|
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: 640.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 7 GIREECGVFGCIASGewptqlDVPHVITLGLVGLQHRGQESAGIVTSDGSSvptFKSHKGMGLVNHVFTEDNLKKLyVSN 86
Cdd:COG0034 3 KLHEECGVFGIYGHE------DVAQLTYYGLYALQHRGQESAGIATSDGGR---FHLHKGMGLVSDVFDEEDLERL-KGN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 87 LGIGHTRYATTGKCELENCQPFVVETLHGKIAVAHNGELVNAARLRKKLLRHGIGLSTSSDSEMITQLLAYtppqeQDDT 166
Cdd:COG0034 73 IAIGHVRYSTTGSSSLENAQPFYVNSPFGSIALAHNGNLTNAEELREELEEEGAIFQTTSDTEVILHLIAR-----ELTK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 167 PDWVARIKNLMKEAPTAYSLLIMHRDVIYAVRDPYGNRPLCIGRLipvsdindkekktseTEGWVVSSESCSFLSIGARY 246
Cdd:COG0034 148 EDLEEAIKEALRRVKGAYSLVILTGDGLIAARDPNGIRPLVLGKL---------------EDGYVVASESCALDILGAEF 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 247 YREVLPGEIVEISRHNVQTLDIisrSEGNPVAFCIFEYVYFARPDSMFEDQMVYTVRYRCGQQLAIEAPVDADLVSTVPE 326
Cdd:COG0034 213 VRDVEPGEIVVIDEDGLRSRQF---AEKPRPAPCIFEYVYFARPDSVIDGRSVYEARKRMGRELAREAPVDADVVIPVPD 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 327 SATPAALAYAGKCGLPYVEVLCKNRYVGRTFIQPNMRLRQLGVAKKFGVLSDNFKGKRIVLVDDSIVRGNTISPIIKLLK 406
Cdd:COG0034 290 SGRPAAIGYAEESGIPYEEGLIKNRYVGRTFIQPTQELRELGVRLKLNPIREVVKGKRVVLVDDSIVRGTTSRRIVKMLR 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 407 ESGAKEVHIRVASPPIKYPCFMGINIPTKEELIANKPEFDHLAEYLGANSVVYLSVEGLVSSVQEGIkfkkqkekkhdim 486
Cdd:COG0034 370 EAGAKEVHFRIASPPIRYPCYYGIDTPTREELIAANRSVEEIREYIGADSLGYLSLEGLIEAVGEPI------------- 436
|
490 500 510
....*....|....*....|....*....|
gi 29570798 487 iqengnglecfekSGHCTACLTGKYPVELE 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: 531.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 12 CGVFGCIASGEwptqlDVPHVITLGLVGLQHRGQESAGIVTSDGSsvpTFKSHKGMGLVNHVFTEDNLKKLyVSNLGIGH 91
Cdd:TIGR01134 1 CGVVGIYGQEE-----VAASLTYYGLYALQHRGQESAGISVFDGN---RFRLHKGNGLVSDVFNEEHLQRL-KGNVGIGH 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 92 TRYATTGKCELENCQPFVVETLHGKIAVAHNGELVNAARLRKKLLRHGIGLSTSSDSEMITQLLAYTPPQEQDDtpdwVA 171
Cdd:TIGR01134 72 VRYSTAGSSGLENAQPFVVNSPYGGLALAHNGNLVNADELRRELEEEGRHFNTTSDSEVLLHLLAHNDESKDDL----FD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 172 RIKNLMKEAPTAYSLLIMHRDVIYAVRDPYGNRPLCIGRLipvsdindkekktseTEGWVVSSESCSFLSIGARYYREVL 251
Cdd:TIGR01134 148 AVARVLERVRGAYALVLMTEDGLVAVRDPHGIRPLVLGRR---------------GDGYVVASESCALDILGAEFVRDVE 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 252 PGEIVEISRHNVQTLdiisRSEGNPVAFCIFEYVYFARPDSMFEDQMVYTVRYRCGQQLAIEAPVDADLVSTVPESATPA 331
Cdd:TIGR01134 213 PGEVVVIFDGGLESR----QCARRPRAPCVFEYVYFARPDSVIDGISVYYARKRMGKELARESPVEADVVVPVPDSGRSA 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 332 ALAYAGKCGLPYVEVLCKNRYVGRTFIQPNMRLRQLGVAKKFGVLSDNFKGKRIVLVDDSIVRGNTISPIIKLLKESGAK 411
Cdd:TIGR01134 289 ALGFAQASGIPYREGLIKNRYVGRTFIMPTQELRELSVRLKLNPVRAVFEGKRVVLVDDSIVRGTTSRQIVEMLRDAGAK 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 412 EVHIRVASPPIKYPCFMGINIPTKEELIANKPEFDHlAEYLGANSVVYLSVEGLVSSVQEGIkfkkqkekkhdimiqeng 491
Cdd:TIGR01134 369 EVHVRIASPPIRYPCYYGIDMPTREELIAARRTVEE-IRKIGADSLAYLSLEGLKEAVGNPE------------------ 429
|
490 500
....*....|....*....|.
gi 29570798 492 nglecfekSGHCTACLTGKYP 512
Cdd:TIGR01134 430 --------SDLCLACFTGEYP 442
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
1-514 |
1.87e-173 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 497.25 E-value: 1.87e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 1 MELEELGIREECGVFGCIAsgewPTQLDVPHVITLGLVGLQHRGQESAGIVTSDGSSvptFKSHKGMGLVNHVFTEDNLK 80
Cdd:PRK05793 4 MDLEGDKFKEECGVFGVFS----KNNIDVASLTYYGLYALQHRGQESAGIAVSDGEK---IKVHKGMGLVSEVFSKEKLK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 81 KLyVSNLGIGHTRYATTGKCELENCQPFVVETLHGKIAVAHNGELVNAARLRKKLLRHGIGLSTSSDSEMITQLLAYTPP 160
Cdd:PRK05793 77 GL-KGNSAIGHVRYSTTGASDLDNAQPLVANYKLGSIAIAHNGNLVNADVIRELLEDGGRIFQTSIDSEVILNLIARSAK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 161 QEQDDTpdwvarIKNLMKEAPTAYSLLIMHRDVIYAVRDPYGNRPLCIGRLipvsdindkekktseTEGWVVSSESCSFL 240
Cdd:PRK05793 156 KGLEKA------LVDAIQAIKGSYALVILTEDKLIGVRDPHGIRPLCLGKL---------------GDDYILSSESCALD 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 241 SIGARYYREVLPGEIVEISRHNVQTLDIisrSEGNPVAFCIFEYVYFARPDSMFEDQMVYTVRYRCGQQLAIEAPVDADL 320
Cdd:PRK05793 215 TIGAEFIRDVEPGEIVIIDEDGIKSIKF---AEKTKCQTCAFEYIYFARPDSVIDGISVYESRVRAGRQLYKEYPVDADI 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 321 VSTVPESATPAALAYAGKCGLPYVEVLCKNRYVGRTFIQPNMRLRQLGVAKKFGVLSDNFKGKRIVLVDDSIVRGNTISP 400
Cdd:PRK05793 292 VIGVPDSGIPAAIGYAEASGIPYGIGFIKNKYVGRTFIAPSQELRERAVRVKLNPLKVNVEGKRVVLIDDSIVRGTTSKR 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 401 IIKLLKESGAKEVHIRVASPPIKYPCFMGINIPTKEELIANKPEFDHLAEYLGANSVVYLSVEGLVSSVQegikfkkqke 480
Cdd:PRK05793 372 LVELLRKAGAKEVHFRVSSPPVKYPCYFGIDTPYRKELIGANMSVEEIREMIGADSLGYLSIEGLLESLN---------- 441
|
490 500 510
....*....|....*....|....*....|....
gi 29570798 481 kkhdimiqengnglecfEKSGHCTACLTGKYPVE 514
Cdd:PRK05793 442 -----------------GDKGFCLGCFNGVYPVS 458
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
11-514 |
3.09e-156 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 453.75 E-value: 3.09e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 11 ECGVFGCIASGEwptqldVPHVITLGLVGLQHRGQESAGIVTSDGSsvpTFKSHKGMGLVNHVFTEDNLKKLYvSNLGIG 90
Cdd:PLN02440 1 ECGVVGIFGDPE------ASRLCYLGLHALQHRGQEGAGIVTVDGN---RLQSITGNGLVSDVFDESKLDQLP-GDIAIG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 91 HTRYATTGKCELENCQPFVVETLHGKIAVAHNGELVNAARLRKKLLRHGIGLSTSSDSEMITQLLAytppqeQDDTPDWV 170
Cdd:PLN02440 71 HVRYSTAGASSLKNVQPFVANYRFGSIGVAHNGNLVNYEELRAKLEENGSIFNTSSDTEVLLHLIA------ISKARPFF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 171 ARIKNLMKEAPTAYSLLIMHRDVIYAVRDPYGNRPLCIGRlipvsdindkeKKTSEtegWVVSSESCSFLSIGARYYREV 250
Cdd:PLN02440 145 SRIVDACEKLKGAYSMVFLTEDKLVAVRDPHGFRPLVMGR-----------RSNGA---VVFASETCALDLIGATYEREV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 251 LPGEIVEISR-HNVQTLDIISRSEGNPvafCIFEYVYFARPDSMFEDQMVYTVRYRCGQQLAIEAPVDADLVSTVPESAT 329
Cdd:PLN02440 211 NPGEVIVVDKdKGVSSQCLMPHPEPKP---CIFEHIYFARPNSIVFGRSVYESRLEFGEILATEIPVDCDVVIPVPDSGR 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 330 PAALAYAGKCGLPYVEVLCKNRYVGRTFIQPNMRLRQLGVAKKFGVLSDNFKGKRIVLVDDSIVRGNTISPIIKLLKESG 409
Cdd:PLN02440 288 VAALGYAAKLGVPFQQGLIRSHYVGRTFIEPSQKIRDFSVKLKLNPVRSVLEGKRVVVVDDSIVRGTTSSKIVRMLREAG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 410 AKEVHIRVASPPIKYPCFMGINIPTKEELIANKPEFDHLAEYLGANSVVYLSVEGLVSSVQEgikfkkqkekkhdimiqe 489
Cdd:PLN02440 368 AKEVHMRIASPPIIASCYYGVDTPSREELISNRMSVEEIRKFIGCDSLAFLPLEDLKKSLGE------------------ 429
|
490 500
....*....|....*....|....*
gi 29570798 490 ngnglecfEKSGHCTACLTGKYPVE 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 |
2.37e-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: 399.53 E-value: 2.37e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 12 CGVFGCIASGewptqlDVPHVITLGLVGLQHRGQESAGIVTSDGSsvpTFKSHKGMGLVNHVFTEDNLKKLyVSNLGIGH 91
Cdd:cd00715 1 CGVFGIYGAE------DAARLTYLGLYALQHRGQESAGIATSDGK---RFHTHKGMGLVSDVFDEEKLRRL-PGNIAIGH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 92 TRYATTGKCELENCQPFVVETLHGKIAVAHNGELVNAARLRKKLLRHGIGLSTSSDSEMITQLLAYTPpqeqdDTPDWVA 171
Cdd:cd00715 71 VRYSTAGSSSLENAQPFVVNSPLGGIALAHNGNLVNAKELREELEEEGRIFQTTSDSEVILHLIARSL-----AKDDLFE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 172 RIKNLMKEAPTAYSLLIMHRDVIYAVRDPYGNRPLCIGRLipvsdindkekktsETEGWVVSSESCSFLSIGARYYREVL 251
Cdd:cd00715 146 AIIDALERVKGAYSLVIMTADGLIAVRDPHGIRPLVLGKL--------------EGDGYVVASESCALDIIGAEFVRDVE 211
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 29570798 252 PGEIVEISRHNVQTldiISRSEGNPVAFCIFEYVYFARPDSMFE 295
Cdd:cd00715 212 PGEIVVIDDDGLES---SQRAPKPKPAPCIFEYVYFARPDSVID 252
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
12-256 |
2.54e-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: 195.36 E-value: 2.54e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 12 CGVFGCIASGEWPTQLDVPHviTLGLVGLQHRGQESAGIVTSDGSSVPTFKSHKGMGLVNhvftEDNLKKLYVSNLGIGH 91
Cdd:cd00352 1 CGIFGIVGADGAASLLLLLL--LRGLAALEHRGPDGAGIAVYDGDGLFVEKRAGPVSDVA----LDLLDEPLKSGVALGH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 92 TRYATTGKCELENCQPFVVETlhGKIAVAHNGELVNAARLRKKLLRHGIGLSTSSDSEMITQLLAYTPpqeqdDTPDWVA 171
Cdd:cd00352 75 VRLATNGLPSEANAQPFRSED--GRIALVHNGEIYNYRELREELEARGYRFEGESDSEVILHLLERLG-----REGGLFE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 172 RIKNLMKEAPTAYSLLIM--HRDVIYAVRDPYGNRPLCIGRLIPvsdindkekktsetEGWVVSSESCSFLSIGARYYRE 249
Cdd:cd00352 148 AVEDALKRLDGPFAFALWdgKPDRLFAARDRFGIRPLYYGITKD--------------GGLVFASEPKALLALPFKGVRR 213
|
....*..
gi 29570798 250 VLPGEIV 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 |
7.31e-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: 7.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 12 CGVFGCIASGEwptqlDVPHVITlGLVGLQHRGQESAGIVTSDGSSVPTFKShKG--MGLVNHVFtednlKKLYVSNLGI 89
Cdd:cd00714 1 CGIVGYIGKRE-----AVDILLE-GLKRLEYRGYDSAGIAVIGDGSLEVVKA-VGkvANLEEKLA-----EKPLSGHVGI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 90 GHTRYATTGKCELENCQPFVVETlhGKIAVAHNGELVNAARLRKKLLRHGIGLSTSSDSEMITQLLAYtppqEQDDTPDW 169
Cdd:cd00714 69 GHTRWATHGEPTDVNAHPHRSCD--GEIAVVHNGIIENYAELKEELEAKGYKFESETDTEVIAHLIEY----YYDGGLDL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 170 VARIKNLMKEAPTAYSLLIMHR---DVIYAVRDpygNRPLCIGrlipvsdINDKEKktsetegwVVSSESCSFLsigaRY 246
Cdd:cd00714 143 LEAVKKALKRLEGAYALAVISKdepDEIVAARN---GSPLVIG-------IGDGEN--------FVASDAPALL----EH 200
|
250
....*....|....*
gi 29570798 247 YREVLP---GEIVEI 258
Cdd:cd00714 201 TRRVIYledGDIAVI 215
|
|
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
12-277 |
2.92e-21 |
|
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: 97.39 E-value: 2.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 12 CGVFGCIASGewptqlDVPHVITLGLVGLQHRGQESAGIVTSDGSSVPTFKShKGmglvnHVfteDNLKKLYV-----SN 86
Cdd:COG0449 2 CGIVGYIGKR------DAAPILLEGLKRLEYRGYDSAGIAVLDDGGLEVRKA-VG-----KL---ANLEEKLAeeplsGT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 87 LGIGHTRYATTGKCELENCQPFVVETlhGKIAVAHNG--ElvNAARLRKKLLRHGIGLSTSSDSEMITQLLAYtppqEQD 164
Cdd:COG0449 67 IGIGHTRWATHGAPSDENAHPHTSCS--GRIAVVHNGiiE--NYAELREELEAKGHTFKSETDTEVIAHLIEE----YLK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 165 DTPDWVARIKNLMKEAPTAYSLLIMHR---DVIYAVRdpYGNrPLCIGrlipvsdINDKEkktsetegWVVSSESCSFLS 241
Cdd:COG0449 139 GGGDLLEAVRKALKRLEGAYALAVISAdepDRIVAAR--KGS-PLVIG-------LGEGE--------NFLASDVPALLP 200
|
250 260 270
....*....|....*....|....*....|....*....
gi 29570798 242 igarYYREVLP---GEIVEISRHNVQTLDIisrsEGNPV 277
Cdd:COG0449 201 ----YTRRVIYledGEIAVLTRDGVEIYDL----DGEPV 231
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
12-266 |
2.39e-19 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 91.24 E-value: 2.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 12 CGVFGCIASGewptqlDVPHVITLGLVGLQHRGQESAGIVT-SDGSSVPTFK---SHKGMGLVNHVftEDNLKKLYV-SN 86
Cdd:PTZ00295 25 CGIVGYLGNE------DASKILLEGIEILQNRGYDSCGISTiSSGGELKTTKyasDGTTSDSIEIL--KEKLLDSHKnST 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 87 LGIGHTRYATTGKCELENCQPFVveTLHGKIAVAHNGELVNAARLRKKLLRHGIGLSTSSDSEMITQLLAYtppqEQDDT 166
Cdd:PTZ00295 97 IGIAHTRWATHGGKTDENAHPHC--DYKKRIALVHNGTIENYVELKSELIAKGIKFRSETDSEVIANLIGL----ELDQG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 167 PDWVARIKNLMKEAPTAYSLLIMHR---DVIYAVRDpygNRPLCIGRlipvsdindkekktsETEGWVVSSESCSFlsig 243
Cdd:PTZ00295 171 EDFQEAVKSAISRLQGTWGLCIIHKdnpDSLIVARN---GSPLLVGI---------------GDDSIYVASEPSAF---- 228
|
250 260
....*....|....*....|....*.
gi 29570798 244 ARYYREVLP---GEIVEISRHNVQTL 266
Cdd:PTZ00295 229 AKYTNEYISlkdGEIAELSLENVNDL 254
|
|
| PRTases_typeI |
cd06223 |
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ... |
306-442 |
7.36e-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: 7.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 306 CGQQLAIEAP---VDADLVSTVPESATPAALAYAGKCGLPYVEVLCKNRYVGRTFIQPNmrlrqlgvaKKFGVLSDNFKG 382
Cdd:cd06223 1 AGRLLAEEIRedlLEPDVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSEPY---------GLELPLGGDVKG 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 383 KRIVLVDDSIVRGNTISPIIKLLKESGAKEVHIRVAsPPIKYPCFMGINIPTKEELIANK 442
Cdd:cd06223 72 KRVLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVL-LDKPEGGARELASPGDPVYSLFT 130
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
12-283 |
1.13e-18 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 89.33 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 12 CGVFGCIAsgewptQLDVPHVITLGLVGLQHRGQESAGIVTSDGSSVPTFKShKGmGLVN--HVFTEDNLKklyvSNLGI 89
Cdd:PRK00331 2 CGIVGYVG------QRNAAEILLEGLKRLEYRGYDSAGIAVLDDGGLEVRKA-VG-KVANleAKLEEEPLP----GTTGI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 90 GHTRYATTGKCELENCQPFVVETlhGKIAVAHNGELVNAARLRKKLLRHGIGLSTSSDSEMITQLLAYtppqEQDDTPDW 169
Cdd:PRK00331 70 GHTRWATHGKPTERNAHPHTDCS--GRIAVVHNGIIENYAELKEELLAKGHVFKSETDTEVIAHLIEE----ELKEGGDL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 170 VARIKNLMKEAPTAYSLLIMHR---DVIYAVRDpygNRPLCIGrlipvsdINDKEkktsetegWVVSSESCSFLSigarY 246
Cdd:PRK00331 144 LEAVRKALKRLEGAYALAVIDKdepDTIVAARN---GSPLVIG-------LGEGE--------NFLASDALALLP----Y 201
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 29570798 247 YREVLP---GEIVEISRHNVQTLDIisrsEGNPVAFCIFE 283
Cdd:PRK00331 202 TRRVIYledGEIAVLTRDGVEIFDF----DGNPVEREVYT 237
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
12-256 |
2.23e-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: 78.85 E-value: 2.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 12 CGVFGCIASGEWPtqlDVPHVITLGLVGLQHRG-QESAG---------IVTSDGSSVPTFKshkGMGLVNHVFTEDNLKK 81
Cdd:cd01907 1 CGIFGIMSKDGEP---FVGALLVEMLDAMQERGpGDGAGfalygdpdaFVYSSGKDMEVFK---GVGYPEDIARRYDLEE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 82 lYVSNLGIGHTRYATTGKCELENCQPFVVetlhGKIAVAHNGELVNAARLRKKLLRHGIGLSTSSDSEMITQLLAYTpPQ 161
Cdd:cd01907 75 -YKGYHWIAHTRQPTNSAVWWYGAHPFSI----GDIAVVHNGEISNYGSNREYLERFGYKFETETDTEVIAYYLDLL-LR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 162 EQDDTPDWVARI-------KNLMKEAPTAYSLLIM---------HRDVIYAVRDPYGNRPLCIGrlipvsdindkekkts 225
Cdd:cd01907 149 KGGLPLEYYKHIirmpeeeRELLLALRLTYRLADLdgpftiivgTPDGFIVIRDRIKLRPAVVA---------------- 212
|
250 260 270
....*....|....*....|....*....|....*.
gi 29570798 226 ETEGWV-VSSESCSFLSI----GARYYrEVLPGEIV 256
Cdd:cd01907 213 ETDDYVaIASEECAIREIpdrdNAKVW-EPRPGEYV 247
|
|
| YafJ |
cd01908 |
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ... |
85-261 |
2.56e-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: 2.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 85 SNLGIGHTRYATTGKCELENCQPFVvetlHGKIAVAHNGELVNAARLRKKLLRHGIGLST-SSDSEM----ITQLLAYTP 159
Cdd:cd01908 80 SPLVLAHVRAATVGPVSLENCHPFT----RGRWLFAHNGQLDGFRLLRRRLLRLLPRLPVgTTDSELafalLLSRLLERD 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 160 PQEQDDTPDWVAR-IKNLMKEA-PTAYSLLIMHRDVIYAVRDPYGNRP--LCIGRLIPVSDINDKEKKTSETEGWVVSSE 235
Cdd:cd01908 156 PLDPAELLDAILQtLRELAALApPGRLNLLLSDGEYLIATRYASAPSLyyLTRRAPFGCARLLFRSVTTPNDDGVVVASE 235
|
170 180
....*....|....*....|....*.
gi 29570798 236 SCSFlsigARYYREVLPGEIVEISRH 261
Cdd:cd01908 236 PLTD----DEGWTEVPPGELVVVSEG 257
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
88-211 |
1.53e-14 |
|
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: 70.41 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 88 GIGHTRYATTGKCELENcQPFVVETlhGKIAVAHNGELVNAARLRKKLLRHGIGLSTSSDSEMITQLLAYTPpqeqddtP 167
Cdd:pfam13522 13 ALGHVRLAIVDLPDAGN-QPMLSRD--GRLVLVHNGEIYNYGELREELADLGHAFRSRSDTEVLLALYEEWG-------E 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 29570798 168 DWVARIKNLMkeAPTAYSlLIMHRDVIyaVRDPYGNRPLCIGRL 211
Cdd:pfam13522 83 DCLERLRGMF--AFAIWD-RRRRTLFL--ARDRLGIKPLYYGIL 121
|
|
| YafJ |
COG0121 |
Predicted glutamine amidotransferase YafJ [General function prediction only]; |
20-260 |
4.94e-14 |
|
Predicted glutamine amidotransferase YafJ [General function prediction only];
Pssm-ID: 439891 [Multi-domain] Cd Length: 248 Bit Score: 71.92 E-value: 4.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 20 SGEWPTQLDvpHVITLGLVGLQHRGQESAGIVTSDGSSVPTFKSHKGMGL---VNHVFTEDNLKKL---YVSNLGIGHTR 93
Cdd:COG0121 7 SGNVPTDLE--FLLLDPEHSLVRQSGATREGPHADGWGIGWYEGDGEPRLyrdPLPAWSDPNLRLLarpIKSRLVIAHVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 94 YATTGKCELENCQPFVvetlHGKIAVAHNGELVNAARLRKKL-------LRHGIGLSTssDSE----MITQLLAYTPPQE 162
Cdd:COG0121 85 KATVGPVSLENTHPFR----GGRWLFAHNGQLDGFDRLRRRLaeelpdeLYFQPVGTT--DSElafaLLLSRLRDGGPDP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 163 QDDTPDWVARIKNLMKeAPTAYSLLIMHRDVIYAVRDPYGNRP--LCIGRLIPVSDindkekktsetEGWVVSSEScsfL 240
Cdd:COG0121 159 AEALAEALRELAELAR-APGRLNLLLSDGERLYATRYTSDDPYptLYYLTRTTPDD-----------RVVVVASEP---L 223
|
250 260
....*....|....*....|
gi 29570798 241 SIGARyYREVLPGEIVEISR 260
Cdd:COG0121 224 TDDEG-WTEVPPGELLVVRD 242
|
|
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
12-187 |
4.25e-13 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 71.71 E-value: 4.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 12 CGVFGCIASGEWPTQLDVPHVITLGLVGLQHRGQESAGIVTSDGSSVPTF------KSHKGMGLVNHVF-----TEDNLK 80
Cdd:PLN02981 2 CGIFAYLNYNVPRERRFILEVLFNGLRRLEYRGYDSAGIAIDNDPSLESSsplvfrEEGKIESLVRSVYeevaeTDLNLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 81 KLYVSNLGIGHTRYATTGKCELENCQPFVVETlHGKIAVAHNGELVNAARLRKKLLRHGIGLSTSSDSEMITQLLAYTPP 160
Cdd:PLN02981 82 LVFENHAGIAHTRWATHGPPAPRNSHPQSSGP-GNEFLVVHNGIITNYEVLKETLLRHGFTFESDTDTEVIPKLAKFVFD 160
|
170 180
....*....|....*....|....*....
gi 29570798 161 QEQDDTPDWVAR--IKNLMKEAPTAYSLL 187
Cdd:PLN02981 161 KLNEEEGDVTFSqvVMEVMRQLEGAYALI 189
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
106-240 |
3.50e-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: 63.31 E-value: 3.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 106 QPFVVETLhGKIAVAHNGELVNAARLRKKLLRHGIGLSTSSDSEMITQLLAYtppqeqddtpDW----VARIkNLMkeap 181
Cdd:pfam13537 14 QPMVSSED-GRYVIVFNGEIYNYRELRAELEAKGYRFRTHSDTEVILHLYEA----------EWgedcVDRL-NGM---- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29570798 182 taYSLLIM--HRDVIYAVRDPYGNRPLCIGRlipvsdindkekktSETEGWVVSSESCSFL 240
Cdd:pfam13537 78 --FAFAIWdrRRQRLFLARDRFGIKPLYYGR--------------DDGGRLLFASELKALL 122
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
12-265 |
2.34e-11 |
|
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: 63.35 E-value: 2.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 12 CGVFGCIAsgeWPTQLDVPHVITLGLVGLQHRGQESAGIVTSDGssvptfkshkgmglvnhvftednlkklyvsnLGIGH 91
Cdd:cd00712 1 CGIAGIIG---LDGASVDRATLERMLDALAHRGPDGSGIWIDEG-------------------------------VALGH 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 92 TRYATTGkceLEN-CQPFVVETlhGKIAVAHNGELVNAARLRKKLLRHGIGLSTSSDSEMItqLLAYtppQEQDdtPDWV 170
Cdd:cd00712 47 RRLSIID---LSGgAQPMVSED--GRLVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVI--LHLY---EEWG--EDCL 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 171 ARIkNLMkeaptaYSLLI--MHRDVIYAVRDPYGNRPL----------------CIGRLIPVSDINDKEKKTSETEGWVV 232
Cdd:cd00712 115 ERL-NGM------FAFALwdKRKRRLFLARDRFGIKPLyygrdggglafaselkALLALPGVPRELDEAALAEYLAFQYV 187
|
250 260 270
....*....|....*....|....*....|...
gi 29570798 233 SSESCSFLSIgaryyREVLPGEIVEISRHNVQT 265
Cdd:cd00712 188 PAPRTIFKGI-----RKLPPGHYLTVDPGGVEI 215
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
12-188 |
2.50e-10 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 62.97 E-value: 2.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 12 CGVFGCIASGEWPTQLDVPHVITLGLVGLQHRGQESAGIVTSDG----------SSVPTFKSH--KGMGLVNH----VFT 75
Cdd:PTZ00394 2 CGIFGYANHNVPRTVEQILNVLLDGIQKVEYRGYDSAGLAIDANigsekedgtaASAPTPRPCvvRSVGNISQlrekVFS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 76 ED------NLKKLYVSNLGIGHTRYATTGKCELENCQPfvVETLHGKIAVAHNGELVNAARLRKKLLRHGIGLSTSSDSE 149
Cdd:PTZ00394 82 EAvaatlpPMDATTSHHVGIAHTRWATHGGVCERNCHP--QQSNNGEFTIVHNGIVTNYMTLKELLKEEGYHFSSDTDTE 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 29570798 150 MITQLLAYTppQEQDDTPDWVARIKNLMKEAPTAYSLLI 188
Cdd:PTZ00394 160 VISVLSEYL--YTRKGIHNFADLALEVSRMVEGSYALLV 196
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
86-210 |
3.92e-08 |
|
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: 56.00 E-value: 3.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 86 NLGIGHTRYATTGKCELENcQPFVVETlhGKIAVAHNGELVNAARLRKKLLRHGIGLSTSSDSEMItqLLAYtppqeQDD 165
Cdd:COG0367 41 GVALGHRRLSIIDLSEGGH-QPMVSED--GRYVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVI--LHAY-----EEW 110
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 29570798 166 TPDWVARIkNLMkeaptaYSLLI--MHRDVIYAVRDPYGNRPLCIGR 210
Cdd:COG0367 111 GEDCLERL-NGM------FAFAIwdRRERRLFLARDRFGIKPLYYAE 150
|
|
| PRK02277 |
PRK02277 |
orotate phosphoribosyltransferase-like protein; Provisional |
370-417 |
1.78e-06 |
|
orotate phosphoribosyltransferase-like protein; Provisional
Pssm-ID: 235023 [Multi-domain] Cd Length: 200 Bit Score: 48.71 E-value: 1.78e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 29570798 370 AKKFGVLSDNF---KGKRIVLVDDSIVRGNTISPIIKLLKESGAKEVHIRV 417
Cdd:PRK02277 125 EKKTGSFSRNFasvEGKRCVIVDDVITSGTTMKETIEYLKEHGGKPVAVVV 175
|
|
| PRK07322 |
PRK07322 |
adenine phosphoribosyltransferase; Provisional |
307-413 |
5.68e-06 |
|
adenine phosphoribosyltransferase; Provisional
Pssm-ID: 180928 Cd Length: 178 Bit Score: 46.89 E-value: 5.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 307 GQQLAIEAPVDADLVSTVPESATPAALAYAGKCGLPYVeVLCKNR--YVGRTFIQPNMRLrQLGVAKKF---GVLSDNFK 381
Cdd:PRK07322 42 AEALAKRLPTEVDVLVTPETKGIPLAHALSRRLGKPYV-VARKSRkpYMQDPIIQEVVSI-TTGKPQLLvldGADAEKLK 119
|
90 100 110
....*....|....*....|....*....|..
gi 29570798 382 GKRIVLVDDSIVRGNTISPIIKLLKESGAKEV 413
Cdd:PRK07322 120 GKRVAIVDDVVSTGGTLTALERLVERAGGQVV 151
|
|
| PLN02549 |
PLN02549 |
asparagine synthase (glutamine-hydrolyzing) |
82-209 |
1.07e-05 |
|
asparagine synthase (glutamine-hydrolyzing)
Pssm-ID: 178164 [Multi-domain] Cd Length: 578 Bit Score: 48.22 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 82 LYVS-NLGIGHTRYA----TTGKcelencQPFVVETlhGKIAVAHNGELVNAARLRKKLLRHgiGLSTSSDSEMITQLLA 156
Cdd:PLN02549 38 LYGNeDCYLAHERLAimdpESGD------QPLYNED--KTIVVTANGEIYNHKELREKLKLH--KFRTGSDCEVIAHLYE 107
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 29570798 157 YTPPQeqddtpdwVARIKNLMkeapTAYSLLIMHRDVIYAVRDPYGNRPLCIG 209
Cdd:PLN02549 108 EHGEE--------FVDMLDGM----FSFVLLDTRDNSFIAARDHIGITPLYIG 148
|
|
| GATase_4 |
pfam13230 |
Glutamine amidotransferases class-II; This family captures members that are not found in ... |
28-151 |
1.96e-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: 46.17 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 28 DVPHVITLGLVGLQHRGQESA------GIVTSDGSSVPTFKSHKGMG--LVNHVFTEDNLKklyvSNLGIGHTRYATTGK 99
Cdd:pfam13230 10 NVPTDICFSFTGFARRGGLTDhhadgwGIAFYEGRGARVFKDPQPSAdsPIAELVRRYPIR----SRNVIAHIRKATQGR 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 29570798 100 CELENCQPFVVEtLHGK-IAVAHNGELvnaARLRKKLLR--HGIGlstSSDSEMI 151
Cdd:pfam13230 86 VTLENTHPFMRE-LWGRyWIFAHNGDL---KGYAPKLSGrfQPVG---STDSELA 133
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
40-210 |
2.19e-05 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 47.02 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 40 LQHRGQESAGI-VTSDGSSVPTFKSHKGMGLVNhvftednlkklyvsnlgightryATTGKcelencQPFVVETlhGKIA 118
Cdd:PTZ00077 28 LRHRGPDWSGIiVLENSPGTYNILAHERLAIVD-----------------------LSDGK------QPLLDDD--ETVA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 119 VAHNGELVNAARLRKKLLRHGIGLSTSSDSEMITQLLaytppqEQDDTPDWVARIKNLMkeaptAYSLLIMHRDVIYAVR 198
Cdd:PTZ00077 77 LMQNGEIYNHWEIRPELEKEGYKFSSNSDCEIIGHLY------KEYGPKDFWNHLDGMF-----ATVIYDMKTNTFFAAR 145
|
170
....*....|..
gi 29570798 199 DPYGNRPLCIGR 210
Cdd:PTZ00077 146 DHIGIIPLYIGY 157
|
|
| PRK00934 |
PRK00934 |
ribose-phosphate pyrophosphokinase; Provisional |
381-415 |
8.68e-05 |
|
ribose-phosphate pyrophosphokinase; Provisional
Pssm-ID: 234868 [Multi-domain] Cd Length: 285 Bit Score: 44.52 E-value: 8.68e-05
10 20 30
....*....|....*....|....*....|....*
gi 29570798 381 KGKRIVLVDDSIVRGNTISPIIKLLKESGAKEVHI 415
Cdd:PRK00934 203 KGKDVLIVDDIISTGGTMATAIKILKEQGAKKVYV 237
|
|
| Hpt1 |
COG2236 |
Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine ... |
374-415 |
2.75e-04 |
|
Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine phosphoribosyltransferase is part of the Pathway/BioSystem: Purine salvage
Pssm-ID: 441837 [Multi-domain] Cd Length: 153 Bit Score: 41.37 E-value: 2.75e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 29570798 374 GVLSDNFKGKRIVLVDDSIVRGNTISPIIKLLKESGAKEVHI 415
Cdd:COG2236 80 GPLDEDLAGKRVLIVDDVADTGRTLEAVRDLLKEAGPAEVRT 121
|
|
| PRK02812 |
PRK02812 |
ribose-phosphate pyrophosphokinase; Provisional |
369-421 |
2.91e-04 |
|
ribose-phosphate pyrophosphokinase; Provisional
Pssm-ID: 235072 [Multi-domain] Cd Length: 330 Bit Score: 43.19 E-value: 2.91e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 29570798 369 VAKKFGVLSDnFKGKRIVLVDDSIVRGNTISPIIKLLKESGAKEVHI----RVASPP 421
Cdd:PRK02812 218 VAEVLNVIGD-VKGKTAILVDDMIDTGGTICEGARLLRKEGAKQVYAcathAVFSPP 273
|
|
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
12-210 |
4.66e-04 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 42.97 E-value: 4.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 12 CGVFGCIASGEwPTQLDVPHVITLgLVGLQHRGQESAGIVTSDGssvptfkshkgmglvnhvftednlkklyvsnlGI-G 90
Cdd:PRK09431 2 CGIFGILDIKT-DADELRKKALEM-SRLMRHRGPDWSGIYASDN--------------------------------AIlG 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29570798 91 HTRYA----TTGKcelencQPFVVEtlHGKIAVAHNGELVNAARLRKKLLRhGIGLSTSSDSEMITQLlaYtppqeQDDT 166
Cdd:PRK09431 48 HERLSivdvNGGA------QPLYNE--DGTHVLAVNGEIYNHQELRAELGD-KYAFQTGSDCEVILAL--Y-----QEKG 111
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 29570798 167 PDWVARIknlmkEAPTAYSLLIMHRDVIYAVRDPYGNRPLCIGR 210
Cdd:PRK09431 112 PDFLDDL-----DGMFAFALYDSEKDAYLIARDPIGIIPLYYGY 150
|
|
| Pribosyltran |
pfam00156 |
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ... |
379-415 |
7.29e-04 |
|
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: 40.04 E-value: 7.29e-04
10 20 30
....*....|....*....|....*....|....*..
gi 29570798 379 NFKGKRIVLVDDSIVRGNTISPIIKLLKESGAKEVHI 415
Cdd:pfam00156 79 DLKGKTVLIVDDILDTGGTLLKVLELLKNVGPKEVKI 115
|
|
| PRK09162 |
PRK09162 |
hypoxanthine-guanine phosphoribosyltransferase; Provisional |
379-433 |
1.28e-03 |
|
hypoxanthine-guanine phosphoribosyltransferase; Provisional
Pssm-ID: 181675 Cd Length: 181 Bit Score: 39.85 E-value: 1.28e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29570798 379 NFKGKRIVLVDDSIVRGNTISPIIKLLKESGAKEVHIRV--------ASPPIKyPCFMGINIP 433
Cdd:PRK09162 94 SLKGRTVLVVDDILDEGHTLAAIRDRCLEMGAAEVYSAVlvdkthdrKAKPLK-ADFVGLEVP 155
|
|
| PrsA |
COG0462 |
Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; ... |
381-415 |
1.50e-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: 1.50e-03
10 20 30
....*....|....*....|....*....|....*
gi 29570798 381 KGKRIVLVDDSIVRGNTISPIIKLLKESGAKEVHI 415
Cdd:COG0462 210 EGKTCIIVDDMIDTGGTLVEAAEALKEAGAKSVYA 244
|
|
| PLN02369 |
PLN02369 |
ribose-phosphate pyrophosphokinase |
379-421 |
6.57e-03 |
|
ribose-phosphate pyrophosphokinase
Pssm-ID: 215209 [Multi-domain] Cd Length: 302 Bit Score: 38.52 E-value: 6.57e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 29570798 379 NFKGKRIVLVDDSIVRGNTISPIIKLLKESGAKEVHI----RVASPP 421
Cdd:PLN02369 199 DVKGKVAIMVDDMIDTAGTITKGAALLHQEGAREVYAcathAVFSPP 245
|
|
| PLN02238 |
PLN02238 |
hypoxanthine phosphoribosyltransferase |
368-413 |
8.00e-03 |
|
hypoxanthine phosphoribosyltransferase
Pssm-ID: 215132 Cd Length: 189 Bit Score: 37.71 E-value: 8.00e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 29570798 368 GVAK-KFGVLSDNFKGKRIVLVDDSIVRGNTISPIIKLLKESGAKEV 413
Cdd:PLN02238 82 GVAKvSGADLKIDVKGKHVLLVEDIVDTGNTLSALVAHLEAKGAASV 128
|
|
| PRK03092 |
PRK03092 |
ribose-phosphate diphosphokinase; |
381-415 |
9.85e-03 |
|
ribose-phosphate diphosphokinase;
Pssm-ID: 179535 [Multi-domain] Cd Length: 304 Bit Score: 38.01 E-value: 9.85e-03
10 20 30
....*....|....*....|....*....|....*
gi 29570798 381 KGKRIVLVDDSIVRGNTISPIIKLLKESGAKEVHI 415
Cdd:PRK03092 200 EGRTCVLVDDMIDTGGTIAGAVRALKEAGAKDVII 234
|
|
| |
