALLVKSVYF----PGQLaasrkgSPLMVGIRRTDDRGCVMKLQTY 233
|
..
gi 739694894 210 DV 211
Cdd:PTZ00394 234 DL 235
|
|
| YafJ |
cd01908 |
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ... |
76-206 |
8.20e-10 |
|
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: 59.32 E-value: 8.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 76 HNAIGHVRYATSGNKGIENIQPFLYHfydmSVAICHNGNLINAQTLRQYLEKHGAIF-HSSSDTEVIMHLI---RRSKAP 151
Cdd:cd01908 81 PLVLAHVRAATVGPVSLENCHPFTRG----RWLFAHNGQLDGFRLLRRRLLRLLPRLpVGTTDSELAFALLlsrLLERDP 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 152 TFEEALKESLRQI---------KGGFTFAILTKDALYG---------------AVDPNAIRPLVVGKM-QDDTYILASET 206
Cdd:cd01908 157 LDPAELLDAILQTlrelaalapPGRLNLLLSDGEYLIAtryasapslyyltrrAPFGCARLLFRSVTTpNDDGVVVASEP 236
|
|
| PLN02549 |
PLN02549 |
asparagine synthase (glutamine-hydrolyzing) |
11-209 |
5.31e-09 |
|
asparagine synthase (glutamine-hydrolyzing)
Pssm-ID: 178164 [Multi-domain] Cd Length: 578 Bit Score: 58.62 E-value: 5.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 11 CGVFGIWNHSEATQ----LTYMGLHSLQHRGQEGAGIVVSDGEVLKGERglglltEAIkgdqMDqlkdghnaighvryAT 86
Cdd:PLN02549 2 CGILAVLGCSDDSQakrsRVLELSRRLRHRGPDWSGLYGNEDCYLAHER------LAI----MD--------------PE 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 87 SGNkgieniQPFLYHfyDMSVAICHNGNLINAQTLRQYLEKHgaIFHSSSDTEVIMHLirrskaptFEEALKESLRQIKG 166
Cdd:PLN02549 58 SGD------QPLYNE--DKTIVVTANGEIYNHKELREKLKLH--KFRTGSDCEVIAHL--------YEEHGEEFVDMLDG 119
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 739694894 167 GFTFAILTK--DALYGAVDPNAIRPLVVGKMQDDTYILASETCAI 209
Cdd:PLN02549 120 MFSFVLLDTrdNSFIAARDHIGITPLYIGWGLDGSVWFASEMKAL 164
|
|
| Pribosyltran |
pfam00156 |
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ... |
268-381 |
4.76e-05 |
|
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl transferase enzymes. This family includes: Adenine phosphoribosyl-transferase EC:2.4.2.7. Hypoxanthine-guanine-xanthine phosphoribosyl-transferase. Hypoxanthine phosphoribosyl-transferase EC:2.4.2.8. Ribose-phosphate pyrophosphokinase i EC:2.7.6.1. Amidophosphoribosyltransferase EC:2.4.2.14. Orotate phosphoribosyl-transferase EC:2.4.2.10. Uracil phosphoribosyl-transferase EC:2.4.2.9. Xanthine-guanine phosphoribosyl-transferase EC:2.4.2.22. In Arabidopsis, At the very N-terminus of this domain is the P-Loop NTPase domain.
Pssm-ID: 425489 [Multi-domain] Cd Length: 150 Bit Score: 43.51 E-value: 4.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 268 AVRKASGKKLaQESPANADMVIGVPNSSLSAASGYAeeSHLpyemglvknqYVARTFIQPTQELREQGVRVKLSAVKDIV 347
Cdd:pfam00156 14 AVARLAAQIN-EDYGGKPDVVVGILRGGLPFAGILA--RRL----------DVPLAFVRKVSYNPDTSEVMKTSSALPDL 80
|
90 100 110
....*....|....*....|....*....|....
gi 739694894 348 EGKRIVLVDDSIVRGTTSKRIVRMLKDSGAKEVH 381
Cdd:pfam00156 81 KGKTVLIVDDILDTGGTLLKVLELLKNVGPKEVK 114
|
|
| PRK00934 |
PRK00934 |
ribose-phosphate pyrophosphokinase; Provisional |
342-382 |
4.85e-05 |
|
ribose-phosphate pyrophosphokinase; Provisional
Pssm-ID: 234868 [Multi-domain] Cd Length: 285 Bit Score: 45.29 E-value: 4.85e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 739694894 342 AVKDI-VEGKRIVLVDDSIVRGTTSKRIVRMLKDSGAKEVHV 382
Cdd:PRK00934 196 APKNLdVKGKDVLIVDDIISTGGTMATAIKILKEQGAKKVYV 237
|
|
| PRK02277 |
PRK02277 |
orotate phosphoribosyltransferase-like protein; Provisional |
347-380 |
1.81e-04 |
|
orotate phosphoribosyltransferase-like protein; Provisional
Pssm-ID: 235023 [Multi-domain] Cd Length: 200 Bit Score: 42.55 E-value: 1.81e-04
10 20 30
....*....|....*....|....*....|....
gi 739694894 347 VEGKRIVLVDDSIVRGTTSKRIVRMLKDSGAKEV 380
Cdd:PRK02277 138 VEGKRCVIVDDVITSGTTMKETIEYLKEHGGKPV 171
|
|
| Hpt1 |
COG2236 |
Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine ... |
347-401 |
8.85e-04 |
|
Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine phosphoribosyltransferase is part of the Pathway/BioSystem: Purine salvage
Pssm-ID: 441837 [Multi-domain] Cd Length: 153 Bit Score: 39.83 E-value: 8.85e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 739694894 347 VEGKRIVLVDDSIVRGTTSKRIVRMLKDSGAKEVHV----RIASPEFMfPSFYGIDVST 401
Cdd:COG2236 86 LAGKRVLIVDDVADTGRTLEAVRDLLKEAGPAEVRTavlyYKPSSKFK-PDYYAEETDA 143
|
|
| PyrE |
COG0461 |
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ... |
267-382 |
1.91e-03 |
|
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate phosphoribosyltransferase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 440229 Cd Length: 201 Bit Score: 39.37 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739694894 267 HAVRKASGKKLAQ---ESPANADMVIGVPNSSLSAASGYAEESHLPYemglvknQYVARtfiqptqELREQGVRVKLsaV 343
Cdd:COG0461 43 PEALELLGEALAElikELGPEFDAVAGPATGGIPLAAAVARALGLPA-------IFVRK-------EAKDHGTGGQI--E 106
|
90 100 110
....*....|....*....|....*....|....*....
gi 739694894 344 KDIVEGKRIVLVDDSIVRGTTSKRIVRMLKDSGAKEVHV 382
Cdd:COG0461 107 GGLLPGERVLVVEDVITTGGSVLEAVEALREAGAEVVGV 145
|
|
| PrsA |
COG0462 |
Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; ... |
347-382 |
3.41e-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: 39.66 E-value: 3.41e-03
10 20 30
....*....|....*....|....*....|....*.
gi 739694894 347 VEGKRIVLVDDSIVRGTTSKRIVRMLKDSGAKEVHV 382
Cdd:COG0462 209 VEGKTCIIVDDMIDTGGTLVEAAEALKEAGAKSVYA 244
|
|
| |
