|
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: 649.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 7 GIREECGVFGCIASGDwptqldVPHVITLGLVGLQHRGQESAGIVTSDGSavpKFRVHKGMGLVNHVFTEDNLKKLyDSN 86
Cdd:COG0034 3 KLHEECGVFGIYGHED------VAQLTYYGLYALQHRGQESAGIATSDGG---RFHLHKGMGLVSDVFDEEDLERL-KGN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 87 LGIGHTRYATTGKCELENCQPFVVETLHGKIAVAHNGELVNAARLRKKLLRQGIGLSTSSDSEMITQLLAYtppqeKDDA 166
Cdd:COG0034 73 IAIGHVRYSTTGSSSLENAQPFYVNSPFGSIALAHNGNLTNAEELREELEEEGAIFQTTSDTEVILHLIAR-----ELTK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 167 PDWVARIKNLMKEAPAAYSLVIMHRDFIYAVRDPYGNRPLCIGRLmpvsdvndkekksseTEGWVVSSESCSFLSIGARY 246
Cdd:COG0034 148 EDLEEAIKEALRRVKGAYSLVILTGDGLIAARDPNGIRPLVLGKL---------------EDGYVVASESCALDILGAEF 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 247 CHEVKPGEIVEISRHGIRTLDIIPRSngdPVAFCIFEYVYFARPDSMFEDQMVYTVRYRCGQQLAIEAPVEADLVSTVPE 326
Cdd:COG0034 213 VRDVEPGEIVVIDEDGLRSRQFAEKP---RPAPCIFEYVYFARPDSVIDGRSVYEARKRMGRELAREAPVDADVVIPVPD 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 327 SATPAALGYATKCGLPYVEVLCKNRYVGRTFIQPNMRLRQLGVAKKFGVLSDNFKGKRIVLIDDSIVRGNTISPIIKLLK 406
Cdd:COG0034 290 SGRPAAIGYAEESGIPYEEGLIKNRYVGRTFIQPTQELRELGVRLKLNPIREVVKGKRVVLVDDSIVRGTTSRRIVKMLR 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 407 ESGAKEVHIRVASPPIKYPCFMGINIPTKEELIANKPEFDCLAEYLGANSVVYLSVEGLVSSVQQEIkfkkqkvkkhdia 486
Cdd:COG0034 370 EAGAKEVHFRIASPPIRYPCYYGIDTPTREELIAANRSVEEIREYIGADSLGYLSLEGLIEAVGEPI------------- 436
|
490 500 510
....*....|....*....|....*....|
gi 26024309 487 iqengngleyfekTGHCTACLTGQYPVELE 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: 533.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 12 CGVFGCiasgdWPTQLDVPHVITLGLVGLQHRGQESAGIVTSDGSavpKFRVHKGMGLVNHVFTEDNLKKLyDSNLGIGH 91
Cdd:TIGR01134 1 CGVVGI-----YGQEEVAASLTYYGLYALQHRGQESAGISVFDGN---RFRLHKGNGLVSDVFNEEHLQRL-KGNVGIGH 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 92 TRYATTGKCELENCQPFVVETLHGKIAVAHNGELVNAARLRKKLLRQGIGLSTSSDSEMITQLLAYTPPQEKDDapdwVA 171
Cdd:TIGR01134 72 VRYSTAGSSGLENAQPFVVNSPYGGLALAHNGNLVNADELRRELEEEGRHFNTTSDSEVLLHLLAHNDESKDDL----FD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 172 RIKNLMKEAPAAYSLVIMHRDFIYAVRDPYGNRPLCIGRLmpvsdvndkekksseTEGWVVSSESCSFLSIGARYCHEVK 251
Cdd:TIGR01134 148 AVARVLERVRGAYALVLMTEDGLVAVRDPHGIRPLVLGRR---------------GDGYVVASESCALDILGAEFVRDVE 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 252 PGEIVEISRHGIRTLdiipRSNGDPVAFCIFEYVYFARPDSMFEDQMVYTVRYRCGQQLAIEAPVEADLVSTVPESATPA 331
Cdd:TIGR01134 213 PGEVVVIFDGGLESR----QCARRPRAPCVFEYVYFARPDSVIDGISVYYARKRMGKELARESPVEADVVVPVPDSGRSA 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 332 ALGYATKCGLPYVEVLCKNRYVGRTFIQPNMRLRQLGVAKKFGVLSDNFKGKRIVLIDDSIVRGNTISPIIKLLKESGAK 411
Cdd:TIGR01134 289 ALGFAQASGIPYREGLIKNRYVGRTFIMPTQELRELSVRLKLNPVRAVFEGKRVVLVDDSIVRGTTSRQIVEMLRDAGAK 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 412 EVHIRVASPPIKYPCFMGINIPTKEELIANKPEFDcLAEYLGANSVVYLSVEGLVSSVQQEIKfkkqkvkkhdiaiqeng 491
Cdd:TIGR01134 369 EVHVRIASPPIRYPCYYGIDMPTREELIAARRTVE-EIRKIGADSLAYLSLEGLKEAVGNPES----------------- 430
|
490 500
....*....|....*....|.
gi 26024309 492 ngleyfektGHCTACLTGQYP 512
Cdd:TIGR01134 431 ---------DLCLACFTGEYP 442
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
1-514 |
2.50e-178 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 509.58 E-value: 2.50e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 1 MELEELGIREECGVFGCIAsgdwPTQLDVPHVITLGLVGLQHRGQESAGIVTSDGSavpKFRVHKGMGLVNHVFTEDNLK 80
Cdd:PRK05793 4 MDLEGDKFKEECGVFGVFS----KNNIDVASLTYYGLYALQHRGQESAGIAVSDGE---KIKVHKGMGLVSEVFSKEKLK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 81 KLyDSNLGIGHTRYATTGKCELENCQPFVVETLHGKIAVAHNGELVNAARLRKKLLRQGIGLSTSSDSEMITQLLAYTPP 160
Cdd:PRK05793 77 GL-KGNSAIGHVRYSTTGASDLDNAQPLVANYKLGSIAIAHNGNLVNADVIRELLEDGGRIFQTSIDSEVILNLIARSAK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 161 QEKDDApdwvarIKNLMKEAPAAYSLVIMHRDFIYAVRDPYGNRPLCIGRLmpvsdvndkekksseTEGWVVSSESCSFL 240
Cdd:PRK05793 156 KGLEKA------LVDAIQAIKGSYALVILTEDKLIGVRDPHGIRPLCLGKL---------------GDDYILSSESCALD 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 241 SIGARYCHEVKPGEIVEISRHGIRTLDIIPRSNGDPvafCIFEYVYFARPDSMFEDQMVYTVRYRCGQQLAIEAPVEADL 320
Cdd:PRK05793 215 TIGAEFIRDVEPGEIVIIDEDGIKSIKFAEKTKCQT---CAFEYIYFARPDSVIDGISVYESRVRAGRQLYKEYPVDADI 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 321 VSTVPESATPAALGYATKCGLPYVEVLCKNRYVGRTFIQPNMRLRQLGVAKKFGVLSDNFKGKRIVLIDDSIVRGNTISP 400
Cdd:PRK05793 292 VIGVPDSGIPAAIGYAEASGIPYGIGFIKNKYVGRTFIAPSQELRERAVRVKLNPLKVNVEGKRVVLIDDSIVRGTTSKR 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 401 IIKLLKESGAKEVHIRVASPPIKYPCFMGINIPTKEELIANKPEFDCLAEYLGANSVVYLSVEGLVSSVQqeikfkkqkv 480
Cdd:PRK05793 372 LVELLRKAGAKEVHFRVSSPPVKYPCYFGIDTPYRKELIGANMSVEEIREMIGADSLGYLSIEGLLESLN---------- 441
|
490 500 510
....*....|....*....|....*....|....
gi 26024309 481 kkhdiaiqengngleyfEKTGHCTACLTGQYPVE 514
Cdd:PRK05793 442 -----------------GDKGFCLGCFNGVYPVS 458
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
11-514 |
2.28e-156 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 454.14 E-value: 2.28e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 11 ECGVFGCIASGDwptqldVPHVITLGLVGLQHRGQESAGIVTSDGSavpKFRVHKGMGLVNHVFTEDNLKKLyDSNLGIG 90
Cdd:PLN02440 1 ECGVVGIFGDPE------ASRLCYLGLHALQHRGQEGAGIVTVDGN---RLQSITGNGLVSDVFDESKLDQL-PGDIAIG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 91 HTRYATTGKCELENCQPFVVETLHGKIAVAHNGELVNAARLRKKLLRQGIGLSTSSDSEMITQLLAytppqeKDDAPDWV 170
Cdd:PLN02440 71 HVRYSTAGASSLKNVQPFVANYRFGSIGVAHNGNLVNYEELRAKLEENGSIFNTSSDTEVLLHLIA------ISKARPFF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 171 ARIKNLMKEAPAAYSLVIMHRDFIYAVRDPYGNRPLCIGRlmpvsdvndkeKKSSEtegWVVSSESCSFLSIGARYCHEV 250
Cdd:PLN02440 145 SRIVDACEKLKGAYSMVFLTEDKLVAVRDPHGFRPLVMGR-----------RSNGA---VVFASETCALDLIGATYEREV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 251 KPGEIVEISR-HGIRTLDIIPRSNGDPvafCIFEYVYFARPDSMFEDQMVYTVRYRCGQQLAIEAPVEADLVSTVPESAT 329
Cdd:PLN02440 211 NPGEVIVVDKdKGVSSQCLMPHPEPKP---CIFEHIYFARPNSIVFGRSVYESRLEFGEILATEIPVDCDVVIPVPDSGR 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 330 PAALGYATKCGLPYVEVLCKNRYVGRTFIQPNMRLRQLGVAKKFGVLSDNFKGKRIVLIDDSIVRGNTISPIIKLLKESG 409
Cdd:PLN02440 288 VAALGYAAKLGVPFQQGLIRSHYVGRTFIEPSQKIRDFSVKLKLNPVRSVLEGKRVVVVDDSIVRGTTSSKIVRMLREAG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 410 AKEVHIRVASPPIKYPCFMGINIPTKEELIANKPEFDCLAEYLGANSVVYLSVEGLVSSVQQeikfkkqkvkkhdiaiqe 489
Cdd:PLN02440 368 AKEVHMRIASPPIIASCYYGVDTPSREELISNRMSVEEIRKFIGCDSLAFLPLEDLKKSLGE------------------ 429
|
490 500
....*....|....*....|....*
gi 26024309 490 ngngleyfEKTGHCTACLTGQYPVE 514
Cdd:PLN02440 430 --------ESPRFCYACFSGDYPVL 446
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
12-295 |
4.27e-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: 398.76 E-value: 4.27e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 12 CGVFGCIASGDwptqldVPHVITLGLVGLQHRGQESAGIVTSDGSavpKFRVHKGMGLVNHVFTEDNLKKLyDSNLGIGH 91
Cdd:cd00715 1 CGVFGIYGAED------AARLTYLGLYALQHRGQESAGIATSDGK---RFHTHKGMGLVSDVFDEEKLRRL-PGNIAIGH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 92 TRYATTGKCELENCQPFVVETLHGKIAVAHNGELVNAARLRKKLLRQGIGLSTSSDSEMITQLLAYTPpqekdDAPDWVA 171
Cdd:cd00715 71 VRYSTAGSSSLENAQPFVVNSPLGGIALAHNGNLVNAKELREELEEEGRIFQTTSDSEVILHLIARSL-----AKDDLFE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 172 RIKNLMKEAPAAYSLVIMHRDFIYAVRDPYGNRPLCIGRLmpvsdvndkekkssETEGWVVSSESCSFLSIGARYCHEVK 251
Cdd:cd00715 146 AIIDALERVKGAYSLVIMTADGLIAVRDPHGIRPLVLGKL--------------EGDGYVVASESCALDIIGAEFVRDVE 211
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 26024309 252 PGEIVEISRHGIRTLDIIPRsngDPVAFCIFEYVYFARPDSMFE 295
Cdd:cd00715 212 PGEIVVIDDDGLESSQRAPK---PKPAPCIFEYVYFARPDSVID 252
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
12-256 |
3.93e-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: 194.97 E-value: 3.93e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 12 CGVFGCIASGDWPTQLDVPHviTLGLVGLQHRGQESAGIVTSDGSavpKFRVHKGMGLVNHVFtEDNLKKLYDSNLGIGH 91
Cdd:cd00352 1 CGIFGIVGADGAASLLLLLL--LRGLAALEHRGPDGAGIAVYDGD---GLFVEKRAGPVSDVA-LDLLDEPLKSGVALGH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 92 TRYATTGKCELENCQPFVVETlhGKIAVAHNGELVNAARLRKKLLRQGIGLSTSSDSEMITQLLAYTPpqekdDAPDWVA 171
Cdd:cd00352 75 VRLATNGLPSEANAQPFRSED--GRIALVHNGEIYNYRELREELEARGYRFEGESDSEVILHLLERLG-----REGGLFE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 172 RIKNLMKEAPAAYSLVIM--HRDFIYAVRDPYGNRPLCIGRlmpvsdvndkekksSETEGWVVSSESCSFLSIGARYCHE 249
Cdd:cd00352 148 AVEDALKRLDGPFAFALWdgKPDRLFAARDRFGIRPLYYGI--------------TKDGGLVFASEPKALLALPFKGVRR 213
|
....*..
gi 26024309 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 ... |
12-209 |
1.88e-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: 109.46 E-value: 1.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 12 CGVFGCIASGDwptqlDVPHVITlGLVGLQHRGQESAGI-VTSDGSavpkFRVHKGMGLVnhvfteDNLKKLY-----DS 85
Cdd:cd00714 1 CGIVGYIGKRE-----AVDILLE-GLKRLEYRGYDSAGIaVIGDGS----LEVVKAVGKV------ANLEEKLaekplSG 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 86 NLGIGHTRYATTGKCELENCQPFVVETlhGKIAVAHNGELVNAARLRKKLLRQGIGLSTSSDSEMITQLLAYtppqEKDD 165
Cdd:cd00714 65 HVGIGHTRWATHGEPTDVNAHPHRSCD--GEIAVVHNGIIENYAELKEELEAKGYKFESETDTEVIAHLIEY----YYDG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 26024309 166 APDWVARIKNLMKEAPAAYSLVIMHRDF---IYAVRDpygNRPLCIG 209
Cdd:cd00714 139 GLDLLEAVKKALKRLEGAYALAVISKDEpdeIVAARN---GSPLVIG 182
|
|
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
12-277 |
6.31e-22 |
|
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase domains [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440218 [Multi-domain] Cd Length: 610 Bit Score: 99.32 E-value: 6.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 12 CGVFGCIASGDwptqldVPHVITLGLVGLQHRGQESAGIVTSDGSavpKFRVHKGMGLVnhvfteDNLKKLYD-----SN 86
Cdd:COG0449 2 CGIVGYIGKRD------AAPILLEGLKRLEYRGYDSAGIAVLDDG---GLEVRKAVGKL------ANLEEKLAeeplsGT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 87 LGIGHTRYATTGKCELENCQPFVVETlhGKIAVAHNG--ElvNAARLRKKLLRQGIGLSTSSDSEMITQLLAYtppqEKD 164
Cdd:COG0449 67 IGIGHTRWATHGAPSDENAHPHTSCS--GRIAVVHNGiiE--NYAELREELEAKGHTFKSETDTEVIAHLIEE----YLK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 165 DAPDWVARIKNLMKEAPAAYSLVIMHRDF---IYAVRdpYGNrPLCIGrlmpvsdVNDKEkkssetegWVVSSESCSFLS 241
Cdd:COG0449 139 GGGDLLEAVRKALKRLEGAYALAVISADEpdrIVAAR--KGS-PLVIG-------LGEGE--------NFLASDVPALLP 200
|
250 260 270
....*....|....*....|....*....|....*....
gi 26024309 242 igarYCHEV---KPGEIVEISRHGIRTLDIiprsNGDPV 277
Cdd:COG0449 201 ----YTRRViylEDGEIAVLTRDGVEIYDL----DGEPV 231
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
12-266 |
1.95e-20 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 94.70 E-value: 1.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 12 CGVFGCIASGDwptqldVPHVITLGLVGLQHRGQESAGIVTsdgsavpkfrVHKGMGLVNHVF-----TEDNLKKLYD-- 84
Cdd:PTZ00295 25 CGIVGYLGNED------ASKILLEGIEILQNRGYDSCGIST----------ISSGGELKTTKYasdgtTSDSIEILKEkl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 85 ------SNLGIGHTRYATTGKCELENCQPFVveTLHGKIAVAHNGELVNAARLRKKLLRQGIGLSTSSDSEMITQLLAYt 158
Cdd:PTZ00295 89 ldshknSTIGIAHTRWATHGGKTDENAHPHC--DYKKRIALVHNGTIENYVELKSELIAKGIKFRSETDSEVIANLIGL- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 159 ppqEKDDAPDWVARIKNLMKEAPAAYSLVIMHRDF---IYAVRDpygNRPLCIGRlmpvsdvndkekkssETEGWVVSSE 235
Cdd:PTZ00295 166 ---ELDQGEDFQEAVKSAISRLQGTWGLCIIHKDNpdsLIVARN---GSPLLVGI---------------GDDSIYVASE 224
|
250 260 270
....*....|....*....|....*....|....
gi 26024309 236 SCSFlsigARYCHE---VKPGEIVEISRHGIRTL 266
Cdd:PTZ00295 225 PSAF----AKYTNEyisLKDGEIAELSLENVNDL 254
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
12-283 |
6.17e-19 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 90.10 E-value: 6.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 12 CGVFGCIAsgdwptQLDVPHVITLGLVGLQHRGQESAGIVTSDGSAVpkfRVHKGMGLVnhvfteDNLKKLYDS-----N 86
Cdd:PRK00331 2 CGIVGYVG------QRNAAEILLEGLKRLEYRGYDSAGIAVLDDGGL---EVRKAVGKV------ANLEAKLEEeplpgT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 87 LGIGHTRYATTGKCELENCQPFVVETlhGKIAVAHNGELVNAARLRKKLLRQGIGLSTSSDSEMITQLLAYtppqEKDDA 166
Cdd:PRK00331 67 TGIGHTRWATHGKPTERNAHPHTDCS--GRIAVVHNGIIENYAELKEELLAKGHVFKSETDTEVIAHLIEE----ELKEG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 167 PDWVARIKNLMKEAPAAYSLVIMHRDF---IYAVRDpygNRPLCIGrlmpvsdVNDKEkkssetegWVVSSESCSFLSig 243
Cdd:PRK00331 141 GDLLEAVRKALKRLEGAYALAVIDKDEpdtIVAARN---GSPLVIG-------LGEGE--------NFLASDALALLP-- 200
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 26024309 244 arYCHEVKP---GEIVEISRHGIRTLDIiprsNGDPVAFCIFE 283
Cdd:PRK00331 201 --YTRRVIYledGEIAVLTRDGVEIFDF----DGNPVEREVYT 237
|
|
| PRTases_typeI |
cd06223 |
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ... |
306-442 |
7.15e-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: 7.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 306 CGQQLAIEAP---VEADLVSTVPESATPAALGYATKCGLPYVEVLCKNRYVGRTFIQPNmrlrqlgvaKKFGVLSDNFKG 382
Cdd:cd06223 1 AGRLLAEEIRedlLEPDVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSEPY---------GLELPLGGDVKG 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 383 KRIVLIDDSIVRGNTISPIIKLLKESGAKEVHIRVAsPPIKYPCFMGINIPTKEELIANK 442
Cdd:cd06223 72 KRVLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVL-LDKPEGGARELASPGDPVYSLFT 130
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
82-211 |
2.57e-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: 75.42 E-value: 2.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 82 LYDSNLGIGHTRYATTGKCELENcQPFVVETlhGKIAVAHNGELVNAARLRKKLLRQGIGLSTSSDSEMITQLLAYTPpq 161
Cdd:pfam13522 7 WVEGGVALGHVRLAIVDLPDAGN-QPMLSRD--GRLVLVHNGEIYNYGELREELADLGHAFRSRSDTEVLLALYEEWG-- 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 26024309 162 ekddaPDWVARIKNLMkeAPAAYSlVIMHRDFIyaVRDPYGNRPLCIGRL 211
Cdd:pfam13522 82 -----EDCLERLRGMF--AFAIWD-RRRRTLFL--ARDRLGIKPLYYGIL 121
|
|
| YafJ |
cd01908 |
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ... |
85-261 |
2.33e-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: 75.89 E-value: 2.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 85 SNLGIGHTRYATTGKCELENCQPFVvetlHGKIAVAHNGELVNAARLRKKLLR---QGIGLSTssDSEM----ITQLLAY 157
Cdd:cd01908 80 SPLVLAHVRAATVGPVSLENCHPFT----RGRWLFAHNGQLDGFRLLRRRLLRllpRLPVGTT--DSELafalLLSRLLE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 158 TPPQEKDDAPDWVAR-IKNLMKEA-PAAYSLVIMHRDFIYAVRDPYGNRP--LCIGRLMPVSDVNDKEKKSSETEGWVVS 233
Cdd:cd01908 154 RDPLDPAELLDAILQtLRELAALApPGRLNLLLSDGEYLIATRYASAPSLyyLTRRAPFGCARLLFRSVTTPNDDGVVVA 233
|
170 180
....*....|....*....|....*...
gi 26024309 234 SESCSFlsigARYCHEVKPGEIVEISRH 261
Cdd:cd01908 234 SEPLTD----DEGWTEVPPGELVVVSEG 257
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
12-256 |
4.52e-15 |
|
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: 75.00 E-value: 4.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 12 CGVFGCIASGDWPtqlDVPHVITLGLVGLQHRG-QESAGIVTSDG------SAVPKFRVHKGMGLVNHVFTEDNLKKlYD 84
Cdd:cd01907 1 CGIFGIMSKDGEP---FVGALLVEMLDAMQERGpGDGAGFALYGDpdafvySSGKDMEVFKGVGYPEDIARRYDLEE-YK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 85 SNLGIGHTRYATTGKCELENCQPFVVetlhGKIAVAHNGELVNAARLRKKLLRQGIGLSTSSDSEMITQLLAYT------ 158
Cdd:cd01907 77 GYHWIAHTRQPTNSAVWWYGAHPFSI----GDIAVVHNGEISNYGSNREYLERFGYKFETETDTEVIAYYLDLLlrkggl 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 159 ----------PPQEKDDAPDWVARI-KNLMKEAPaaYSLVIMHRDFIYAVRDPYGNRPLCIGrlmpvsdvndkekkssET 227
Cdd:cd01907 153 pleyykhiirMPEEERELLLALRLTyRLADLDGP--FTIIVGTPDGFIVIRDRIKLRPAVVA----------------ET 214
|
250 260 270
....*....|....*....|....*....|...
gi 26024309 228 EGWV-VSSESCSFLSIGARYCHEV---KPGEIV 256
Cdd:cd01907 215 DDYVaIASEECAIREIPDRDNAKVwepRPGEYV 247
|
|
| YafJ |
COG0121 |
Predicted glutamine amidotransferase YafJ [General function prediction only]; |
20-260 |
2.42e-14 |
|
Predicted glutamine amidotransferase YafJ [General function prediction only];
Pssm-ID: 439891 [Multi-domain] Cd Length: 248 Bit Score: 72.69 E-value: 2.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 20 SGDWPTQLDvpHVITLGLVGLQHRGQESAGIVTSDG------SAVPKFRVHKGmglVNHVFTEDNLKKL---YDSNLGIG 90
Cdd:COG0121 7 SGNVPTDLE--FLLLDPEHSLVRQSGATREGPHADGwgigwyEGDGEPRLYRD---PLPAWSDPNLRLLarpIKSRLVIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 91 HTRYATTGKCELENCQPFVvetlHGKIAVAHNGELVNAARLRKKL-------LRQGIGLSTssDSE----MITQLLAYTP 159
Cdd:COG0121 82 HVRKATVGPVSLENTHPFR----GGRWLFAHNGQLDGFDRLRRRLaeelpdeLYFQPVGTT--DSElafaLLLSRLRDGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 160 PQEKDDAPDWVARIKNLMKeAPAAYSLVIMHRDFIYAVRDPYGNRP--LCIGRLMPVSDvndkekkssetEGWVVSSESc 237
Cdd:COG0121 156 PDPAEALAEALRELAELAR-APGRLNLLLSDGERLYATRYTSDDPYptLYYLTRTTPDD-----------RVVVVASEP- 222
|
250 260
....*....|....*....|...
gi 26024309 238 sfLSIGARYcHEVKPGEIVEISR 260
Cdd:COG0121 223 --LTDDEGW-TEVPPGELLVVRD 242
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
12-265 |
2.31e-13 |
|
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: 69.12 E-value: 2.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 12 CGVFGCIasgDWPTQLDVPHVITLGLVGLQHRGQESAGIVTsdgsavpkfrvhkgmglvnhvftednlkklyDSNLGIGH 91
Cdd:cd00712 1 CGIAGII---GLDGASVDRATLERMLDALAHRGPDGSGIWI-------------------------------DEGVALGH 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 92 TRYATTGkceLEN-CQPFVVETlhGKIAVAHNGELVNAARLRKKLLRQGIGLSTSSDSEMItqLLAYtppQEKDdaPDWV 170
Cdd:cd00712 47 RRLSIID---LSGgAQPMVSED--GRLVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVI--LHLY---EEWG--EDCL 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 171 ARIkNLMkeapaaYSLVI--MHRDFIYAVRDPYGNRPL----------------CIGRLMPVSDVNDKEKKSSETEGWVV 232
Cdd:cd00712 115 ERL-NGM------FAFALwdKRKRRLFLARDRFGIKPLyygrdggglafaselkALLALPGVPRELDEAALAEYLAFQYV 187
|
250 260 270
....*....|....*....|....*....|...
gi 26024309 233 SSESCSFLSIgarycHEVKPGEIVEISRHGIRT 265
Cdd:cd00712 188 PAPRTIFKGI-----RKLPPGHYLTVDPGGVEI 215
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
106-240 |
1.11e-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: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 106 QPFVVETLhGKIAVAHNGELVNAARLRKKLLRQGIGLSTSSDSEMITQLLaytppqEKDDAPDWVARIkNLMkeapaaYS 185
Cdd:pfam13537 14 QPMVSSED-GRYVIVFNGEIYNYRELRAELEAKGYRFRTHSDTEVILHLY------EAEWGEDCVDRL-NGM------FA 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 26024309 186 LVIM--HRDFIYAVRDPYGNRPLCIGRlmpvsdvndkekksSETEGWVVSSESCSFL 240
Cdd:pfam13537 80 FAIWdrRRQRLFLARDRFGIKPLYYGR--------------DDGGRLLFASELKALL 122
|
|
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
12-187 |
2.78e-12 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 69.39 E-value: 2.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 12 CGVFGCIASGDWPTQLDVPHVITLGLVGLQHRGQESAGIVTSDGSAVPKFR--VHKGMG----LVNHVF-----TEDNLK 80
Cdd:PLN02981 2 CGIFAYLNYNVPRERRFILEVLFNGLRRLEYRGYDSAGIAIDNDPSLESSSplVFREEGkiesLVRSVYeevaeTDLNLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 81 KLYDSNLGIGHTRYATTGKCELENCQPFVVETlHGKIAVAHNGELVNAARLRKKLLRQGIGLSTSSDSEMITQLLAYTPP 160
Cdd:PLN02981 82 LVFENHAGIAHTRWATHGPPAPRNSHPQSSGP-GNEFLVVHNGIITNYEVLKETLLRHGFTFESDTDTEVIPKLAKFVFD 160
|
170 180
....*....|....*....|....*....
gi 26024309 161 QEKDDAPDWVAR--IKNLMKEAPAAYSLV 187
Cdd:PLN02981 161 KLNEEEGDVTFSqvVMEVMRQLEGAYALI 189
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
12-188 |
1.00e-10 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 64.13 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 12 CGVFGCIASGDWPTQLDVPHVITLGLVGLQHRGQESAGIV--------TSDGSA--VPKFR--VHKGMGLVNH----VFT 75
Cdd:PTZ00394 2 CGIFGYANHNVPRTVEQILNVLLDGIQKVEYRGYDSAGLAidanigseKEDGTAasAPTPRpcVVRSVGNISQlrekVFS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 76 EDNLKKLYDSN------LGIGHTRYATTGKCELENCQPfvVETLHGKIAVAHNGELVNAARLRKKLLRQGIGLSTSSDSE 149
Cdd:PTZ00394 82 EAVAATLPPMDattshhVGIAHTRWATHGGVCERNCHP--QQSNNGEFTIVHNGIVTNYMTLKELLKEEGYHFSSDTDTE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 26024309 150 MITQLLAYTPPQE-KDDAPDWVARIknlMKEAPAAYSLVI 188
Cdd:PTZ00394 160 VISVLSEYLYTRKgIHNFADLALEV---SRMVEGSYALLV 196
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
84-210 |
9.01e-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: 57.92 E-value: 9.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 84 DSNLGIGHTRYATTGKCELENcQPFVVETlhGKIAVAHNGELVNAARLRKKLLRQGIGLSTSSDSEMItqLLAYtppQEK 163
Cdd:COG0367 39 DGGVALGHRRLSIIDLSEGGH-QPMVSED--GRYVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVI--LHAY---EEW 110
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 26024309 164 DdaPDWVARIkNLMkeapaaYSLVI--MHRDFIYAVRDPYGNRPLCIGR 210
Cdd:COG0367 111 G--EDCLERL-NGM------FAFAIwdRRERRLFLARDRFGIKPLYYAE 150
|
|
| PRK02277 |
PRK02277 |
orotate phosphoribosyltransferase-like protein; Provisional |
370-417 |
3.69e-06 |
|
orotate phosphoribosyltransferase-like protein; Provisional
Pssm-ID: 235023 [Multi-domain] Cd Length: 200 Bit Score: 47.56 E-value: 3.69e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 26024309 370 AKKFGVLSDNF---KGKRIVLIDDSIVRGNTISPIIKLLKESGAKEVHIRV 417
Cdd:PRK02277 125 EKKTGSFSRNFasvEGKRCVIVDDVITSGTTMKETIEYLKEHGGKPVAVVV 175
|
|
| PLN02549 |
PLN02549 |
asparagine synthase (glutamine-hydrolyzing) |
12-209 |
5.93e-06 |
|
asparagine synthase (glutamine-hydrolyzing)
Pssm-ID: 178164 [Multi-domain] Cd Length: 578 Bit Score: 48.99 E-value: 5.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 12 CGVFGCIASGDWPTQLDVpHVITLGlVGLQHRGQESAGIvtsdgsavpkfRVHKGMGLVnhvftednlkklydsnlgigH 91
Cdd:PLN02549 2 CGILAVLGCSDDSQAKRS-RVLELS-RRLRHRGPDWSGL-----------YGNEDCYLA--------------------H 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 92 TRYA----TTGKcelencQPFVVETlhGKIAVAHNGELVNAARLRKKLlrQGIGLSTSSDSEMITQLLaytppqeKDDAP 167
Cdd:PLN02549 49 ERLAimdpESGD------QPLYNED--KTIVVTANGEIYNHKELREKL--KLHKFRTGSDCEVIAHLY-------EEHGE 111
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 26024309 168 DWVariknlmKEAPAAYSLVIM--HRDFIYAVRDPYGNRPLCIG 209
Cdd:PLN02549 112 EFV-------DMLDGMFSFVLLdtRDNSFIAARDHIGITPLYIG 148
|
|
| PRK07322 |
PRK07322 |
adenine phosphoribosyltransferase; Provisional |
307-413 |
1.57e-05 |
|
adenine phosphoribosyltransferase; Provisional
Pssm-ID: 180928 Cd Length: 178 Bit Score: 45.35 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 307 GQQLAIEAPVEADLVSTVPESATPAALGYATKCGLPYVeVLCKNR--YVGRTFIQPNMRLrQLGVAKKF---GVLSDNFK 381
Cdd:PRK07322 42 AEALAKRLPTEVDVLVTPETKGIPLAHALSRRLGKPYV-VARKSRkpYMQDPIIQEVVSI-TTGKPQLLvldGADAEKLK 119
|
90 100 110
....*....|....*....|....*....|..
gi 26024309 382 GKRIVLIDDSIVRGNTISPIIKLLKESGAKEV 413
Cdd:PRK07322 120 GKRVAIVDDVVSTGGTLTALERLVERAGGQVV 151
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
89-210 |
2.09e-05 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 47.02 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 89 IGHTRYA----TTGKcelencQPFVVETlhGKIAVAHNGELVNAARLRKKLLRQGIGLSTSSDSEMITQLLaytppqEKD 164
Cdd:PTZ00077 51 LAHERLAivdlSDGK------QPLLDDD--ETVALMQNGEIYNHWEIRPELEKEGYKFSSNSDCEIIGHLY------KEY 116
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 26024309 165 DAPDWVARIKNLmkeapaaYSLVI--MHRDFIYAVRDPYGNRPLCIGR 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 |
4.14e-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: 45.40 E-value: 4.14e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 85 SNLGIGHTRYATTGKCELENCQPFVVEtLHGK-IAVAHNGELvnaARLRKKLLR--QGIGlstSSDSEMI 151
Cdd:pfam13230 71 SRNVIAHIRKATQGRVTLENTHPFMRE-LWGRyWIFAHNGDL---KGYAPKLSGrfQPVG---STDSELA 133
|
|
| PRK00934 |
PRK00934 |
ribose-phosphate pyrophosphokinase; Provisional |
381-415 |
1.47e-04 |
|
ribose-phosphate pyrophosphokinase; Provisional
Pssm-ID: 234868 [Multi-domain] Cd Length: 285 Bit Score: 43.75 E-value: 1.47e-04
10 20 30
....*....|....*....|....*....|....*
gi 26024309 381 KGKRIVLIDDSIVRGNTISPIIKLLKESGAKEVHI 415
Cdd:PRK00934 203 KGKDVLIVDDIISTGGTMATAIKILKEQGAKKVYV 237
|
|
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
12-210 |
3.82e-04 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 42.97 E-value: 3.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 12 CGVFGCIASGDwPTQLDVPHVITLgLVGLQHRGQESAGIVTSDGsavpkfrvhkgmglvnhvftednlkklydsnlGI-G 90
Cdd:PRK09431 2 CGIFGILDIKT-DADELRKKALEM-SRLMRHRGPDWSGIYASDN--------------------------------AIlG 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26024309 91 HTRYA----TTGKcelencQPFVVEtlHGKIAVAHNGELVNAARLRKKLLRqGIGLSTSSDSEMITQLlaYtppQEKddA 166
Cdd:PRK09431 48 HERLSivdvNGGA------QPLYNE--DGTHVLAVNGEIYNHQELRAELGD-KYAFQTGSDCEVILAL--Y---QEK--G 111
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 26024309 167 PDWVARIknlmkEAPAAYSLVIMHRDFIYAVRDPYGNRPLCIGR 210
Cdd:PRK09431 112 PDFLDDL-----DGMFAFALYDSEKDAYLIARDPIGIIPLYYGY 150
|
|
| PRK02812 |
PRK02812 |
ribose-phosphate pyrophosphokinase; Provisional |
369-421 |
4.00e-04 |
|
ribose-phosphate pyrophosphokinase; Provisional
Pssm-ID: 235072 [Multi-domain] Cd Length: 330 Bit Score: 42.42 E-value: 4.00e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 26024309 369 VAKKFGVLSDnFKGKRIVLIDDSIVRGNTISPIIKLLKESGAKEVHI----RVASPP 421
Cdd:PRK02812 218 VAEVLNVIGD-VKGKTAILVDDMIDTGGTICEGARLLRKEGAKQVYAcathAVFSPP 273
|
|
| Hpt1 |
COG2236 |
Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine ... |
374-415 |
1.17e-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: 1.17e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 26024309 374 GVLSDNFKGKRIVLIDDSIVRGNTISPIIKLLKESGAKEVHI 415
Cdd:COG2236 80 GPLDEDLAGKRVLIVDDVADTGRTLEAVRDLLKEAGPAEVRT 121
|
|
| PRK09162 |
PRK09162 |
hypoxanthine-guanine phosphoribosyltransferase; Provisional |
379-433 |
1.97e-03 |
|
hypoxanthine-guanine phosphoribosyltransferase; Provisional
Pssm-ID: 181675 Cd Length: 181 Bit Score: 39.46 E-value: 1.97e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26024309 379 NFKGKRIVLIDDSIVRGNTISPIIKLLKESGAKEVHIRV--------ASPPIKyPCFMGINIP 433
Cdd:PRK09162 94 SLKGRTVLVVDDILDEGHTLAAIRDRCLEMGAAEVYSAVlvdkthdrKAKPLK-ADFVGLEVP 155
|
|
| PrsA |
COG0462 |
Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; ... |
381-415 |
2.15e-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: 40.04 E-value: 2.15e-03
10 20 30
....*....|....*....|....*....|....*
gi 26024309 381 KGKRIVLIDDSIVRGNTISPIIKLLKESGAKEVHI 415
Cdd:COG0462 210 EGKTCIIVDDMIDTGGTLVEAAEALKEAGAKSVYA 244
|
|
| 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 26024309 379 NFKGKRIVLIDDSIVRGNTISPIIKLLKESGAKEVHI 415
Cdd:pfam00156 79 DLKGKTVLIVDDILDTGGTLLKVLELLKNVGPKEVKI 115
|
|
| |
