|
Name |
Accession |
Description |
Interval |
E-value |
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
1-368 |
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: 625.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 1 MHDACGVVGISFNEtgnNVAKSIYYALYALQHRGQEAAGISVHDGKAIRTHRGMGLVSEVFDDAQIALLRGQVGIGHVRY 80
Cdd:COG0034 4 LHEECGVFGIYGHE---DVAQLTYYGLYALQHRGQESAGIATSDGGRFHLHKGMGLVSDVFDEEDLERLKGNIAIGHVRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 81 PTSGRSCIENSQPLLVKYKDGAIAIAHNGNLVNSCQLREQLEQAGDIFYSTSDTEVIAHLFVKELLRYDLQEAVRALMRK 160
Cdd:COG0034 81 STTGSSSLENAQPFYVNSPFGSIALAHNGNLTNAEELREELEEEGAIFQTTSDTEVILHLIARELTKEDLEEAIKEALRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 161 LVGSYSLVFLWGDTVLAVRDPLGIKPLCIGEIDSGFMVASESVAIDTLNGQLIRDVKPGELVVIRHGQMTSHQLVRLPHP 240
Cdd:COG0034 161 VKGAYSLVILTGDGLIAARDPNGIRPLVLGKLEDGYVVASESCALDILGAEFVRDVEPGEIVVIDEDGLRSRQFAEKPRP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 241 AHCIFEYIYFARPDSIMEGRLIYDVRVNIGSNLAAEHPACADTVTPIPDSGITLAVGYHQRSGISYKECLMKNRYIGRTF 320
Cdd:COG0034 241 APCIFEYVYFARPDSVIDGRSVYEARKRMGRELAREAPVDADVVIPVPDSGRPAAIGYAEESGIPYEEGLIKNRYVGRTF 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1519874227 321 IMPDQNMRETAVRLKMNTIRPNIEGHKLVMVDDSIVRGTTSRRIVNMV 368
Cdd:COG0034 321 IQPTQELRELGVRLKLNPIREVVKGKRVVLVDDSIVRGTTSRRIVKML 368
|
|
| purF |
TIGR01134 |
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ... |
5-368 |
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: 510.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 5 CGVVGISFNEtgNNVAKSIYYALYALQHRGQEAAGISVHDGKAIRTHRGMGLVSEVFDDAQIALLRGQVGIGHVRYPTSG 84
Cdd:TIGR01134 1 CGVVGIYGQE--EVAASLTYYGLYALQHRGQESAGISVFDGNRFRLHKGNGLVSDVFNEEHLQRLKGNVGIGHVRYSTAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 85 RSCIENSQPLLVKYKDGAIAIAHNGNLVNSCQLREQLEQAGDIFYSTSDTEVIAHLF-VKELLRYDLQEAVRALMRKLVG 163
Cdd:TIGR01134 79 SSGLENAQPFVVNSPYGGLALAHNGNLVNADELRRELEEEGRHFNTTSDSEVLLHLLaHNDESKDDLFDAVARVLERVRG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 164 SYSLVFLWGDTVLAVRDPLGIKPLCIGEIDSGFMVASESVAIDTLNGQLIRDVKPGELVVIRHGQMtSHQLVRLPHPAHC 243
Cdd:TIGR01134 159 AYALVLMTEDGLVAVRDPHGIRPLVLGRRGDGYVVASESCALDILGAEFVRDVEPGEVVVIFDGGL-ESRQCARRPRAPC 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 244 IFEYIYFARPDSIMEGRLIYDVRVNIGSNLAAEHPACADTVTPIPDSGITLAVGYHQRSGISYKECLMKNRYIGRTFIMP 323
Cdd:TIGR01134 238 VFEYVYFARPDSVIDGISVYYARKRMGKELARESPVEADVVVPVPDSGRSAALGFAQASGIPYREGLIKNRYVGRTFIMP 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1519874227 324 DQNMRETAVRLKMNTIRPNIEGHKLVMVDDSIVRGTTSRRIVNMV 368
Cdd:TIGR01134 318 TQELRELSVRLKLNPVRAVFEGKRVVLVDDSIVRGTTSRQIVEML 362
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
1-367 |
1.30e-169 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 481.46 E-value: 1.30e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 1 MHDACGVVGIsFNETGNNVAKSIYYALYALQHRGQEAAGISVHDGKAIRTHRGMGLVSEVFDDAQIALLRGQVGIGHVRY 80
Cdd:PRK05793 11 FKEECGVFGV-FSKNNIDVASLTYYGLYALQHRGQESAGIAVSDGEKIKVHKGMGLVSEVFSKEKLKGLKGNSAIGHVRY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 81 PTSGRSCIENSQPLLVKYKDGAIAIAHNGNLVNSCQLREQLEQAGDIFYSTSDTEVIAHLFVKELlRYDLQEAVRALMRK 160
Cdd:PRK05793 90 STTGASDLDNAQPLVANYKLGSIAIAHNGNLVNADVIRELLEDGGRIFQTSIDSEVILNLIARSA-KKGLEKALVDAIQA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 161 LVGSYSLVFLWGDTVLAVRDPLGIKPLCIGEIDSGFMVASESVAIDTLNGQLIRDVKPGELVVIRHGQMTSHQLVRLPHP 240
Cdd:PRK05793 169 IKGSYALVILTEDKLIGVRDPHGIRPLCLGKLGDDYILSSESCALDTIGAEFIRDVEPGEIVIIDEDGIKSIKFAEKTKC 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 241 AHCIFEYIYFARPDSIMEGRLIYDVRVNIGSNLAAEHPACADTVTPIPDSGITLAVGYHQRSGISYKECLMKNRYIGRTF 320
Cdd:PRK05793 249 QTCAFEYIYFARPDSVIDGISVYESRVRAGRQLYKEYPVDADIVIGVPDSGIPAAIGYAEASGIPYGIGFIKNKYVGRTF 328
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1519874227 321 IMPDQNMRETAVRLKMNTIRPNIEGHKLVMVDDSIVRGTTSRRIVNM 367
Cdd:PRK05793 329 IAPSQELRERAVRVKLNPLKVNVEGKRVVLIDDSIVRGTTSKRLVEL 375
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
5-368 |
4.87e-146 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 421.78 E-value: 4.87e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 5 CGVVGISFNEtgnNVAKSIYYALYALQHRGQEAAGISVHDGKAIRTHRGMGLVSEVFDDAQIALLRGQVGIGHVRYPTSG 84
Cdd:PLN02440 2 CGVVGIFGDP---EASRLCYLGLHALQHRGQEGAGIVTVDGNRLQSITGNGLVSDVFDESKLDQLPGDIAIGHVRYSTAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 85 RSCIENSQPLLVKYKDGAIAIAHNGNLVNSCQLREQLEQAGDIFYSTSDTEVIAHLFVKELLRYDLQEAVRAlMRKLVGS 164
Cdd:PLN02440 79 ASSLKNVQPFVANYRFGSIGVAHNGNLVNYEELRAKLEENGSIFNTSSDTEVLLHLIAISKARPFFSRIVDA-CEKLKGA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 165 YSLVFLWGDTVLAVRDPLGIKPLCIGEIDSG-FMVASESVAIDTLNGQLIRDVKPGELVVIRHGQMTSHQLVrLPHPAH- 242
Cdd:PLN02440 158 YSMVFLTEDKLVAVRDPHGFRPLVMGRRSNGaVVFASETCALDLIGATYEREVNPGEVIVVDKDKGVSSQCL-MPHPEPk 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 243 -CIFEYIYFARPDSIMEGRLIYDVRVNIGSNLAAEHPACADTVTPIPDSGITLAVGYHQRSGISYKECLMKNRYIGRTFI 321
Cdd:PLN02440 237 pCIFEHIYFARPNSIVFGRSVYESRLEFGEILATEIPVDCDVVIPVPDSGRVAALGYAAKLGVPFQQGLIRSHYVGRTFI 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1519874227 322 MPDQNMRETAVRLKMNTIRPNIEGHKLVMVDDSIVRGTTSRRIVNMV 368
Cdd:PLN02440 317 EPSQKIRDFSVKLKLNPVRSVLEGKRVVVVDDSIVRGTTSSKIVRML 363
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
5-258 |
2.03e-137 |
|
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: 391.05 E-value: 2.03e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 5 CGVVGISFNEtgnNVAKSIYYALYALQHRGQEAAGISVHDGKAIRTHRGMGLVSEVFDDAQIALLRGQVGIGHVRYPTSG 84
Cdd:cd00715 1 CGVFGIYGAE---DAARLTYLGLYALQHRGQESAGIATSDGKRFHTHKGMGLVSDVFDEEKLRRLPGNIAIGHVRYSTAG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 85 RSCIENSQPLLVKYKDGAIAIAHNGNLVNSCQLREQLEQAGDIFYSTSDTEVIAHLFVKELLRYDLQEAVRALMRKLVGS 164
Cdd:cd00715 78 SSSLENAQPFVVNSPLGGIALAHNGNLVNAKELREELEEEGRIFQTTSDSEVILHLIARSLAKDDLFEAIIDALERVKGA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 165 YSLVFLWGDTVLAVRDPLGIKPLCIGEIDS-GFMVASESVAIDTLNGQLIRDVKPGELVVIRHGQMTSHQLVRLPHPAHC 243
Cdd:cd00715 158 YSLVIMTADGLIAVRDPHGIRPLVLGKLEGdGYVVASESCALDIIGAEFVRDVEPGEIVVIDDDGLESSQRAPKPKPAPC 237
|
250
....*....|....*
gi 1519874227 244 IFEYIYFARPDSIME 258
Cdd:cd00715 238 IFEYVYFARPDSVID 252
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
5-222 |
2.08e-64 |
|
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: 2.08e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 5 CGVVGI-SFNETGNNVAKSIYYALYALQHRGQEAAGISVHDGKAIRTHRGMGLVSEVFDDAQIALLRGQVGIGHVRYPTS 83
Cdd:cd00352 1 CGIFGIvGADGAASLLLLLLLRGLAALEHRGPDGAGIAVYDGDGLFVEKRAGPVSDVALDLLDEPLKSGVALGHVRLATN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 84 GRSCIENSQPLLvkYKDGAIAIAHNGNLVNSCQLREQLEQAGDIFYSTSDTEVIAHLFVKELLRYDLQEAVRALMRKLVG 163
Cdd:cd00352 81 GLPSEANAQPFR--SEDGRIALVHNGEIYNYRELREELEARGYRFEGESDSEVILHLLERLGREGGLFEAVEDALKRLDG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1519874227 164 SYSLVFL--WGDTVLAVRDPLGIKPLCIGE-IDSGFMVASESVAIDTLNGQLIRDVKPGELV 222
Cdd:cd00352 159 PFAFALWdgKPDRLFAARDRFGIRPLYYGItKDGGLVFASEPKALLALPFKGVRRLPPGELL 220
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
5-205 |
9.13e-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: 124.48 E-value: 9.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 5 CGVVGISFNetgNNVAKSIYYALYALQHRGQEAAGISVHDGKAIRTHRGMGLVSEVFDDAQIALLRGQVGIGHVRYPTSG 84
Cdd:cd00714 1 CGIVGYIGK---REAVDILLEGLKRLEYRGYDSAGIAVIGDGSLEVVKAVGKVANLEEKLAEKPLSGHVGIGHTRWATHG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 85 RSCIENSQPLLVKykDGAIAIAHNGNLVNSCQLREQLEQAGDIFYSTSDTEVIAHLfVKELLRY--DLQEAVRALMRKLV 162
Cdd:cd00714 78 EPTDVNAHPHRSC--DGEIAVVHNGIIENYAELKEELEAKGYKFESETDTEVIAHL-IEYYYDGglDLLEAVKKALKRLE 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1519874227 163 GSYSLVFL---WGDTVLAVRdplgiK--PLCIGEIDSGFMVASESVAI 205
Cdd:cd00714 155 GAYALAVIskdEPDEIVAAR-----NgsPLVIGIGDGENFVASDAPAL 197
|
|
| glmS |
TIGR01135 |
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ... |
5-205 |
2.52e-31 |
|
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: 124.67 E-value: 2.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 5 CGVVGIsfneTGNNVAKSIYY-ALYALQHRGQEAAGISVHDGKAIRTHRGMGLVSEVFDDAQIALLRGQVGIGHVRYPTS 83
Cdd:TIGR01135 1 CGIVGY----IGQRDAVPILLeGLKRLEYRGYDSAGIAVVDEGKLFVRKAVGKVAELANKLGEKPLPGGVGIGHTRWATH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 84 GRSCIENSQPLLVKYkdGAIAIAHNGNLVNSCQLREQLEQAGDIFYSTSDTEVIAHLFVKELLR-YDLQEAVRALMRKLV 162
Cdd:TIGR01135 77 GKPTDENAHPHTDEG--GRIAVVHNGIIENYAELREELEARGHVFSSDTDTEVIAHLIEEELREgGDLLEAVQKALKQLR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1519874227 163 GSYSLVFLWGD---TVLAVRDPlgiKPLCIGEIDSGFMVASESVAI 205
Cdd:TIGR01135 155 GAYALAVLHADhpeTLVAARSG---SPLIVGLGDGENFVASDVTAL 197
|
|
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
5-230 |
7.57e-30 |
|
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: 120.50 E-value: 7.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 5 CGVVGIsfneTGN-NVAKSIYYALYALQHRGQEAAGISVHDGKAIRTHRGMGLVSEVFDDAQIALLRGQVGIGHVRYPTS 83
Cdd:COG0449 2 CGIVGY----IGKrDAAPILLEGLKRLEYRGYDSAGIAVLDDGGLEVRKAVGKLANLEEKLAEEPLSGTIGIGHTRWATH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 84 GRSCIENSQPLLVKykDGAIAIAHNGNLVNSCQLREQLEQAGDIFYSTSDTEVIAHLFVKELLRY-DLQEAVRALMRKLV 162
Cdd:COG0449 78 GAPSDENAHPHTSC--SGRIAVVHNGIIENYAELREELEAKGHTFKSETDTEVIAHLIEEYLKGGgDLLEAVRKALKRLE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1519874227 163 GSYSLVFLWG---DTVLAVRdplgiK--PLCIGEIDSGFMVASESVAIdtlnGQLIRDV---KPGELVVIRHGQMT 230
Cdd:COG0449 156 GAYALAVISAdepDRIVAAR-----KgsPLVIGLGEGENFLASDVPAL----LPYTRRViylEDGEIAVLTRDGVE 222
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
5-227 |
1.21e-28 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 117.07 E-value: 1.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 5 CGVVGIsfneTGNNVAKSI-YYALYALQHRGQEAAGISVHDGKAIRTHRGMGLVSEVFDDAQIALLRGQVGIGHVRYPTS 83
Cdd:PRK00331 2 CGIVGY----VGQRNAAEIlLEGLKRLEYRGYDSAGIAVLDDGGLEVRKAVGKVANLEAKLEEEPLPGTTGIGHTRWATH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 84 GRSCIENSQPLLVKykDGAIAIAHNGNLVNSCQLREQLEQAGDIFYSTSDTEVIAHLFVKELLRY-DLQEAVRALMRKLV 162
Cdd:PRK00331 78 GKPTERNAHPHTDC--SGRIAVVHNGIIENYAELKEELLAKGHVFKSETDTEVIAHLIEEELKEGgDLLEAVRKALKRLE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1519874227 163 GSYSLVFLWG---DTVLAVR-DPlgikPLCIGEIDSGFMVASESVAIdtlnGQLIRDVKP---GELVVIRHG 227
Cdd:PRK00331 156 GAYALAVIDKdepDTIVAARnGS----PLVIGLGEGENFLASDALAL----LPYTRRVIYledGEIAVLTRD 219
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
92-205 |
1.32e-23 |
|
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: 94.51 E-value: 1.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 92 QPLlVKYKDGAIAIAHNGNLVNSCQLREQLEQAGDIFYSTSDTEVIAHLFVKEllryDLQEAVralmRKLVGSYSLVfLW 171
Cdd:pfam13537 14 QPM-VSSEDGRYVIVFNGEIYNYRELRAELEAKGYRFRTHSDTEVILHLYEAE----WGEDCV----DRLNGMFAFA-IW 83
|
90 100 110
....*....|....*....|....*....|....*...
gi 1519874227 172 ---GDTVLAVRDPLGIKPLCIGEID-SGFMVASESVAI 205
Cdd:pfam13537 84 drrRQRLFLARDRFGIKPLYYGRDDgGRLLFASELKAL 121
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
63-201 |
1.93e-23 |
|
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: 94.29 E-value: 1.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 63 DAQIALLRGQVGIGHVRYPTSGRSCIENsQPLLVKykDGAIAIAHNGNLVNSCQLREQLEQAGDIFYSTSDTEVIAHLFv 142
Cdd:pfam13522 2 DFSGIWVEGGVALGHVRLAIVDLPDAGN-QPMLSR--DGRLVLVHNGEIYNYGELREELADLGHAFRSRSDTEVLLALY- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1519874227 143 kellrydlQEAVRALMRKLVGSYSLVfLWG---DTVLAVRDPLGIKPLCIGEIDSGFMVASE 201
Cdd:pfam13522 78 --------EEWGEDCLERLRGMFAFA-IWDrrrRTLFLARDRLGIKPLYYGILGGGFVFASE 130
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
5-224 |
2.62e-23 |
|
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: 97.34 E-value: 2.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 5 CGVVGISFNETGNNVAKSIYYALYALQHRG-QEAAGISVHD---------GKAIRTHRGMGLVSEVFDDAQIALLRGQVG 74
Cdd:cd01907 1 CGIFGIMSKDGEPFVGALLVEMLDAMQERGpGDGAGFALYGdpdafvyssGKDMEVFKGVGYPEDIARRYDLEEYKGYHW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 75 IGHVRYPTSGRSCIENSQPLLVkykdGAIAIAHNGNLVNSCQLREQLEQAGDIFYSTSDTEVIAHLFVKELLRYDLQEAV 154
Cdd:cd01907 81 IAHTRQPTNSAVWWYGAHPFSI----GDIAVVHNGEISNYGSNREYLERFGYKFETETDTEVIAYYLDLLLRKGGLPLEY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 155 RALMRKLV--------------------GSYSLVFLWGDTVLAVRDPLGIKPLCIGEIDSGFMVASESVAIDTL---NGQ 211
Cdd:cd01907 157 YKHIIRMPeeerelllalrltyrladldGPFTIIVGTPDGFIVIRDRIKLRPAVVAETDDYVAIASEECAIREIpdrDNA 236
|
250
....*....|...
gi 1519874227 212 LIRDVKPGELVVI 224
Cdd:cd01907 237 KVWEPRPGEYVIW 249
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
5-233 |
9.18e-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: 94.93 E-value: 9.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 5 CGVVGIsFNETGNNVAKSIYYA-LYALQHRGQEAAGISVHDGkairthrgmglvsevfddaqiallrgqVGIGHVRY--- 80
Cdd:cd00712 1 CGIAGI-IGLDGASVDRATLERmLDALAHRGPDGSGIWIDEG---------------------------VALGHRRLsii 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 81 -PTSGRsciensQPLLvkYKDGAIAIAHNGNLVNSCQLREQLEQAGDIFYSTSDTEVIAHLFvkelLRYDLqeavrALMR 159
Cdd:cd00712 53 dLSGGA------QPMV--SEDGRLVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHLY----EEWGE-----DCLE 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 160 KLVGSYSLVfLW---GDTVLAVRDPLGIKPLCIGEIDSGFMVASE----------------SVAIDTLNGQL-------- 212
Cdd:cd00712 116 RLNGMFAFA-LWdkrKRRLFLARDRFGIKPLYYGRDGGGLAFASElkallalpgvpreldeAALAEYLAFQYvpaprtif 194
|
250 260
....*....|....*....|...
gi 1519874227 213 --IRDVKPGELVVIRHGQMTSHQ 233
Cdd:cd00712 195 kgIRKLPPGHYLTVDPGGVEIRR 217
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
5-242 |
9.59e-21 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 93.55 E-value: 9.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 5 CGVVGISFNETGNNVaksIYYALYALQHRGQEAAGIS-VHDGKAIRTHRGMGLVSEVfdDAqIALLRG---------QVG 74
Cdd:PTZ00295 25 CGIVGYLGNEDASKI---LLEGIEILQNRGYDSCGIStISSGGELKTTKYASDGTTS--DS-IEILKEklldshknsTIG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 75 IGHVRYPTSGRSCIENSQPLlVKYKDgAIAIAHNGNLVNSCQLREQLEQAGDIFYSTSDTEVIAHLFVKEL-LRYDLQEA 153
Cdd:PTZ00295 99 IAHTRWATHGGKTDENAHPH-CDYKK-RIALVHNGTIENYVELKSELIAKGIKFRSETDSEVIANLIGLELdQGEDFQEA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 154 VRALMRKLVGSYSLVFL---WGDTVLAVRDPlgiKPLCIGEIDSGFMVASESVAIDTLNGQLIRdVKPGELVVIRHGQM- 229
Cdd:PTZ00295 177 VKSAISRLQGTWGLCIIhkdNPDSLIVARNG---SPLLVGIGDDSIYVASEPSAFAKYTNEYIS-LKDGEIAELSLENVn 252
|
250
....*....|....*.
gi 1519874227 230 ---TSHQLVRLPHPAH 242
Cdd:PTZ00295 253 dlyTQRRVEKIPEEVI 268
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
5-201 |
3.04e-20 |
|
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: 91.82 E-value: 3.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 5 CGVVGIsFNETGNNVAKSIYYALYALQHRGqeaagisvhdgkairthrgmglvsevfDDAQIALLRGQVGIGHVRyptsg 84
Cdd:COG0367 2 CGIAGI-IDFDGGADREVLERMLDALAHRG---------------------------PDGSGIWVDGGVALGHRR----- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 85 RSCI---ENS-QPLLvkYKDGAIAIAHNGNLVNSCQLREQLEQAGDIFYSTSDTEVIAHLFvkelLRYDLqeavrALMRK 160
Cdd:COG0367 49 LSIIdlsEGGhQPMV--SEDGRYVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHAY----EEWGE-----DCLER 117
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1519874227 161 LVGSYSLVfLW---GDTVLAVRDPLGIKPLCIGEIDSGFMVASE 201
Cdd:COG0367 118 LNGMFAFA-IWdrrERRLFLARDRFGIKPLYYAEDGGGLAFASE 160
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
51-253 |
7.97e-17 |
|
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: 81.61 E-value: 7.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 51 HRGMglvsevfDDAQIALLRGQVGIGHVRY----PTSGRsciensQPLlvKYKDGAIAIAHNGNLVNSCQLREQLEQAGD 126
Cdd:TIGR01536 27 HRGP-------DASGIEYKDGNAILGHRRLaiidLSGGA------QPM--SNEGKTYVIVFNGEIYNHEELREELEAKGY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 127 IFYSTSDTEVIAHLFvkellrydlQEAVRALMRKLVGSYSLVfLW---GDTVLAVRDPLGIKPLCIGEIDSGFMVASESV 203
Cdd:TIGR01536 92 TFQTDSDTEVILHLY---------EEWGEECVDRLDGMFAFA-LWdseKGELFLARDRFGIKPLYYAYDGGQLYFASEIK 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1519874227 204 AIDTLNGQlirDVKPGELVVIrhgQMTSHQLVRLPhpaHCIFEYIYFARP 253
Cdd:TIGR01536 162 ALLAHPNI---KPFPDGAALA---PGFGFVRVPPP---STFFRGVFELEP 202
|
|
| YafJ |
COG0121 |
Predicted glutamine amidotransferase YafJ [General function prediction only]; |
5-227 |
3.24e-15 |
|
Predicted glutamine amidotransferase YafJ [General function prediction only];
Pssm-ID: 439891 [Multi-domain] Cd Length: 248 Bit Score: 74.62 E-value: 3.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 5 CGVVGISFNeTGNNVAKSIYYALYALQHRGQEAA--------GIS-VHDGKAIRTHRGmglVSEVFDDAQIALLRGQV-- 73
Cdd:COG0121 1 CRLLGYSGN-VPTDLEFLLLDPEHSLVRQSGATRegphadgwGIGwYEGDGEPRLYRD---PLPAWSDPNLRLLARPIks 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 74 --GIGHVRYPTSGRSCIENSQPllvkYKDGAIAIAHNGNLVNSCQLREQLEQAGDIFY-----STSDTEVIAHLFVKEL- 145
Cdd:COG0121 77 rlVIAHVRKATVGPVSLENTHP----FRGGRWLFAHNGQLDGFDRLRRRLAEELPDELyfqpvGTTDSELAFALLLSRLr 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 146 -----LRYDLQEAVRAL--MRKLVGSYSLVFLWGDTVLAVRDPLGIKP--LCI----GEIDSGFMVASESVaidTLNGQl 212
Cdd:COG0121 153 dggpdPAEALAEALRELaeLARAPGRLNLLLSDGERLYATRYTSDDPYptLYYltrtTPDDRVVVVASEPL---TDDEG- 228
|
250
....*....|....*
gi 1519874227 213 IRDVKPGELVVIRHG 227
Cdd:COG0121 229 WTEVPPGELLVVRDG 243
|
|
| YafJ |
cd01908 |
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ... |
58-227 |
1.63e-14 |
|
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: 72.42 E-value: 1.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 58 SEVFDDAQIALLRGQVGIGHVRYPTSGRSCIENSQPLLVKYkdgaIAIAHNGNLVNSCQLREQLEQAGDIFY-STSDTEV 136
Cdd:cd01908 67 SDINLESLARPIKSPLVLAHVRAATVGPVSLENCHPFTRGR----WLFAHNGQLDGFRLLRRRLLRLLPRLPvGTTDSEL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 137 IAHLFVKELLRYD------LQEAVRALMRKL-----VGSYSLVFLWGDTVLAVRDP-----------------LGIKPLC 188
Cdd:cd01908 143 AFALLLSRLLERDpldpaeLLDAILQTLRELaalapPGRLNLLLSDGEYLIATRYAsapslyyltrrapfgcaRLLFRSV 222
|
170 180 190
....*....|....*....|....*....|....*....
gi 1519874227 189 IGEIDSGFMVASEsvaIDTLNGQLiRDVKPGELVVIRHG 227
Cdd:cd01908 223 TTPNDDGVVVASE---PLTDDEGW-TEVPPGELVVVSEG 257
|
|
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
5-201 |
1.75e-14 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 74.56 E-value: 1.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 5 CGVVGIsFNETGNNVA--KSIYYALYALQHRGQEAAGIsVHDGKAIrthrgmglvsevfddaqiallrgqvgIGHVRY-- 80
Cdd:PRK09431 2 CGIFGI-LDIKTDADElrKKALEMSRLMRHRGPDWSGI-YASDNAI--------------------------LGHERLsi 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 81 --PTSGRsciensQPLLVKykDGAIAIAHNGNLVNSCQLREQLEQAGDiFYSTSDTEVIAHLFvkellrydlQEAVRALM 158
Cdd:PRK09431 54 vdVNGGA------QPLYNE--DGTHVLAVNGEIYNHQELRAELGDKYA-FQTGSDCEVILALY---------QEKGPDFL 115
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1519874227 159 RKLVGSYSLVfLW---GDTVLAVRDPLGIKPLCIGEIDSG-FMVASE 201
Cdd:PRK09431 116 DDLDGMFAFA-LYdseKDAYLIARDPIGIIPLYYGYDEHGnLYFASE 161
|
|
| PLN02549 |
PLN02549 |
asparagine synthase (glutamine-hydrolyzing) |
5-205 |
4.56e-13 |
|
asparagine synthase (glutamine-hydrolyzing)
Pssm-ID: 178164 [Multi-domain] Cd Length: 578 Bit Score: 70.18 E-value: 4.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 5 CGVVGIsFNETGNNVAK-SIYYALYA-LQHRGQEAAGISVHdgkairthrgmglvsevfddaqiallrGQVGIGHVRY-- 80
Cdd:PLN02549 2 CGILAV-LGCSDDSQAKrSRVLELSRrLRHRGPDWSGLYGN---------------------------EDCYLAHERLai 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 81 --PTSGrscienSQPLLvkYKDGAIAIAHNGNLVNSCQLREQLeqaGDIFYST-SDTEVIAHLFvkellrydlQEAVRAL 157
Cdd:PLN02549 54 mdPESG------DQPLY--NEDKTIVVTANGEIYNHKELREKL---KLHKFRTgSDCEVIAHLY---------EEHGEEF 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1519874227 158 MRKLVGSYSLVFL--WGDTVLAVRDPLGIKPLCIG-EIDSGFMVASESVAI 205
Cdd:PLN02549 114 VDMLDGMFSFVLLdtRDNSFIAARDHIGITPLYIGwGLDGSVWFASEMKAL 164
|
|
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
27-169 |
2.39e-12 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 68.24 E-value: 2.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 27 LYALQHRGQEAAGISVHDGKAIRTH-----RGMG----LVSEVFDDAQIALL------RGQVGIGHVRYPTSGRSCIENS 91
Cdd:PLN02981 27 LRRLEYRGYDSAGIAIDNDPSLESSsplvfREEGkiesLVRSVYEEVAETDLnldlvfENHAGIAHTRWATHGPPAPRNS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 92 QPLlVKYKDGAIAIAHNGNLVNSCQLREQLEQAGDIFYSTSDTEVIAHL--FV-----KELLRYDLQEAVRALMRKLVGS 164
Cdd:PLN02981 107 HPQ-SSGPGNEFLVVHNGIITNYEVLKETLLRHGFTFESDTDTEVIPKLakFVfdklnEEEGDVTFSQVVMEVMRQLEGA 185
|
....*
gi 1519874227 165 YSLVF 169
Cdd:PLN02981 186 YALIF 190
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
5-206 |
4.42e-12 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 67.05 E-value: 4.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 5 CGVVGIsFNETGNNV-AKSIYYALYA-LQHRGQEAAGI---SVHDGK-AIRTHRGMGLVSevfddaqiallrgqvgighv 78
Cdd:PTZ00077 2 CGILAI-FNSKGERHeLRRKALELSKrLRHRGPDWSGIivlENSPGTyNILAHERLAIVD-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 79 ryPTSGRsciensQPLLVKykDGAIAIAHNGNLVNSCQLREQLEQAGDIFYSTSDTEVIAHLFvKEllrYDLQEavraLM 158
Cdd:PTZ00077 61 --LSDGK------QPLLDD--DETVALMQNGEIYNHWEIRPELEKEGYKFSSNSDCEIIGHLY-KE---YGPKD----FW 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1519874227 159 RKLVGSYSLVFLWG--DTVLAVRDPLGIKPLCIG-EIDSGFMVASESVAID 206
Cdd:PTZ00077 123 NHLDGMFATVIYDMktNTFFAARDHIGIIPLYIGyAKDGSIWFSSELKALH 173
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
5-168 |
1.72e-09 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 59.12 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 5 CGVVG-ISFN--ETGNNVAKSIYYALYALQHRGQEAAGISVHDGKAIRTH---------------RGMGLVSE----VFD 62
Cdd:PTZ00394 2 CGIFGyANHNvpRTVEQILNVLLDGIQKVEYRGYDSAGLAIDANIGSEKEdgtaasaptprpcvvRSVGNISQlrekVFS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 63 DAQIALL-------RGQVGIGHVRYPTSGRSCIENSQPLlvKYKDGAIAIAHNGNLVNSCQLREQLEQAGDIFYSTSDTE 135
Cdd:PTZ00394 82 EAVAATLppmdattSHHVGIAHTRWATHGGVCERNCHPQ--QSNNGEFTIVHNGIVTNYMTLKELLKEEGYHFSSDTDTE 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 1519874227 136 VIA----HLFVKELLrYDLQEAVRALMRKLVGSYSLV 168
Cdd:PTZ00394 160 VISvlseYLYTRKGI-HNFADLALEVSRMVEGSYALL 195
|
|
| PRTases_typeI |
cd06223 |
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ... |
269-368 |
5.31e-07 |
|
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: 48.16 E-value: 5.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519874227 269 IGSNLAAEHPAC---ADTVTPIPDSGITLAVGYHQRSGISYKECLMKNRYIGRTFIMPDQnmretavrlKMNTIRPNIEG 345
Cdd:cd06223 1 AGRLLAEEIREDllePDVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSEPYG---------LELPLGGDVKG 71
|
90 100
....*....|....*....|...
gi 1519874227 346 HKLVMVDDSIVRGTTSRRIVNMV 368
Cdd:cd06223 72 KRVLLVDDVIATGGTLLAAIELL 94
|
|
| |
