|
Name |
Accession |
Description |
Interval |
E-value |
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
7-516 |
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: 647.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 7 GIREECGVFGCIASGDwptqldVPHVITLGLVGLQHRGQESAGIVTSDGSsvpKFRVHKGMGLVNHVFTEDNLKKLyVSN 86
Cdd:COG0034 3 KLHEECGVFGIYGHED------VAQLTYYGLYALQHRGQESAGIATSDGG---RFHLHKGMGLVSDVFDEEDLERL-KGN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 87 LGIGHTRYATTGKCELENCQPFVVETLHGKIAVAHNGELVNAARLRKKLLRHGIGLSTSSDSEMITQLLAYtppqeQDDT 166
Cdd:COG0034 73 IAIGHVRYSTTGSSSLENAQPFYVNSPFGSIALAHNGNLTNAEELREELEEEGAIFQTTSDTEVILHLIAR-----ELTK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 167 PDWVARIKNLMKEAPAAYSLVIMHRDVIYAVRDPYGNRPLCIGRLmpvsdindkekksseTEGWVVSSESCSFLSIGARY 246
Cdd:COG0034 148 EDLEEAIKEALRRVKGAYSLVILTGDGLIAARDPNGIRPLVLGKL---------------EDGYVVASESCALDILGAEF 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 247 CHEVKPGEIVEISRHGVRTLDIIPRSngdPVAFCIFEYVYFARPDSMFEDQMVYTVRYRCGQQLAVEAPVEADLVSTVPE 326
Cdd:COG0034 213 VRDVEPGEIVVIDEDGLRSRQFAEKP---RPAPCIFEYVYFARPDSVIDGRSVYEARKRMGRELAREAPVDADVVIPVPD 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 327 SATPAALGYATKCGLPYVEVLCKNRYVGRTFIQPNMRLRQLGVAKKFGVLSDNFKGKRIVLIDDSIVRGNTISPIIKLLK 406
Cdd:COG0034 290 SGRPAAIGYAEESGIPYEEGLIKNRYVGRTFIQPTQELRELGVRLKLNPIREVVKGKRVVLVDDSIVRGTTSRRIVKMLR 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 407 ESGAKEVHIRVASPPIKHPCFMGINIPTKEELIANKPEFEYLAEYLGANSVVYLSVEGLVSSVQQEIkfkkqkvkkrdit 486
Cdd:COG0034 370 EAGAKEVHFRIASPPIRYPCYYGIDTPTREELIAANRSVEEIREYIGADSLGYLSLEGLIEAVGEPI------------- 436
|
490 500 510
....*....|....*....|....*....|
gi 17105352 487 iqengngleyfekTGHCTACLTGQYPVDLE 516
Cdd:COG0034 437 -------------EGFCTACFTGDYPTGIP 453
|
|
| purF |
TIGR01134 |
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ... |
12-512 |
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: 530.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 12 CGVFGCiasgdWPTQLDVPHVITLGLVGLQHRGQESAGIVTSDGSsvpKFRVHKGMGLVNHVFTEDNLKKLyVSNLGIGH 91
Cdd:TIGR01134 1 CGVVGI-----YGQEEVAASLTYYGLYALQHRGQESAGISVFDGN---RFRLHKGNGLVSDVFNEEHLQRL-KGNVGIGH 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 92 TRYATTGKCELENCQPFVVETLHGKIAVAHNGELVNAARLRKKLLRHGIGLSTSSDSEMITQLLAYTPPQEQDDtpdwVA 171
Cdd:TIGR01134 72 VRYSTAGSSGLENAQPFVVNSPYGGLALAHNGNLVNADELRRELEEEGRHFNTTSDSEVLLHLLAHNDESKDDL----FD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 172 RIKNLMKEAPAAYSLVIMHRDVIYAVRDPYGNRPLCIGRLmpvsdindkekksseTEGWVVSSESCSFLSIGARYCHEVK 251
Cdd:TIGR01134 148 AVARVLERVRGAYALVLMTEDGLVAVRDPHGIRPLVLGRR---------------GDGYVVASESCALDILGAEFVRDVE 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 252 PGEIVEISRHGVRTLdiipRSNGDPVAFCIFEYVYFARPDSMFEDQMVYTVRYRCGQQLAVEAPVEADLVSTVPESATPA 331
Cdd:TIGR01134 213 PGEVVVIFDGGLESR----QCARRPRAPCVFEYVYFARPDSVIDGISVYYARKRMGKELARESPVEADVVVPVPDSGRSA 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 332 ALGYATKCGLPYVEVLCKNRYVGRTFIQPNMRLRQLGVAKKFGVLSDNFKGKRIVLIDDSIVRGNTISPIIKLLKESGAK 411
Cdd:TIGR01134 289 ALGFAQASGIPYREGLIKNRYVGRTFIMPTQELRELSVRLKLNPVRAVFEGKRVVLVDDSIVRGTTSRQIVEMLRDAGAK 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 412 EVHIRVASPPIKHPCFMGINIPTKEELIANKPEFEYlAEYLGANSVVYLSVEGLVSSVQQEIKfkkqkvkkrditiqeng 491
Cdd:TIGR01134 369 EVHVRIASPPIRYPCYYGIDMPTREELIAARRTVEE-IRKIGADSLAYLSLEGLKEAVGNPES----------------- 430
|
490 500
....*....|....*....|.
gi 17105352 492 ngleyfektGHCTACLTGQYP 512
Cdd:TIGR01134 431 ---------DLCLACFTGEYP 442
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
1-514 |
8.53e-177 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 505.72 E-value: 8.53e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 1 MELEESGIREECGVFGCIAsgdwPTQLDVPHVITLGLVGLQHRGQESAGIVTSDGSsvpKFRVHKGMGLVNHVFTEDNLK 80
Cdd:PRK05793 4 MDLEGDKFKEECGVFGVFS----KNNIDVASLTYYGLYALQHRGQESAGIAVSDGE---KIKVHKGMGLVSEVFSKEKLK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 81 KLyVSNLGIGHTRYATTGKCELENCQPFVVETLHGKIAVAHNGELVNAARLRKKLLRHGIGLSTSSDSEMITQLLAYTPP 160
Cdd:PRK05793 77 GL-KGNSAIGHVRYSTTGASDLDNAQPLVANYKLGSIAIAHNGNLVNADVIRELLEDGGRIFQTSIDSEVILNLIARSAK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 161 QEQDDTpdwvarIKNLMKEAPAAYSLVIMHRDVIYAVRDPYGNRPLCIGRLmpvsdindkekksseTEGWVVSSESCSFL 240
Cdd:PRK05793 156 KGLEKA------LVDAIQAIKGSYALVILTEDKLIGVRDPHGIRPLCLGKL---------------GDDYILSSESCALD 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 241 SIGARYCHEVKPGEIVEISRHGVRTLDIIPRSNGDPvafCIFEYVYFARPDSMFEDQMVYTVRYRCGQQLAVEAPVEADL 320
Cdd:PRK05793 215 TIGAEFIRDVEPGEIVIIDEDGIKSIKFAEKTKCQT---CAFEYIYFARPDSVIDGISVYESRVRAGRQLYKEYPVDADI 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 321 VSTVPESATPAALGYATKCGLPYVEVLCKNRYVGRTFIQPNMRLRQLGVAKKFGVLSDNFKGKRIVLIDDSIVRGNTISP 400
Cdd:PRK05793 292 VIGVPDSGIPAAIGYAEASGIPYGIGFIKNKYVGRTFIAPSQELRERAVRVKLNPLKVNVEGKRVVLIDDSIVRGTTSKR 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 401 IIKLLKESGAKEVHIRVASPPIKHPCFMGINIPTKEELIANKPEFEYLAEYLGANSVVYLSVEGLVSSVQqeikfkkqkv 480
Cdd:PRK05793 372 LVELLRKAGAKEVHFRVSSPPVKYPCYFGIDTPYRKELIGANMSVEEIREMIGADSLGYLSIEGLLESLN---------- 441
|
490 500 510
....*....|....*....|....*....|....
gi 17105352 481 kkrditiqengngleyfEKTGHCTACLTGQYPVD 514
Cdd:PRK05793 442 -----------------GDKGFCLGCFNGVYPVS 458
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
11-513 |
7.56e-155 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 450.28 E-value: 7.56e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 11 ECGVFGCIASGDwptqldVPHVITLGLVGLQHRGQESAGIVTSDGSsvpKFRVHKGMGLVNHVFTEDNLKKLyVSNLGIG 90
Cdd:PLN02440 1 ECGVVGIFGDPE------ASRLCYLGLHALQHRGQEGAGIVTVDGN---RLQSITGNGLVSDVFDESKLDQL-PGDIAIG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 91 HTRYATTGKCELENCQPFVVETLHGKIAVAHNGELVNAARLRKKLLRHGIGLSTSSDSEMITQLLAytppqeQDDTPDWV 170
Cdd:PLN02440 71 HVRYSTAGASSLKNVQPFVANYRFGSIGVAHNGNLVNYEELRAKLEENGSIFNTSSDTEVLLHLIA------ISKARPFF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 171 ARIKNLMKEAPAAYSLVIMHRDVIYAVRDPYGNRPLCIGRlmpvsdindkeKKSSEtegWVVSSESCSFLSIGARYCHEV 250
Cdd:PLN02440 145 SRIVDACEKLKGAYSMVFLTEDKLVAVRDPHGFRPLVMGR-----------RSNGA---VVFASETCALDLIGATYEREV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 251 KPGEIVEISR-HGVRTLDIIPRSNGDPvafCIFEYVYFARPDSMFEDQMVYTVRYRCGQQLAVEAPVEADLVSTVPESAT 329
Cdd:PLN02440 211 NPGEVIVVDKdKGVSSQCLMPHPEPKP---CIFEHIYFARPNSIVFGRSVYESRLEFGEILATEIPVDCDVVIPVPDSGR 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 330 PAALGYATKCGLPYVEVLCKNRYVGRTFIQPNMRLRQLGVAKKFGVLSDNFKGKRIVLIDDSIVRGNTISPIIKLLKESG 409
Cdd:PLN02440 288 VAALGYAAKLGVPFQQGLIRSHYVGRTFIEPSQKIRDFSVKLKLNPVRSVLEGKRVVVVDDSIVRGTTSSKIVRMLREAG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 410 AKEVHIRVASPPIKHPCFMGINIPTKEELIANKPEFEYLAEYLGANSVVYLSVEGLVSSVQQeikfkkqkvkkrditiqe 489
Cdd:PLN02440 368 AKEVHMRIASPPIIASCYYGVDTPSREELISNRMSVEEIRKFIGCDSLAFLPLEDLKKSLGE------------------ 429
|
490 500
....*....|....*....|....
gi 17105352 490 ngngleyfEKTGHCTACLTGQYPV 513
Cdd:PLN02440 430 --------ESPRFCYACFSGDYPV 445
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
12-295 |
1.57e-138 |
|
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the N-terminus of glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase) . The glutaminase domain catalyzes amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. GPATase catalyzes the first step in purine biosynthesis, an amide transfer from glutamine to PRPP, resulting in phosphoribosylamine, pyrophosphate and glutamate. GPATase crystalizes as a homotetramer, but can also exist as a homdimer.
Pssm-ID: 238367 [Multi-domain] Cd Length: 252 Bit Score: 399.91 E-value: 1.57e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 12 CGVFGCIASGDwptqldVPHVITLGLVGLQHRGQESAGIVTSDGSsvpKFRVHKGMGLVNHVFTEDNLKKLyVSNLGIGH 91
Cdd:cd00715 1 CGVFGIYGAED------AARLTYLGLYALQHRGQESAGIATSDGK---RFHTHKGMGLVSDVFDEEKLRRL-PGNIAIGH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 92 TRYATTGKCELENCQPFVVETLHGKIAVAHNGELVNAARLRKKLLRHGIGLSTSSDSEMITQLLAYTPpqeqdDTPDWVA 171
Cdd:cd00715 71 VRYSTAGSSSLENAQPFVVNSPLGGIALAHNGNLVNAKELREELEEEGRIFQTTSDSEVILHLIARSL-----AKDDLFE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 172 RIKNLMKEAPAAYSLVIMHRDVIYAVRDPYGNRPLCIGRLmpvsdindkekkssETEGWVVSSESCSFLSIGARYCHEVK 251
Cdd:cd00715 146 AIIDALERVKGAYSLVIMTADGLIAVRDPHGIRPLVLGKL--------------EGDGYVVASESCALDIIGAEFVRDVE 211
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 17105352 252 PGEIVEISRHGVRTLDIIPRsngDPVAFCIFEYVYFARPDSMFE 295
Cdd:cd00715 212 PGEIVVIDDDGLESSQRAPK---PKPAPCIFEYVYFARPDSVID 252
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
12-256 |
1.28e-59 |
|
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. This domain is related to members of the Ntn (N-terminal nucleophile) hydrolase superfamily and is found at the N-terminus of enzymes such as glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). GLMS catalyzes the formation of glucosamine 6-phosphate from fructose 6-phosphate and glutamine in amino sugar synthesis. GPATase catalyzes the first step in purine biosynthesis, an amide transfer from glutamine to PRPP, resulting in phosphoribosylamine, pyrophosphate and glutamate. Asparagine synthetase B synthesizes asparagine from aspartate and glutamine. Beta-LS catalyzes the formation of the beta-lactam ring in the beta-lactamase inhibitor clavulanic acid. GltS synthesizes L-glutamate from 2-oxoglutarate and L-glutamine. These enzymes are generally dimers, but GPATase also exists as a homotetramer.
Pssm-ID: 238212 [Multi-domain] Cd Length: 220 Bit Score: 196.13 E-value: 1.28e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 12 CGVFGCIASGDWPTQLDVPHviTLGLVGLQHRGQESAGIVTSDGSsvpKFRVHKGMGLVNHVFtEDNLKKLYVSNLGIGH 91
Cdd:cd00352 1 CGIFGIVGADGAASLLLLLL--LRGLAALEHRGPDGAGIAVYDGD---GLFVEKRAGPVSDVA-LDLLDEPLKSGVALGH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 92 TRYATTGKCELENCQPFVVETlhGKIAVAHNGELVNAARLRKKLLRHGIGLSTSSDSEMITQLLAYTPpqeqdDTPDWVA 171
Cdd:cd00352 75 VRLATNGLPSEANAQPFRSED--GRIALVHNGEIYNYRELREELEARGYRFEGESDSEVILHLLERLG-----REGGLFE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 172 RIKNLMKEAPAAYSLVIM--HRDVIYAVRDPYGNRPLCIGRlmpvsdindkekksSETEGWVVSSESCSFLSIGARYCHE 249
Cdd:cd00352 148 AVEDALKRLDGPFAFALWdgKPDRLFAARDRFGIRPLYYGI--------------TKDGGLVFASEPKALLALPFKGVRR 213
|
....*..
gi 17105352 250 VKPGEIV 256
Cdd:cd00352 214 LPPGELL 220
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
12-258 |
6.43e-27 |
|
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: 107.92 E-value: 6.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 12 CGVFGCIASGDwptqlDVPHVITlGLVGLQHRGQESAGI-VTSDGSsvpkFRVHKGMGLVNHVftEDNLKKLYV-SNLGI 89
Cdd:cd00714 1 CGIVGYIGKRE-----AVDILLE-GLKRLEYRGYDSAGIaVIGDGS----LEVVKAVGKVANL--EEKLAEKPLsGHVGI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 90 GHTRYATTGKCELENCQPFVVETlhGKIAVAHNGELVNAARLRKKLLRHGIGLSTSSDSEMITQLLAYtppqEQDDTPDW 169
Cdd:cd00714 69 GHTRWATHGEPTDVNAHPHRSCD--GEIAVVHNGIIENYAELKEELEAKGYKFESETDTEVIAHLIEY----YYDGGLDL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 170 VARIKNLMKEAPAAYSLVIMHR---DVIYAVRDpygNRPLCIGrlmpvsdINDKEKkssetegwVVSSESCSFLSIGARY 246
Cdd:cd00714 143 LEAVKKALKRLEGAYALAVISKdepDEIVAARN---GSPLVIG-------IGDGEN--------FVASDAPALLEHTRRV 204
|
250
....*....|..
gi 17105352 247 CHeVKPGEIVEI 258
Cdd:cd00714 205 IY-LEDGDIAVI 215
|
|
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
12-277 |
4.65e-22 |
|
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase domains [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440218 [Multi-domain] Cd Length: 610 Bit Score: 99.70 E-value: 4.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 12 CGVFGCIASGDwptqldVPHVITLGLVGLQHRGQESAGIVTSDGSsvpKFRVHKGMGLVnhvfteDNLKKLYV-----SN 86
Cdd:COG0449 2 CGIVGYIGKRD------AAPILLEGLKRLEYRGYDSAGIAVLDDG---GLEVRKAVGKL------ANLEEKLAeeplsGT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 87 LGIGHTRYATTGKCELENCQPFVVETlhGKIAVAHNG--ElvNAARLRKKLLRHGIGLSTSSDSEMITQLLAYtppqEQD 164
Cdd:COG0449 67 IGIGHTRWATHGAPSDENAHPHTSCS--GRIAVVHNGiiE--NYAELREELEAKGHTFKSETDTEVIAHLIEE----YLK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 165 DTPDWVARIKNLMKEAPAAYSLVIMHR---DVIYAVRdpYGNrPLCIGrlmpvsdINDKEkkssetegWVVSSESCSFLS 241
Cdd:COG0449 139 GGGDLLEAVRKALKRLEGAYALAVISAdepDRIVAAR--KGS-PLVIG-------LGEGE--------NFLASDVPALLP 200
|
250 260 270
....*....|....*....|....*....|....*....
gi 17105352 242 igarYCHEV---KPGEIVEISRHGVRTLDIiprsNGDPV 277
Cdd:COG0449 201 ----YTRRViylEDGEIAVLTRDGVEIYDL----DGEPV 231
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
12-266 |
3.30e-20 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 93.93 E-value: 3.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 12 CGVFGCIASGDwptqldVPHVITLGLVGLQHRGQESAGIVTSDGSSvpKFRVHKGMGLVNHVFTEDNLKKLYV-----SN 86
Cdd:PTZ00295 25 CGIVGYLGNED------ASKILLEGIEILQNRGYDSCGISTISSGG--ELKTTKYASDGTTSDSIEILKEKLLdshknST 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 87 LGIGHTRYATTGKCELENCQPFVveTLHGKIAVAHNGELVNAARLRKKLLRHGIGLSTSSDSEMITQLLAYtppqEQDDT 166
Cdd:PTZ00295 97 IGIAHTRWATHGGKTDENAHPHC--DYKKRIALVHNGTIENYVELKSELIAKGIKFRSETDSEVIANLIGL----ELDQG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 167 PDWVARIKNLMKEAPAAYSLVIMHR---DVIYAVRDpygNRPLCIGRlmpvsdindkekkssETEGWVVSSESCSFlsig 243
Cdd:PTZ00295 171 EDFQEAVKSAISRLQGTWGLCIIHKdnpDSLIVARN---GSPLLVGI---------------GDDSIYVASEPSAF---- 228
|
250 260
....*....|....*....|....*.
gi 17105352 244 ARYCHE---VKPGEIVEISRHGVRTL 266
Cdd:PTZ00295 229 AKYTNEyisLKDGEIAELSLENVNDL 254
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
12-283 |
5.07e-19 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 90.10 E-value: 5.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 12 CGVFGCIAsgdwptQLDVPHVITLGLVGLQHRGQESAGIVTSDGSSVpkfRVHKGMGLVNHVftEDNLKKLYVS-NLGIG 90
Cdd:PRK00331 2 CGIVGYVG------QRNAAEILLEGLKRLEYRGYDSAGIAVLDDGGL---EVRKAVGKVANL--EAKLEEEPLPgTTGIG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 91 HTRYATTGKCELENCQPFVVETlhGKIAVAHNGELVNAARLRKKLLRHGIGLSTSSDSEMITQLLAYtppqEQDDTPDWV 170
Cdd:PRK00331 71 HTRWATHGKPTERNAHPHTDCS--GRIAVVHNGIIENYAELKEELLAKGHVFKSETDTEVIAHLIEE----ELKEGGDLL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 171 ARIKNLMKEAPAAYSLVIMHR---DVIYAVRDpygNRPLCIGrlmpvsdINDKEkkssetegWVVSSESCSFLSigarYC 247
Cdd:PRK00331 145 EAVRKALKRLEGAYALAVIDKdepDTIVAARN---GSPLVIG-------LGEGE--------NFLASDALALLP----YT 202
|
250 260 270
....*....|....*....|....*....|....*....
gi 17105352 248 HEVKP---GEIVEISRHGVRTLDIiprsNGDPVAFCIFE 283
Cdd:PRK00331 203 RRVIYledGEIAVLTRDGVEIFDF----DGNPVEREVYT 237
|
|
| PRTases_typeI |
cd06223 |
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ... |
306-442 |
6.30e-19 |
|
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: 82.83 E-value: 6.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 306 CGQQLAVEAP---VEADLVSTVPESATPAALGYATKCGLPYVEVLCKNRYVGRTFIQPNmrlrqlgvaKKFGVLSDNFKG 382
Cdd:cd06223 1 AGRLLAEEIRedlLEPDVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSEPY---------GLELPLGGDVKG 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 383 KRIVLIDDSIVRGNTISPIIKLLKESGAKEVHIRVAsPPIKHPCFMGINIPTKEELIANK 442
Cdd:cd06223 72 KRVLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVL-LDKPEGGARELASPGDPVYSLFT 130
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
12-256 |
1.03e-16 |
|
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: 79.62 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 12 CGVFGCIASGDWPtqlDVPHVITLGLVGLQHRG-QESAGIVTSDG------SSVPKFRVHKGMGLVNHVFTEDNLKKlYV 84
Cdd:cd01907 1 CGIFGIMSKDGEP---FVGALLVEMLDAMQERGpGDGAGFALYGDpdafvySSGKDMEVFKGVGYPEDIARRYDLEE-YK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 85 SNLGIGHTRYATTGKCELENCQPFVVetlhGKIAVAHNGELVNAARLRKKLLRHGIGLSTSSDSEMITQLLAYTpPQEQD 164
Cdd:cd01907 77 GYHWIAHTRQPTNSAVWWYGAHPFSI----GDIAVVHNGEISNYGSNREYLERFGYKFETETDTEVIAYYLDLL-LRKGG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 165 DTPDWVARIKNL------------MKEAPAA----YSLVIMHRDVIYAVRDPYGNRPLCIGrlmpvsdindkekkssETE 228
Cdd:cd01907 152 LPLEYYKHIIRMpeeerelllalrLTYRLADldgpFTIIVGTPDGFIVIRDRIKLRPAVVA----------------ETD 215
|
250 260 270
....*....|....*....|....*....|..
gi 17105352 229 GWV-VSSESCSFLSIGARYCHEV---KPGEIV 256
Cdd:cd01907 216 DYVaIASEECAIREIPDRDNAKVwepRPGEYV 247
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
88-211 |
6.79e-16 |
|
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain found in a variety of enzymes, such as asparagine synthetase and glutamine--fructose-6-phosphate transaminase.
Pssm-ID: 433279 [Multi-domain] Cd Length: 130 Bit Score: 74.26 E-value: 6.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 88 GIGHTRYATTGKCELENcQPFVVETlhGKIAVAHNGELVNAARLRKKLLRHGIGLSTSSDSEMITQLLAYTPpqeqddtP 167
Cdd:pfam13522 13 ALGHVRLAIVDLPDAGN-QPMLSRD--GRLVLVHNGEIYNYGELREELADLGHAFRSRSDTEVLLALYEEWG-------E 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 17105352 168 DWVARIKNLMkeAPAAYSlVIMHRDVIyaVRDPYGNRPLCIGRL 211
Cdd:pfam13522 83 DCLERLRGMF--AFAIWD-RRRRTLFL--ARDRLGIKPLYYGIL 121
|
|
| YafJ |
cd01908 |
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ... |
85-261 |
3.83e-15 |
|
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: 75.50 E-value: 3.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 85 SNLGIGHTRYATTGKCELENCQPFVvetlHGKIAVAHNGELVNAARLRKKLLRHGIGLST-SSDSEM----ITQLLAYTP 159
Cdd:cd01908 80 SPLVLAHVRAATVGPVSLENCHPFT----RGRWLFAHNGQLDGFRLLRRRLLRLLPRLPVgTTDSELafalLLSRLLERD 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 160 PQEQDDTPDWVAR-IKNLMKEA-PAAYSLVIMHRDVIYAVRDPYGNRP--LCIGRLMPVSDINDKEKKSSETEGWVVSSE 235
Cdd:cd01908 156 PLDPAELLDAILQtLRELAALApPGRLNLLLSDGEYLIATRYASAPSLyyLTRRAPFGCARLLFRSVTTPNDDGVVVASE 235
|
170 180
....*....|....*....|....*.
gi 17105352 236 SCSFlsigARYCHEVKPGEIVEISRH 261
Cdd:cd01908 236 PLTD----DEGWTEVPPGELVVVSEG 257
|
|
| YafJ |
COG0121 |
Predicted glutamine amidotransferase YafJ [General function prediction only]; |
20-260 |
1.68e-14 |
|
Predicted glutamine amidotransferase YafJ [General function prediction only];
Pssm-ID: 439891 [Multi-domain] Cd Length: 248 Bit Score: 73.08 E-value: 1.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 20 SGDWPTQLDvpHVITLGLVGLQHRGQESAGIVTSDG------SSVPKFRVHKGmglVNHVFTEDNLKKL---YVSNLGIG 90
Cdd:COG0121 7 SGNVPTDLE--FLLLDPEHSLVRQSGATREGPHADGwgigwyEGDGEPRLYRD---PLPAWSDPNLRLLarpIKSRLVIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 91 HTRYATTGKCELENCQPFVvetlHGKIAVAHNGELVNAARLRKKL-------LRHGIGLSTssDSE----MITQLLAYTP 159
Cdd:COG0121 82 HVRKATVGPVSLENTHPFR----GGRWLFAHNGQLDGFDRLRRRLaeelpdeLYFQPVGTT--DSElafaLLLSRLRDGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 160 PQEQDDTPDWVARIKNLMKeAPAAYSLVIMHRDVIYAVRDPYGNRP--LCIGRLMPVSDindkekkssetEGWVVSSESc 237
Cdd:COG0121 156 PDPAEALAEALRELAELAR-APGRLNLLLSDGERLYATRYTSDDPYptLYYLTRTTPDD-----------RVVVVASEP- 222
|
250 260
....*....|....*....|...
gi 17105352 238 sfLSIGARYcHEVKPGEIVEISR 260
Cdd:COG0121 223 --LTDDEGW-TEVPPGELLVVRD 242
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
12-265 |
3.04e-14 |
|
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: 71.82 E-value: 3.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 12 CGVFGCIasgDWPTQLDVPHVITLGLVGLQHRGQESAGIVTSDGssvpkfrvhkgmglvnhvftednlkklyvsnLGIGH 91
Cdd:cd00712 1 CGIAGII---GLDGASVDRATLERMLDALAHRGPDGSGIWIDEG-------------------------------VALGH 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 92 TRYATTGkceLEN-CQPFVVETlhGKIAVAHNGELVNAARLRKKLLRHGIGLSTSSDSEMItqLLAYtppQEQDdtPDWV 170
Cdd:cd00712 47 RRLSIID---LSGgAQPMVSED--GRLVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVI--LHLY---EEWG--EDCL 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 171 ARIkNLMkeapaaYSLVI--MHRDVIYAVRDPYGNRPL----------------CIGRLMPVSDINDKEKKSSETEGWVV 232
Cdd:cd00712 115 ERL-NGM------FAFALwdKRKRRLFLARDRFGIKPLyygrdggglafaselkALLALPGVPRELDEAALAEYLAFQYV 187
|
250 260 270
....*....|....*....|....*....|...
gi 17105352 233 SSESCSFLSIgarycHEVKPGEIVEISRHGVRT 265
Cdd:cd00712 188 PAPRTIFKGI-----RKLPPGHYLTVDPGGVEI 215
|
|
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
12-187 |
2.15e-13 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 72.86 E-value: 2.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 12 CGVFGCIASGDWPTQLDVPHVITLGLVGLQHRGQESAGIVTSDGSSVPKFR--VHKGMG----LVNHVF-----TEDNLK 80
Cdd:PLN02981 2 CGIFAYLNYNVPRERRFILEVLFNGLRRLEYRGYDSAGIAIDNDPSLESSSplVFREEGkiesLVRSVYeevaeTDLNLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 81 KLYVSNLGIGHTRYATTGKCELENCQPFVVETlHGKIAVAHNGELVNAARLRKKLLRHGIGLSTSSDSEMITQLLAYTPP 160
Cdd:PLN02981 82 LVFENHAGIAHTRWATHGPPAPRNSHPQSSGP-GNEFLVVHNGIITNYEVLKETLLRHGFTFESDTDTEVIPKLAKFVFD 160
|
170 180
....*....|....*....|....*....
gi 17105352 161 QEQDDTPDWVAR--IKNLMKEAPAAYSLV 187
Cdd:PLN02981 161 KLNEEEGDVTFSqvVMEVMRQLEGAYALI 189
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
106-240 |
1.09e-12 |
|
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: 64.85 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 106 QPFVVETLhGKIAVAHNGELVNAARLRKKLLRHGIGLSTSSDSEMITQLLAYtppqeqddtpDW----VARIkNLMkeap 181
Cdd:pfam13537 14 QPMVSSED-GRYVIVFNGEIYNYRELRAELEAKGYRFRTHSDTEVILHLYEA----------EWgedcVDRL-NGM---- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17105352 182 aaYSLVIM--HRDVIYAVRDPYGNRPLCIGRlmpvsdindkekksSETEGWVVSSESCSFL 240
Cdd:pfam13537 78 --FAFAIWdrRRQRLFLARDRFGIKPLYYGR--------------DDGGRLLFASELKALL 122
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
12-188 |
3.30e-10 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 62.59 E-value: 3.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 12 CGVFGCIASGDWPTQLDVPHVITLGLVGLQHRGQESAGIVTSDG----------SSVPKFR--VHKGMGLVNH----VFT 75
Cdd:PTZ00394 2 CGIFGYANHNVPRTVEQILNVLLDGIQKVEYRGYDSAGLAIDANigsekedgtaASAPTPRpcVVRSVGNISQlrekVFS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 76 ED------NLKKLYVSNLGIGHTRYATTGKCELENCQPfvVETLHGKIAVAHNGELVNAARLRKKLLRHGIGLSTSSDSE 149
Cdd:PTZ00394 82 EAvaatlpPMDATTSHHVGIAHTRWATHGGVCERNCHP--QQSNNGEFTIVHNGIVTNYMTLKELLKEEGYHFSSDTDTE 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 17105352 150 MITQLLAYTppQEQDDTPDWVARIKNLMKEAPAAYSLVI 188
Cdd:PTZ00394 160 VISVLSEYL--YTRKGIHNFADLALEVSRMVEGSYALLV 196
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
12-210 |
3.64e-09 |
|
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; Asparagine synthetase B (glutamine-hydrolyzing) is part of the Pathway/BioSystem: Asparagine biosynthesis
Pssm-ID: 440136 [Multi-domain] Cd Length: 558 Bit Score: 59.08 E-value: 3.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 12 CGVFGCIasgDWPTQLDvPHVITLGLVGLQHRGQESAGIVTSDGssvpkfrvhkgmglvnhvftednlkklyvsnLGIGH 91
Cdd:COG0367 2 CGIAGII---DFDGGAD-REVLERMLDALAHRGPDGSGIWVDGG-------------------------------VALGH 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 92 TRYATTGKCELENcQPFVVETlhGKIAVAHNGELVNAARLRKKLLRHGIGLSTSSDSEMItqLLAYtppqeQDDTPDWVA 171
Cdd:COG0367 47 RRLSIIDLSEGGH-QPMVSED--GRYVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVI--LHAY-----EEWGEDCLE 116
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 17105352 172 RIkNLMkeapaaYSLVI--MHRDVIYAVRDPYGNRPLCIGR 210
Cdd:COG0367 117 RL-NGM------FAFAIwdRRERRLFLARDRFGIKPLYYAE 150
|
|
| PLN02549 |
PLN02549 |
asparagine synthase (glutamine-hydrolyzing) |
12-209 |
1.42e-06 |
|
asparagine synthase (glutamine-hydrolyzing)
Pssm-ID: 178164 [Multi-domain] Cd Length: 578 Bit Score: 50.92 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 12 CGVFGCIASGDWPTQLDVpHVITLGlVGLQHRGQESAGIvtsdgssvpkfRVHKGMGLVnhvftednlkklyvsnlgigH 91
Cdd:PLN02549 2 CGILAVLGCSDDSQAKRS-RVLELS-RRLRHRGPDWSGL-----------YGNEDCYLA--------------------H 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 92 TRYA----TTGKcelencQPFVVETlhGKIAVAHNGELVNAARLRKKLLRHgiGLSTSSDSEMITQLLAYTPPqeqddtp 167
Cdd:PLN02549 49 ERLAimdpESGD------QPLYNED--KTIVVTANGEIYNHKELREKLKLH--KFRTGSDCEVIAHLYEEHGE------- 111
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 17105352 168 dwvarikNLMKEAPAAYSLVIM--HRDVIYAVRDPYGNRPLCIG 209
Cdd:PLN02549 112 -------EFVDMLDGMFSFVLLdtRDNSFIAARDHIGITPLYIG 148
|
|
| PRK02277 |
PRK02277 |
orotate phosphoribosyltransferase-like protein; Provisional |
370-417 |
4.09e-06 |
|
orotate phosphoribosyltransferase-like protein; Provisional
Pssm-ID: 235023 [Multi-domain] Cd Length: 200 Bit Score: 47.56 E-value: 4.09e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 17105352 370 AKKFGVLSDNF---KGKRIVLIDDSIVRGNTISPIIKLLKESGAKEVHIRV 417
Cdd:PRK02277 125 EKKTGSFSRNFasvEGKRCVIVDDVITSGTTMKETIEYLKEHGGKPVAVVV 175
|
|
| PRK07322 |
PRK07322 |
adenine phosphoribosyltransferase; Provisional |
307-413 |
1.51e-05 |
|
adenine phosphoribosyltransferase; Provisional
Pssm-ID: 180928 Cd Length: 178 Bit Score: 45.74 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 307 GQQLAVEAPVEADLVSTVPESATPAALGYATKCGLPYVeVLCKNR--YVGRTFIQPNMRLrQLGVAKKF---GVLSDNFK 381
Cdd:PRK07322 42 AEALAKRLPTEVDVLVTPETKGIPLAHALSRRLGKPYV-VARKSRkpYMQDPIIQEVVSI-TTGKPQLLvldGADAEKLK 119
|
90 100 110
....*....|....*....|....*....|..
gi 17105352 382 GKRIVLIDDSIVRGNTISPIIKLLKESGAKEV 413
Cdd:PRK07322 120 GKRVAIVDDVVSTGGTLTALERLVERAGGQVV 151
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
89-210 |
2.81e-05 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 46.63 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 89 IGHTRYA----TTGKcelencQPFVVETlhGKIAVAHNGELVNAARLRKKLLRHGIGLSTSSDSEMITQLLaytppqEQD 164
Cdd:PTZ00077 51 LAHERLAivdlSDGK------QPLLDDD--ETVALMQNGEIYNHWEIRPELEKEGYKFSSNSDCEIIGHLY------KEY 116
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 17105352 165 DTPDWVARIKNLmkeapaaYSLVI--MHRDVIYAVRDPYGNRPLCIGR 210
Cdd:PTZ00077 117 GPKDFWNHLDGM-------FATVIydMKTNTFFAARDHIGIIPLYIGY 157
|
|
| GATase_4 |
pfam13230 |
Glutamine amidotransferases class-II; This family captures members that are not found in ... |
85-151 |
4.78e-05 |
|
Glutamine amidotransferases class-II; This family captures members that are not found in pfam00310.
Pssm-ID: 433047 [Multi-domain] Cd Length: 272 Bit Score: 45.01 E-value: 4.78e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 85 SNLGIGHTRYATTGKCELENCQPFVVEtLHGK-IAVAHNGELvnaARLRKKLLR--HGIGlstSSDSEMI 151
Cdd:pfam13230 71 SRNVIAHIRKATQGRVTLENTHPFMRE-LWGRyWIFAHNGDL---KGYAPKLSGrfQPVG---STDSELA 133
|
|
| PRK00934 |
PRK00934 |
ribose-phosphate pyrophosphokinase; Provisional |
381-415 |
1.42e-04 |
|
ribose-phosphate pyrophosphokinase; Provisional
Pssm-ID: 234868 [Multi-domain] Cd Length: 285 Bit Score: 43.75 E-value: 1.42e-04
10 20 30
....*....|....*....|....*....|....*
gi 17105352 381 KGKRIVLIDDSIVRGNTISPIIKLLKESGAKEVHI 415
Cdd:PRK00934 203 KGKDVLIVDDIISTGGTMATAIKILKEQGAKKVYV 237
|
|
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
12-210 |
3.89e-04 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 42.97 E-value: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 12 CGVFGCIASGDwPTQLDVPHVITLgLVGLQHRGQESAGIVTSDGssvpkfrvhkgmglvnhvftednlkklyvsnlGI-G 90
Cdd:PRK09431 2 CGIFGILDIKT-DADELRKKALEM-SRLMRHRGPDWSGIYASDN--------------------------------AIlG 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 91 HTRYA----TTGKcelencQPFVVEtlHGKIAVAHNGELVNAARLRKKLLRhGIGLSTSSDSEMITQLlaYtppqeQDDT 166
Cdd:PRK09431 48 HERLSivdvNGGA------QPLYNE--DGTHVLAVNGEIYNHQELRAELGD-KYAFQTGSDCEVILAL--Y-----QEKG 111
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 17105352 167 PDWVARIknlmkEAPAAYSLVIMHRDVIYAVRDPYGNRPLCIGR 210
Cdd:PRK09431 112 PDFLDDL-----DGMFAFALYDSEKDAYLIARDPIGIIPLYYGY 150
|
|
| PRK02812 |
PRK02812 |
ribose-phosphate pyrophosphokinase; Provisional |
369-421 |
4.07e-04 |
|
ribose-phosphate pyrophosphokinase; Provisional
Pssm-ID: 235072 [Multi-domain] Cd Length: 330 Bit Score: 42.42 E-value: 4.07e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 17105352 369 VAKKFGVLSDnFKGKRIVLIDDSIVRGNTISPIIKLLKESGAKEVHI----RVASPP 421
Cdd:PRK02812 218 VAEVLNVIGD-VKGKTAILVDDMIDTGGTICEGARLLRKEGAKQVYAcathAVFSPP 273
|
|
| PrsA |
COG0462 |
Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; ... |
381-429 |
5.66e-04 |
|
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: 41.97 E-value: 5.66e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 17105352 381 KGKRIVLIDDSIVRGNTISPIIKLLKESGAKEVHIrVASppikHPCFMG 429
Cdd:COG0462 210 EGKTCIIVDDMIDTGGTLVEAAEALKEAGAKSVYA-AAT----HGVLSG 253
|
|
| Hpt1 |
COG2236 |
Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine ... |
374-415 |
1.21e-03 |
|
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: 39.44 E-value: 1.21e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 17105352 374 GVLSDNFKGKRIVLIDDSIVRGNTISPIIKLLKESGAKEVHI 415
Cdd:COG2236 80 GPLDEDLAGKRVLIVDDVADTGRTLEAVRDLLKEAGPAEVRT 121
|
|
| PRK09162 |
PRK09162 |
hypoxanthine-guanine phosphoribosyltransferase; Provisional |
379-433 |
1.60e-03 |
|
hypoxanthine-guanine phosphoribosyltransferase; Provisional
Pssm-ID: 181675 Cd Length: 181 Bit Score: 39.46 E-value: 1.60e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17105352 379 NFKGKRIVLIDDSIVRGNTISPIIKLLKESGAKEVHIRV--------ASPPIkHPCFMGINIP 433
Cdd:PRK09162 94 SLKGRTVLVVDDILDEGHTLAAIRDRCLEMGAAEVYSAVlvdkthdrKAKPL-KADFVGLEVP 155
|
|
| Pribosyltran |
pfam00156 |
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ... |
379-415 |
2.68e-03 |
|
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: 38.50 E-value: 2.68e-03
10 20 30
....*....|....*....|....*....|....*..
gi 17105352 379 NFKGKRIVLIDDSIVRGNTISPIIKLLKESGAKEVHI 415
Cdd:pfam00156 79 DLKGKTVLIVDDILDTGGTLLKVLELLKNVGPKEVKI 115
|
|
| GltS |
cd00713 |
Glutamine amidotransferases class-II (Gn-AT), glutamate synthase (GltS)-type. GltS is a ... |
63-138 |
4.92e-03 |
|
Glutamine amidotransferases class-II (Gn-AT), glutamate synthase (GltS)-type. GltS is a homodimer that synthesizes L-glutamate from 2-oxoglutarate and L-glutamine, an important step in ammonia assimilation in bacteria, cyanobacteria and plants. The N-terminal glutaminase domain catalyzes the hydrolysis of glutamine to glutamic acid and ammonia, and has a fold similar to that of other glutamine amidotransferases such as glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), and beta lactam synthetase (beta-LS), as well as the Ntn hydrolase folds of the proteasomal alpha and beta subunits.
Pssm-ID: 238365 [Multi-domain] Cd Length: 413 Bit Score: 39.43 E-value: 4.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17105352 63 VHKGMGLVNHV--FTEDNLKKLYVSNLGIGHTRYATT--GKCELenCQPFVVetlhgkiaVAHNGE------LVNAARLR 132
Cdd:cd00713 177 VYKGMLLPEQLgqFYPDLQDPRFESAFALVHSRFSTNtfPSWPL--AQPFRY--------LAHNGEintirgNRNWMRAR 246
|
....*.
gi 17105352 133 KKLLRH 138
Cdd:cd00713 247 EGLLKS 252
|
|
| |
