|
Name |
Accession |
Description |
Interval |
E-value |
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
30-499 |
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: 779.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 30 SPREECGVFGVWAPgEDVSKLTYYGLFALQHRGQEAAGIAVGDGDQILVFKDLGLVSQVFDEQTLDALKGHVAVGHTRYT 109
Cdd:COG0034 3 KLHEECGVFGIYGH-EDVAQLTYYGLYALQHRGQESAGIATSDGGRFHLHKGMGLVSDVFDEEDLERLKGNIAIGHVRYS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 110 TAGAPAWENAQPMFQMASDGTdIALGHNGNLTNHLTLFHEavdkglLREEGELP---SDSAIMTTLLADETGKidhpedy 186
Cdd:COG0034 82 TTGSSSLENAQPFYVNSPFGS-IALAHNGNLTNAEELREE------LEEEGAIFqttSDTEVILHLIARELTK------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 187 gcsTNVEAAAMALLPRLKGAFCLTFTDGETLYAARDPYGVRPLCLGRLSGGWVVASETCALDIVGASFVREIEPGEMVTI 266
Cdd:COG0034 148 ---EDLEEAIKEALRRVKGAYSLVILTGDGLIAARDPNGIRPLVLGKLEDGYVVASESCALDILGAEFVRDVEPGEIVVI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 267 DASGVRSQRFAETT-HAGCIFEYVYLARPDSNIRGRSVNAVRLELGRQLAREFPADGDLVMPVPESGTPAAVGYAQESGI 345
Cdd:COG0034 225 DEDGLRSRQFAEKPrPAPCIFEYVYFARPDSVIDGRSVYEARKRMGRELAREAPVDADVVIPVPDSGRPAAIGYAEESGI 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 346 PFGQGLTKNGYVGRTFIQPSQTIRQLGIRLKLNPLKEVIAGKRLVVVDDSIVRGNTQRALIRMLREAGAKEVHVRIAAPP 425
Cdd:COG0034 305 PYEEGLIKNRYVGRTFIQPTQELRELGVRLKLNPIREVVKGKRVVLVDDSIVRGTTSRRIVKMLREAGAKEVHFRIASPP 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896182530 426 VKWPCFYGIDFASPGELLANGVDendiVAGIATAIGADSLGFVSIDGMVAASEQAKTEVCCACFDGKYPLGLPE 499
Cdd:COG0034 385 IRYPCYYGIDTPTREELIAANRS----VEEIREYIGADSLGYLSLEGLIEAVGEPIEGFCTACFTGDYPTGIPD 454
|
|
| purF |
TIGR01134 |
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ... |
35-494 |
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: 631.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 35 CGVFGVWAPGEDVSKLTYYGLFALQHRGQEAAGIAVGDGDQILVFKDLGLVSQVFDEQTLDALKGHVAVGHTRYTTAGAP 114
Cdd:TIGR01134 1 CGVVGIYGQEEVAASLTYYGLYALQHRGQESAGISVFDGNRFRLHKGNGLVSDVFNEEHLQRLKGNVGIGHVRYSTAGSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 115 AWENAQPMFQMASDGtDIALGHNGNLTNHLTLFHEavdkglLREEGEL---PSDSAIMTTLLAdetgKIDHPEDygcstN 191
Cdd:TIGR01134 81 GLENAQPFVVNSPYG-GLALAHNGNLVNADELRRE------LEEEGRHfntTSDSEVLLHLLA----HNDESKD-----D 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 192 VEAAAMALLPRLKGAFCLTFTDGETLYAARDPYGVRPLCLGRLSGGWVVASETCALDIVGASFVREIEPGEMVTIDASGV 271
Cdd:TIGR01134 145 LFDAVARVLERVRGAYALVLMTEDGLVAVRDPHGIRPLVLGRRGDGYVVASESCALDILGAEFVRDVEPGEVVVIFDGGL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 272 RSQRFAETTHAGCIFEYVYLARPDSNIRGRSVNAVRLELGRQLAREFPADGDLVMPVPESGTPAAVGYAQESGIPFGQGL 351
Cdd:TIGR01134 225 ESRQCARRPRAPCVFEYVYFARPDSVIDGISVYYARKRMGKELARESPVEADVVVPVPDSGRSAALGFAQASGIPYREGL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 352 TKNGYVGRTFIQPSQTIRQLGIRLKLNPLKEVIAGKRLVVVDDSIVRGNTQRALIRMLREAGAKEVHVRIAAPPVKWPCF 431
Cdd:TIGR01134 305 IKNRYVGRTFIMPTQELRELSVRLKLNPVRAVFEGKRVVLVDDSIVRGTTSRQIVEMLRDAGAKEVHVRIASPPIRYPCY 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896182530 432 YGIDFASPGELLANGVDENDIvagiaTAIGADSLGFVSIDGMVAASEQAKTEVCCACFDGKYP 494
Cdd:TIGR01134 385 YGIDMPTREELIAARRTVEEI-----RKIGADSLAYLSLEGLKEAVGNPESDLCLACFTGEYP 442
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
25-503 |
0e+00 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 580.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 25 DLGETSPREECGVFGVWAPGE-DVSKLTYYGLFALQHRGQEAAGIAVGDGDQILVFKDLGLVSQVFDEQTLDALKGHVAV 103
Cdd:PRK05793 5 DLEGDKFKEECGVFGVFSKNNiDVASLTYYGLYALQHRGQESAGIAVSDGEKIKVHKGMGLVSEVFSKEKLKGLKGNSAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 104 GHTRYTTAGAPAWENAQPMFQMASDGTdIALGHNGNLTNhltlfhEAVDKGLLREEGEL---PSDSAIMTTLLADETGKi 180
Cdd:PRK05793 85 GHVRYSTTGASDLDNAQPLVANYKLGS-IAIAHNGNLVN------ADVIRELLEDGGRIfqtSIDSEVILNLIARSAKK- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 181 dhpedygcstNVEAAAMALLPRLKGAFCLTFTDGETLYAARDPYGVRPLCLGRLSGGWVVASETCALDIVGASFVREIEP 260
Cdd:PRK05793 157 ----------GLEKALVDAIQAIKGSYALVILTEDKLIGVRDPHGIRPLCLGKLGDDYILSSESCALDTIGAEFIRDVEP 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 261 GEMVTIDASGVRSQRFAETT-HAGCIFEYVYLARPDSNIRGRSVNAVRLELGRQLAREFPADGDLVMPVPESGTPAAVGY 339
Cdd:PRK05793 227 GEIVIIDEDGIKSIKFAEKTkCQTCAFEYIYFARPDSVIDGISVYESRVRAGRQLYKEYPVDADIVIGVPDSGIPAAIGY 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 340 AQESGIPFGQGLTKNGYVGRTFIQPSQTIRQLGIRLKLNPLKEVIAGKRLVVVDDSIVRGNTQRALIRMLREAGAKEVHV 419
Cdd:PRK05793 307 AEASGIPYGIGFIKNKYVGRTFIAPSQELRERAVRVKLNPLKVNVEGKRVVLIDDSIVRGTTSKRLVELLRKAGAKEVHF 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 420 RIAAPPVKWPCFYGIDFASPGELLANgvdeNDIVAGIATAIGADSLGFVSIDGMVAASEqAKTEVCCACFDGKYPLGLPE 499
Cdd:PRK05793 387 RVSSPPVKYPCYFGIDTPYRKELIGA----NMSVEEIREMIGADSLGYLSIEGLLESLN-GDKGFCLGCFNGVYPVSAPK 461
|
....
gi 896182530 500 GNPN 503
Cdd:PRK05793 462 EGPK 465
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
34-494 |
1.79e-172 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 495.35 E-value: 1.79e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 34 ECGVFGVWApGEDVSKLTYYGLFALQHRGQEAAGIAVGDGDQILVFKDLGLVSQVFDEQTLDALKGHVAVGHTRYTTAGA 113
Cdd:PLN02440 1 ECGVVGIFG-DPEASRLCYLGLHALQHRGQEGAGIVTVDGNRLQSITGNGLVSDVFDESKLDQLPGDIAIGHVRYSTAGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 114 PAWENAQPMFQMASDGTdIALGHNGNLTNHLTLfheavdKGLLREEGEL---PSDSAIMTTLLADETGKidhpedygcst 190
Cdd:PLN02440 80 SSLKNVQPFVANYRFGS-IGVAHNGNLVNYEEL------RAKLEENGSIfntSSDTEVLLHLIAISKAR----------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 191 NVEAAAMALLPRLKGAFCLTFTDGETLYAARDPYGVRPLCLGRLSGG-WVVASETCALDIVGASFVREIEPGEMVTIDAS 269
Cdd:PLN02440 142 PFFSRIVDACEKLKGAYSMVFLTEDKLVAVRDPHGFRPLVMGRRSNGaVVFASETCALDLIGATYEREVNPGEVIVVDKD 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 270 GVRSQRFAETT--HAGCIFEYVYLARPDSNIRGRSVNAVRLELGRQLAREFPADGDLVMPVPESGTPAAVGYAQESGIPF 347
Cdd:PLN02440 222 KGVSSQCLMPHpePKPCIFEHIYFARPNSIVFGRSVYESRLEFGEILATEIPVDCDVVIPVPDSGRVAALGYAAKLGVPF 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 348 GQGLTKNGYVGRTFIQPSQTIRQLGIRLKLNPLKEVIAGKRLVVVDDSIVRGNTQRALIRMLREAGAKEVHVRIAAPPVK 427
Cdd:PLN02440 302 QQGLIRSHYVGRTFIEPSQKIRDFSVKLKLNPVRSVLEGKRVVVVDDSIVRGTTSSKIVRMLREAGAKEVHMRIASPPII 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 896182530 428 WPCFYGIDFASPGELLANGVDENdivaGIATAIGADSLGFVSIDGMVAASEQAKTEVCCACFDGKYP 494
Cdd:PLN02440 382 ASCYYGVDTPSREELISNRMSVE----EIRKFIGCDSLAFLPLEDLKKSLGEESPRFCYACFSGDYP 444
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
35-298 |
2.18e-123 |
|
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: 361.39 E-value: 2.18e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 35 CGVFGVWAPgEDVSKLTYYGLFALQHRGQEAAGIAVGDGDQILVFKDLGLVSQVFDEQTLDALKGHVAVGHTRYTTAGAP 114
Cdd:cd00715 1 CGVFGIYGA-EDAARLTYLGLYALQHRGQESAGIATSDGKRFHTHKGMGLVSDVFDEEKLRRLPGNIAIGHVRYSTAGSS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 115 AWENAQPMFQMASDGtDIALGHNGNLTNHLTLfheavdKGLLREEGEL---PSDSAIMTTLLADETGKIDhpedygcstn 191
Cdd:cd00715 80 SLENAQPFVVNSPLG-GIALAHNGNLVNAKEL------REELEEEGRIfqtTSDSEVILHLIARSLAKDD---------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 192 VEAAAMALLPRLKGAFCLTFTDGETLYAARDPYGVRPLCLGRL-SGGWVVASETCALDIVGASFVREIEPGEMVTIDASG 270
Cdd:cd00715 143 LFEAIIDALERVKGAYSLVIMTADGLIAVRDPHGIRPLVLGKLeGDGYVVASESCALDIIGAEFVRDVEPGEIVVIDDDG 222
|
250 260
....*....|....*....|....*....
gi 896182530 271 VRS-QRFAETTHAGCIFEYVYLARPDSNI 298
Cdd:cd00715 223 LESsQRAPKPKPAPCIFEYVYFARPDSVI 251
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
35-264 |
1.38e-62 |
|
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: 203.83 E-value: 1.38e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 35 CGVFGVWAPGEDVSKLTY---YGLFALQHRGQEAAGIAVGDGDQILVFKDLGLVSQVFDEQTLDALKGHVAVGHTRYTTA 111
Cdd:cd00352 1 CGIFGIVGADGAASLLLLlllRGLAALEHRGPDGAGIAVYDGDGLFVEKRAGPVSDVALDLLDEPLKSGVALGHVRLATN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 112 GAPAWENAQPMFqmaSDGTDIALGHNGNLTNHLTLFHEAVDKGLLREEGelpSDSAIMTTLLadetgkidhpEDYGCSTN 191
Cdd:cd00352 81 GLPSEANAQPFR---SEDGRIALVHNGEIYNYRELREELEARGYRFEGE---SDSEVILHLL----------ERLGREGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 896182530 192 VEAAAMALLPRLKGAFCLTFTDG--ETLYAARDPYGVRPLCLGRLS-GGWVVASETCALDIVGASFVREIEPGEMV 264
Cdd:cd00352 145 LFEAVEDALKRLDGPFAFALWDGkpDRLFAARDRFGIRPLYYGITKdGGLVFASEPKALLALPFKGVRRLPPGELL 220
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
35-266 |
1.01e-21 |
|
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: 93.28 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 35 CGVFGVWAPGEDVSKLTYyGLFALQHRGQEAAGIAVGDGDQILVFKDLGLVSQVFDEQTLDALKGHVAVGHTRYTTAGAP 114
Cdd:cd00714 1 CGIVGYIGKREAVDILLE-GLKRLEYRGYDSAGIAVIGDGSLEVVKAVGKVANLEEKLAEKPLSGHVGIGHTRWATHGEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 115 AWENAQPMFqmaSDGTDIALGHNGNLTNHLTLfheavdKGLLREEG-ELPS--DSAIMTTLLADETGKIDHPEDygcstn 191
Cdd:cd00714 80 TDVNAHPHR---SCDGEIAVVHNGIIENYAEL------KEELEAKGyKFESetDTEVIAHLIEYYYDGGLDLLE------ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 192 veaAAMALLPRLKGAFCLTFTD---GETLYAARdpygvR--PLCLGRLSGGWVVASETCALdivgASFVREI---EPGEM 263
Cdd:cd00714 145 ---AVKKALKRLEGAYALAVISkdePDEIVAAR-----NgsPLVIGIGDGENFVASDAPAL----LEHTRRViylEDGDI 212
|
...
gi 896182530 264 VTI 266
Cdd:cd00714 213 AVI 215
|
|
| PRTases_typeI |
cd06223 |
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ... |
310-436 |
6.33e-21 |
|
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: 88.61 E-value: 6.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 310 LGRQLAREFPADG---DLVMPVPESGTPAAVGYAQESGIPFGQGLTKNGYVGRTFIQPSQtirqlgirlKLNPLKEVIAG 386
Cdd:cd06223 1 AGRLLAEEIREDLlepDVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSEPYG---------LELPLGGDVKG 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 896182530 387 KRLVVVDDSIVRGNTQRALIRMLREAGAKEVHVrIAAPPVKWPCFYGIDF 436
Cdd:cd06223 72 KRVLLVDDVIATGGTLLAAIELLKEAGAKVVGV-AVLLDKPEGGARELAS 120
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
35-264 |
3.13e-20 |
|
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: 90.02 E-value: 3.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 35 CGVFGVWA------PGEDVSKltyyGLFALQHRG--QEAAGIAVGDGDQIL--------VFKDLGLVSQVFDEQTLDALK 98
Cdd:cd01907 1 CGIFGIMSkdgepfVGALLVE----MLDAMQERGpgDGAGFALYGDPDAFVyssgkdmeVFKGVGYPEDIARRYDLEEYK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 99 GHVAVGHTRYTTAGAPAWENAQPMFQMasdgtDIALGHNGNLTNHLTLfheavdKGLLREEG---ELPSDSAIMTTLLAD 175
Cdd:cd01907 77 GYHWIAHTRQPTNSAVWWYGAHPFSIG-----DIAVVHNGEISNYGSN------REYLERFGykfETETDTEVIAYYLDL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 176 ETGKIDHPEDYGCSTNVEAAAMALLP----------RLKGAFCLTFTDGETLYAARDPYGVRPLCLGRLSGGWVVASETC 245
Cdd:cd01907 146 LLRKGGLPLEYYKHIIRMPEEERELLlalrltyrlaDLDGPFTIIVGTPDGFIVIRDRIKLRPAVVAETDDYVAIASEEC 225
|
250 260
....*....|....*....|..
gi 896182530 246 ALDIVGAS---FVREIEPGEMV 264
Cdd:cd01907 226 AIREIPDRdnaKVWEPRPGEYV 247
|
|
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
35-272 |
2.12e-18 |
|
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: 88.53 E-value: 2.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 35 CGVFGVWAPgEDVSKLTYYGLFALQHRGQEAAGIAVGDGDQILVFKDLGLVSQVFDEQTLDALKGHVAVGHTRYTTAGAP 114
Cdd:COG0449 2 CGIVGYIGK-RDAAPILLEGLKRLEYRGYDSAGIAVLDDGGLEVRKAVGKLANLEEKLAEEPLSGTIGIGHTRWATHGAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 115 AWENAQPmfQMASDGtDIALGHNGNLTNHLTLfheavdKGLLREEG-ELPS--DSAIMTTLLADEtgkidhpedYGCSTN 191
Cdd:COG0449 81 SDENAHP--HTSCSG-RIAVVHNGIIENYAEL------REELEAKGhTFKSetDTEVIAHLIEEY---------LKGGGD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 192 VEAAAMALLPRLKGAF--CLTFTD-GETLYAAR-DPygvrPLCLGRLSGGWVVASETCALdivgASFVREI---EPGEMV 264
Cdd:COG0449 143 LLEAVRKALKRLEGAYalAVISADePDRIVAARkGS----PLVIGLGEGENFLASDVPAL----LPYTRRViylEDGEIA 214
|
....*...
gi 896182530 265 TIDASGVR 272
Cdd:COG0449 215 VLTRDGVE 222
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
35-272 |
6.62e-18 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 86.64 E-value: 6.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 35 CGVFGVWAPgEDVSKLTYYGLFALQHRGQEAAGIAVGDGDQILVFKDLGLVSQVFDEQTLDALKGHVAVGHTRYTTAGAP 114
Cdd:PRK00331 2 CGIVGYVGQ-RNAAEILLEGLKRLEYRGYDSAGIAVLDDGGLEVRKAVGKVANLEAKLEEEPLPGTTGIGHTRWATHGKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 115 AWENAQPmfQMASDGtDIALGHNGNLTNHLTLfheavdKGLLREEG-ELPS--DSAIMTTLLADEtgkidhpEDYGCSTn 191
Cdd:PRK00331 81 TERNAHP--HTDCSG-RIAVVHNGIIENYAEL------KEELLAKGhVFKSetDTEVIAHLIEEE-------LKEGGDL- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 192 vEAAAMALLPRLKGAF--CLTFTD-GETLYAAR-DPygvrPLCLGRLSGGWVVASETCALdivgASFVREI---EPGEMV 264
Cdd:PRK00331 144 -LEAVRKALKRLEGAYalAVIDKDePDTIVAARnGS----PLVIGLGEGENFLASDALAL----LPYTRRViylEDGEIA 214
|
....*...
gi 896182530 265 TIDASGVR 272
Cdd:PRK00331 215 VLTRDGVE 222
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
35-271 |
6.40e-17 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 83.92 E-value: 6.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 35 CGVFGVWApGEDVSKLTYYGLFALQHRGQEAAGIA-VGDGDQILVFKdlgLVSqvfDEQTLDA---LKG---------HV 101
Cdd:PTZ00295 25 CGIVGYLG-NEDASKILLEGIEILQNRGYDSCGIStISSGGELKTTK---YAS---DGTTSDSieiLKEklldshknsTI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 102 AVGHTRYTTAGAPAWENAQPMFQMASDgtdIALGHNGNLTNHLTLFHEAVDKGL-LREEgelpSDSAIMTTLLADEtgkI 180
Cdd:PTZ00295 98 GIAHTRWATHGGKTDENAHPHCDYKKR---IALVHNGTIENYVELKSELIAKGIkFRSE----TDSEVIANLIGLE---L 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 181 DHPEDYgcstnvEAAAMALLPRLKG--AFCLTFTDG-ETLYAARDPygvRPLCLGRLSGGWVVASETCALdivgASFVRE 257
Cdd:PTZ00295 168 DQGEDF------QEAVKSAISRLQGtwGLCIIHKDNpDSLIVARNG---SPLLVGIGDDSIYVASEPSAF----AKYTNE 234
|
250
....*....|....*..
gi 896182530 258 ---IEPGEMVTIDASGV 271
Cdd:PTZ00295 235 yisLKDGEIAELSLENV 251
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
119-247 |
1.03e-15 |
|
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: 73.32 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 119 AQPMFqmASDGTDIALGHNGNLTNHLTLFHEAVDKGLLREEGelpSDSAIMTTLLADETGKidhpedygcstnveaaamA 198
Cdd:pfam13537 13 AQPMV--SSEDGRYVIVFNGEIYNYRELRAELEAKGYRFRTH---SDTEVILHLYEAEWGE------------------D 69
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 896182530 199 LLPRLKG--AFCLTFTDGETLYAARDPYGVRPLCLGRLSG-GWVVASETCAL 247
Cdd:pfam13537 70 CVDRLNGmfAFAIWDRRRQRLFLARDRFGIKPLYYGRDDGgRLLFASELKAL 121
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
99-243 |
2.65e-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: 63.86 E-value: 2.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 99 GHVAVGHTRYTTAGAPAwENAQPMFqmASDGTdIALGHNGNLTNHLTLFHEAVDKGLlreEGELPSDSAIMTTLLAdETG 178
Cdd:pfam13522 10 GGVALGHVRLAIVDLPD-AGNQPML--SRDGR-LVLVHNGEIYNYGELREELADLGH---AFRSRSDTEVLLALYE-EWG 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 896182530 179 KidhpedygcstnveaaamALLPRLKGAFCLTFTDGE--TLYAARDPYGVRPLCLGRLSGGWVVASE 243
Cdd:pfam13522 82 E------------------DCLERLRGMFAFAIWDRRrrTLFLARDRLGIKPLYYGILGGGFVFASE 130
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
35-276 |
4.11e-12 |
|
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: 65.66 E-value: 4.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 35 CGVFGVW---APGEDVSKLTYyGLFALQHRGQEAAGIAVGDGdqilvfkdlglvsqvfdeqtldalkghVAVGHTRY--- 108
Cdd:cd00712 1 CGIAGIIgldGASVDRATLER-MLDALAHRGPDGSGIWIDEG---------------------------VALGHRRLsii 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 109 -TTAGApawenaQPMFqmaSDGTDIALGHNGNLTNHLTLFHEAVDKGLLREEGelpSDSAImttLLA--DETGKidhped 185
Cdd:cd00712 53 dLSGGA------QPMV---SEDGRLVLVFNGEIYNYRELRAELEALGHRFRTH---SDTEV---ILHlyEEWGE------ 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 186 ygcstnveaaamALLPRLKG--AFCLTFTDGETLYAARDPYGVRPLCLGRLSGGWVVASE---------------TCALD 248
Cdd:cd00712 112 ------------DCLERLNGmfAFALWDKRKRRLFLARDRFGIKPLYYGRDGGGLAFASElkallalpgvpreldEAALA 179
|
250 260 270
....*....|....*....|....*....|....*....
gi 896182530 249 IVGA-----------SFVREIEPGEMVTIDASGVRSQRF 276
Cdd:cd00712 180 EYLAfqyvpaprtifKGIRKLPPGHYLTVDPGGVEIRRY 218
|
|
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
54-211 |
6.16e-12 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 68.24 E-value: 6.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 54 GLFALQHRGQEAAGIAVGDGDQI-----LVFKDLG----LVSQVFDEQTLDALKG------HVAVGHTRYTTAGAPAWEN 118
Cdd:PLN02981 26 GLRRLEYRGYDSAGIAIDNDPSLessspLVFREEGkiesLVRSVYEEVAETDLNLdlvfenHAGIAHTRWATHGPPAPRN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 119 AQPmfQMASDGTDIALGHNGNLTNHLTLFHEAVDKGllrEEGELPSDSAIMTTL-------LADETGKIDHPEdygcstn 191
Cdd:PLN02981 106 SHP--QSSGPGNEFLVVHNGIITNYEVLKETLLRHG---FTFESDTDTEVIPKLakfvfdkLNEEEGDVTFSQ------- 173
|
170 180
....*....|....*....|
gi 896182530 192 veaAAMALLPRLKGAFCLTF 211
Cdd:PLN02981 174 ---VVMEVMRQLEGAYALIF 190
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
35-275 |
1.51e-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: 60.24 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 35 CGVFGVWAPGEDVSKLTYYGLF-ALQHRGQEAAGIAVGdgdqilvfkdlglvsqvfdeqtldalkGHVAVGHTR-----Y 108
Cdd:COG0367 2 CGIAGIIDFDGGADREVLERMLdALAHRGPDGSGIWVD---------------------------GGVALGHRRlsiidL 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 109 TTAGApawenaQPMFqmaSDGTDIALGHNGNLTNHLTLFHEavdkglLREEGELP---SDSAIMTTLLadetgkidhpED 185
Cdd:COG0367 55 SEGGH------QPMV---SEDGRYVLVFNGEIYNYRELRAE------LEALGHRFrthSDTEVILHAY----------EE 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 186 YGcstnveaaaMALLPRLKG--AFCLTFTDGETLYAARDPYGVRPLCLGRLSGGWVVASE----------TCALDIVG-- 251
Cdd:COG0367 110 WG---------EDCLERLNGmfAFAIWDRRERRLFLARDRFGIKPLYYAEDGGGLAFASElkallahpgvDRELDPEAla 180
|
250 260 270
....*....|....*....|....*....|....*...
gi 896182530 252 -----------ASF---VREIEPGEMVTIDASGVRSQR 275
Cdd:COG0367 181 eyltlgyvpapRTIfkgIRKLPPGHYLTVDAGGELEIR 218
|
|
| YafJ |
cd01908 |
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ... |
67-268 |
3.06e-09 |
|
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: 57.78 E-value: 3.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 67 GIAV--GDGDQILVFKDLGLV-SQVFDEQTLDALKGHVAVGHTRYTTAGAPAWENAQPmFQMASdgtdIALGHNGNLTNH 143
Cdd:cd01908 45 GIGWyeGKGGRPFRYRSPLPAwSDINLESLARPIKSPLVLAHVRAATVGPVSLENCHP-FTRGR----WLFAHNGQLDGF 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 144 LTLfheavDKGLLREEGELP---SDSAImttLLADETGKIDHPEDYGCSTNVEAAAMALL----PRLKGAFCLTFTDGET 216
Cdd:cd01908 120 RLL-----RRRLLRLLPRLPvgtTDSEL---AFALLLSRLLERDPLDPAELLDAILQTLRelaaLAPPGRLNLLLSDGEY 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 896182530 217 LYAARDP------YGVRPLCLGRL-----------SGGWVVASETCALDIVgasfVREIEPGEMVTIDA 268
Cdd:cd01908 192 LIATRYAsapslyYLTRRAPFGCArllfrsvttpnDDGVVVASEPLTDDEG----WTEVPPGELVVVSE 256
|
|
| YafJ |
COG0121 |
Predicted glutamine amidotransferase YafJ [General function prediction only]; |
67-270 |
8.26e-09 |
|
Predicted glutamine amidotransferase YafJ [General function prediction only];
Pssm-ID: 439891 [Multi-domain] Cd Length: 248 Bit Score: 56.51 E-value: 8.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 67 GIA-VGDGDQILVFKDlglVSQVFDEQTLDALKGHV----AVGHTRYTTAGAPAWENAQPmFQmasdGTDIALGHNGNLT 141
Cdd:COG0121 42 GIGwYEGDGEPRLYRD---PLPAWSDPNLRLLARPIksrlVIAHVRKATVGPVSLENTHP-FR----GGRWLFAHNGQLD 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 142 N----HLTLFHEAVDKGLLREEGElpSDSAIMTTLLADETgkidhpeDYGCSTNVEA--AAMALLPRL---KGAFCLTFT 212
Cdd:COG0121 114 GfdrlRRRLAEELPDELYFQPVGT--TDSELAFALLLSRL-------RDGGPDPAEAlaEALRELAELaraPGRLNLLLS 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896182530 213 DGETLYAARDPYGVRPLCLGRL------SGGWVVASETCALDivgASFvREIEPGEMVTIDASG 270
Cdd:COG0121 185 DGERLYATRYTSDDPYPTLYYLtrttpdDRVVVVASEPLTDD---EGW-TEVPPGELLVVRDGL 244
|
|
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
35-260 |
9.83e-08 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 54.53 E-value: 9.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 35 CGVFGVWAPGEDVSKLTYYGLFALQ---HRGQEAAGIAVGDgDQILVFKDLGLVSqvfdeqtldalkghVAVGhtrytta 111
Cdd:PRK09431 2 CGIFGILDIKTDADELRKKALEMSRlmrHRGPDWSGIYASD-NAILGHERLSIVD--------------VNGG------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 112 gapawenAQPMFqmaSDGTDIALGHNGNLTNHLTLFHEAVDKGLLREEgelpSDSAIMTTLLadetgkidhpEDYGCstn 191
Cdd:PRK09431 60 -------AQPLY---NEDGTHVLAVNGEIYNHQELRAELGDKYAFQTG----SDCEVILALY----------QEKGP--- 112
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896182530 192 veaaamALLPRLKG--AFCLTFTDGETLYAARDPYGVRPLCLGR-LSGGWVVASETCALdivgASFVREIEP 260
Cdd:PRK09431 113 ------DFLDDLDGmfAFALYDSEKDAYLIARDPIGIIPLYYGYdEHGNLYFASEMKAL----VPVCKTIKE 174
|
|
| Pribosyltran |
pfam00156 |
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ... |
309-418 |
1.50e-06 |
|
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: 48.13 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 309 ELGRQLAREFPADGDLVMPVPESGTPAAVGYAQESGIPFGqGLTKNGYVGRTFIQpsqtirqlgirLKLNPLKEVIAGKR 388
Cdd:pfam00156 17 RLAAQINEDYGGKPDVVVGILRGGLPFAGILARRLDVPLA-FVRKVSYNPDTSEV-----------MKTSSALPDLKGKT 84
|
90 100 110
....*....|....*....|....*....|
gi 896182530 389 LVVVDDSIVRGNTQRALIRMLREAGAKEVH 418
Cdd:pfam00156 85 VLIVDDILDTGGTLLKVLELLKNVGPKEVK 114
|
|
| GltS |
cd00713 |
Glutamine amidotransferases class-II (Gn-AT), glutamate synthase (GltS)-type. GltS is a ... |
78-267 |
4.79e-06 |
|
Glutamine amidotransferases class-II (Gn-AT), glutamate synthase (GltS)-type. GltS is a homodimer that synthesizes L-glutamate from 2-oxoglutarate and L-glutamine, an important step in ammonia assimilation in bacteria, cyanobacteria and plants. The N-terminal glutaminase domain catalyzes the hydrolysis of glutamine to glutamic acid and ammonia, and has a fold similar to that of other glutamine amidotransferases such as glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), and beta lactam synthetase (beta-LS), as well as the Ntn hydrolase folds of the proteasomal alpha and beta subunits.
Pssm-ID: 238365 [Multi-domain] Cd Length: 413 Bit Score: 49.06 E-value: 4.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 78 VFKDLGLVSQV---FDEQTLDALKGHVAVGHTRYTTAGAPAWENAQPmFQMasdgtdiaLGHNG---------------- 138
Cdd:cd00713 177 VYKGMLLPEQLgqfYPDLQDPRFESAFALVHSRFSTNTFPSWPLAQP-FRY--------LAHNGeintirgnrnwmrare 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 139 NLTNHLTLFHEAVDKGLLREEGelPSDSAI----MTTLLADetgkidhpedyGCStnVEAAAMALLPR----------LK 204
Cdd:cd00713 248 GLLKSPLFGEDLKKLKPIINPG--GSDSASldnvLELLVRS-----------GRS--LPEAMMMLIPEawqnnptmdpEL 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 205 GAF---------------CLTFTDGETLYAARDPYGVRPLCLGRLSGGWVV-ASETCALDIvGASFVRE---IEPGEMVT 265
Cdd:cd00713 313 RAFyeyhsslmepwdgpaAIAFTDGRQVGASLDRNGLRPARYVITKDGLLImSSEVGVVDV-PPEKVVEkgrLGPGEMLL 391
|
..
gi 896182530 266 ID 267
Cdd:cd00713 392 VD 393
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
35-160 |
6.91e-06 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 48.72 E-value: 6.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 35 CGVFG-----VWAPGEDVSKLTYYGLFALQHRGQEAAGIAVGDGDQI---------------LVFKDLGLVSQ----VFD 90
Cdd:PTZ00394 2 CGIFGyanhnVPRTVEQILNVLLDGIQKVEYRGYDSAGLAIDANIGSekedgtaasaptprpCVVRSVGNISQlrekVFS 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 896182530 91 EQT------LDA-LKGHVAVGHTRYTTAGAPAWENAQPmfqMASDGTDIALGHNGNLTNHLTLfheavdKGLLREEG 160
Cdd:PTZ00394 82 EAVaatlppMDAtTSHHVGIAHTRWATHGGVCERNCHP---QQSNNGEFTIVHNGIVTNYMTL------KELLKEEG 149
|
|
| PRK07322 |
PRK07322 |
adenine phosphoribosyltransferase; Provisional |
311-417 |
8.15e-06 |
|
adenine phosphoribosyltransferase; Provisional
Pssm-ID: 180928 Cd Length: 178 Bit Score: 46.51 E-value: 8.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 311 GRQLAREFPADGDLVMPVPESGTPAAVGYAQESGIPFGQgLTKN--GYVGRTFIQPSQTI----RQLgirLKLN-PLKEV 383
Cdd:PRK07322 42 AEALAKRLPTEVDVLVTPETKGIPLAHALSRRLGKPYVV-ARKSrkPYMQDPIIQEVVSIttgkPQL---LVLDgADAEK 117
|
90 100 110
....*....|....*....|....*....|....
gi 896182530 384 IAGKRLVVVDDSIVRGNTQRALIRMLREAGAKEV 417
Cdd:PRK07322 118 LKGKRVAIVDDVVSTGGTLTALERLVERAGGQVV 151
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
58-248 |
2.66e-05 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 47.02 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 58 LQHRGQEAAGIAV---GDG-DQILVFKDLGLVsqvfdeqtlDALKGHvavghtryttagapawenaQPMFqmaSDGTDIA 133
Cdd:PTZ00077 28 LRHRGPDWSGIIVlenSPGtYNILAHERLAIV---------DLSDGK-------------------QPLL---DDDETVA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 134 LGHNGNLTNHLTLfheavdKGLLREEG---ELPSDSAIMTTLLadetgkidhpEDYGcstnveaaAMALLPRLKGAFCLT 210
Cdd:PTZ00077 77 LMQNGEIYNHWEI------RPELEKEGykfSSNSDCEIIGHLY----------KEYG--------PKDFWNHLDGMFATV 132
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 896182530 211 FTDG--ETLYAARDPYGVRPLCLGRLSGGWV-VASETCALD 248
Cdd:PTZ00077 133 IYDMktNTFFAARDHIGIIPLYIGYAKDGSIwFSSELKALH 173
|
|
| ComFC |
COG1040 |
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General ... |
310-419 |
8.52e-05 |
|
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General function prediction only];
Pssm-ID: 440662 [Multi-domain] Cd Length: 196 Bit Score: 43.66 E-value: 8.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 310 LGRQLAREFPADGDLVMPVPesGTPAAV---GY----------AQESGIPF-GQGLTKngyVGRTfiqPSQTirQLGI-- 373
Cdd:COG1040 67 LARALREALLPRPDLIVPVP--LHRRRLrrrGFnqaellaralARALGIPVlPDLLRR---VRAT---PSQA--GLSRae 136
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 896182530 374 RLK-------LNPlKEVIAGKRLVVVDDsiVR--GNTQRALIRMLREAGAKEVHV 419
Cdd:COG1040 137 RRRnlrgafaVRP-PARLAGKHVLLVDD--VLttGATLAEAARALKAAGAARVDV 188
|
|
| Hpt1 |
COG2236 |
Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine ... |
379-419 |
1.95e-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: 41.76 E-value: 1.95e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 896182530 379 PLKEVIAGKRLVVVDDSIVRGNTQRALIRMLREAGAKEVHV 419
Cdd:COG2236 81 PLDEDLAGKRVLIVDDVADTGRTLEAVRDLLKEAGPAEVRT 121
|
|
| PLN02238 |
PLN02238 |
hypoxanthine phosphoribosyltransferase |
309-419 |
2.04e-04 |
|
hypoxanthine phosphoribosyltransferase
Pssm-ID: 215132 Cd Length: 189 Bit Score: 42.33 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 309 ELGRQLAREFPADGDLVMPVpesGTPAAVGYAQ--ESGIPFGQGLTKN-----GYVGRTfiQPSQTIRqlgirLKLNPLK 381
Cdd:PLN02238 23 ELAAQIASDYAGKSPVVLGV---ATGAFMFLADlvRAIQPLPRGLTVDfirasSYGGGT--ESSGVAK-----VSGADLK 92
|
90 100 110
....*....|....*....|....*....|....*...
gi 896182530 382 EVIAGKRLVVVDDSIVRGNTQRALIRMLREAGAKEVHV 419
Cdd:PLN02238 93 IDVKGKHVLLVEDIVDTGNTLSALVAHLEAKGAASVSV 130
|
|
| PRK02277 |
PRK02277 |
orotate phosphoribosyltransferase-like protein; Provisional |
384-417 |
1.68e-03 |
|
orotate phosphoribosyltransferase-like protein; Provisional
Pssm-ID: 235023 [Multi-domain] Cd Length: 200 Bit Score: 39.85 E-value: 1.68e-03
10 20 30
....*....|....*....|....*....|....
gi 896182530 384 IAGKRLVVVDDSIVRGNTQRALIRMLREAGAKEV 417
Cdd:PRK02277 138 VEGKRCVIVDDVITSGTTMKETIEYLKEHGGKPV 171
|
|
| PRK08558 |
PRK08558 |
adenine phosphoribosyltransferase; Provisional |
385-419 |
1.99e-03 |
|
adenine phosphoribosyltransferase; Provisional
Pssm-ID: 181466 [Multi-domain] Cd Length: 238 Bit Score: 39.98 E-value: 1.99e-03
10 20 30
....*....|....*....|....*....|....*
gi 896182530 385 AGKRLVVVDDSIVRGNTQRALIRMLREAGAKEVHV 419
Cdd:PRK08558 175 KGDRVLIVDDIIRSGETQRALLDLARQAGADVVGV 209
|
|
| PRK00934 |
PRK00934 |
ribose-phosphate pyrophosphokinase; Provisional |
386-419 |
2.32e-03 |
|
ribose-phosphate pyrophosphokinase; Provisional
Pssm-ID: 234868 [Multi-domain] Cd Length: 285 Bit Score: 39.90 E-value: 2.32e-03
10 20 30
....*....|....*....|....*....|....
gi 896182530 386 GKRLVVVDDSIVRGNTQRALIRMLREAGAKEVHV 419
Cdd:PRK00934 204 GKDVLIVDDIISTGGTMATAIKILKEQGAKKVYV 237
|
|
| Apt |
COG0503 |
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ... |
309-415 |
2.41e-03 |
|
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide transport and metabolism]; Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein is part of the Pathway/BioSystem: Purine salvage
Pssm-ID: 440269 Cd Length: 171 Bit Score: 38.90 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896182530 309 ELGRQLAREFPADG-DLVMPVPESGTPAAVGYAQESGIPFgqgLT--KNGYV-GRTFIQPSQTIRQLGIRLKLNPlKEVI 384
Cdd:COG0503 35 AAGDELAERFADKGiDKVVGIEARGFILAAALAYALGVPF---VParKPGKLpGETVSEEYDLEYGTGDTLELHK-DALK 110
|
90 100 110
....*....|....*....|....*....|.
gi 896182530 385 AGKRLVVVDDSIVRGNTQRALIRMLREAGAK 415
Cdd:COG0503 111 PGDRVLIVDDLLATGGTAKAAIKLVEEAGAE 141
|
|
| Gn_AT_II_novel |
cd03766 |
Gn_AT_II_novel. This asparagine synthase-related domain is present in eukaryotes but its ... |
179-237 |
4.40e-03 |
|
Gn_AT_II_novel. This asparagine synthase-related domain is present in eukaryotes but its function has not yet been determined. 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: 239735 [Multi-domain] Cd Length: 181 Bit Score: 38.42 E-value: 4.40e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896182530 179 KIDHPEDYGCST-----------NVEAAAMALLPRLKGAFCLTFTDGE--TLYAARDPYGVRPLCLGRLSGG 237
Cdd:cd03766 84 NIDGVEDEENDTevifellancsSESQDILDVLSSIEGPFAFIYYDASenKLYFGRDCLGRRSLLYKLDPNG 155
|
|
| |
