|
Name |
Accession |
Description |
Interval |
E-value |
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
1-483 |
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: 742.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773798955 1 MCGIVGVIGRGPVNQLLYDSLLLLQHRGQDAAGIATLQGNHFNMYKAHGLVRDVFRTRNMRALPGTSGVGQVRYPTAGSS 80
Cdd:COG0034 7 ECGVFGIYGHEDVAQLTYYGLYALQHRGQESAGIATSDGGRFHLHKGMGLVSDVFDEEDLERLKGNIAIGHVRYSTTGSS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773798955 81 aSEEEAQPFYVNAPFG-IMFAHNGNLTNWRELRESLYRADRrHINTNSDSEVLLNVLAHELQsaasgvsldDDTIFRAVS 159
Cdd:COG0034 87 -SLENAQPFYVNSPFGsIALAHNGNLTNAEELREELEEEGA-IFQTTSDTEVILHLIARELT---------KEDLEEAIK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773798955 160 AVHQRVKGAYAVVAQIsGYGMLAFRDPHGIRPLCIGRQETEegveWMAASESVALEGSGFAFVRDVEPGEAIFVDLDGrM 239
Cdd:COG0034 156 EALRRVKGAYSLVILT-GDGLIAARDPNGIRPLVLGKLEDG----YVVASESCALDILGAEFVRDVEPGEIVVIDEDG-L 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773798955 240 TSRQCADNAQLVPCIFEYVYFARPDSLIDGVSVYDARLRMGEYLADK--VarsmrlgDIDVVMPIPDSSRPAAMQLAHRL 317
Cdd:COG0034 230 RSRQFAEKPRPAPCIFEYVYFARPDSVIDGRSVYEARKRMGRELAREapV-------DADVVIPVPDSGRPAAIGYAEES 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773798955 318 GLDYREGLIKNRYVGRTFIMPGQAVRRKSVRQKLNAIGMEFKGKNVLLVDDSIVRGTTSREIVDMARAAGANKVYFASAA 397
Cdd:COG0034 303 GIPYEEGLIKNRYVGRTFIQPTQELRELGVRLKLNPIREVVKGKRVVLVDDSIVRGTTSRRIVKMLREAGAKEVHFRIAS 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773798955 398 PPVRFPNVYGIDMPTQKELIATGRTDDEIARTIGADALIYQDLQDMQQAVRDINPrlsRFEASCFDGEYVTGdITAEYLA 477
Cdd:COG0034 383 PPIRYPCYYGIDTPTREELIAANRSVEEIREYIGADSLGYLSLEGLIEAVGEPIE---GFCTACFTGDYPTG-IPDEEKK 458
|
....*.
gi 1773798955 478 RLGQSR 483
Cdd:COG0034 459 RLELLR 464
|
|
| purF |
TIGR01134 |
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ... |
2-467 |
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: 612.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773798955 2 CGIVGVIGRGPVNQLLYDSLLLL-QHRGQDAAGIATLQGNHFNMYKAHGLVRDVFRTRNMRALPGTSGVGQVRYPTAGSS 80
Cdd:TIGR01134 1 CGVVGIYGQEEVAASLTYYGLYAlQHRGQESAGISVFDGNRFRLHKGNGLVSDVFNEEHLQRLKGNVGIGHVRYSTAGSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773798955 81 ASEEeAQPFYVNAPFG-IMFAHNGNLTNWRELRESLyRADRRHINTNSDSEVLLNVLAHELQSaasgvsldDDTIFRAVS 159
Cdd:TIGR01134 81 GLEN-AQPFVVNSPYGgLALAHNGNLVNADELRREL-EEEGRHFNTTSDSEVLLHLLAHNDES--------KDDLFDAVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773798955 160 AVHQRVKGAYAVVAqISGYGMLAFRDPHGIRPLCIGRQETEegveWMAASESVALEGSGFAFVRDVEPGEAIFVDlDGRM 239
Cdd:TIGR01134 151 RVLERVRGAYALVL-MTEDGLVAVRDPHGIRPLVLGRRGDG----YVVASESCALDILGAEFVRDVEPGEVVVIF-DGGL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773798955 240 TSRQCADNAQlVPCIFEYVYFARPDSLIDGVSVYDARLRMGEYLADKVARsmrlgDIDVVMPIPDSSRPAAMQLAHRLGL 319
Cdd:TIGR01134 225 ESRQCARRPR-APCVFEYVYFARPDSVIDGISVYYARKRMGKELARESPV-----EADVVVPVPDSGRSAALGFAQASGI 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773798955 320 DYREGLIKNRYVGRTFIMPGQAVRRKSVRQKLNAIGMEFKGKNVLLVDDSIVRGTTSREIVDMARAAGANKVYFASAAPP 399
Cdd:TIGR01134 299 PYREGLIKNRYVGRTFIMPTQELRELSVRLKLNPVRAVFEGKRVVLVDDSIVRGTTSRQIVEMLRDAGAKEVHVRIASPP 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1773798955 400 VRFPNVYGIDMPTQKELIATGRTDDEIaRTIGADALIYQDLQDMQQAVRdiNPRlSRFEASCFDGEYV 467
Cdd:TIGR01134 379 IRYPCYYGIDMPTREELIAARRTVEEI-RKIGADSLAYLSLEGLKEAVG--NPE-SDLCLACFTGEYP 442
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
1-479 |
0e+00 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 571.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773798955 1 MCGIVGVIGRGPVNQLLYDSLLLLQHRGQDAAGIATLQGNHFNMYKAHGLVRDVFRTRNMRALPGTSGVGQVRYPTAGSS 80
Cdd:PLN02440 1 ECGVVGIFGDPEASRLCYLGLHALQHRGQEGAGIVTVDGNRLQSITGNGLVSDVFDESKLDQLPGDIAIGHVRYSTAGAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773798955 81 aSEEEAQPFYVNAPFG-IMFAHNGNLTNWRELRESLyRADRRHINTNSDSEVLLNVLAHELQsaasgvslddDTIFRAVS 159
Cdd:PLN02440 81 -SLKNVQPFVANYRFGsIGVAHNGNLVNYEELRAKL-EENGSIFNTSSDTEVLLHLIAISKA----------RPFFSRIV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773798955 160 AVHQRVKGAYAVVAQISGYgMLAFRDPHGIRPLCIGRQETEEgveWMAASESVALEGSGFAFVRDVEPGEAIFVDlDGRM 239
Cdd:PLN02440 149 DACEKLKGAYSMVFLTEDK-LVAVRDPHGFRPLVMGRRSNGA---VVFASETCALDLIGATYEREVNPGEVIVVD-KDKG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773798955 240 TSRQCA-DNAQLVPCIFEYVYFARPDSLIDGVSVYDARLRMGEYLADKVARsmrlgDIDVVMPIPDSSRPAAMQLAHRLG 318
Cdd:PLN02440 224 VSSQCLmPHPEPKPCIFEHIYFARPNSIVFGRSVYESRLEFGEILATEIPV-----DCDVVIPVPDSGRVAALGYAAKLG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773798955 319 LDYREGLIKNRYVGRTFIMPGQAVRRKSVRQKLNAIGMEFKGKNVLLVDDSIVRGTTSREIVDMARAAGANKVYFASAAP 398
Cdd:PLN02440 299 VPFQQGLIRSHYVGRTFIEPSQKIRDFSVKLKLNPVRSVLEGKRVVVVDDSIVRGTTSSKIVRMLREAGAKEVHMRIASP 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773798955 399 PVRFPNVYGIDMPTQKELIATGRTDDEIARTIGADALIYQDLQDMQQAVRDINPrlsRFEASCFDGEY------VTGDIT 472
Cdd:PLN02440 379 PIIASCYYGVDTPSREELISNRMSVEEIRKFIGCDSLAFLPLEDLKKSLGEESP---RFCYACFSGDYpvlpkrVGGDID 455
|
....*..
gi 1773798955 473 AEYLARL 479
Cdd:PLN02440 456 DGYLESL 462
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
2-466 |
2.28e-146 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 427.91 E-value: 2.28e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773798955 2 CGIVGVIGRGP--VNQLLYDSLLLLQHRGQDAAGIATLQGNHFNMYKAHGLVRDVFRTRNMRALPGTSGVGQVRYPTAGS 79
Cdd:PRK05793 15 CGVFGVFSKNNidVASLTYYGLYALQHRGQESAGIAVSDGEKIKVHKGMGLVSEVFSKEKLKGLKGNSAIGHVRYSTTGA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773798955 80 SASEEeAQPFYVNAPFG-IMFAHNGNLTNWRELRESLYRADRRhINTNSDSEVLLNVLAHELQSAasgvsldddtIFRAV 158
Cdd:PRK05793 95 SDLDN-AQPLVANYKLGsIAIAHNGNLVNADVIRELLEDGGRI-FQTSIDSEVILNLIARSAKKG----------LEKAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773798955 159 SAVHQRVKGAYAVVAqISGYGMLAFRDPHGIRPLCIGRQEteegVEWMAASESVALEGSGFAFVRDVEPGEAIFVDLDGr 238
Cdd:PRK05793 163 VDAIQAIKGSYALVI-LTEDKLIGVRDPHGIRPLCLGKLG----DDYILSSESCALDTIGAEFIRDVEPGEIVIIDEDG- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773798955 239 MTSRQCADNAQLVPCIFEYVYFARPDSLIDGVSVYDARLRMGEYLADKVARsmrlgDIDVVMPIPDSSRPAAMQLAHRLG 318
Cdd:PRK05793 237 IKSIKFAEKTKCQTCAFEYIYFARPDSVIDGISVYESRVRAGRQLYKEYPV-----DADIVIGVPDSGIPAAIGYAEASG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773798955 319 LDYREGLIKNRYVGRTFIMPGQAVRRKSVRQKLNAIGMEFKGKNVLLVDDSIVRGTTSREIVDMARAAGANKVYFASAAP 398
Cdd:PRK05793 312 IPYGIGFIKNKYVGRTFIAPSQELRERAVRVKLNPLKVNVEGKRVVLIDDSIVRGTTSKRLVELLRKAGAKEVHFRVSSP 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1773798955 399 PVRFPNVYGIDMPTQKELIATGRTDDEIARTIGADALIYQDLQDMQQAVRDinprLSRFEASCFDGEY 466
Cdd:PRK05793 392 PVKYPCYFGIDTPYRKELIGANMSVEEIREMIGADSLGYLSIEGLLESLNG----DKGFCLGCFNGVY 455
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
2-268 |
2.46e-126 |
|
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: 368.33 E-value: 2.46e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773798955 2 CGIVGVIGRGPVNQLLYDSLLLLQHRGQDAAGIATLQGNHFNMYKAHGLVRDVFRTRNMRALPGTSGVGQVRYPTAGSSA 81
Cdd:cd00715 1 CGVFGIYGAEDAARLTYLGLYALQHRGQESAGIATSDGKRFHTHKGMGLVSDVFDEEKLRRLPGNIAIGHVRYSTAGSSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773798955 82 SeEEAQPFYVNAPFG-IMFAHNGNLTNWRELRESLYRADrRHINTNSDSEVLLNVLAHelqsaasgvSLDDDTIFRAVSA 160
Cdd:cd00715 81 L-ENAQPFVVNSPLGgIALAHNGNLVNAKELREELEEEG-RIFQTTSDSEVILHLIAR---------SLAKDDLFEAIID 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773798955 161 VHQRVKGAYAVVAqISGYGMLAFRDPHGIRPLCIGRQETEegvEWMAASESVALEGSGFAFVRDVEPGEAIFVDLDGrMT 240
Cdd:cd00715 150 ALERVKGAYSLVI-MTADGLIAVRDPHGIRPLVLGKLEGD---GYVVASESCALDIIGAEFVRDVEPGEIVVIDDDG-LE 224
|
250 260
....*....|....*....|....*...
gi 1773798955 241 SRQCADNAQLVPCIFEYVYFARPDSLID 268
Cdd:cd00715 225 SSQRAPKPKPAPCIFEYVYFARPDSVID 252
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
2-231 |
9.22e-53 |
|
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: 178.03 E-value: 9.22e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773798955 2 CGIVGVIGRGPVNQLLYDSLLLL----QHRGQDAAGIATLQGNHFNMYKAHGLVRDVFRTRNMRALPGTSGVGQVRYPTA 77
Cdd:cd00352 1 CGIFGIVGADGAASLLLLLLLRGlaalEHRGPDGAGIAVYDGDGLFVEKRAGPVSDVALDLLDEPLKSGVALGHVRLATN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773798955 78 GSSaSEEEAQPFYVNaPFGIMFAHNGNLTNWRELRESLyRADRRHINTNSDSEVLLNVLAHElqsaasgvsLDDDTIFRA 157
Cdd:cd00352 81 GLP-SEANAQPFRSE-DGRIALVHNGEIYNYRELREEL-EARGYRFEGESDSEVILHLLERL---------GREGGLFEA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1773798955 158 VSAVHQRVKGAYAVVAQISGYG-MLAFRDPHGIRPLCIGRqeTEEGvEWMAASESVALEGSGFAFVRDVEPGEAI 231
Cdd:cd00352 149 VEDALKRLDGPFAFALWDGKPDrLFAARDRFGIRPLYYGI--TKDG-GLVFASEPKALLALPFKGVRRLPPGELL 220
|
|
| PRTases_typeI |
cd06223 |
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ... |
279-398 |
8.08e-20 |
|
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: 85.53 E-value: 8.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773798955 279 MGEYLADKVARSmrLGDIDVVMPIPDSSRPAAMQLAHRLGLDYREGLIKNRYVGRTFIMPgqavrrksvRQKLNAIGMEF 358
Cdd:cd06223 1 AGRLLAEEIRED--LLEPDVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSEP---------YGLELPLGGDV 69
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1773798955 359 KGKNVLLVDDSIVRGTTSREIVDMARAAGANKVYFASAAP 398
Cdd:cd06223 70 KGKRVLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVLLD 109
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
2-225 |
3.37e-18 |
|
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: 83.27 E-value: 3.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773798955 2 CGIVGVIGRGPVNQLLYDSLLLLQHRGQDAAGIATLQGNHFNMYKAHGLVRDVFRTRNMRALPGTSGVGQVRYPTAGsSA 81
Cdd:cd00714 1 CGIVGYIGKREAVDILLEGLKRLEYRGYDSAGIAVIGDGSLEVVKAVGKVANLEEKLAEKPLSGHVGIGHTRWATHG-EP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773798955 82 SEEEAQPfYVNAPFGIMFAHNGNLTNWRELRESLyrADRRHI-NTNSDSEVLLNVLAHELQSaasgvsldDDTIFRAVSA 160
Cdd:cd00714 80 TDVNAHP-HRSCDGEIAVVHNGIIENYAELKEEL--EAKGYKfESETDTEVIAHLIEYYYDG--------GLDLLEAVKK 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1773798955 161 VHQRVKGAYAVVAQISGYgmlafrdPHGI---R---PLCIGRQETEEGVewmaASESVALegsgFAFVRDV 225
Cdd:cd00714 149 ALKRLEGAYALAVISKDE-------PDEIvaaRngsPLVIGIGDGENFV----ASDAPAL----LEHTRRV 204
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
2-214 |
6.94e-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: 74.23 E-value: 6.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773798955 2 CGIVGVIGRGPVNQLLYDSL---LLLQHRG-QDAAGIATLQGNH---------FNMYKAHGLVRDVFRTRNMRALPGTSG 68
Cdd:cd01907 1 CGIFGIMSKDGEPFVGALLVemlDAMQERGpGDGAGFALYGDPDafvyssgkdMEVFKGVGYPEDIARRYDLEEYKGYHW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773798955 69 VGQVRYPTaGSSASEEEAQPFYVnapFGIMFAHNGNLTNWRELRESLYRAdRRHINTNSDSEVLLNVLAHELQSAASGVS 148
Cdd:cd01907 81 IAHTRQPT-NSAVWWYGAHPFSI---GDIAVVHNGEISNYGSNREYLERF-GYKFETETDTEVIAYYLDLLLRKGGLPLE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1773798955 149 LDDDTIFR-----------AVSAVHQRVKGAYAVVAQISGyGMLAFRDPHGIRPLCIGrqETEEgvEWMAASESVAL 214
Cdd:cd01907 156 YYKHIIRMpeeerelllalRLTYRLADLDGPFTIIVGTPD-GFIVIRDRIKLRPAVVA--ETDD--YVAIASEECAI 227
|
|
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
1-243 |
5.35e-13 |
|
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: 71.20 E-value: 5.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773798955 1 MCGIVGVIGRGPVnqllydsllllQ-----------HRGQDAAGIATLQGNHFNMYKAHGLVRDVFRTRNMRALPGTSGV 69
Cdd:COG0449 1 MCGIVGYIGKRDA-----------ApilleglkrleYRGYDSAGIAVLDDGGLEVRKAVGKLANLEEKLAEEPLSGTIGI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773798955 70 GQVRYPTAGsSASEEEAQP-------FYVnapfgimfAHNGNLTNWRELRESLyRADRRHINTNSDSEVLLNVLAHELQS 142
Cdd:COG0449 70 GHTRWATHG-APSDENAHPhtscsgrIAV--------VHNGIIENYAELREEL-EAKGHTFKSETDTEVIAHLIEEYLKG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773798955 143 AASgvsldddtIFRAVSAVHQRVKGAYAVVAqisgygMLAfRDPHGI---R---PLCIGRQETeegvEWMAASESVALEG 216
Cdd:COG0449 140 GGD--------LLEAVRKALKRLEGAYALAV------ISA-DEPDRIvaaRkgsPLVIGLGEG----ENFLASDVPALLP 200
|
250 260 270
....*....|....*....|....*....|....
gi 1773798955 217 --SGFAFVRD-----VEPGEAIFVDLDGRMTSRQ 243
Cdd:COG0449 201 ytRRVIYLEDgeiavLTRDGVEIYDLDGEPVERE 234
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-215 |
8.45e-13 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 70.82 E-value: 8.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773798955 1 MCGIVGVIGRGPVNQLLYDSLLLLQHRGQDAAGIATLQ----------------GNHFNMYKAHGLvrdvfrtrnMRALP 64
Cdd:PTZ00295 24 CCGIVGYLGNEDASKILLEGIEILQNRGYDSCGISTISsggelkttkyasdgttSDSIEILKEKLL---------DSHKN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773798955 65 GTSGVGQVRYPTAGSSaSEEEAQPfYVNAPFGIMFAHNGNLTNWRELRESLYrADRRHINTNSDSEVLLNVLAHELQsaa 144
Cdd:PTZ00295 95 STIGIAHTRWATHGGK-TDENAHP-HCDYKKRIALVHNGTIENYVELKSELI-AKGIKFRSETDSEVIANLIGLELD--- 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1773798955 145 sgvslDDDTIFRAVSAVHQRVKG--AYAVVAQISGYGMLAFRdpHGiRPLCIGRQETEEGVewmaASESVALE 215
Cdd:PTZ00295 169 -----QGEDFQEAVKSAISRLQGtwGLCIIHKDNPDSLIVAR--NG-SPLLVGIGDDSIYV----ASEPSAFA 229
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
1-173 |
1.68e-12 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 69.69 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773798955 1 MCGIVGVIGRGPVNQLLYDSLLLLQHRGQDAAGIATLQGNHFNMYKAHGLVRDVFRTRNMRALPGTSGVGQVRYPTAGsS 80
Cdd:PRK00331 1 MCGIVGYVGQRNAAEILLEGLKRLEYRGYDSAGIAVLDDGGLEVRKAVGKVANLEAKLEEEPLPGTTGIGHTRWATHG-K 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773798955 81 ASEEEAQP-------FYVnapfgimfAHNGNLTNWRELRESLyRADRRHINTNSDSEVLLNVLAHELQsaasgvslDDDT 153
Cdd:PRK00331 80 PTERNAHPhtdcsgrIAV--------VHNGIIENYAELKEEL-LAKGHVFKSETDTEVIAHLIEEELK--------EGGD 142
|
170 180
....*....|....*....|
gi 1773798955 154 IFRAVSAVHQRVKGAYAVVA 173
Cdd:PRK00331 143 LLEAVRKALKRLEGAYALAV 162
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
65-210 |
6.93e-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: 433279 [Multi-domain] Cd Length: 130 Bit Score: 62.71 E-value: 6.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773798955 65 GTSGVGQVRYPTAGssASEEEAQPFYVNAPfGIMFAHNGNLTNWRELREsLYRADRRHINTNSDSEVLLNVLAHelqsaa 144
Cdd:pfam13522 10 GGVALGHVRLAIVD--LPDAGNQPMLSRDG-RLVLVHNGEIYNYGELRE-ELADLGHAFRSRSDTEVLLALYEE------ 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1773798955 145 sgvsLDDDTIfravsavhQRVKGAYAVVA--QISGYGMLAfRDPHGIRPLCIGrqETEEGVEWmaASE 210
Cdd:pfam13522 80 ----WGEDCL--------ERLRGMFAFAIwdRRRRTLFLA-RDRLGIKPLYYG--ILGGGFVF--ASE 130
|
|
| YafJ |
COG0121 |
Predicted glutamine amidotransferase YafJ [General function prediction only]; |
72-241 |
8.78e-11 |
|
Predicted glutamine amidotransferase YafJ [General function prediction only];
Pssm-ID: 439891 [Multi-domain] Cd Length: 248 Bit Score: 62.29 E-value: 8.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773798955 72 VRYPTAGSSaSEEEAQPFYVnapFGIMFAHNGNLTNW----RELRESLYRADRRHINTNSDSEVLLNVLAHELQsaaSGV 147
Cdd:COG0121 83 VRKATVGPV-SLENTHPFRG---GRWLFAHNGQLDGFdrlrRRLAEELPDELYFQPVGTTDSELAFALLLSRLR---DGG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773798955 148 SLDDDTIFRAVSAVHQ--RVKGAYAVVAqISGYGMLAFRDPHGIRP--LCIGRQETEEGVEWMAASESVALEGSGfafvR 223
Cdd:COG0121 156 PDPAEALAEALRELAElaRAPGRLNLLL-SDGERLYATRYTSDDPYptLYYLTRTTPDDRVVVVASEPLTDDEGW----T 230
|
170
....*....|....*...
gi 1773798955 224 DVEPGEAIFVDLDGRMTS 241
Cdd:COG0121 231 EVPPGELLVVRDGLEVEV 248
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
82-214 |
1.24e-09 |
|
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: 55.99 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773798955 82 SEEEAQPFYVNAPFGIMFAHNGNLTNWRELRESLYRADRRHiNTNSDSEVLLNVLAHElqsaasgvsldddtifRAVSAV 161
Cdd:pfam13537 9 LEGGAQPMVSSEDGRYVIVFNGEIYNYRELRAELEAKGYRF-RTHSDTEVILHLYEAE----------------WGEDCV 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1773798955 162 HqRVKGAYAVV-----AQIsgygMLAFRDPHGIRPLCIGRQeteEGVEWMAASESVAL 214
Cdd:pfam13537 72 D-RLNGMFAFAiwdrrRQR----LFLARDRFGIKPLYYGRD---DGGRLLFASELKAL 121
|
|
| ComFC |
COG1040 |
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General ... |
273-397 |
2.35e-08 |
|
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General function prediction only];
Pssm-ID: 440662 [Multi-domain] Cd Length: 196 Bit Score: 54.06 E-value: 2.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773798955 273 YDARLRMGEYLADKVARSMR---LGDIDVVMPIPdsSRPAAM-------------QLAHRLGLDYR-EGLIKNRYVGRTF 335
Cdd:COG1040 53 YRGRLDLARLLARLLARALRealLPRPDLIVPVP--LHRRRLrrrgfnqaellarALARALGIPVLpDLLRRVRATPSQA 130
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1773798955 336 IMPGQAvRRKSVRQKLNAIGME-FKGKNVLLVDDsiVR--GTTSREIVDMARAAGANKVYFASAA 397
Cdd:COG1040 131 GLSRAE-RRRNLRGAFAVRPPArLAGKHVLLVDD--VLttGATLAEAARALKAAGAARVDVLVLA 192
|
|
| YafJ |
cd01908 |
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ... |
72-236 |
2.62e-08 |
|
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: 55.09 E-value: 2.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773798955 72 VRYPTAGSsASEEEAQPFYVNapfGIMFAHNGNLTNWRELRESLYRADRRHINTNSDSEVLLNVLAHELQSAasgvslDD 151
Cdd:cd01908 87 VRAATVGP-VSLENCHPFTRG---RWLFAHNGQLDGFRLLRRRLLRLLPRLPVGTTDSELAFALLLSRLLER------DP 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773798955 152 DTIFRAVSAVHQRVK-----------------GAYAVVAQISGYGMLAF--RDPHGIRPLCIGRQETEEGVE-WMAASES 211
Cdd:cd01908 157 LDPAELLDAILQTLRelaalappgrlnlllsdGEYLIATRYASAPSLYYltRRAPFGCARLLFRSVTTPNDDgVVVASEP 236
|
170 180
....*....|....*....|....*
gi 1773798955 212 VALEGSgfafVRDVEPGEAIFVDLD 236
Cdd:cd01908 237 LTDDEG----WTEVPPGELVVVSEG 257
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-237 |
2.56e-07 |
|
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: 51.40 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773798955 2 CGIVGVIGRGPVNQLLYDSLLLLQ---HRGQDAAGIATLQGNHFnmykAHglvrdvfrtrnmRALpgtSGVGqvryPTAG 78
Cdd:cd00712 1 CGIAGIIGLDGASVDRATLERMLDalaHRGPDGSGIWIDEGVAL----GH------------RRL---SIID----LSGG 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773798955 79 ssaseeeAQPFYvNAPFGIMFAHNGNLTNWRELRESLyRADRRHINTNSDSEVLLNVLAHelqsaasgvsLDDDTIfrav 158
Cdd:cd00712 58 -------AQPMV-SEDGRLVLVFNGEIYNYRELRAEL-EALGHRFRTHSDTEVILHLYEE----------WGEDCL---- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773798955 159 savhQRVKGAYAVV-----AQIsgygMLAFRDPHGIRPLCIGRQE----------------------TEEGVEWMAASES 211
Cdd:cd00712 115 ----ERLNGMFAFAlwdkrKRR----LFLARDRFGIKPLYYGRDGgglafaselkallalpgvprelDEAALAEYLAFQY 186
|
250 260
....*....|....*....|....*.
gi 1773798955 212 VALEGSGFAFVRDVEPGEAIFVDLDG 237
Cdd:cd00712 187 VPAPRTIFKGIRKLPPGHYLTVDPGG 212
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-243 |
5.41e-07 |
|
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: 52.15 E-value: 5.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773798955 1 MCGIVGVIGR-GPVNQLLYDSLLLLQ-HRGQDAAGIATLQGNHFnmykAHglVR----DVfrtrnmralpgtsgvgqvry 74
Cdd:COG0367 1 MCGIAGIIDFdGGADREVLERMLDALaHRGPDGSGIWVDGGVAL----GH--RRlsiiDL-------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773798955 75 ptagssaSEEEAQPFyVNAPFGIMFAHNGNLTNWRELRESLyRADRRHINTNSDSEVLLNVLAHElqsaasGVSLDDDti 154
Cdd:COG0367 55 -------SEGGHQPM-VSEDGRYVLVFNGEIYNYRELRAEL-EALGHRFRTHSDTEVILHAYEEW------GEDCLER-- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773798955 155 FR---AVsAVHQRVKGAyavvaqisgygMLAFRDPHGIRPLCIGrqETEEGveWMAASESVALEGSG------------- 218
Cdd:COG0367 118 LNgmfAF-AIWDRRERR-----------LFLARDRFGIKPLYYA--EDGGG--LAFASELKALLAHPgvdreldpealae 181
|
250 260 270
....*....|....*....|....*....|....*...
gi 1773798955 219 -FAF------------VRDVEPGEAIFVDLDGRMTSRQ 243
Cdd:COG0367 182 yLTLgyvpaprtifkgIRKLPPGHYLTVDAGGELEIRR 219
|
|
| pyrE |
PRK00455 |
orotate phosphoribosyltransferase; Validated |
274-389 |
6.69e-06 |
|
orotate phosphoribosyltransferase; Validated
Pssm-ID: 234771 Cd Length: 202 Bit Score: 47.07 E-value: 6.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773798955 274 DARLRMGEYLADKVARSmrLGDIDVVM-P----IPdssrpAAMQLAHRLGLDY----REGliKNRYVGRTFImpgqavrr 344
Cdd:PRK00455 45 EALALLGRFLAEAIKDS--GIEFDVVAgPatggIP-----LAAAVARALDLPAifvrKEA--KDHGEGGQIE-------- 107
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1773798955 345 ksvrqklnaiGMEFKGKNVLLVDDSIVRGTTSREIVDMARAAGAN 389
Cdd:PRK00455 108 ----------GRRLFGKRVLVVEDVITTGGSVLEAVEAIRAAGAE 142
|
|
| PRK08558 |
PRK08558 |
adenine phosphoribosyltransferase; Provisional |
281-391 |
4.37e-05 |
|
adenine phosphoribosyltransferase; Provisional
Pssm-ID: 181466 [Multi-domain] Cd Length: 238 Bit Score: 44.98 E-value: 4.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773798955 281 EYLADKVARSMRLGDIDVVMPIPDSSRPAAMQLAHRLGLD------YREGLIKNRYVGR---------TFIMPGQAVRRk 345
Cdd:PRK08558 97 RLIAPVVAERFMGLRVDVVLTAATDGIPLAVAIASYFGADlvyakkSKETGVEKFYEEYqrlasgievTLYLPASALKK- 175
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1773798955 346 svrqklnaigmefkGKNVLLVDDSIVRGTTSREIVDMARAAGANKV 391
Cdd:PRK08558 176 --------------GDRVLIVDDIIRSGETQRALLDLARQAGADVV 207
|
|
| Pribosyltran |
pfam00156 |
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ... |
296-411 |
2.60e-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: 41.58 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773798955 296 IDVVMPIPDSSRPAAMQLAHRLGLDYrEGLIKNRYVGRTfiMPGQAVRRKSvrqklnaigMEFKGKNVLLVDDSIVRGTT 375
Cdd:pfam00156 30 PDVVVGILRGGLPFAGILARRLDVPL-AFVRKVSYNPDT--SEVMKTSSAL---------PDLKGKTVLIVDDILDTGGT 97
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1773798955 376 SREIVDMARAAGANKVYFA------SAAPPVRFPNVYGIDMP 411
Cdd:pfam00156 98 LLKVLELLKNVGPKEVKIAvlidkpAGTEPKDKYDKRVDDWI 139
|
|
| PyrE |
COG0461 |
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ... |
274-389 |
3.63e-04 |
|
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate phosphoribosyltransferase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 440229 Cd Length: 201 Bit Score: 41.68 E-value: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773798955 274 DARLRMGEYLADKVARSmrLGDIDVVMPIPDSSRPAAMQLAHRLGLDYRegliknrYVgrtfimpgqavrRKSVRQ--KL 351
Cdd:COG0461 44 EALELLGEALAELIKEL--GPEFDAVAGPATGGIPLAAAVARALGLPAI-------FV------------RKEAKDhgTG 102
|
90 100 110
....*....|....*....|....*....|....*....
gi 1773798955 352 NAI-GMEFKGKNVLLVDDSIVRGTTSREIVDMARAAGAN 389
Cdd:COG0461 103 GQIeGGLLPGERVLVVEDVITTGGSVLEAVEALREAGAE 141
|
|
| PRK00934 |
PRK00934 |
ribose-phosphate pyrophosphokinase; Provisional |
280-400 |
1.04e-03 |
|
ribose-phosphate pyrophosphokinase; Provisional
Pssm-ID: 234868 [Multi-domain] Cd Length: 285 Bit Score: 41.05 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773798955 280 GEYLADKVARSMRLGdidvvmpiPDSsrpAAMQLAHR----LGLDYrEGLIKNRYVGRTFIMpgqAVRRKSVrqklnaig 355
Cdd:PRK00934 146 AEYIGDKLDDPLVLA--------PDK---GALELAKEaaeiLGCEY-DYLEKTRISPTEVEI---APKNLDV-------- 202
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1773798955 356 mefKGKNVLLVDDSIVRGTTSREIVDMARAAGANKVYfASAAPPV 400
Cdd:PRK00934 203 ---KGKDVLIVDDIISTGGTMATAIKILKEQGAKKVY-VACVHPV 243
|
|
| PRK11595 |
PRK11595 |
DNA utilization protein GntX; Provisional |
275-391 |
1.42e-03 |
|
DNA utilization protein GntX; Provisional
Pssm-ID: 183221 [Multi-domain] Cd Length: 227 Bit Score: 40.41 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773798955 275 ARLRMGEYLadKVARSMRLGDIDVVMPIP-----------DSSRPAAMQLAHRLGLDYREGLIKnryvgRTFIMPGQ--- 340
Cdd:PRK11595 94 ARLLLLEWL--QARRSTGLQKPDRIISVPlhqrrhwrrgfNQSDLLCRPLARWLGCDYDSEALT-----RTRATATQhfl 166
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1773798955 341 --AVRRKSVRqklNAIGME--FKGKNVLLVDDSIVRGTTSREIVDMARAAGANKV 391
Cdd:PRK11595 167 saRLRKRNLK---NAFRLElpVQGQHMAIVDDVVTTGSTVAEIAQLLLRNGAASV 218
|
|
| Hpt1 |
COG2236 |
Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine ... |
307-394 |
1.78e-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: 39.06 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773798955 307 RPAAMqLAHRLGLDYREGLIKNRYVGrtfimPGQAVRRKSVRQKLNAigmEFKGKNVLLVDDSIVRGTTSREIVDMARAA 386
Cdd:COG2236 44 VPARI-LADALGVPDLASIRVSSYTG-----TAKRLEEPVVKGPLDE---DLAGKRVLIVDDVADTGRTLEAVRDLLKEA 114
|
....*...
gi 1773798955 387 GANKVYFA 394
Cdd:COG2236 115 GPAEVRTA 122
|
|
| |
