|
Name |
Accession |
Description |
Interval |
E-value |
| UDPGlcNAc_PPase |
cd04193 |
UDPGlcNAc pyrophosphorylase catalayzes the synthesis of UDPGlcNAc; UDP-N-acetylglucosamine ... |
88-410 |
0e+00 |
|
UDPGlcNAc pyrophosphorylase catalayzes the synthesis of UDPGlcNAc; UDP-N-acetylglucosamine (UDPGlcNAc) pyrophosphorylase (UAP) (also named GlcNAc1P uridyltransferase), catalyzes the reversible conversion of UTP and GlcNAc1 to PPi and UDPGlcNAc. UDP-N-acetylglucosamine (UDPGlcNAc), the activated form of GlcNAc, is a key precursor of N- and O-linked glycosylations. It is essential for the synthesis of chitin (a major component of the fungal cell wall) and of the glycosylphosphatidylinositol (GPI) linker which anchors a variety of cell surface proteins to the plasma membrane. In bacteria, UDPGlcNAc represents an essential precursor for both peptidoglycan and lipopolysaccharide biosynthesis. Human UAP has two isoforms, resulting from alternative splicing of a single gene and differing by the presence or absence of 17 amino acids. UDPGlcNAc pyrophosphorylase shares significant sequence and structure conservation with UDPglucose pyrophosphorylase.
Pssm-ID: 133036 Cd Length: 323 Bit Score: 588.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68566143 88 QAWESEGLSQISQNKVAVLLLAGGQGTRLGVSYPKGMYDVGLPSHKTLFQIQAERILKLQQLAEKHHGNKCTIPWYIMTS 167
Cdd:cd04193 1 KEWEEAGLKAIAEGKVAVLLLAGGQGTRLGFDGPKGMFPVGLPSKKSLFQLQAERILKLQELAGEASGKKVPIPWYIMTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68566143 168 GRTMESTKEFFTKHKFFGLKKENVVFFQQGMLPAMSFDGKIILEEKNKVSMAPDGNGGLYRALAAQNIVEDMEQRGICSI 247
Cdd:cd04193 81 EATHEETRKFFKENNYFGLDPEQVHFFQQGMLPCVDFDGKILLEEKGKIAMAPNGNGGLYKALQTAGILEDMKKRGIKYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68566143 248 HVYCVDNILVKVADPRFIGFCIQKGADCGAKVVEKTNPTEPVGVVCRVDGVYQVVEYSEISLATAQRRSSDGRLLFNAGN 327
Cdd:cd04193 161 HVYSVDNILVKVADPVFIGFCISKGADVGAKVVRKRYPTEKVGVVVLVDGKPQVVEYSEISDELAEKRDADGELQYNAGN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68566143 328 IANHFFTVPFLKDVVNVYEPQLQHHVAQKKIPYVDSQGYFIKPDKPNGIKMEKFVFDIFQFAKKFVVYEVLREDEFSPLK 407
Cdd:cd04193 241 IANHFFSLDFLEKAAEMEEPSLPYHIAKKKIPYVDLEGGLVKPDEPNGIKLELFIFDVFPFAKNFVCLEVDREEEFSPLK 320
|
...
gi 68566143 408 NAD 410
Cdd:cd04193 321 NAD 323
|
|
| PLN02435 |
PLN02435 |
probable UDP-N-acetylglucosamine pyrophosphorylase |
6-506 |
8.72e-142 |
|
probable UDP-N-acetylglucosamine pyrophosphorylase
Pssm-ID: 215238 Cd Length: 493 Bit Score: 417.74 E-value: 8.72e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68566143 6 LKQRLSQAGQEHLLQFWNELSEAQQVELYMELQAMNFEELNSFFRKAIGEfdrsshQEKVDARMEPVPRQVLGSAT-RDQ 84
Cdd:PLN02435 25 LLERLKDYGQEDAFALWDELSPEERDLLVRDIESLDLPRIDRIIRCSLRS------QGLPVPAIEPVPENSVSTVEeRTP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68566143 85 EQLQAWESEGLSQISQNKVAVLLLAGGQGTRLGVSYPKGMYDVGLPSHKTLFQIQAERILKLQQLA----EKHHGNKCTI 160
Cdd:PLN02435 99 EDRERWWKMGLKAISEGKLAVVLLSGGQGTRLGSSDPKGCFNIGLPSGKSLFQLQAERILCVQRLAaqasSEGPGRPVTI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68566143 161 PWYIMTSGRTMESTKEFFTKHKFFGLKKENVVFFQQGMLPAMSFDGKIILEEKNKVSMAPDGNGGLYRALAAQNIVEDME 240
Cdd:PLN02435 179 HWYIMTSPFTDEATRKFFESHKYFGLEADQVTFFQQGTLPCVSKDGKFIMETPFKVAKAPDGNGGVYAALKSSRLLEDMA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68566143 241 QRGICSIHVYCVDNILVKVADPRFIGFCIQKGADCGAKVVEKTNPTEPVGVVCR--VDGVYQVVEYSEI--SLATAQRRS 316
Cdd:PLN02435 259 SRGIKYVDCYGVDNALVRVADPTFLGYFIDKGVASAAKVVRKAYPQEKVGVFVRrgKGGPLTVVEYSELdqAMASAINQQ 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68566143 317 SdGRLLFNAGNIANHFFTVPFLKDVVNVYEPQLQHHVAQKKIPYVDsqGYFIkpdkpnGIKMEKFVFDIFQFAKKFVVYE 396
Cdd:PLN02435 339 T-GRLRYCWSNVCLHMFTLDFLNQVANGLEKDSIYHLAEKKIPSIH--GYTM------GLKLEQFIFDAFPYAPSTALFE 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68566143 397 VLREDEFSPLKNADSQNgKDNPTTARHALMSLHHCWVLNAGGhFIdengsrLPAIPRSATNgkseaitadvnhnlkdand 476
Cdd:PLN02435 410 VLREEEFAPVKNANGSN-FDTPESARLLVLRLHTRWVVAAGG-FL------THSVPLYATG------------------- 462
|
490 500 510
....*....|....*....|....*....|
gi 68566143 477 vpiqCEISPLISYAGEGLEGYVADKEFHAP 506
Cdd:PLN02435 463 ----VEVSPLCSYAGENLEAICRGRTFHAP 488
|
|
| QRI1 |
COG4284 |
UDP-N-acetylglucosamine pyrophosphorylase [Carbohydrate transport and metabolism]; |
6-418 |
3.44e-137 |
|
UDP-N-acetylglucosamine pyrophosphorylase [Carbohydrate transport and metabolism];
Pssm-ID: 443425 Cd Length: 402 Bit Score: 402.34 E-value: 3.44e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68566143 6 LKQRLSQAGQEHLLQFWNELSEAQQVELYMELQAMNFEElnsfFRKAIGEFDRSSHQEKVDAR--MEPVPRQVLGSATRD 83
Cdd:COG4284 1 LIEKLEPHGQEHLLRFWDELSEAQQKMLEAQIEEIDIDV----FQHLYRQLVLAEGATGLIPEsdIEPAPVTDLPLTDLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68566143 84 QEQLQAWESEGLSQISQNKVAVLLLAGGQGTRLGVSYPKGMYDVGLPSHKTLFQIQAERILKlqqlAEKHHGnkCTIPWY 163
Cdd:COG4284 77 EVDRDRAEEAGEEALRAGKVAVILLAGGQGTRLGFDGPKGLLPVRPVKGKSLFDLIAEQVLA----ARRRYG--VPLPLY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68566143 164 IMTSGRTMESTKEFFTKHKFFGLKKENVVFFQQGMLPAM-SFDGKIILEEKNKVSMAPDGNGGLYRALAAQNIVEDMEQR 242
Cdd:COG4284 151 IMTSFRTHEDTLAFLEEHDYFGLDGLPVHFFLQGMEPALdADLGPVLLPADPELELCPPGHGGIYTALLASGLLDKLLER 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68566143 243 GICSIHVYCVDNILVKVADPRFIGFCIQKGADCGAKVVEKTNPTEPVGVVCRVDGVYQVVEYSEisLATAQRRSSDGRLL 322
Cdd:COG4284 231 GIRYLFVSNVDNPLGAVPDPAFAGWHAASGAPFTAKVVRRTPPDEKVGHLARVDGRLILREYSQ--LPDEEAEAFTGELR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68566143 323 FNAGNIANHFFTVPFLKDVVNVYEPQLQHHVAQKKIPYVDSQGyfiKPDKPNGIKMEKFVFDIFQFAKKFVVYEVLREDE 402
Cdd:COG4284 309 HPYGNINNHWFDLDFLKRLLDERGLGLPLHRAEKKVDPLDESG---KPTSPNVIKFETFMFDAIPLFDGAVAIEVDREER 385
|
410
....*....|....*.
gi 68566143 403 FSPLKNAdsqNGKDNP 418
Cdd:COG4284 386 FAPVKNT---NGSDSP 398
|
|
| UDPGP |
pfam01704 |
UTP--glucose-1-phosphate uridylyltransferase; This family consists of UTP--glucose-1-phosphate ... |
45-472 |
2.56e-120 |
|
UTP--glucose-1-phosphate uridylyltransferase; This family consists of UTP--glucose-1-phosphate uridylyltransferases, EC:2.7.7.9. Also known as UDP-glucose pyrophosphorylase (UDPGP) and Glucose-1-phosphate uridylyltransferase. UTP--glucose-1-phosphate uridylyltransferase catalyzes the interconversion of MgUTP + glucose-1-phosphate and UDP-glucose + MgPPi. UDP-glucose is an important intermediate in mammalian carbohydrate interconversion involved in various metabolic roles depending on tissue type. In Dictyostelium (slime mold) mutants in this enzyme abort the development cycle. Also within the family is UDP-N-acetylglucosamine or AGX1 and two hypothetical proteins from Borrelia burgdorferi the lyme disease spirochaete Swiss:O51893 and Swiss:O51036.
Pssm-ID: 460300 Cd Length: 412 Bit Score: 359.52 E-value: 2.56e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68566143 45 LNSFFRKAIGEFDRSSHQEKVD-ARMEPVPRQVLgsatRDQEQLQA--WESEGLsqisQNKVAVLLLAGGQGTRLGVSYP 121
Cdd:pfam01704 1 LDGFFKLFSRYLSEKGKQEKIDwDKIKPPPEEEI----VDYEDLQEpeEEIKEL----LNKLAVLKLNGGLGTSMGCVGP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68566143 122 KGMYDVGlpSHKTLFQIQAERILKLqqlaekHHGNKCTIPWYIMTSGRTMESTKEFFTKHKFfglKKENVVFFQQGMLPA 201
Cdd:pfam01704 73 KSLIEVR--DGLTFLDLIVQQIEHL------NKKYNVDVPLVLMNSFNTDEDTKKIIRKYKG---HKVDILTFNQSRYPR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68566143 202 MSFDGKIILEEK---NKVSMAPDGNGGLYRALAAQNIVEDMEQRGICSIHVYCVDNiLVKVADPRFIGFCIQKGADCGAK 278
Cdd:pfam01704 142 IDKDTLLPVPKSadsDEEEWYPPGHGDLYESLYNSGLLDKLLAEGKEYLFVSNIDN-LGATVDLNILNYMVDNGAEFLME 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68566143 279 VVEKTNPTEPVGVVCRVDGVYQVVEYSEI-SLATAQRRSSDGRLLFNAGNIanhFFTVPFLKDVVNvyEPQLQHHVAQKK 357
Cdd:pfam01704 221 VTDKTRADVKGGTLIEYDGKLRLLEIAQVpKEHVDEFKSIKKFKIFNTNNI---WINLKALKRVVE--EGELQLEIIVNK 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68566143 358 iPYVDSQGYFIKPDKPNGIKMEKFvfdifqfaKKFVVYEVLReDEFSPLKNADSqngkdnpttarhALMSLHHCWVLNAG 437
Cdd:pfam01704 296 -KTLDNGENVIQLETAVGAAIKNF--------KNAIGINVPR-SRFLPVKTTSD------------LLLVMSDLYVLNHG 353
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 68566143 438 -------------------GHF--IDENGSRLPAIPrSATNGKSEAITADV----NHNLK 472
Cdd:pfam01704 354 slimnpkrmfgtppvvllgDHFkkVDEFLKRFPSIP-DLLELDHLTVSGDVtfgrNVTLK 412
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| UDPGlcNAc_PPase |
cd04193 |
UDPGlcNAc pyrophosphorylase catalayzes the synthesis of UDPGlcNAc; UDP-N-acetylglucosamine ... |
88-410 |
0e+00 |
|
UDPGlcNAc pyrophosphorylase catalayzes the synthesis of UDPGlcNAc; UDP-N-acetylglucosamine (UDPGlcNAc) pyrophosphorylase (UAP) (also named GlcNAc1P uridyltransferase), catalyzes the reversible conversion of UTP and GlcNAc1 to PPi and UDPGlcNAc. UDP-N-acetylglucosamine (UDPGlcNAc), the activated form of GlcNAc, is a key precursor of N- and O-linked glycosylations. It is essential for the synthesis of chitin (a major component of the fungal cell wall) and of the glycosylphosphatidylinositol (GPI) linker which anchors a variety of cell surface proteins to the plasma membrane. In bacteria, UDPGlcNAc represents an essential precursor for both peptidoglycan and lipopolysaccharide biosynthesis. Human UAP has two isoforms, resulting from alternative splicing of a single gene and differing by the presence or absence of 17 amino acids. UDPGlcNAc pyrophosphorylase shares significant sequence and structure conservation with UDPglucose pyrophosphorylase.
Pssm-ID: 133036 Cd Length: 323 Bit Score: 588.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68566143 88 QAWESEGLSQISQNKVAVLLLAGGQGTRLGVSYPKGMYDVGLPSHKTLFQIQAERILKLQQLAEKHHGNKCTIPWYIMTS 167
Cdd:cd04193 1 KEWEEAGLKAIAEGKVAVLLLAGGQGTRLGFDGPKGMFPVGLPSKKSLFQLQAERILKLQELAGEASGKKVPIPWYIMTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68566143 168 GRTMESTKEFFTKHKFFGLKKENVVFFQQGMLPAMSFDGKIILEEKNKVSMAPDGNGGLYRALAAQNIVEDMEQRGICSI 247
Cdd:cd04193 81 EATHEETRKFFKENNYFGLDPEQVHFFQQGMLPCVDFDGKILLEEKGKIAMAPNGNGGLYKALQTAGILEDMKKRGIKYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68566143 248 HVYCVDNILVKVADPRFIGFCIQKGADCGAKVVEKTNPTEPVGVVCRVDGVYQVVEYSEISLATAQRRSSDGRLLFNAGN 327
Cdd:cd04193 161 HVYSVDNILVKVADPVFIGFCISKGADVGAKVVRKRYPTEKVGVVVLVDGKPQVVEYSEISDELAEKRDADGELQYNAGN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68566143 328 IANHFFTVPFLKDVVNVYEPQLQHHVAQKKIPYVDSQGYFIKPDKPNGIKMEKFVFDIFQFAKKFVVYEVLREDEFSPLK 407
Cdd:cd04193 241 IANHFFSLDFLEKAAEMEEPSLPYHIAKKKIPYVDLEGGLVKPDEPNGIKLELFIFDVFPFAKNFVCLEVDREEEFSPLK 320
|
...
gi 68566143 408 NAD 410
Cdd:cd04193 321 NAD 323
|
|
| PLN02435 |
PLN02435 |
probable UDP-N-acetylglucosamine pyrophosphorylase |
6-506 |
8.72e-142 |
|
probable UDP-N-acetylglucosamine pyrophosphorylase
Pssm-ID: 215238 Cd Length: 493 Bit Score: 417.74 E-value: 8.72e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68566143 6 LKQRLSQAGQEHLLQFWNELSEAQQVELYMELQAMNFEELNSFFRKAIGEfdrsshQEKVDARMEPVPRQVLGSAT-RDQ 84
Cdd:PLN02435 25 LLERLKDYGQEDAFALWDELSPEERDLLVRDIESLDLPRIDRIIRCSLRS------QGLPVPAIEPVPENSVSTVEeRTP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68566143 85 EQLQAWESEGLSQISQNKVAVLLLAGGQGTRLGVSYPKGMYDVGLPSHKTLFQIQAERILKLQQLA----EKHHGNKCTI 160
Cdd:PLN02435 99 EDRERWWKMGLKAISEGKLAVVLLSGGQGTRLGSSDPKGCFNIGLPSGKSLFQLQAERILCVQRLAaqasSEGPGRPVTI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68566143 161 PWYIMTSGRTMESTKEFFTKHKFFGLKKENVVFFQQGMLPAMSFDGKIILEEKNKVSMAPDGNGGLYRALAAQNIVEDME 240
Cdd:PLN02435 179 HWYIMTSPFTDEATRKFFESHKYFGLEADQVTFFQQGTLPCVSKDGKFIMETPFKVAKAPDGNGGVYAALKSSRLLEDMA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68566143 241 QRGICSIHVYCVDNILVKVADPRFIGFCIQKGADCGAKVVEKTNPTEPVGVVCR--VDGVYQVVEYSEI--SLATAQRRS 316
Cdd:PLN02435 259 SRGIKYVDCYGVDNALVRVADPTFLGYFIDKGVASAAKVVRKAYPQEKVGVFVRrgKGGPLTVVEYSELdqAMASAINQQ 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68566143 317 SdGRLLFNAGNIANHFFTVPFLKDVVNVYEPQLQHHVAQKKIPYVDsqGYFIkpdkpnGIKMEKFVFDIFQFAKKFVVYE 396
Cdd:PLN02435 339 T-GRLRYCWSNVCLHMFTLDFLNQVANGLEKDSIYHLAEKKIPSIH--GYTM------GLKLEQFIFDAFPYAPSTALFE 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68566143 397 VLREDEFSPLKNADSQNgKDNPTTARHALMSLHHCWVLNAGGhFIdengsrLPAIPRSATNgkseaitadvnhnlkdand 476
Cdd:PLN02435 410 VLREEEFAPVKNANGSN-FDTPESARLLVLRLHTRWVVAAGG-FL------THSVPLYATG------------------- 462
|
490 500 510
....*....|....*....|....*....|
gi 68566143 477 vpiqCEISPLISYAGEGLEGYVADKEFHAP 506
Cdd:PLN02435 463 ----VEVSPLCSYAGENLEAICRGRTFHAP 488
|
|
| QRI1 |
COG4284 |
UDP-N-acetylglucosamine pyrophosphorylase [Carbohydrate transport and metabolism]; |
6-418 |
3.44e-137 |
|
UDP-N-acetylglucosamine pyrophosphorylase [Carbohydrate transport and metabolism];
Pssm-ID: 443425 Cd Length: 402 Bit Score: 402.34 E-value: 3.44e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68566143 6 LKQRLSQAGQEHLLQFWNELSEAQQVELYMELQAMNFEElnsfFRKAIGEFDRSSHQEKVDAR--MEPVPRQVLGSATRD 83
Cdd:COG4284 1 LIEKLEPHGQEHLLRFWDELSEAQQKMLEAQIEEIDIDV----FQHLYRQLVLAEGATGLIPEsdIEPAPVTDLPLTDLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68566143 84 QEQLQAWESEGLSQISQNKVAVLLLAGGQGTRLGVSYPKGMYDVGLPSHKTLFQIQAERILKlqqlAEKHHGnkCTIPWY 163
Cdd:COG4284 77 EVDRDRAEEAGEEALRAGKVAVILLAGGQGTRLGFDGPKGLLPVRPVKGKSLFDLIAEQVLA----ARRRYG--VPLPLY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68566143 164 IMTSGRTMESTKEFFTKHKFFGLKKENVVFFQQGMLPAM-SFDGKIILEEKNKVSMAPDGNGGLYRALAAQNIVEDMEQR 242
Cdd:COG4284 151 IMTSFRTHEDTLAFLEEHDYFGLDGLPVHFFLQGMEPALdADLGPVLLPADPELELCPPGHGGIYTALLASGLLDKLLER 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68566143 243 GICSIHVYCVDNILVKVADPRFIGFCIQKGADCGAKVVEKTNPTEPVGVVCRVDGVYQVVEYSEisLATAQRRSSDGRLL 322
Cdd:COG4284 231 GIRYLFVSNVDNPLGAVPDPAFAGWHAASGAPFTAKVVRRTPPDEKVGHLARVDGRLILREYSQ--LPDEEAEAFTGELR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68566143 323 FNAGNIANHFFTVPFLKDVVNVYEPQLQHHVAQKKIPYVDSQGyfiKPDKPNGIKMEKFVFDIFQFAKKFVVYEVLREDE 402
Cdd:COG4284 309 HPYGNINNHWFDLDFLKRLLDERGLGLPLHRAEKKVDPLDESG---KPTSPNVIKFETFMFDAIPLFDGAVAIEVDREER 385
|
410
....*....|....*.
gi 68566143 403 FSPLKNAdsqNGKDNP 418
Cdd:COG4284 386 FAPVKNT---NGSDSP 398
|
|
| UDPGP |
pfam01704 |
UTP--glucose-1-phosphate uridylyltransferase; This family consists of UTP--glucose-1-phosphate ... |
45-472 |
2.56e-120 |
|
UTP--glucose-1-phosphate uridylyltransferase; This family consists of UTP--glucose-1-phosphate uridylyltransferases, EC:2.7.7.9. Also known as UDP-glucose pyrophosphorylase (UDPGP) and Glucose-1-phosphate uridylyltransferase. UTP--glucose-1-phosphate uridylyltransferase catalyzes the interconversion of MgUTP + glucose-1-phosphate and UDP-glucose + MgPPi. UDP-glucose is an important intermediate in mammalian carbohydrate interconversion involved in various metabolic roles depending on tissue type. In Dictyostelium (slime mold) mutants in this enzyme abort the development cycle. Also within the family is UDP-N-acetylglucosamine or AGX1 and two hypothetical proteins from Borrelia burgdorferi the lyme disease spirochaete Swiss:O51893 and Swiss:O51036.
Pssm-ID: 460300 Cd Length: 412 Bit Score: 359.52 E-value: 2.56e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68566143 45 LNSFFRKAIGEFDRSSHQEKVD-ARMEPVPRQVLgsatRDQEQLQA--WESEGLsqisQNKVAVLLLAGGQGTRLGVSYP 121
Cdd:pfam01704 1 LDGFFKLFSRYLSEKGKQEKIDwDKIKPPPEEEI----VDYEDLQEpeEEIKEL----LNKLAVLKLNGGLGTSMGCVGP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68566143 122 KGMYDVGlpSHKTLFQIQAERILKLqqlaekHHGNKCTIPWYIMTSGRTMESTKEFFTKHKFfglKKENVVFFQQGMLPA 201
Cdd:pfam01704 73 KSLIEVR--DGLTFLDLIVQQIEHL------NKKYNVDVPLVLMNSFNTDEDTKKIIRKYKG---HKVDILTFNQSRYPR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68566143 202 MSFDGKIILEEK---NKVSMAPDGNGGLYRALAAQNIVEDMEQRGICSIHVYCVDNiLVKVADPRFIGFCIQKGADCGAK 278
Cdd:pfam01704 142 IDKDTLLPVPKSadsDEEEWYPPGHGDLYESLYNSGLLDKLLAEGKEYLFVSNIDN-LGATVDLNILNYMVDNGAEFLME 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68566143 279 VVEKTNPTEPVGVVCRVDGVYQVVEYSEI-SLATAQRRSSDGRLLFNAGNIanhFFTVPFLKDVVNvyEPQLQHHVAQKK 357
Cdd:pfam01704 221 VTDKTRADVKGGTLIEYDGKLRLLEIAQVpKEHVDEFKSIKKFKIFNTNNI---WINLKALKRVVE--EGELQLEIIVNK 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68566143 358 iPYVDSQGYFIKPDKPNGIKMEKFvfdifqfaKKFVVYEVLReDEFSPLKNADSqngkdnpttarhALMSLHHCWVLNAG 437
Cdd:pfam01704 296 -KTLDNGENVIQLETAVGAAIKNF--------KNAIGINVPR-SRFLPVKTTSD------------LLLVMSDLYVLNHG 353
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 68566143 438 -------------------GHF--IDENGSRLPAIPrSATNGKSEAITADV----NHNLK 472
Cdd:pfam01704 354 slimnpkrmfgtppvvllgDHFkkVDEFLKRFPSIP-DLLELDHLTVSGDVtfgrNVTLK 412
|
|
| UGPase_euk_like |
cd04180 |
Eukaryotic UGPase-like includes UDPase and UDPGlcNAc pyrophosphorylase enzymes; This family ... |
103-408 |
1.75e-118 |
|
Eukaryotic UGPase-like includes UDPase and UDPGlcNAc pyrophosphorylase enzymes; This family includes UDP-Glucose Pyrophosphorylase (UDPase) and UDPGlcNAc pyrophosphorylase enzymes. The two enzymes share significant sequence and structure similarity. UDP-Glucose Pyrophosphorylase catalyzes a reversible production of UDP-Glucose and pyrophosphate (PPi) from Glucose-1-phosphate and UTP. UDP-glucose plays pivotal roles in galactose utilization, in glycogen synthesis, and in the synthesis of the carbohydrate moieties of glycolipids , glycoproteins , and proteoglycans . UDP-N-acetylglucosamine (UDPGlcNAc) pyrophosphorylase (UAP) (also named GlcNAc1P uridyltransferase), catalyzes the reversible conversion of UTP and GlcNAc1P from PPi and UDPGlcNAc, which is a key precursor of N- and O-linked glycosylations and is essential for the synthesis of chitin (a major component of the fungal cell wall) and of the glycosylphosphatidylinositol (GPI) linker anchoring a variety of cell surface proteins to the plasma membrane. In bacteria, UDPGlcNAc represents an essential precursor for both peptidoglycan and lipopolysaccharide biosynthesis.
Pssm-ID: 133023 Cd Length: 266 Bit Score: 349.55 E-value: 1.75e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68566143 103 VAVLLLAGGQGTRLGVSYPKGMYDVGLPSHKTLFQIQAERILKLQQLAEkhhgNKCTIPWYIMTSGRTMESTKEFFTKHK 182
Cdd:cd04180 1 VAVVLLAGGLGTRLGKDGPKSSTDVGLPSGQCFLQLIGEKILTLQEIDL----YSCKIPEQLMNSKYTHEKTQCYFEKIN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68566143 183 ffgLKKENVVFFQQGMLPAMSFDGKIILEEKNKVSMAPDGNGGLYRALAAQNIVEDMEQRGICSIHVYCVDNILVKVADP 262
Cdd:cd04180 77 ---QKNSYVITFMQGKLPLKNDDDARDPHNKTKCHLFPCGHGDVVLALIHSGHLNKLLEKGYRYIHFIGVDNLLVKVADP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68566143 263 RFIGFCIQKGADCGAKVVEKTNPTEPVGVVCRVD-GVYQVVEYSEISLATAQRR------SSDGRLLFNAGNIANHFFTV 335
Cdd:cd04180 154 LFIGIAIQNRKAINQKVVPKTRNEESGGYRIANInGRVQLLEYDQIKKLLKQKMvnnqipKDIDDAPFFLFNTNNLINFL 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 68566143 336 PFLKDVVNvyepqlqhhvaqkkipyvdsqgyfikpdkpngikmekfvfDIFQFAKKFVVYEVLREDEFSPLKN 408
Cdd:cd04180 234 VEFKDRVD----------------------------------------DIIEFTDDIVGVMVHRAEEFAPVKN 266
|
|
| PTZ00339 |
PTZ00339 |
UDP-N-acetylglucosamine pyrophosphorylase; Provisional |
8-508 |
1.80e-116 |
|
UDP-N-acetylglucosamine pyrophosphorylase; Provisional
Pssm-ID: 240368 Cd Length: 482 Bit Score: 352.51 E-value: 1.80e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68566143 8 QRLSQAGQEHLLQFWNELSEAQQvelyMELQAMNFEELNSFFRKAIGEFDRSSHQEKVDAR-------------MEPVPR 74
Cdd:PTZ00339 3 KVLTGDGQDHLREALKRRSEGEF----TPLATQILSSLTNVDFKHRNAVLEPKLEEYNAEApvgididsihncnIEPPNN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68566143 75 QVLGSATRDQEQLQAWESEGLSQISQNKVAVLLLAGGQGTRLGVSYPKGMYDVGLPSHKTLFQIQAERILKLQQLAEKHH 154
Cdd:PTZ00339 79 NTFIDIYEKEKERKELKESGLEIIKKGEVAVLILAGGLGTRLGSDKPKGLLECTPVKKKTLFQFHCEKVRRLEEMAVAVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68566143 155 --GNKCTIPWYIMTSGRTMESTKEFFTKHKFFGLKKENVVFFQQGMLPAMS-FDGKIILEEKNKVSMAPDGNGGLYRALA 231
Cdd:PTZ00339 159 ggGDDPTIYILVLTSSFNHDQTRQFLEENNFFGLDKEQVIFFKQSSLPCYDeNTGRFIMSSQGSLCTAPGGNGDVFKALA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68566143 232 AQNIVEDMEQRGICSIHVYCVDNILVKVADPRFIGFCIQKGADCGAKVVEKTNPTEPVGVVCRVDGVYQVVEYSEIS-LA 310
Cdd:PTZ00339 239 KCSELMDIVRKGIKYVQVISIDNILAKVLDPEFIGLASSFPAHDVLNKCVKREDDESVGVFCLKDYEWQVVEYTEINeRI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68566143 311 TAQRRSSDGRLLFNAGNIANHFFTVPFLKDVVNVY-EPQLQHHVAQKKIPYVDSQGyfikpDKPNGIKMEKFVFDIFQFA 389
Cdd:PTZ00339 319 LNNDELLTGELAFNYGNICSHIFSLDFLKKVAANRlYESTPYHAARKKIPYINGPT-----DKTMGIKLEAFIFDIFRYA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68566143 390 KKFVVYEVLREDEFSPLKNADSQNGkDNPTTARHALMSLHHCWVLNAgghfidenGSRLPAIPRSATNGkseaitadvnh 469
Cdd:PTZ00339 394 KNVLILEVDREDEFAPIKNADGAAA-DTILNAQKLLLSLHTRWLEAA--------LETVAGNPREGLNL----------- 453
|
490 500 510
....*....|....*....|....*....|....*....
gi 68566143 470 nlkdandvpiqCEISPLISYAGEGLEGYVADKEFHAPLI 508
Cdd:PTZ00339 454 -----------CEISPLVSYGGEGLFQYPGKKILGLPEI 481
|
|
| UGGPase |
cd06424 |
UGGPase catalyzes the synthesis of UDP-Glucose/UDP-Galactose; UGGPase: UDP-Galactose/Glucose ... |
103-294 |
1.67e-18 |
|
UGGPase catalyzes the synthesis of UDP-Glucose/UDP-Galactose; UGGPase: UDP-Galactose/Glucose Pyrophosphorylase catalyzes the reversible production of UDP-Glucose/UDP-Galactose and pyrophosphate (PPi) from Glucose-1-phosphate/Galactose-1-phosphate and UTP. Its dual substrate specificity distinguishes it from the single substrate enzyme UDP-glucose pyrophosphorylase. It may play a key role in the galactose metabolism in raffinose oligosaccharide (RFO) metabolizing plants. RFO raffinose is a major photoassimilate and is a galactosylderivative of sucrose (Suc) containing a galactose (Gal) moiety. Upon arriving at the sink tissue, the Gal moieties of the RFOs are initially removed by alpha-galactosidase and then are phosphorylated to Gal-1-P. Gal-1-P is converted to UDP-Gal. The UDP-Gal is further metabolized to UDP-Glc via an epimerase reaction. The UDP-Glc can be directly utilized in cell wall metabolism or in Suc synthesis. However, for the Suc synthesis UDP-Glc must be further metabolized to Glc-1-P. This can be carried out either by the UGPase in the reverse direction or by the dual substrate PPase itself operating in the reverse direction. According to the latter possibility, the three-step pathway of Gal-1-P to Glc-1-P could be carried out by a single PPase, functioning sequentially in reverse directions separated by the epimerase reaction.
Pssm-ID: 133046 Cd Length: 315 Bit Score: 86.36 E-value: 1.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68566143 103 VAVLLLAGGQGTRLGVSYPKGMYDVGLPSHKTLFQIQAERILKLQQLAEKHHGNKctIPWYIMTSGRTMESTKEFFTKHK 182
Cdd:cd06424 1 AVFVLVAGGLGERLGYSGIKIGLPVELTTNTTYLQYYLNYIRAFQEASKKGEKME--IPFVIMTSDDTHSKTLKLLEENN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68566143 183 FFGLKKENVVFFQQGMLPAM-SFDGKIILEEKNKVSMA--PDGNGGLYRALAAQNIVEDMEQRGICSIHVYCVDNILVKV 259
Cdd:cd06424 79 YFGLEKDQVHILKQEKVFCLiDNDAHLALDPDNTYSILtkPHGHGDVHTLLYNSGLLKKWIEAGYKWLVFFQDTNALAFK 158
|
170 180 190
....*....|....*....|....*....|....*
gi 68566143 260 ADPRFIGFCIQKGADCGAKVVEKTnPTEPVGVVCR 294
Cdd:cd06424 159 AIPAVLGVSATKSLDMNSLTVPRK-PKEAIGALCK 192
|
|
| PLN02830 |
PLN02830 |
UDP-sugar pyrophosphorylase |
4-224 |
2.06e-17 |
|
UDP-sugar pyrophosphorylase
Pssm-ID: 215444 Cd Length: 615 Bit Score: 85.51 E-value: 2.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68566143 4 NDLKQRLSQAGQEHLLQFWNELSEAQQVELYMELQAMNFEE-----LNSFFRKAIgEFDRSSHQEK--VDARMEPVPR-Q 75
Cdd:PLN02830 28 RALVRRLLELGQSHLFEHWPEPGVDDDDKRRLLEQVARLDEsypggLAAYVSNAK-ELLADSKEGVnpFEGWTPSVPEgE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68566143 76 VLGSATRDQEQLqawESEGLSQIsqNKVAVLLLAGGQGTRLGVSYPKgmydVGLPSHKT----LFQIQAERILKLQQLAE 151
Cdd:PLN02830 107 VLEYGSEEFVEL---EEAGLREA--GNAAFVLVAGGLGERLGYSGIK----VALPTETAtgtcYLQLYIESILALQERAK 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 68566143 152 KHHGNKCT-IPWYIMTSGRTMESTKEFFTKHKFFGLKKENVVFFQQGMLPAMS-FDGKIILEEKN--KVSMAPDGNG 224
Cdd:PLN02830 178 KRKAKKGRkIPLVIMTSDDTHARTLKLLERNDYFGMDPDQVTLLKQEKVACLMdNDARLALDPNDpyKIQTKPHGHG 254
|
|
| UGPase_euk |
cd00897 |
Eukaryotic UGPase catalyses the synthesis of UDP-Glucose; UGPase (UDP-Glucose ... |
101-303 |
1.46e-08 |
|
Eukaryotic UGPase catalyses the synthesis of UDP-Glucose; UGPase (UDP-Glucose Pyrophosphorylase) catalyzes the reversible production of UDP-Glucose and pyrophosphate (PPi) from Glucose-1-phosphate and UTP. UDP-glucose plays pivotal roles in galactose utilization, in glycogen synthesis, and in the synthesis of the carbohydrate moieties of glycolipids, glycoproteins, and proteoglycans. UGPase is found in both prokaryotes and eukaryotes. Interestingly, while the prokaryotic and eukaryotic forms of UGPase catalyze the same reaction, they share low sequence similarity. This family consists of mainly eukaryotic UTP-glucose-1-phosphate uridylyltransferases.
Pssm-ID: 132998 Cd Length: 300 Bit Score: 56.10 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68566143 101 NKVAVLLLAGGQGTRLGVSYPKGMYDVglPSHKTLFQIQAERILKLQqlaeKHHGnkCTIPWYIMTSGRTMESTKEFFTK 180
Cdd:cd00897 2 NKLVVLKLNGGLGTSMGCTGPKSLIEV--RDGKTFLDLTVQQIEHLN----KTYG--VDVPLVLMNSFNTDEDTKKILKK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68566143 181 hkfFGLKKENVVFFQQGMLPAMSFDGKIILEEK---NKVSMAPDGNGGLYRALAAQNIVEDMEQRGICSIHVYCVDNiLV 257
Cdd:cd00897 74 ---YAGVNVDIHTFNQSRYPRISKETLLPVPSWadsPDEEWYPPGHGDIFESLYNSGLLDTLLAQGKEYLFVSNIDN-LG 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 68566143 258 KVADPRFIGFCIQKGADCGAKVVEKTNPTEPVGVVCRVDGVYQVVE 303
Cdd:cd00897 150 ATVDLRILNHMVDNKAEYIMEVTDKTRADVKGGTLIQYEGKLRLLE 195
|
|
| PLN02474 |
PLN02474 |
UTP--glucose-1-phosphate uridylyltransferase |
101-307 |
7.00e-04 |
|
UTP--glucose-1-phosphate uridylyltransferase
Pssm-ID: 178092 Cd Length: 469 Bit Score: 42.17 E-value: 7.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68566143 101 NKVAVLLLAGGQGTRLGVSYPKGMYDV--GLpSHKTLFQIQAERIlklqqlaekHHGNKCTIPWYIMTSGRTMESTKEFF 178
Cdd:PLN02474 78 DKLVVLKLNGGLGTTMGCTGPKSVIEVrnGL-TFLDLIVIQIENL---------NKKYGCNVPLLLMNSFNTHDDTQKIV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68566143 179 TKHKFFGLKkenVVFFQQGMLPAMSFDGKIILEEKNKVSMA---PDGNGGLYRALAAQNIVEDMEQRGICSIHVYCVDNi 255
Cdd:PLN02474 148 EKYTNSNIE---IHTFNQSQYPRVVADDFVPWPSKGKTDKDgwyPPGHGDVFPSLMNSGKLDALLSQGKEYVFIANSDN- 223
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 68566143 256 LVKVADPRFIGFCIQKGADCGAKVVEKTNPTEPVGVVCRVDGVYQVVEYSEI 307
Cdd:PLN02474 224 LGAIVDLKILNHLIQNKNEYCMEVTPKTLADVKGGTLISYEGKVQLLEIAQV 275
|
|
| CDP-ME_synthetase |
cd02516 |
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ... |
103-137 |
6.75e-03 |
|
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; 4-diphosphocytidyl-2-methyl-D-erythritol synthase (CDP-ME), also called 2C-methyl-d-erythritol 4-phosphate cytidylyltransferase catalyzes the third step in the alternative (non-mevalonate) pathway of Isopentenyl diphosphate (IPP) biosynthesis: the formation of 4-diphosphocytidyl-2C-methyl-D-erythritol from CTP and 2C-methyl-D-erythritol 4-phosphate. This mevalonate independent pathway that utilizes pyruvate and glyceraldehydes 3-phosphate as starting materials for production of IPP occurs in a variety of bacteria, archaea and plant cells, but is absent in mammals. Thus, CDP-ME synthetase is an attractive targets for the structure-based design of selective antibacterial, herbicidal and antimalarial drugs.
Pssm-ID: 133009 [Multi-domain] Cd Length: 218 Bit Score: 38.27 E-value: 6.75e-03
10 20 30
....*....|....*....|....*....|....*
gi 68566143 103 VAVLLLAGGQGTRLGVSYPKGMYDVGlpsHKTLFQ 137
Cdd:cd02516 1 VAAIILAAGSGSRMGADIPKQFLELG---GKPVLE 32
|
|
| |
