|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02474 |
PLN02474 |
UTP--glucose-1-phosphate uridylyltransferase |
1-469 |
0e+00 |
|
UTP--glucose-1-phosphate uridylyltransferase
Pssm-ID: 178092 Cd Length: 469 Bit Score: 925.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228498 1 MAATTENLPQLKSAVDGLTEMSESEKSGFISLVSRYLSGEAQHIEWSKIQTPTDEIVVPYEKMTPVSQDVAETKNLLDKL 80
Cdd:PLN02474 1 AATADEKLPQLRSAVAGLDQISENEKSGFISLVSRYLSGEAQHIEWSKIQTPTDEVVVPYDKLAPVPEDPEETKKLLDKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228498 81 VVLKLNGGLGTTMGCTGPKSVIEVRDGLTFLDLIVIQIENLNNKYGCKVPLVLMNSFNTHDDTHKIVEKYTNSNVDIHTF 160
Cdd:PLN02474 81 VVLKLNGGLGTTMGCTGPKSVIEVRNGLTFLDLIVIQIENLNKKYGCNVPLLLMNSFNTHDDTQKIVEKYTNSNIEIHTF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228498 161 NQSKYPRVVADEFVPWPSKGKTDKEGWYPPGHGDVFPALMNSGKLDTFLSQGKEYVFVANSDNLGAIVDLTILKHLIQNK 240
Cdd:PLN02474 161 NQSQYPRVVADDFVPWPSKGKTDKDGWYPPGHGDVFPSLMNSGKLDALLSQGKEYVFIANSDNLGAIVDLKILNHLIQNK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228498 241 NEYCMEVTPKTLADVKGGTLISYEGKVQLLEIAQVPDEHVNEFKSIEKFKIFNTNNLWVNLKAIKKLVEADALKMEIIPN 320
Cdd:PLN02474 241 NEYCMEVTPKTLADVKGGTLISYEGKVQLLEIAQVPDEHVNEFKSIEKFKIFNTNNLWVNLKAIKRLVEADALKMEIIPN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228498 321 PKEVDGVKVLQLETAAGAAIRFFDNAIGVNVPRSRFLPVKASSDLLLVQSDLYTLVDGFVTRNKARTNPSNPSIELGPEF 400
Cdd:PLN02474 321 PKEVDGVKVLQLETAAGAAIRFFDNAIGINVPRSRFLPVKATSDLLLVQSDLYTLVDGFVIRNKARTNPSNPSIELGPEF 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15228498 401 KKVATFLSRFKSIPSIVELDSLKVSGDVWFGSSIVLKGKVTVAAKSGVKLEIPDRAVVENKNINGPEDL 469
Cdd:PLN02474 401 KKVANFLSRFKSIPSIVELDSLKVSGDVWFGSGIVLKGKVTITAKSGVKLEIPDGAVLENKDINGPEDL 469
|
|
| UDPGP |
pfam01704 |
UTP--glucose-1-phosphate uridylyltransferase; This family consists of UTP--glucose-1-phosphate ... |
27-437 |
0e+00 |
|
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: 676.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228498 27 SGFISLVSRYLS--GEAQHIEWSKIQTPTDEIVVPYEKMTpvsQDVAETKNLLDKLVVLKLNGGLGTTMGCTGPKSVIEV 104
Cdd:pfam01704 2 DGFFKLFSRYLSekGKQEKIDWDKIKPPPEEEIVDYEDLQ---EPEEEIKELLNKLAVLKLNGGLGTSMGCVGPKSLIEV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228498 105 RDGLTFLDLIVIQIENLNNKYGCKVPLVLMNSFNTHDDTHKIVEKYTNSNVDIHTFNQSKYPRVVADEFVPWPSKGKTDK 184
Cdd:pfam01704 79 RDGLTFLDLIVQQIEHLNKKYNVDVPLVLMNSFNTDEDTKKIIRKYKGHKVDILTFNQSRYPRIDKDTLLPVPKSADSDE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228498 185 EGWYPPGHGDVFPALMNSGKLDTFLSQGKEYVFVANSDNLGAIVDLTILKHLIQNKNEYCMEVTPKTLADVKGGTLISYE 264
Cdd:pfam01704 159 EEWYPPGHGDLYESLYNSGLLDKLLAEGKEYLFVSNIDNLGATVDLNILNYMVDNGAEFLMEVTDKTRADVKGGTLIEYD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228498 265 GKVQLLEIAQVPDEHVNEFKSIEKFKIFNTNNLWVNLKAIKKLVEADALKMEIIPNPKEVD-GVKVLQLETAAGAAIRFF 343
Cdd:pfam01704 239 GKLRLLEIAQVPKEHVDEFKSIKKFKIFNTNNIWINLKALKRVVEEGELQLEIIVNKKTLDnGENVIQLETAVGAAIKNF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228498 344 DNAIGVNVPRSRFLPVKASSDLLLVQSDLYTLVDGFVTRNKARTNPSNPSIELGPEFKKVATFLSRFKSIPSIVELDSLK 423
Cdd:pfam01704 319 KNAIGINVPRSRFLPVKTTSDLLLVMSDLYVLNHGSLIMNPKRMFGTPPVVLLGDHFKKVDEFLKRFPSIPDLLELDHLT 398
|
410
....*....|....
gi 15228498 424 VSGDVWFGSSIVLK 437
Cdd:pfam01704 399 VSGDVTFGRNVTLK 412
|
|
| UGPase_euk |
cd00897 |
Eukaryotic UGPase catalyses the synthesis of UDP-Glucose; UGPase (UDP-Glucose ... |
86-375 |
0e+00 |
|
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: 576.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228498 86 NGGLGTTMGCTGPKSVIEVRDGLTFLDLIVIQIENLNNKYGCKVPLVLMNSFNTHDDTHKIVEKYTNSNVDIHTFNQSKY 165
Cdd:cd00897 10 NGGLGTSMGCTGPKSLIEVRDGKTFLDLTVQQIEHLNKTYGVDVPLVLMNSFNTDEDTKKILKKYAGVNVDIHTFNQSRY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228498 166 PRVVADEFVPWPSKGKTDKEGWYPPGHGDVFPALMNSGKLDTFLSQGKEYVFVANSDNLGAIVDLTILKHLIQNKNEYCM 245
Cdd:cd00897 90 PRISKETLLPVPSWADSPDEEWYPPGHGDIFESLYNSGLLDTLLAQGKEYLFVSNIDNLGATVDLRILNHMVDNKAEYIM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228498 246 EVTPKTLADVKGGTLISYEGKVQLLEIAQVPDEHVNEFKSIEKFKIFNTNNLWVNLKAIKKLVEADALKMEIIPNPKEVD 325
Cdd:cd00897 170 EVTDKTRADVKGGTLIQYEGKLRLLEIAQVPKEHVDEFKSIKKFKIFNTNNLWVNLKAVKRVVEENALDLEIIVNPKTVD 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 15228498 326 G-VKVLQLETAAGAAIRFFDNAIGVNVPRSRFLPVKASSDLLLVQSDLYTL 375
Cdd:cd00897 250 GgLNVIQLETAVGAAIKNFDNALGVNVPRSRFLPVKTTSDLLLVRSDLYSL 300
|
|
| QRI1 |
COG4284 |
UDP-N-acetylglucosamine pyrophosphorylase [Carbohydrate transport and metabolism]; |
86-360 |
1.46e-83 |
|
UDP-N-acetylglucosamine pyrophosphorylase [Carbohydrate transport and metabolism];
Pssm-ID: 443425 Cd Length: 402 Bit Score: 262.90 E-value: 1.46e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228498 86 NGGLGTTMGCTGPKSVIEVRD--GLTFLDLIVIQIENLNNKYGCKVPLVLMNSFNTHDDTHKIVEKYTNSNVD---IHTF 160
Cdd:COG4284 102 AGGQGTRLGFDGPKGLLPVRPvkGKSLFDLIAEQVLAARRRYGVPLPLYIMTSFRTHEDTLAFLEEHDYFGLDglpVHFF 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228498 161 NQSKYPRVVADEF-VPWPSKGktDKEgWYPPGHGDVFPALMNSGKLDTFLSQGKEYVFVANSDN-LGAIVDLTILKHLIQ 238
Cdd:COG4284 182 LQGMEPALDADLGpVLLPADP--ELE-LCPPGHGGIYTALLASGLLDKLLERGIRYLFVSNVDNpLGAVPDPAFAGWHAA 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228498 239 NKNEYCMEVTPKTLADVKGGTLISYEGKVQLLEIAQVPDEHVNEFKSIEKFKIFNTNNLWVNLKAIKKLVEADALKMEII 318
Cdd:COG4284 259 SGAPFTAKVVRRTPPDEKVGHLARVDGRLILREYSQLPDEEAEAFTGELRHPYGNINNHWFDLDFLKRLLDERGLGLPLH 338
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 15228498 319 PNPKEVDGV---------KVLQLETAAGAAIRFFDNAIGVNVPR-SRFLPVK 360
Cdd:COG4284 339 RAEKKVDPLdesgkptspNVIKFETFMFDAIPLFDGAVAIEVDReERFAPVK 390
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02474 |
PLN02474 |
UTP--glucose-1-phosphate uridylyltransferase |
1-469 |
0e+00 |
|
UTP--glucose-1-phosphate uridylyltransferase
Pssm-ID: 178092 Cd Length: 469 Bit Score: 925.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228498 1 MAATTENLPQLKSAVDGLTEMSESEKSGFISLVSRYLSGEAQHIEWSKIQTPTDEIVVPYEKMTPVSQDVAETKNLLDKL 80
Cdd:PLN02474 1 AATADEKLPQLRSAVAGLDQISENEKSGFISLVSRYLSGEAQHIEWSKIQTPTDEVVVPYDKLAPVPEDPEETKKLLDKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228498 81 VVLKLNGGLGTTMGCTGPKSVIEVRDGLTFLDLIVIQIENLNNKYGCKVPLVLMNSFNTHDDTHKIVEKYTNSNVDIHTF 160
Cdd:PLN02474 81 VVLKLNGGLGTTMGCTGPKSVIEVRNGLTFLDLIVIQIENLNKKYGCNVPLLLMNSFNTHDDTQKIVEKYTNSNIEIHTF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228498 161 NQSKYPRVVADEFVPWPSKGKTDKEGWYPPGHGDVFPALMNSGKLDTFLSQGKEYVFVANSDNLGAIVDLTILKHLIQNK 240
Cdd:PLN02474 161 NQSQYPRVVADDFVPWPSKGKTDKDGWYPPGHGDVFPSLMNSGKLDALLSQGKEYVFIANSDNLGAIVDLKILNHLIQNK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228498 241 NEYCMEVTPKTLADVKGGTLISYEGKVQLLEIAQVPDEHVNEFKSIEKFKIFNTNNLWVNLKAIKKLVEADALKMEIIPN 320
Cdd:PLN02474 241 NEYCMEVTPKTLADVKGGTLISYEGKVQLLEIAQVPDEHVNEFKSIEKFKIFNTNNLWVNLKAIKRLVEADALKMEIIPN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228498 321 PKEVDGVKVLQLETAAGAAIRFFDNAIGVNVPRSRFLPVKASSDLLLVQSDLYTLVDGFVTRNKARTNPSNPSIELGPEF 400
Cdd:PLN02474 321 PKEVDGVKVLQLETAAGAAIRFFDNAIGINVPRSRFLPVKATSDLLLVQSDLYTLVDGFVIRNKARTNPSNPSIELGPEF 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15228498 401 KKVATFLSRFKSIPSIVELDSLKVSGDVWFGSSIVLKGKVTVAAKSGVKLEIPDRAVVENKNINGPEDL 469
Cdd:PLN02474 401 KKVANFLSRFKSIPSIVELDSLKVSGDVWFGSGIVLKGKVTITAKSGVKLEIPDGAVLENKDINGPEDL 469
|
|
| UDPGP |
pfam01704 |
UTP--glucose-1-phosphate uridylyltransferase; This family consists of UTP--glucose-1-phosphate ... |
27-437 |
0e+00 |
|
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: 676.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228498 27 SGFISLVSRYLS--GEAQHIEWSKIQTPTDEIVVPYEKMTpvsQDVAETKNLLDKLVVLKLNGGLGTTMGCTGPKSVIEV 104
Cdd:pfam01704 2 DGFFKLFSRYLSekGKQEKIDWDKIKPPPEEEIVDYEDLQ---EPEEEIKELLNKLAVLKLNGGLGTSMGCVGPKSLIEV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228498 105 RDGLTFLDLIVIQIENLNNKYGCKVPLVLMNSFNTHDDTHKIVEKYTNSNVDIHTFNQSKYPRVVADEFVPWPSKGKTDK 184
Cdd:pfam01704 79 RDGLTFLDLIVQQIEHLNKKYNVDVPLVLMNSFNTDEDTKKIIRKYKGHKVDILTFNQSRYPRIDKDTLLPVPKSADSDE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228498 185 EGWYPPGHGDVFPALMNSGKLDTFLSQGKEYVFVANSDNLGAIVDLTILKHLIQNKNEYCMEVTPKTLADVKGGTLISYE 264
Cdd:pfam01704 159 EEWYPPGHGDLYESLYNSGLLDKLLAEGKEYLFVSNIDNLGATVDLNILNYMVDNGAEFLMEVTDKTRADVKGGTLIEYD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228498 265 GKVQLLEIAQVPDEHVNEFKSIEKFKIFNTNNLWVNLKAIKKLVEADALKMEIIPNPKEVD-GVKVLQLETAAGAAIRFF 343
Cdd:pfam01704 239 GKLRLLEIAQVPKEHVDEFKSIKKFKIFNTNNIWINLKALKRVVEEGELQLEIIVNKKTLDnGENVIQLETAVGAAIKNF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228498 344 DNAIGVNVPRSRFLPVKASSDLLLVQSDLYTLVDGFVTRNKARTNPSNPSIELGPEFKKVATFLSRFKSIPSIVELDSLK 423
Cdd:pfam01704 319 KNAIGINVPRSRFLPVKTTSDLLLVMSDLYVLNHGSLIMNPKRMFGTPPVVLLGDHFKKVDEFLKRFPSIPDLLELDHLT 398
|
410
....*....|....
gi 15228498 424 VSGDVWFGSSIVLK 437
Cdd:pfam01704 399 VSGDVTFGRNVTLK 412
|
|
| UGPase_euk |
cd00897 |
Eukaryotic UGPase catalyses the synthesis of UDP-Glucose; UGPase (UDP-Glucose ... |
86-375 |
0e+00 |
|
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: 576.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228498 86 NGGLGTTMGCTGPKSVIEVRDGLTFLDLIVIQIENLNNKYGCKVPLVLMNSFNTHDDTHKIVEKYTNSNVDIHTFNQSKY 165
Cdd:cd00897 10 NGGLGTSMGCTGPKSLIEVRDGKTFLDLTVQQIEHLNKTYGVDVPLVLMNSFNTDEDTKKILKKYAGVNVDIHTFNQSRY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228498 166 PRVVADEFVPWPSKGKTDKEGWYPPGHGDVFPALMNSGKLDTFLSQGKEYVFVANSDNLGAIVDLTILKHLIQNKNEYCM 245
Cdd:cd00897 90 PRISKETLLPVPSWADSPDEEWYPPGHGDIFESLYNSGLLDTLLAQGKEYLFVSNIDNLGATVDLRILNHMVDNKAEYIM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228498 246 EVTPKTLADVKGGTLISYEGKVQLLEIAQVPDEHVNEFKSIEKFKIFNTNNLWVNLKAIKKLVEADALKMEIIPNPKEVD 325
Cdd:cd00897 170 EVTDKTRADVKGGTLIQYEGKLRLLEIAQVPKEHVDEFKSIKKFKIFNTNNLWVNLKAVKRVVEENALDLEIIVNPKTVD 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 15228498 326 G-VKVLQLETAAGAAIRFFDNAIGVNVPRSRFLPVKASSDLLLVQSDLYTL 375
Cdd:cd00897 250 GgLNVIQLETAVGAAIKNFDNALGVNVPRSRFLPVKTTSDLLLVRSDLYSL 300
|
|
| UGPase_euk_like |
cd04180 |
Eukaryotic UGPase-like includes UDPase and UDPGlcNAc pyrophosphorylase enzymes; This family ... |
86-361 |
9.46e-109 |
|
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: 322.97 E-value: 9.46e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228498 86 NGGLGTTMGCTGPKSVIEVR--DGLTFLDLIVIQIENLNNK--YGCKVPLVLMNSFNTHDDTHKIVEKYTNSNVDIHTFN 161
Cdd:cd04180 7 AGGLGTRLGKDGPKSSTDVGlpSGQCFLQLIGEKILTLQEIdlYSCKIPEQLMNSKYTHEKTQCYFEKINQKNSYVITFM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228498 162 QSKYPRVVADEFVpwpSKGKTDKEGWYPPGHGDVFPALMNSGKLDTFLSQGKEYVFVANSDNLGAIV-DLTILKHLIQNK 240
Cdd:cd04180 87 QGKLPLKNDDDAR---DPHNKTKCHLFPCGHGDVVLALIHSGHLNKLLEKGYRYIHFIGVDNLLVKVaDPLFIGIAIQNR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228498 241 NEYCMEVTPKTLADVKGGTLISYE-GKVQLLEIAQVPDEHVNE--------FKSIEKFKIFNTNNLWVNLKAIKKLVEad 311
Cdd:cd04180 164 KAINQKVVPKTRNEESGGYRIANInGRVQLLEYDQIKKLLKQKmvnnqipkDIDDAPFFLFNTNNLINFLVEFKDRVD-- 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 15228498 312 alkmeiipnpkevdgvkvlqletaagAAIRFFDNAIGVNVPRS-RFLPVKA 361
Cdd:cd04180 242 --------------------------DIIEFTDDIVGVMVHRAeEFAPVKN 266
|
|
| QRI1 |
COG4284 |
UDP-N-acetylglucosamine pyrophosphorylase [Carbohydrate transport and metabolism]; |
86-360 |
1.46e-83 |
|
UDP-N-acetylglucosamine pyrophosphorylase [Carbohydrate transport and metabolism];
Pssm-ID: 443425 Cd Length: 402 Bit Score: 262.90 E-value: 1.46e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228498 86 NGGLGTTMGCTGPKSVIEVRD--GLTFLDLIVIQIENLNNKYGCKVPLVLMNSFNTHDDTHKIVEKYTNSNVD---IHTF 160
Cdd:COG4284 102 AGGQGTRLGFDGPKGLLPVRPvkGKSLFDLIAEQVLAARRRYGVPLPLYIMTSFRTHEDTLAFLEEHDYFGLDglpVHFF 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228498 161 NQSKYPRVVADEF-VPWPSKGktDKEgWYPPGHGDVFPALMNSGKLDTFLSQGKEYVFVANSDN-LGAIVDLTILKHLIQ 238
Cdd:COG4284 182 LQGMEPALDADLGpVLLPADP--ELE-LCPPGHGGIYTALLASGLLDKLLERGIRYLFVSNVDNpLGAVPDPAFAGWHAA 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228498 239 NKNEYCMEVTPKTLADVKGGTLISYEGKVQLLEIAQVPDEHVNEFKSIEKFKIFNTNNLWVNLKAIKKLVEADALKMEII 318
Cdd:COG4284 259 SGAPFTAKVVRRTPPDEKVGHLARVDGRLILREYSQLPDEEAEAFTGELRHPYGNINNHWFDLDFLKRLLDERGLGLPLH 338
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 15228498 319 PNPKEVDGV---------KVLQLETAAGAAIRFFDNAIGVNVPR-SRFLPVK 360
Cdd:COG4284 339 RAEKKVDPLdesgkptspNVIKFETFMFDAIPLFDGAVAIEVDReERFAPVK 390
|
|
| UDPGlcNAc_PPase |
cd04193 |
UDPGlcNAc pyrophosphorylase catalayzes the synthesis of UDPGlcNAc; UDP-N-acetylglucosamine ... |
87-360 |
1.26e-15 |
|
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: 77.65 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228498 87 GGLGTTMGCTGPKSVIEVrDGLTFLDLIVIQIEN---LNNKYG------CKVPLVLMNSFNTHDDTHKIVEK--YTNSNV 155
Cdd:cd04193 23 GGQGTRLGFDGPKGMFPV-GLPSKKSLFQLQAERilkLQELAGeasgkkVPIPWYIMTSEATHEETRKFFKEnnYFGLDP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228498 156 D-IHTFNQSKYPRVVADEFVPWPSKGKTdkeGWYPPGHGDVFPALMNSGKLDTFLSQGKEYVFVANSDN-LGAIVDLTIL 233
Cdd:cd04193 102 EqVHFFQQGMLPCVDFDGKILLEEKGKI---AMAPNGNGGLYKALQTAGILEDMKKRGIKYIHVYSVDNiLVKVADPVFI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228498 234 KHLIQNKNEYCMEVTPKTLADVKGGTLISYEGKVQLLEIAQVPDEhVNEFKSIEKFKIFNTNNLWVNL------------ 301
Cdd:cd04193 179 GFCISKGADVGAKVVRKRYPTEKVGVVVLVDGKPQVVEYSEISDE-LAEKRDADGELQYNAGNIANHFfsldflekaaem 257
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15228498 302 --------KAIKKLVEADalKMEIIPNPKEVDGVKvlqLETAAGAAIRFFDNAIGVNVPRS-RFLPVK 360
Cdd:cd04193 258 eepslpyhIAKKKIPYVD--LEGGLVKPDEPNGIK---LELFIFDVFPFAKNFVCLEVDREeEFSPLK 320
|
|
| UGGPase |
cd06424 |
UGGPase catalyzes the synthesis of UDP-Glucose/UDP-Galactose; UGGPase: UDP-Galactose/Glucose ... |
87-226 |
3.07e-09 |
|
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: 58.24 E-value: 3.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228498 87 GGLGTTMGCTGPKSVIEVR--DGLTFLDLIVIQI----ENLNNKYGCKVPLVLMNSFNTHDDTHKIVE--KYTNSNVD-I 157
Cdd:cd06424 8 GGLGERLGYSGIKIGLPVEltTNTTYLQYYLNYIrafqEASKKGEKMEIPFVIMTSDDTHSKTLKLLEenNYFGLEKDqV 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15228498 158 HTFNQSKYP-------RVVADEfvpwPSKGKTDKEgwyPPGHGDVFPALMNSGKLDTFLSQGKEYVFVANSDNLGA 226
Cdd:cd06424 88 HILKQEKVFclidndaHLALDP----DNTYSILTK---PHGHGDVHTLLYNSGLLKKWIEAGYKWLVFFQDTNALA 156
|
|
| PLN02830 |
PLN02830 |
UDP-sugar pyrophosphorylase |
87-216 |
3.98e-08 |
|
UDP-sugar pyrophosphorylase
Pssm-ID: 215444 Cd Length: 615 Bit Score: 55.46 E-value: 3.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228498 87 GGLGTTMGCTGPKSVI--EVRDGLTFLDLIV-----IQIENLNNKYGC--KVPLVLMNSFNTHDDTHKIVEKYTNSNVD- 156
Cdd:PLN02830 136 GGLGERLGYSGIKVALptETATGTCYLQLYIesilaLQERAKKRKAKKgrKIPLVIMTSDDTHARTLKLLERNDYFGMDp 215
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15228498 157 --IHTFNQSKYP-------RVVADEFVPWPSKGKtdkegwyPPGHGDVFPALMNSGKLDTFLSQGKEYV 216
Cdd:PLN02830 216 dqVTLLKQEKVAclmdndaRLALDPNDPYKIQTK-------PHGHGDVHALLYSSGLLDKWLSAGKKWV 277
|
|
| PTZ00339 |
PTZ00339 |
UDP-N-acetylglucosamine pyrophosphorylase; Provisional |
87-224 |
4.78e-06 |
|
UDP-N-acetylglucosamine pyrophosphorylase; Provisional
Pssm-ID: 240368 Cd Length: 482 Bit Score: 48.97 E-value: 4.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228498 87 GGLGTTMGCTGPKSVIEVR--DGLTFLDLIVIQIENL--------NNKYGCKVPLVLMNSFNTHDDTHKIVEKYTNSNVD 156
Cdd:PTZ00339 114 GGLGTRLGSDKPKGLLECTpvKKKTLFQFHCEKVRRLeemavavsGGGDDPTIYILVLTSSFNHDQTRQFLEENNFFGLD 193
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15228498 157 ---IHTFNQSKYPRVVADEFVPWPSKGKTDKEGwyPPGHGDVFPALMNSGKLDTFLSQGKEYVFVANSDNL 224
Cdd:PTZ00339 194 keqVIFFKQSSLPCYDENTGRFIMSSQGSLCTA--PGGNGDVFKALAKCSELMDIVRKGIKYVQVISIDNI 262
|
|
| PLN02435 |
PLN02435 |
probable UDP-N-acetylglucosamine pyrophosphorylase |
87-237 |
3.50e-03 |
|
probable UDP-N-acetylglucosamine pyrophosphorylase
Pssm-ID: 215238 Cd Length: 493 Bit Score: 39.85 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228498 87 GGLGTTMGCTGPKSVIEVrdGL-TFLDLIVIQIENL-----------NNKYGCKVPL--VLMNSFNTHDDTHKIVE--KY 150
Cdd:PLN02435 124 GGQGTRLGSSDPKGCFNI--GLpSGKSLFQLQAERIlcvqrlaaqasSEGPGRPVTIhwYIMTSPFTDEATRKFFEshKY 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228498 151 TNSNVD-IHTFNQSKYPRVVADEFVPWPSKGKTDKEgwyPPGHGDVFPALMNSGKLDTFLSQGKEYVFVANSDN-LGAIV 228
Cdd:PLN02435 202 FGLEADqVTFFQQGTLPCVSKDGKFIMETPFKVAKA---PDGNGGVYAALKSSRLLEDMASRGIKYVDCYGVDNaLVRVA 278
|
....*....
gi 15228498 229 DLTILKHLI 237
Cdd:PLN02435 279 DPTFLGYFI 287
|
|
| |
