|
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: 848.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 6 KGLNEECGIFGIWDHPNAAEITYYGLHSLQHRGQEGAGIVSTDGETLKGHRNLGLLADVFKHGELDDLKGKAAIGHVRYA 85
Cdd:COG0034 2 DKLHEECGVFGIYGHEDVAQLTYYGLYALQHRGQESAGIATSDGGRFHLHKGMGLVSDVFDEEDLERLKGNIAIGHVRYS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 86 TAGQKNLGNVQPFLFHFHSSSLALAHNGNLVNAKSLRRELEEEGAIFQTSSDTEVLAHLIKRSHTG-DFVEDLKVALNKV 164
Cdd:COG0034 82 TTGSSSLENAQPFYVNSPFGSIALAHNGNLTNAEELREELEEEGAIFQTTSDTEVILHLIARELTKeDLEEAIKEALRRV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 165 KGGFAYMLLTEDTMYAALDPNGFRPLSIGRIGDSYVVASETCAFETVGAEFVRDVEPGELIIINDDGLRIEKFTENVTHS 244
Cdd:COG0034 162 KGAYSLVILTGDGLIAARDPNGIRPLVLGKLEDGYVVASESCALDILGAEFVRDVEPGEIVVIDEDGLRSRQFAEKPRPA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 245 ICSMEYIYFARPDSNIAGINVHSARKRSGKRLAKEAFIDADVVTGVPDSSISAAIGYAEEAGLPYELGLIKNRYVARTFI 324
Cdd:COG0034 242 PCIFEYVYFARPDSVIDGRSVYEARKRMGRELAREAPVDADVVIPVPDSGRPAAIGYAEESGIPYEEGLIKNRYVGRTFI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 325 QPSQELREQGVRMKLSAVRGVVEGKRVVMIDDSIVRGTTSKRIVQLLREAGAAEVHVRIASPPLAYPCFYGIDIQTRNEL 404
Cdd:COG0034 322 QPTQELRELGVRLKLNPIREVVKGKRVVLVDDSIVRGTTSRRIVKMLREAGAKEVHFRIASPPIRYPCYYGIDTPTREEL 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489818430 405 IASNYSVDEICRIIGADSLEYLSEEGLVDSIGRPYPnepygGLCMAYFNGDYPTPLYDYEAEYL 468
Cdd:COG0034 402 IAANRSVEEIREYIGADSLGYLSLEGLIEAVGEPIE-----GFCTACFTGDYPTGIPDEEKKRL 460
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
8-457 |
0e+00 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 672.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 8 LNEECGIFGIW--DHPNAAEITYYGLHSLQHRGQEGAGIVSTDGETLKGHRNLGLLADVFKHGELDDLKGKAAIGHVRYA 85
Cdd:PRK05793 11 FKEECGVFGVFskNNIDVASLTYYGLYALQHRGQESAGIAVSDGEKIKVHKGMGLVSEVFSKEKLKGLKGNSAIGHVRYS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 86 TAGQKNLGNVQPFLFHFHSSSLALAHNGNLVNAKSLRRELEEEGAIFQTSSDTEVLAHLIKRSHTGDFVEDLKVALNKVK 165
Cdd:PRK05793 91 TTGASDLDNAQPLVANYKLGSIAIAHNGNLVNADVIRELLEDGGRIFQTSIDSEVILNLIARSAKKGLEKALVDAIQAIK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 166 GGFAYMLLTEDTMYAALDPNGFRPLSIGRIGDSYVVASETCAFETVGAEFVRDVEPGELIIINDDGLRIEKFTENVTHSI 245
Cdd:PRK05793 171 GSYALVILTEDKLIGVRDPHGIRPLCLGKLGDDYILSSESCALDTIGAEFIRDVEPGEIVIIDEDGIKSIKFAEKTKCQT 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 246 CSMEYIYFARPDSNIAGINVHSARKRSGKRLAKEAFIDADVVTGVPDSSISAAIGYAEEAGLPYELGLIKNRYVARTFIQ 325
Cdd:PRK05793 251 CAFEYIYFARPDSVIDGISVYESRVRAGRQLYKEYPVDADIVIGVPDSGIPAAIGYAEASGIPYGIGFIKNKYVGRTFIA 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 326 PSQELREQGVRMKLSAVRGVVEGKRVVMIDDSIVRGTTSKRIVQLLREAGAAEVHVRIASPPLAYPCFYGIDIQTRNELI 405
Cdd:PRK05793 331 PSQELRERAVRVKLNPLKVNVEGKRVVLIDDSIVRGTTSKRLVELLRKAGAKEVHFRVSSPPVKYPCYFGIDTPYRKELI 410
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 489818430 406 ASNYSVDEICRIIGADSLEYLSEEGLVDSIGRPypnepyGGLCMAYFNGDYP 457
Cdd:PRK05793 411 GANMSVEEIREMIGADSLGYLSIEGLLESLNGD------KGFCLGCFNGVYP 456
|
|
| purF |
TIGR01134 |
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ... |
12-457 |
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: 664.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 12 CGIFGIWDHPN-AAEITYYGLHSLQHRGQEGAGIVSTDGETLKGHRNLGLLADVFKHGELDDLKGKAAIGHVRYATAGQK 90
Cdd:TIGR01134 1 CGVVGIYGQEEvAASLTYYGLYALQHRGQESAGISVFDGNRFRLHKGNGLVSDVFNEEHLQRLKGNVGIGHVRYSTAGSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 91 NLGNVQPFLFHFHSSSLALAHNGNLVNAKSLRRELEEEGAIFQTSSDTEVLAHLIKRSHTG--DFVEDLKVALNKVKGGF 168
Cdd:TIGR01134 81 GLENAQPFVVNSPYGGLALAHNGNLVNADELRRELEEEGRHFNTTSDSEVLLHLLAHNDESkdDLFDAVARVLERVRGAY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 169 AYMLLTEDTMYAALDPNGFRPLSIGRIGDSYVVASETCAFETVGAEFVRDVEPGELIIINDDGLRIEKFtENVTHSICSM 248
Cdd:TIGR01134 161 ALVLMTEDGLVAVRDPHGIRPLVLGRRGDGYVVASESCALDILGAEFVRDVEPGEVVVIFDGGLESRQC-ARRPRAPCVF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 249 EYIYFARPDSNIAGINVHSARKRSGKRLAKEAFIDADVVTGVPDSSISAAIGYAEEAGLPYELGLIKNRYVARTFIQPSQ 328
Cdd:TIGR01134 240 EYVYFARPDSVIDGISVYYARKRMGKELARESPVEADVVVPVPDSGRSAALGFAQASGIPYREGLIKNRYVGRTFIMPTQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 329 ELREQGVRMKLSAVRGVVEGKRVVMIDDSIVRGTTSKRIVQLLREAGAAEVHVRIASPPLAYPCFYGIDIQTRNELIASN 408
Cdd:TIGR01134 320 ELRELSVRLKLNPVRAVFEGKRVVLVDDSIVRGTTSRQIVEMLRDAGAKEVHVRIASPPIRYPCYYGIDMPTREELIAAR 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 489818430 409 YSVDEICRiIGADSLEYLSEEGLVDSIGRPYPnepygGLCMAYFNGDYP 457
Cdd:TIGR01134 400 RTVEEIRK-IGADSLAYLSLEGLKEAVGNPES-----DLCLACFTGEYP 442
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
11-473 |
0e+00 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 572.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 11 ECGIFGIWDHPNAAEITYYGLHSLQHRGQEGAGIVSTDGETLKGHRNLGLLADVFKHGELDDLKGKAAIGHVRYATAGQK 90
Cdd:PLN02440 1 ECGVVGIFGDPEASRLCYLGLHALQHRGQEGAGIVTVDGNRLQSITGNGLVSDVFDESKLDQLPGDIAIGHVRYSTAGAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 91 NLGNVQPFLFHFHSSSLALAHNGNLVNAKSLRRELEEEGAIFQTSSDTEVLAHLIKRSHTGDFVEDLKVALNKVKGGFAY 170
Cdd:PLN02440 81 SLKNVQPFVANYRFGSIGVAHNGNLVNYEELRAKLEENGSIFNTSSDTEVLLHLIAISKARPFFSRIVDACEKLKGAYSM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 171 MLLTEDTMYAALDPNGFRPLSIG-RIGDSYVVASETCAFETVGAEFVRDVEPGELIIINDDGLRIEKF-TENVTHSICSM 248
Cdd:PLN02440 161 VFLTEDKLVAVRDPHGFRPLVMGrRSNGAVVFASETCALDLIGATYEREVNPGEVIVVDKDKGVSSQClMPHPEPKPCIF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 249 EYIYFARPDSNIAGINVHSARKRSGKRLAKEAFIDADVVTGVPDSSISAAIGYAEEAGLPYELGLIKNRYVARTFIQPSQ 328
Cdd:PLN02440 241 EHIYFARPNSIVFGRSVYESRLEFGEILATEIPVDCDVVIPVPDSGRVAALGYAAKLGVPFQQGLIRSHYVGRTFIEPSQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 329 ELREQGVRMKLSAVRGVVEGKRVVMIDDSIVRGTTSKRIVQLLREAGAAEVHVRIASPPLAYPCFYGIDIQTRNELIASN 408
Cdd:PLN02440 321 KIRDFSVKLKLNPVRSVLEGKRVVVVDDSIVRGTTSSKIVRMLREAGAKEVHMRIASPPIIASCYYGVDTPSREELISNR 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489818430 409 YSVDEICRIIGADSLEYLSEEGLVDSIGRPYPNepyggLCMAYFNGDYPTPLY----DYEAEYLASLEA 473
Cdd:PLN02440 401 MSVEEIRKFIGCDSLAFLPLEDLKKSLGEESPR-----FCYACFSGDYPVLPKrvggDIDDGYLESLEE 464
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
12-260 |
9.70e-143 |
|
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: 408.77 E-value: 9.70e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 12 CGIFGIWDHPNAAEITYYGLHSLQHRGQEGAGIVSTDGETLKGHRNLGLLADVFKHGELDDLKGKAAIGHVRYATAGQKN 91
Cdd:cd00715 1 CGVFGIYGAEDAARLTYLGLYALQHRGQESAGIATSDGKRFHTHKGMGLVSDVFDEEKLRRLPGNIAIGHVRYSTAGSSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 92 LGNVQPFLFHFHSSSLALAHNGNLVNAKSLRRELEEEGAIFQTSSDTEVLAHLIKRS-HTGDFVEDLKVALNKVKGGFAY 170
Cdd:cd00715 81 LENAQPFVVNSPLGGIALAHNGNLVNAKELREELEEEGRIFQTTSDSEVILHLIARSlAKDDLFEAIIDALERVKGAYSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 171 MLLTEDTMYAALDPNGFRPLSIGRIG-DSYVVASETCAFETVGAEFVRDVEPGELIIINDDGLRIEKFTENVTHSICSME 249
Cdd:cd00715 161 VIMTADGLIAVRDPHGIRPLVLGKLEgDGYVVASESCALDIIGAEFVRDVEPGEIVVIDDDGLESSQRAPKPKPAPCIFE 240
|
250
....*....|.
gi 489818430 250 YIYFARPDSNI 260
Cdd:cd00715 241 YVYFARPDSVI 251
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
12-225 |
6.53e-67 |
|
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: 213.85 E-value: 6.53e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 12 CGIFGIWDHPNAAEITYY----GLHSLQHRGQEGAGIVSTDGETLKGHRNLGLLADVFKHGELDDLKGKAAIGHVRYATA 87
Cdd:cd00352 1 CGIFGIVGADGAASLLLLlllrGLAALEHRGPDGAGIAVYDGDGLFVEKRAGPVSDVALDLLDEPLKSGVALGHVRLATN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 88 GQKNLGNVQPflFHFHSSSLALAHNGNLVNAKSLRRELEEEGAIFQTSSDTEVLAHLIKRS-HTGDFVEDLKVALNKVKG 166
Cdd:cd00352 81 GLPSEANAQP--FRSEDGRIALVHNGEIYNYRELREELEARGYRFEGESDSEVILHLLERLgREGGLFEAVEDALKRLDG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489818430 167 GFAYMLLT--EDTMYAALDPNGFRPLSIG-RIGDSYVVASETCAFETVGAEFVRDVEPGELI 225
Cdd:cd00352 159 PFAFALWDgkPDRLFAARDRFGIRPLYYGiTKDGGLVFASEPKALLALPFKGVRRLPPGELL 220
|
|
| glmS |
TIGR01135 |
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ... |
12-241 |
1.80e-30 |
|
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: 1.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 12 CGIFGIWDHPNAAEITYYGLHSLQHRGQEGAGIVSTDGETLKGHRNLGLLADVFKHGELDDLKGKAAIGHVRYATAGQKN 91
Cdd:TIGR01135 1 CGIVGYIGQRDAVPILLEGLKRLEYRGYDSAGIAVVDEGKLFVRKAVGKVAELANKLGEKPLPGGVGIGHTRWATHGKPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 92 LGNVQPflfHF-HSSSLALAHNGNLVNAKSLRRELEEEGAIFQTSSDTEVLAHLIKR--SHTGDFVEDLKVALNKVKGGF 168
Cdd:TIGR01135 81 DENAHP---HTdEGGRIAVVHNGIIENYAELREELEARGHVFSSDTDTEVIAHLIEEelREGGDLLEAVQKALKQLRGAY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 169 AYMLLTED---TMYAAldpngfR---PLSIGrIGDS-YVVASETCAFetvgAEFVRDV---EPGELIIINDDGLRIEKFT 238
Cdd:TIGR01135 158 ALAVLHADhpeTLVAA------RsgsPLIVG-LGDGeNFVASDVTAL----LPYTRRViylEDGDIAILTKDGVEIYNFE 226
|
...
gi 489818430 239 ENV 241
Cdd:TIGR01135 227 GAP 229
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
12-241 |
2.03e-30 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 124.39 E-value: 2.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 12 CGIFGIWDHPNAAEITYYGLHSLQHRGQEGAGIVSTDGETLKGHRNLGLLADVFKHGELDDLKGKAAIGHVRYATAGQKN 91
Cdd:PRK00331 2 CGIVGYVGQRNAAEILLEGLKRLEYRGYDSAGIAVLDDGGLEVRKAVGKVANLEAKLEEEPLPGTTGIGHTRWATHGKPT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 92 LGNVQPflfHFHSS-SLALAHNGNLVNAKSLRRELEEEGAIFQTSSDTEVLAHLI--KRSHTGDFVEDLKVALNKVKGGF 168
Cdd:PRK00331 82 ERNAHP---HTDCSgRIAVVHNGIIENYAELKEELLAKGHVFKSETDTEVIAHLIeeELKEGGDLLEAVRKALKRLEGAY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 169 AYMLLTE---DTMYAAldpngfR---PLSIGrIGDS-YVVASETCAFetvgAEFVRDV---EPGELIIINDDGLRIEKFT 238
Cdd:PRK00331 159 ALAVIDKdepDTIVAA------RngsPLVIG-LGEGeNFLASDALAL----LPYTRRViylEDGEIAVLTRDGVEIFDFD 227
|
...
gi 489818430 239 ENV 241
Cdd:PRK00331 228 GNP 230
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
12-227 |
3.13e-30 |
|
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: 116.78 E-value: 3.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 12 CGIFGIWDHPNAAEITYYGLHSLQHRGQEGAGIVSTDGETLKGHRNLGLLADVFKHGELDDLKGKAAIGHVRYATAGQKN 91
Cdd:cd00714 1 CGIVGYIGKREAVDILLEGLKRLEYRGYDSAGIAVIGDGSLEVVKAVGKVANLEEKLAEKPLSGHVGIGHTRWATHGEPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 92 LGNVQPflfhfHSS---SLALAHNGNLVNAKSLRRELEEEGAIFQTSSDTEVLAHLIKRS--HTGDFVEDLKVALNKVKG 166
Cdd:cd00714 81 DVNAHP-----HRScdgEIAVVHNGIIENYAELKEELEAKGYKFESETDTEVIAHLIEYYydGGLDLLEAVKKALKRLEG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489818430 167 GFAYMLLTE---DTMYAAldpngfR---PLSIGrIGD-SYVVASETCAFetvgAEFVRDV---EPGELIII 227
Cdd:cd00714 156 AYALAVISKdepDEIVAA------RngsPLVIG-IGDgENFVASDAPAL----LEHTRRViylEDGDIAVI 215
|
|
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
12-241 |
1.37e-28 |
|
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: 118.96 E-value: 1.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 12 CGIFGIWDHPNAAEITYYGLHSLQHRGQEGAGIVSTDGETLKGHRNLGLLADVFKHGELDDLKGKAAIGHVRYATAGQKN 91
Cdd:COG0449 2 CGIVGYIGKRDAAPILLEGLKRLEYRGYDSAGIAVLDDGGLEVRKAVGKLANLEEKLAEEPLSGTIGIGHTRWATHGAPS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 92 LGNVQPflfHF-HSSSLALAHNGNLVNAKSLRRELEEEGAIFQTSSDTEVLAHLIKR--SHTGDFVEDLKVALNKVKGGF 168
Cdd:COG0449 82 DENAHP---HTsCSGRIAVVHNGIIENYAELREELEAKGHTFKSETDTEVIAHLIEEylKGGGDLLEAVRKALKRLEGAY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 169 AYMLLTE---DTMYAAldpngfR---PLSIGrIGDS-YVVASETCAFetvgAEFVRDV---EPGELIIINDDGLRIEKFT 238
Cdd:COG0449 159 ALAVISAdepDRIVAA------RkgsPLVIG-LGEGeNFLASDVPAL----LPYTRRViylEDGEIAVLTRDGVEIYDLD 227
|
...
gi 489818430 239 ENV 241
Cdd:COG0449 228 GEP 230
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
12-237 |
1.08e-24 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 107.41 E-value: 1.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 12 CGIFGIWDHPNAAEITYYGLHSLQHRGQEGAGIVS-TDGETLK--GHRNLGLLADVFKHgelddLKGKAA---------I 79
Cdd:PTZ00295 25 CGIVGYLGNEDASKILLEGIEILQNRGYDSCGISTiSSGGELKttKYASDGTTSDSIEI-----LKEKLLdshknstigI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 80 GHVRYATAGQKNLGNVQPflfHF-HSSSLALAHNGNLVNAKSLRRELEEEGAIFQTSSDTEVLAHLI--KRSHTGDFVED 156
Cdd:PTZ00295 100 AHTRWATHGGKTDENAHP---HCdYKKRIALVHNGTIENYVELKSELIAKGIKFRSETDSEVIANLIglELDQGEDFQEA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 157 LKVALNKVKGGFAYMLLTE---DTMYAAldPNGfRPLSIGRIGDSYVVASETCAFETVGAEFVRdVEPGELIIINDDGlr 233
Cdd:PTZ00295 177 VKSAISRLQGTWGLCIIHKdnpDSLIVA--RNG-SPLLVGIGDDSIYVASEPSAFAKYTNEYIS-LKDGEIAELSLEN-- 250
|
....
gi 489818430 234 IEKF 237
Cdd:PTZ00295 251 VNDL 254
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
12-227 |
1.88e-24 |
|
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: 101.58 E-value: 1.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 12 CGIFGIWD---HPNAAEITYYGLHSLQHRG-QEGAGI------------VSTDGETLKGhrnLGLLADVFKHGELDDLKG 75
Cdd:cd01907 1 CGIFGIMSkdgEPFVGALLVEMLDAMQERGpGDGAGFalygdpdafvysSGKDMEVFKG---VGYPEDIARRYDLEEYKG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 76 KAAIGHVRYATAGQKNLGNVQPFlfhfHSSSLALAHNGNLVNAKSLRRELEEEGAIFQTSSDTEVLAHLI---------- 145
Cdd:cd01907 78 YHWIAHTRQPTNSAVWWYGAHPF----SIGDIAVVHNGEISNYGSNREYLERFGYKFETETDTEVIAYYLdlllrkgglp 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 146 --KRSHTGDFVEDLKVALNKVK---------GGFAYMLLTEDTMYAALDPNGFRPLSIGRIGDSYVVASETCAF-ETVGA 213
Cdd:cd01907 154 leYYKHIIRMPEEERELLLALRltyrladldGPFTIIVGTPDGFIVIRDRIKLRPAVVAETDDYVAIASEECAIrEIPDR 233
|
250
....*....|....*.
gi 489818430 214 EFVRDVEP--GELIII 227
Cdd:cd01907 234 DNAKVWEPrpGEYVIW 249
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
12-237 |
4.29e-21 |
|
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: 91.46 E-value: 4.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 12 CGIFGIWD---HPNAAEITYYGLHSLQHRGQEGAGIVSTDGetlkghrnlglladvfkhgelddlkgkAAIGHVRYA--- 85
Cdd:cd00712 1 CGIAGIIGldgASVDRATLERMLDALAHRGPDGSGIWIDEG---------------------------VALGHRRLSiid 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 86 -TAGQknlgnvQPFlfHFHSSSLALAHNGNLVNAKSLRRELEEEGAIFQTSSDTEVLAHLIKRSHTGdfvedlkvALNKV 164
Cdd:cd00712 54 lSGGA------QPM--VSEDGRLVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHLYEEWGED--------CLERL 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 165 KGGFAYMLL--TEDTMYAALDPNGFRPLSIGRIGDSYVVASETCAFETVG-----------AEF---------------V 216
Cdd:cd00712 118 NGMFAFALWdkRKRRLFLARDRFGIKPLYYGRDGGGLAFASELKALLALPgvpreldeaalAEYlafqyvpaprtifkgI 197
|
250 260
....*....|....*....|.
gi 489818430 217 RDVEPGELIIINDDGLRIEKF 237
Cdd:cd00712 198 RKLPPGHYLTVDPGGVEIRRY 218
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
75-204 |
1.97e-20 |
|
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: 86.98 E-value: 1.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 75 GKAAIGHVRYATAGQKNLGNvQPFLFHfhSSSLALAHNGNLVNAKSLRRELEEEGAIFQTSSDTEVLAHLIkrSHTGdfv 154
Cdd:pfam13522 10 GGVALGHVRLAIVDLPDAGN-QPMLSR--DGRLVLVHNGEIYNYGELREELADLGHAFRSRSDTEVLLALY--EEWG--- 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 489818430 155 EDlkvALNKVKGGFAYML--LTEDTMYAALDPNGFRPLSIGRIGDSYVVASE 204
Cdd:pfam13522 82 ED---CLERLRGMFAFAIwdRRRRTLFLARDRLGIKPLYYGILGGGFVFASE 130
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
96-208 |
2.56e-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: 83.34 E-value: 2.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 96 QPFLFHfHSSSLALAHNGNLVNAKSLRRELEEEGAIFQTSSDTEVLAHLIKRSHTGDFVEDLkvalnkvKGGFAYMLLT- 174
Cdd:pfam13537 14 QPMVSS-EDGRYVIVFNGEIYNYRELRAELEAKGYRFRTHSDTEVILHLYEAEWGEDCVDRL-------NGMFAFAIWDr 85
|
90 100 110
....*....|....*....|....*....|....*.
gi 489818430 175 -EDTMYAALDPNGFRPLSIGRI-GDSYVVASETCAF 208
Cdd:pfam13537 86 rRQRLFLARDRFGIKPLYYGRDdGGRLLFASELKAL 121
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
12-237 |
1.08e-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: 88.74 E-value: 1.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 12 CGIFGIW--DHPNAAEITYYGLHSLQHRGQEGAGIVSTDGETLkGHRNLGLLadvfkhgeldDLkgkaaighvryATAGQ 89
Cdd:COG0367 2 CGIAGIIdfDGGADREVLERMLDALAHRGPDGSGIWVDGGVAL-GHRRLSII----------DL-----------SEGGH 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 90 knlgnvQPFlfHFHSSSLALAHNGNLVNAKSLRRELEEEGAIFQTSSDTEVLAHLIKRSHTgDFVEDLkvalnkvKGGFA 169
Cdd:COG0367 60 ------QPM--VSEDGRYVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHAYEEWGE-DCLERL-------NGMFA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 170 YML--LTEDTMYAALDPNGFRPLSIGRIGDSYVVASETCAFETVG-----------AEF---------------VRDVEP 221
Cdd:COG0367 124 FAIwdRRERRLFLARDRFGIKPLYYAEDGGGLAFASELKALLAHPgvdreldpealAEYltlgyvpaprtifkgIRKLPP 203
|
250
....*....|....*..
gi 489818430 222 GELIIINDDG-LRIEKF 237
Cdd:COG0367 204 GHYLTVDAGGeLEIRRY 220
|
|
| PRTases_typeI |
cd06223 |
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ... |
273-384 |
4.44e-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: 80.13 E-value: 4.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 273 GKRLAKEA---FIDADVVTGVPDSSISAAIGYAEEAGLPYELGLIKNRYVARTFIQPSQelreqgvrmKLSAVRGVVEGK 349
Cdd:cd06223 2 GRLLAEEIredLLEPDVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSEPYG---------LELPLGGDVKGK 72
|
90 100 110
....*....|....*....|....*....|....*
gi 489818430 350 RVVMIDDSIVRGTTSKRIVQLLREAGAAEVHVRIA 384
Cdd:cd06223 73 RVLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVL 107
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
14-212 |
1.71e-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: 84.69 E-value: 1.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 14 IFGIWDHPNAAEITYYGLHSLQ----HRGQEGAGIVSTDGETLKGHRNLGLLadvfkhgeldDLKGKAaighvryatagq 89
Cdd:TIGR01536 1 IAGFFDLDDKAVEEDEAIKRMSdtiaHRGPDASGIEYKDGNAILGHRRLAII----------DLSGGA------------ 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 90 knlgnvQPFlfHFHSSSLALAHNGNLVNAKSLRRELEEEGAIFQTSSDTEVLAHLIkRSHTGDFVEDLkvalnkvKGGFA 169
Cdd:TIGR01536 59 ------QPM--SNEGKTYVIVFNGEIYNHEELREELEAKGYTFQTDSDTEVILHLY-EEWGEECVDRL-------DGMFA 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489818430 170 YMLLTE--DTMYAALDPNGFRPLSIGRIGDSYVVASETCAFETVG 212
Cdd:TIGR01536 123 FALWDSekGELFLARDRFGIKPLYYAYDGGQLYFASEIKALLAHP 167
|
|
| YafJ |
cd01908 |
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ... |
73-230 |
5.97e-16 |
|
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: 77.43 E-value: 5.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 73 LKGKAAIGHVRYATAGQKNLGNVQPFLFHfhssSLALAHNGNLVNAKSLRRELEEEGAIF-QTSSDTEVLAHLI---KRS 148
Cdd:cd01908 78 IKSPLVLAHVRAATVGPVSLENCHPFTRG----RWLFAHNGQLDGFRLLRRRLLRLLPRLpVGTTDSELAFALLlsrLLE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 149 HTGDFVEDLKVALNKV---------KGGFAYMLLTEDTMYA---ALDPN-----GFRPLSIGRIG---------DSYVVA 202
Cdd:cd01908 154 RDPLDPAELLDAILQTlrelaalapPGRLNLLLSDGEYLIAtryASAPSlyyltRRAPFGCARLLfrsvttpndDGVVVA 233
|
170 180
....*....|....*....|....*...
gi 489818430 203 SETCAFETVgaefVRDVEPGELIIINDD 230
Cdd:cd01908 234 SEPLTDDEG----WTEVPPGELVVVSEG 257
|
|
| YafJ |
COG0121 |
Predicted glutamine amidotransferase YafJ [General function prediction only]; |
71-235 |
2.50e-15 |
|
Predicted glutamine amidotransferase YafJ [General function prediction only];
Pssm-ID: 439891 [Multi-domain] Cd Length: 248 Bit Score: 75.39 E-value: 2.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 71 DDLKGKAAIGHVRYATAGQKNLGNVQPflfhFHSSSLALAHNGNLVNAKSLRRELEEEG--AIFQT---SSDTEVLAHLI 145
Cdd:COG0121 72 RPIKSRLVIAHVRKATVGPVSLENTHP----FRGGRWLFAHNGQLDGFDRLRRRLAEELpdELYFQpvgTTDSELAFALL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 146 K---RSHTGDFVEDLKVALNKVK------GGFAYMLLTEDTMYAALDPNGFRPLSI------GRIGDSYVVASETCafeT 210
Cdd:COG0121 148 LsrlRDGGPDPAEALAEALRELAelarapGRLNLLLSDGERLYATRYTSDDPYPTLyyltrtTPDDRVVVVASEPL---T 224
|
170 180
....*....|....*....|....*
gi 489818430 211 VGAEFvRDVEPGELIIInDDGLRIE 235
Cdd:COG0121 225 DDEGW-TEVPPGELLVV-RDGLEVE 247
|
|
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
12-299 |
1.97e-14 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 75.33 E-value: 1.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 12 CGIFGIWD--------HPNAAEItyygLHSLQHRGQEGAGIVSTDgetlkghrnlglladvfkhgelddlkgKAAIGHVR 83
Cdd:PRK09431 2 CGIFGILDiktdadelRKKALEM----SRLMRHRGPDWSGIYASD---------------------------NAILGHER 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 84 YATAGQKNLGnvQPfLFHfHSSSLALAHNGNLVNAKSLRRELEEEGAiFQTSSDTEVLAHLIKRshTG-DFVEDLkvaln 162
Cdd:PRK09431 51 LSIVDVNGGA--QP-LYN-EDGTHVLAVNGEIYNHQELRAELGDKYA-FQTGSDCEVILALYQE--KGpDFLDDL----- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 163 kvKGGFAYMLLTE--DTMYAALDPNGFRPLSIGRIGD-SYVVASETCAFETVgAEFVRDVEPGElIIINDDGlrieKFTE 239
Cdd:PRK09431 119 --DGMFAFALYDSekDAYLIARDPIGIIPLYYGYDEHgNLYFASEMKALVPV-CKTIKEFPPGH-YYWSKDG----EFVR 190
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489818430 240 NVTHSicSMEYIYFARPDSNIAGIN---VHSARKRsgkrlakeafIDADVVTGVP-----DSSISAAI 299
Cdd:PRK09431 191 YYQRD--WFDYDAVKDNVTDKNELRdalEAAVKKR----------LMSDVPYGVLlsgglDSSLISAI 246
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
96-204 |
8.17e-13 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 70.51 E-value: 8.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 96 QPFLFHfhSSSLALAHNGNLVNAKSLRRELEEEGAIFQTSSDTEVLAHLIKRSHTGDFVedlkvalNKVKGGFAYMLL-- 173
Cdd:PTZ00077 66 QPLLDD--DETVALMQNGEIYNHWEIRPELEKEGYKFSSNSDCEIIGHLYKEYGPKDFW-------NHLDGMFATVIYdm 136
|
90 100 110
....*....|....*....|....*....|..
gi 489818430 174 TEDTMYAALDPNGFRPLSIGRIGD-SYVVASE 204
Cdd:PTZ00077 137 KTNTFFAARDHIGIIPLYIGYAKDgSIWFSSE 168
|
|
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
12-146 |
1.37e-09 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 60.53 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 12 CGIFGIWDHpNAA-------EITYYGLHSLQHRGQEGAGIVSTDGETLKGH-----RNLG----LLADVFKHGELDDLKG 75
Cdd:PLN02981 2 CGIFAYLNY-NVPrerrfilEVLFNGLRRLEYRGYDSAGIAIDNDPSLESSsplvfREEGkiesLVRSVYEEVAETDLNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 76 K------AAIGHVRYATAGQKNLGNVQPflfhfHSSSLA----LAHNGNLVNAKSLRRELEEEGAIFQTSSDTEVLAHLI 145
Cdd:PLN02981 81 DlvfenhAGIAHTRWATHGPPAPRNSHP-----QSSGPGneflVVHNGIITNYEVLKETLLRHGFTFESDTDTEVIPKLA 155
|
.
gi 489818430 146 K 146
Cdd:PLN02981 156 K 156
|
|
| PLN02549 |
PLN02549 |
asparagine synthase (glutamine-hydrolyzing) |
12-204 |
9.08e-09 |
|
asparagine synthase (glutamine-hydrolyzing)
Pssm-ID: 178164 [Multi-domain] Cd Length: 578 Bit Score: 57.85 E-value: 9.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 12 CGIFGIW---DHPNAAEITYYGLHS-LQHRGQEGAGivstdgetLKGHRNLGLladvfkhgelddlkgkaaiGHVRYA-- 85
Cdd:PLN02549 2 CGILAVLgcsDDSQAKRSRVLELSRrLRHRGPDWSG--------LYGNEDCYL-------------------AHERLAim 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 86 --TAGQknlgnvQPfLFHfHSSSLALAHNGNLVNAKSLRRELEEEgaIFQTSSDTEVLAHLIKRsHTGDFVEDLkvalnk 163
Cdd:PLN02549 55 dpESGD------QP-LYN-EDKTIVVTANGEIYNHKELREKLKLH--KFRTGSDCEVIAHLYEE-HGEEFVDML------ 117
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489818430 164 vKGGFAYMLLT--EDTMYAALDPNGFRPLSIGRIGDSYV-VASE 204
Cdd:PLN02549 118 -DGMFSFVLLDtrDNSFIAARDHIGITPLYIGWGLDGSVwFASE 160
|
|
| PyrE |
COG0461 |
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ... |
268-381 |
1.10e-05 |
|
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate phosphoribosyltransferase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 440229 Cd Length: 201 Bit Score: 46.30 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 268 ARKRSGKRLA---KEAFIDADVVTGVPDSSISAAIGYAEEAGLPYelgliknRYVARtfiqpsqELREQGVRMKLsaVRG 344
Cdd:COG0461 45 ALELLGEALAeliKELGPEFDAVAGPATGGIPLAAAVARALGLPA-------IFVRK-------EAKDHGTGGQI--EGG 108
|
90 100 110
....*....|....*....|....*....|....*..
gi 489818430 345 VVEGKRVVMIDDSIVRGTTSKRIVQLLREAGAAEVHV 381
Cdd:COG0461 109 LLPGERVLVVEDVITTGGSVLEAVEALREAGAEVVGV 145
|
|
| ComFC |
COG1040 |
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General ... |
273-381 |
1.18e-05 |
|
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General function prediction only];
Pssm-ID: 440662 [Multi-domain] Cd Length: 196 Bit Score: 45.97 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 273 GKRLAKEAFIDADVVTGVPdSSISAAI--GY----------AEEAGLPYEL-GLIKNRYVartfiqPSQ-----ELREQG 334
Cdd:COG1040 68 ARALREALLPRPDLIVPVP-LHRRRLRrrGFnqaellaralARALGIPVLPdLLRRVRAT------PSQaglsrAERRRN 140
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 489818430 335 VRMKLSAVRG-VVEGKRVVMIDDsiVR--GTTSKRIVQLLREAGAAEVHV 381
Cdd:COG1040 141 LRGAFAVRPPaRLAGKHVLLVDD--VLttGATLAEAARALKAAGAARVDV 188
|
|
| Pribosyltran |
pfam00156 |
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ... |
266-380 |
3.58e-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: 43.89 E-value: 3.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 266 HSARKRSGKRLAKEAFIDA----DVVTGVPDSSISAAIGYAEEAGLPYElGLIKNRYVARTFIQpsqelreqgvrMKLSA 341
Cdd:pfam00156 8 NPAILKAVARLAAQINEDYggkpDVVVGILRGGLPFAGILARRLDVPLA-FVRKVSYNPDTSEV-----------MKTSS 75
|
90 100 110
....*....|....*....|....*....|....*....
gi 489818430 342 VRGVVEGKRVVMIDDSIVRGTTSKRIVQLLREAGAAEVH 380
Cdd:pfam00156 76 ALPDLKGKTVLIVDDILDTGGTLLKVLELLKNVGPKEVK 114
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
79-172 |
1.11e-04 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 44.87 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 79 IGHVRYATAGQKNLGNVQPFlfHFHSSSLALAHNGNLVNAKSLRRELEEEGAIFQTSSDTEVLA----HLIKRSHTGDFV 154
Cdd:PTZ00394 101 IAHTRWATHGGVCERNCHPQ--QSNNGEFTIVHNGIVTNYMTLKELLKEEGYHFSSDTDTEVISvlseYLYTRKGIHNFA 178
|
90
....*....|....*...
gi 489818430 155 EDLKVALNKVKGGFAYML 172
Cdd:PTZ00394 179 DLALEVSRMVEGSYALLV 196
|
|
| PRK02277 |
PRK02277 |
orotate phosphoribosyltransferase-like protein; Provisional |
267-376 |
1.76e-04 |
|
orotate phosphoribosyltransferase-like protein; Provisional
Pssm-ID: 235023 [Multi-domain] Cd Length: 200 Bit Score: 42.55 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 267 SARKRSGKRL----------AKEAFIDADVVTGVPDSSISAAIGYAEEAGLpyELGLiknrYVARTFIQPSQElREQGVr 336
Cdd:PRK02277 59 SSIGSSSSRLryiasamadmLEKEDEEVDVVVGIAKSGVPLATLVADELGK--DLAI----YHPKKWDHGEGE-KKTGS- 130
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 489818430 337 mkLSAVRGVVEGKRVVMIDDSIVRGTTSKRIVQLLREAGA 376
Cdd:PRK02277 131 --FSRNFASVEGKRCVIVDDVITSGTTMKETIEYLKEHGG 168
|
|
| GATase_4 |
pfam13230 |
Glutamine amidotransferases class-II; This family captures members that are not found in ... |
72-115 |
2.90e-04 |
|
Glutamine amidotransferases class-II; This family captures members that are not found in pfam00310.
Pssm-ID: 433047 [Multi-domain] Cd Length: 272 Bit Score: 42.70 E-value: 2.90e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 489818430 72 DLKGKAAIGHVRYATAGQKNLGNVQPFLFHFHSSSLALAHNGNL 115
Cdd:pfam13230 68 PIRSRNVIAHIRKATQGRVTLENTHPFMRELWGRYWIFAHNGDL 111
|
|
| pyrE |
PRK00455 |
orotate phosphoribosyltransferase; Validated |
263-381 |
9.40e-04 |
|
orotate phosphoribosyltransferase; Validated
Pssm-ID: 234771 Cd Length: 202 Bit Score: 40.53 E-value: 9.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818430 263 INVHSARKRSGKRLA---KEAFIDADVVTG-----VPdssISAAIgyAEEAGLPYelglIKNRYVARTFiqpsqelREQG 334
Cdd:PRK00455 41 LSYPEALALLGRFLAeaiKDSGIEFDVVAGpatggIP---LAAAV--ARALDLPA----IFVRKEAKDH-------GEGG 104
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 489818430 335 vRMKLSavrgVVEGKRVVMIDDSIVRGTTSKRIVQLLREAGAAEVHV 381
Cdd:PRK00455 105 -QIEGR----RLFGKRVLVVEDVITTGGSVLEAVEAIRAAGAEVVGV 146
|
|
| PrsA |
COG0462 |
Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; ... |
340-381 |
1.29e-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: 40.81 E-value: 1.29e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 489818430 340 SAVRGVVEGKRVVMIDDSIVRGTTSKRIVQLLREAGAAEVHV 381
Cdd:COG0462 203 MNIIGDVEGKTCIIVDDMIDTGGTLVEAAEALKEAGAKSVYA 244
|
|
| ribP_PPkin |
TIGR01251 |
ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In ... |
341-381 |
4.09e-03 |
|
ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In some systems, close homologs lacking enzymatic activity exist and perform regulatory functions. The model is designated subfamily rather than equivalog for this reason. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273523 [Multi-domain] Cd Length: 308 Bit Score: 39.18 E-value: 4.09e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 489818430 341 AVRGVVEGKRVVMIDDSIVRGTTSKRIVQLLREAGAAEVHV 381
Cdd:TIGR01251 203 NLVGDVEGKDVVIVDDIIDTGGTIAKAAEILKSAGAKRVIA 243
|
|
| PRK03092 |
PRK03092 |
ribose-phosphate diphosphokinase; |
342-379 |
7.44e-03 |
|
ribose-phosphate diphosphokinase;
Pssm-ID: 179535 [Multi-domain] Cd Length: 304 Bit Score: 38.39 E-value: 7.44e-03
10 20 30
....*....|....*....|....*....|....*...
gi 489818430 342 VRGVVEGKRVVMIDDSIVRGTTSKRIVQLLREAGAAEV 379
Cdd:PRK03092 195 VVGDVEGRTCVLVDDMIDTGGTIAGAVRALKEAGAKDV 232
|
|
| PRK11595 |
PRK11595 |
DNA utilization protein GntX; Provisional |
343-381 |
7.94e-03 |
|
DNA utilization protein GntX; Provisional
Pssm-ID: 183221 [Multi-domain] Cd Length: 227 Bit Score: 37.71 E-value: 7.94e-03
10 20 30
....*....|....*....|....*....|....*....
gi 489818430 343 RGVVEGKRVVMIDDSIVRGTTSKRIVQLLREAGAAEVHV 381
Cdd:PRK11595 182 ELPVQGQHMAIVDDVVTTGSTVAEIAQLLLRNGAASVQV 220
|
|
| |
