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Conserved domains on  [gi|594591591|ref|NP_001277563|]
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UTP--glucose-1-phosphate uridylyltransferase isoform 2 [Mus musculus]

Protein Classification

UTP--glucose-1-phosphate uridylyltransferase( domain architecture ID 10484167)

UTP--glucose-1-phosphate uridylyltransferase catalyzes the formation of UDP-glucose from glucose-1-phosphate and UTP, which is an intermediate step in the biosynthesis of diglucosyl-diacylglycerol (Glc2-DAG)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
UDPGP pfam01704
UTP--glucose-1-phosphate uridylyltransferase; This family consists of UTP--glucose-1-phosphate ...
44-462 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: 775.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591591   44 LDGFRKLFHRFLQEKG--PSVDWGKIQRPPEDSIQPYEKIKArgLPDNISSVLNKLVVVKLNGGLGTSMGCKGPKSLIGV 121
Cdd:pfam01704   1 LDGFFKLFSRYLSEKGkqEKIDWDKIKPPPEEEIVDYEDLQE--PEEEIKELLNKLAVLKLNGGLGTSMGCVGPKSLIEV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591591  122 RNENTFLDLTVQQIEHLNKTYNTDVPLVLMNSFNTDEDTKKILQKYNHCRVKIYTFNQSRYPRINKESLLPIAKDvsySG 201
Cdd:pfam01704  79 RDGLTFLDLIVQQIEHLNKKYNVDVPLVLMNSFNTDEDTKKIIRKYKGHKVDILTFNQSRYPRIDKDTLLPVPKS---AD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591591  202 ENTEAWYPPGHGDIYASFYNSGLLDTFIEEGKEYIFVSNIDNLGATVDLYILNHLMNppngKRCEFVMEVTNKTRADVKG 281
Cdd:pfam01704 156 SDEEEWYPPGHGDLYESLYNSGLLDKLLAEGKEYLFVSNIDNLGATVDLNILNYMVD----NGAEFLMEVTDKTRADVKG 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591591  282 GTLTQYEGKLRLVEIAQVPKAHVDEFKSVSKFKIFNTNNLWISLGAVKRLQEQNAIDMEIIVNPKTLDGGLNVIQLETAV 361
Cdd:pfam01704 232 GTLIEYDGKLRLLEIAQVPKEHVDEFKSIKKFKIFNTNNIWINLKALKRVVEEGELQLEIIVNKKTLDNGENVIQLETAV 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591591  362 GAAIKSFENSLGINVPRSRFLPVKTTSDLLLVMSNLYSLNAGSLTMSEKREFPTVPLVKLGSSFTKVQDYLRRFESIPDM 441
Cdd:pfam01704 312 GAAIKNFKNAIGINVPRSRFLPVKTTSDLLLVMSDLYVLNHGSLIMNPKRMFGTPPVVLLGDHFKKVDEFLKRFPSIPDL 391
                         410       420
                  ....*....|....*....|.
gi 594591591  442 LELDHLTVSGDVTFGKNVSLK 462
Cdd:pfam01704 392 LELDHLTVSGDVTFGRNVTLK 412
 
Name Accession Description Interval E-value
UDPGP pfam01704
UTP--glucose-1-phosphate uridylyltransferase; This family consists of UTP--glucose-1-phosphate ...
44-462 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: 775.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591591   44 LDGFRKLFHRFLQEKG--PSVDWGKIQRPPEDSIQPYEKIKArgLPDNISSVLNKLVVVKLNGGLGTSMGCKGPKSLIGV 121
Cdd:pfam01704   1 LDGFFKLFSRYLSEKGkqEKIDWDKIKPPPEEEIVDYEDLQE--PEEEIKELLNKLAVLKLNGGLGTSMGCVGPKSLIEV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591591  122 RNENTFLDLTVQQIEHLNKTYNTDVPLVLMNSFNTDEDTKKILQKYNHCRVKIYTFNQSRYPRINKESLLPIAKDvsySG 201
Cdd:pfam01704  79 RDGLTFLDLIVQQIEHLNKKYNVDVPLVLMNSFNTDEDTKKIIRKYKGHKVDILTFNQSRYPRIDKDTLLPVPKS---AD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591591  202 ENTEAWYPPGHGDIYASFYNSGLLDTFIEEGKEYIFVSNIDNLGATVDLYILNHLMNppngKRCEFVMEVTNKTRADVKG 281
Cdd:pfam01704 156 SDEEEWYPPGHGDLYESLYNSGLLDKLLAEGKEYLFVSNIDNLGATVDLNILNYMVD----NGAEFLMEVTDKTRADVKG 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591591  282 GTLTQYEGKLRLVEIAQVPKAHVDEFKSVSKFKIFNTNNLWISLGAVKRLQEQNAIDMEIIVNPKTLDGGLNVIQLETAV 361
Cdd:pfam01704 232 GTLIEYDGKLRLLEIAQVPKEHVDEFKSIKKFKIFNTNNIWINLKALKRVVEEGELQLEIIVNKKTLDNGENVIQLETAV 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591591  362 GAAIKSFENSLGINVPRSRFLPVKTTSDLLLVMSNLYSLNAGSLTMSEKREFPTVPLVKLGSSFTKVQDYLRRFESIPDM 441
Cdd:pfam01704 312 GAAIKNFKNAIGINVPRSRFLPVKTTSDLLLVMSDLYVLNHGSLIMNPKRMFGTPPVVLLGDHFKKVDEFLKRFPSIPDL 391
                         410       420
                  ....*....|....*....|.
gi 594591591  442 LELDHLTVSGDVTFGKNVSLK 462
Cdd:pfam01704 392 LELDHLTVSGDVTFGRNVTLK 412
UGPase_euk cd00897
Eukaryotic UGPase catalyses the synthesis of UDP-Glucose; UGPase (UDP-Glucose ...
94-400 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: 615.41  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591591  94 LNKLVVVKLNGGLGTSMGCKGPKSLIGVRNENTFLDLTVQQIEHLNKTYNTDVPLVLMNSFNTDEDTKKILQKYNHCRVK 173
Cdd:cd00897    1 LNKLVVLKLNGGLGTSMGCTGPKSLIEVRDGKTFLDLTVQQIEHLNKTYGVDVPLVLMNSFNTDEDTKKILKKYAGVNVD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591591 174 IYTFNQSRYPRINKESLLPIAkdvSYSGENTEAWYPPGHGDIYASFYNSGLLDTFIEEGKEYIFVSNIDNLGATVDLYIL 253
Cdd:cd00897   81 IHTFNQSRYPRISKETLLPVP---SWADSPDEEWYPPGHGDIFESLYNSGLLDTLLAQGKEYLFVSNIDNLGATVDLRIL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591591 254 NHLMNPPngkrCEFVMEVTNKTRADVKGGTLTQYEGKLRLVEIAQVPKAHVDEFKSVSKFKIFNTNNLWISLGAVKRLQE 333
Cdd:cd00897  158 NHMVDNK----AEYIMEVTDKTRADVKGGTLIQYEGKLRLLEIAQVPKEHVDEFKSIKKFKIFNTNNLWVNLKAVKRVVE 233
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 594591591 334 QNAIDMEIIVNPKTLDGGLNVIQLETAVGAAIKSFENSLGINVPRSRFLPVKTTSDLLLVMSNLYSL 400
Cdd:cd00897  234 ENALDLEIIVNPKTVDGGLNVIQLETAVGAAIKNFDNALGVNVPRSRFLPVKTTSDLLLVRSDLYSL 300
PLN02474 PLN02474
UTP--glucose-1-phosphate uridylyltransferase
46-490 0e+00

UTP--glucose-1-phosphate uridylyltransferase


Pssm-ID: 178092  Cd Length: 469  Bit Score: 548.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591591  46 GFRKLFHRFLQEKGPSVDWGKIQRPPEDSIQPYEKIKARGL-PDNISSVLNKLVVVKLNGGLGTSMGCKGPKSLIGVRNE 124
Cdd:PLN02474  28 GFISLVSRYLSGEAQHIEWSKIQTPTDEVVVPYDKLAPVPEdPEETKKLLDKLVVLKLNGGLGTTMGCTGPKSVIEVRNG 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591591 125 NTFLDLTVQQIEHLNKTYNTDVPLVLMNSFNTDEDTKKILQKYNHCRVKIYTFNQSRYPRINKESLLPIAkdvSYSGENT 204
Cdd:PLN02474 108 LTFLDLIVIQIENLNKKYGCNVPLLLMNSFNTHDDTQKIVEKYTNSNIEIHTFNQSQYPRVVADDFVPWP---SKGKTDK 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591591 205 EAWYPPGHGDIYASFYNSGLLDTFIEEGKEYIFVSNIDNLGATVDLYILNHLMNPPNgkrcEFVMEVTNKTRADVKGGTL 284
Cdd:PLN02474 185 DGWYPPGHGDVFPSLMNSGKLDALLSQGKEYVFIANSDNLGAIVDLKILNHLIQNKN----EYCMEVTPKTLADVKGGTL 260
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591591 285 TQYEGKLRLVEIAQVPKAHVDEFKSVSKFKIFNTNNLWISLGAVKRLQEQNAIDMEIIVNPKTLDGgLNVIQLETAVGAA 364
Cdd:PLN02474 261 ISYEGKVQLLEIAQVPDEHVNEFKSIEKFKIFNTNNLWVNLKAIKRLVEADALKMEIIPNPKEVDG-VKVLQLETAAGAA 339
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591591 365 IKSFENSLGINVPRSRFLPVKTTSDLLLVMSNLYSLNAGSLTMSEKREFPTVPLVKLGSSFTKVQDYLRRFESIPDMLEL 444
Cdd:PLN02474 340 IRFFDNAIGINVPRSRFLPVKATSDLLLVQSDLYTLVDGFVIRNKARTNPSNPSIELGPEFKKVANFLSRFKSIPSIVEL 419
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 594591591 445 DHLTVSGDVTFGKNVSLKGTVIIIANHGDRIDIPPGAVLENKIVSG 490
Cdd:PLN02474 420 DSLKVSGDVWFGSGIVLKGKVTITAKSGVKLEIPDGAVLENKDING 465
QRI1 COG4284
UDP-N-acetylglucosamine pyrophosphorylase [Carbohydrate transport and metabolism];
43-389 1.44e-89

UDP-N-acetylglucosamine pyrophosphorylase [Carbohydrate transport and metabolism];


Pssm-ID: 443425  Cd Length: 402  Bit Score: 279.46  E-value: 1.44e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591591  43 DLDGFRKLFHRFLQEKGPSVdwgkiqRPPEDSIQPyekIKARGLPDNISSVLN---------------KLVVVKLNGGLG 107
Cdd:COG4284   36 DIDVFQHLYRQLVLAEGATG------LIPESDIEP---APVTDLPLTDLDEVDrdraeeageealragKVAVILLAGGQG 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591591 108 TSMGCKGPKSL--IGVRNENTFLDLTVQQIEHLNKTYNTDVPLVLMNSFNTDEDTKKILQKYNHCRV---KIYTFNQSRY 182
Cdd:COG4284  107 TRLGFDGPKGLlpVRPVKGKSLFDLIAEQVLAARRRYGVPLPLYIMTSFRTHEDTLAFLEEHDYFGLdglPVHFFLQGME 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591591 183 PRINKE--SLLPIAKDvsysgenTEAWYPPGHGDIYASFYNSGLLDTFIEEGKEYIFVSNIDN-LGATVDLYIL-NHLMn 258
Cdd:COG4284  187 PALDADlgPVLLPADP-------ELELCPPGHGGIYTALLASGLLDKLLERGIRYLFVSNVDNpLGAVPDPAFAgWHAA- 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591591 259 ppngKRCEFVMEVTNKTRADVKGGTLTQYEGKLRLVEIAQVPKAHVDEFKSVSKFKIFNTNNLWISLGAVKRLQEQNAID 338
Cdd:COG4284  259 ----SGAPFTAKVVRRTPPDEKVGHLARVDGRLILREYSQLPDEEAEAFTGELRHPYGNINNHWFDLDFLKRLLDERGLG 334
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591591 339 MEIIVNPKTLD----GGL----NVIQLETAVGAAIKSFENSLGINVPR-SRFLPVKTTSD 389
Cdd:COG4284  335 LPLHRAEKKVDpldeSGKptspNVIKFETFMFDAIPLFDGAVAIEVDReERFAPVKNTNG 394
 
Name Accession Description Interval E-value
UDPGP pfam01704
UTP--glucose-1-phosphate uridylyltransferase; This family consists of UTP--glucose-1-phosphate ...
44-462 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: 775.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591591   44 LDGFRKLFHRFLQEKG--PSVDWGKIQRPPEDSIQPYEKIKArgLPDNISSVLNKLVVVKLNGGLGTSMGCKGPKSLIGV 121
Cdd:pfam01704   1 LDGFFKLFSRYLSEKGkqEKIDWDKIKPPPEEEIVDYEDLQE--PEEEIKELLNKLAVLKLNGGLGTSMGCVGPKSLIEV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591591  122 RNENTFLDLTVQQIEHLNKTYNTDVPLVLMNSFNTDEDTKKILQKYNHCRVKIYTFNQSRYPRINKESLLPIAKDvsySG 201
Cdd:pfam01704  79 RDGLTFLDLIVQQIEHLNKKYNVDVPLVLMNSFNTDEDTKKIIRKYKGHKVDILTFNQSRYPRIDKDTLLPVPKS---AD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591591  202 ENTEAWYPPGHGDIYASFYNSGLLDTFIEEGKEYIFVSNIDNLGATVDLYILNHLMNppngKRCEFVMEVTNKTRADVKG 281
Cdd:pfam01704 156 SDEEEWYPPGHGDLYESLYNSGLLDKLLAEGKEYLFVSNIDNLGATVDLNILNYMVD----NGAEFLMEVTDKTRADVKG 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591591  282 GTLTQYEGKLRLVEIAQVPKAHVDEFKSVSKFKIFNTNNLWISLGAVKRLQEQNAIDMEIIVNPKTLDGGLNVIQLETAV 361
Cdd:pfam01704 232 GTLIEYDGKLRLLEIAQVPKEHVDEFKSIKKFKIFNTNNIWINLKALKRVVEEGELQLEIIVNKKTLDNGENVIQLETAV 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591591  362 GAAIKSFENSLGINVPRSRFLPVKTTSDLLLVMSNLYSLNAGSLTMSEKREFPTVPLVKLGSSFTKVQDYLRRFESIPDM 441
Cdd:pfam01704 312 GAAIKNFKNAIGINVPRSRFLPVKTTSDLLLVMSDLYVLNHGSLIMNPKRMFGTPPVVLLGDHFKKVDEFLKRFPSIPDL 391
                         410       420
                  ....*....|....*....|.
gi 594591591  442 LELDHLTVSGDVTFGKNVSLK 462
Cdd:pfam01704 392 LELDHLTVSGDVTFGRNVTLK 412
UGPase_euk cd00897
Eukaryotic UGPase catalyses the synthesis of UDP-Glucose; UGPase (UDP-Glucose ...
94-400 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: 615.41  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591591  94 LNKLVVVKLNGGLGTSMGCKGPKSLIGVRNENTFLDLTVQQIEHLNKTYNTDVPLVLMNSFNTDEDTKKILQKYNHCRVK 173
Cdd:cd00897    1 LNKLVVLKLNGGLGTSMGCTGPKSLIEVRDGKTFLDLTVQQIEHLNKTYGVDVPLVLMNSFNTDEDTKKILKKYAGVNVD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591591 174 IYTFNQSRYPRINKESLLPIAkdvSYSGENTEAWYPPGHGDIYASFYNSGLLDTFIEEGKEYIFVSNIDNLGATVDLYIL 253
Cdd:cd00897   81 IHTFNQSRYPRISKETLLPVP---SWADSPDEEWYPPGHGDIFESLYNSGLLDTLLAQGKEYLFVSNIDNLGATVDLRIL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591591 254 NHLMNPPngkrCEFVMEVTNKTRADVKGGTLTQYEGKLRLVEIAQVPKAHVDEFKSVSKFKIFNTNNLWISLGAVKRLQE 333
Cdd:cd00897  158 NHMVDNK----AEYIMEVTDKTRADVKGGTLIQYEGKLRLLEIAQVPKEHVDEFKSIKKFKIFNTNNLWVNLKAVKRVVE 233
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 594591591 334 QNAIDMEIIVNPKTLDGGLNVIQLETAVGAAIKSFENSLGINVPRSRFLPVKTTSDLLLVMSNLYSL 400
Cdd:cd00897  234 ENALDLEIIVNPKTVDGGLNVIQLETAVGAAIKNFDNALGVNVPRSRFLPVKTTSDLLLVRSDLYSL 300
PLN02474 PLN02474
UTP--glucose-1-phosphate uridylyltransferase
46-490 0e+00

UTP--glucose-1-phosphate uridylyltransferase


Pssm-ID: 178092  Cd Length: 469  Bit Score: 548.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591591  46 GFRKLFHRFLQEKGPSVDWGKIQRPPEDSIQPYEKIKARGL-PDNISSVLNKLVVVKLNGGLGTSMGCKGPKSLIGVRNE 124
Cdd:PLN02474  28 GFISLVSRYLSGEAQHIEWSKIQTPTDEVVVPYDKLAPVPEdPEETKKLLDKLVVLKLNGGLGTTMGCTGPKSVIEVRNG 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591591 125 NTFLDLTVQQIEHLNKTYNTDVPLVLMNSFNTDEDTKKILQKYNHCRVKIYTFNQSRYPRINKESLLPIAkdvSYSGENT 204
Cdd:PLN02474 108 LTFLDLIVIQIENLNKKYGCNVPLLLMNSFNTHDDTQKIVEKYTNSNIEIHTFNQSQYPRVVADDFVPWP---SKGKTDK 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591591 205 EAWYPPGHGDIYASFYNSGLLDTFIEEGKEYIFVSNIDNLGATVDLYILNHLMNPPNgkrcEFVMEVTNKTRADVKGGTL 284
Cdd:PLN02474 185 DGWYPPGHGDVFPSLMNSGKLDALLSQGKEYVFIANSDNLGAIVDLKILNHLIQNKN----EYCMEVTPKTLADVKGGTL 260
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591591 285 TQYEGKLRLVEIAQVPKAHVDEFKSVSKFKIFNTNNLWISLGAVKRLQEQNAIDMEIIVNPKTLDGgLNVIQLETAVGAA 364
Cdd:PLN02474 261 ISYEGKVQLLEIAQVPDEHVNEFKSIEKFKIFNTNNLWVNLKAIKRLVEADALKMEIIPNPKEVDG-VKVLQLETAAGAA 339
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591591 365 IKSFENSLGINVPRSRFLPVKTTSDLLLVMSNLYSLNAGSLTMSEKREFPTVPLVKLGSSFTKVQDYLRRFESIPDMLEL 444
Cdd:PLN02474 340 IRFFDNAIGINVPRSRFLPVKATSDLLLVQSDLYTLVDGFVIRNKARTNPSNPSIELGPEFKKVANFLSRFKSIPSIVEL 419
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 594591591 445 DHLTVSGDVTFGKNVSLKGTVIIIANHGDRIDIPPGAVLENKIVSG 490
Cdd:PLN02474 420 DSLKVSGDVWFGSGIVLKGKVTITAKSGVKLEIPDGAVLENKDING 465
QRI1 COG4284
UDP-N-acetylglucosamine pyrophosphorylase [Carbohydrate transport and metabolism];
43-389 1.44e-89

UDP-N-acetylglucosamine pyrophosphorylase [Carbohydrate transport and metabolism];


Pssm-ID: 443425  Cd Length: 402  Bit Score: 279.46  E-value: 1.44e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591591  43 DLDGFRKLFHRFLQEKGPSVdwgkiqRPPEDSIQPyekIKARGLPDNISSVLN---------------KLVVVKLNGGLG 107
Cdd:COG4284   36 DIDVFQHLYRQLVLAEGATG------LIPESDIEP---APVTDLPLTDLDEVDrdraeeageealragKVAVILLAGGQG 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591591 108 TSMGCKGPKSL--IGVRNENTFLDLTVQQIEHLNKTYNTDVPLVLMNSFNTDEDTKKILQKYNHCRV---KIYTFNQSRY 182
Cdd:COG4284  107 TRLGFDGPKGLlpVRPVKGKSLFDLIAEQVLAARRRYGVPLPLYIMTSFRTHEDTLAFLEEHDYFGLdglPVHFFLQGME 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591591 183 PRINKE--SLLPIAKDvsysgenTEAWYPPGHGDIYASFYNSGLLDTFIEEGKEYIFVSNIDN-LGATVDLYIL-NHLMn 258
Cdd:COG4284  187 PALDADlgPVLLPADP-------ELELCPPGHGGIYTALLASGLLDKLLERGIRYLFVSNVDNpLGAVPDPAFAgWHAA- 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591591 259 ppngKRCEFVMEVTNKTRADVKGGTLTQYEGKLRLVEIAQVPKAHVDEFKSVSKFKIFNTNNLWISLGAVKRLQEQNAID 338
Cdd:COG4284  259 ----SGAPFTAKVVRRTPPDEKVGHLARVDGRLILREYSQLPDEEAEAFTGELRHPYGNINNHWFDLDFLKRLLDERGLG 334
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591591 339 MEIIVNPKTLD----GGL----NVIQLETAVGAAIKSFENSLGINVPR-SRFLPVKTTSD 389
Cdd:COG4284  335 LPLHRAEKKVDpldeSGKptspNVIKFETFMFDAIPLFDGAVAIEVDReERFAPVKNTNG 394
UGPase_euk_like cd04180
Eukaryotic UGPase-like includes UDPase and UDPGlcNAc pyrophosphorylase enzymes; This family ...
97-385 4.56e-63

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: 206.25  E-value: 4.56e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591591  97 LVVVKLNGGLGTSMGCKGPKSLIGVRNEN--TFLDLTVQQIEHLNKTYNT--DVPLVLMNSFNTDEDTKKILQKYNHCRV 172
Cdd:cd04180    1 VAVVLLAGGLGTRLGKDGPKSSTDVGLPSgqCFLQLIGEKILTLQEIDLYscKIPEQLMNSKYTHEKTQCYFEKINQKNS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591591 173 KIYTFNQSRYPRINKESLlpiakdVSYSGENTEAWYPPGHGDIYASFYNSGLLDTFIEEGKEYIFVSNIDNLGATV-DLY 251
Cdd:cd04180   81 YVITFMQGKLPLKNDDDA------RDPHNKTKCHLFPCGHGDVVLALIHSGHLNKLLEKGYRYIHFIGVDNLLVKVaDPL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591591 252 ILNHLMNppngKRCEFVMEVTNKTRADVKGGTLTQYE-GKLRLVEIAQVPKAHVDE--------FKSVSKFKIFNTNNLW 322
Cdd:cd04180  155 FIGIAIQ----NRKAINQKVVPKTRNEESGGYRIANInGRVQLLEYDQIKKLLKQKmvnnqipkDIDDAPFFLFNTNNLI 230
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 594591591 323 ISLGAVKRLqeqnaidmeiivnpktldgglnviqletaVGAAIKSFENSLGINVPRS-RFLPVK 385
Cdd:cd04180  231 NFLVEFKDR-----------------------------VDDIIEFTDDIVGVMVHRAeEFAPVK 265
UGGPase cd06424
UGGPase catalyzes the synthesis of UDP-Glucose/UDP-Galactose; UGGPase: UDP-Galactose/Glucose ...
98-349 1.82e-16

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: 80.19  E-value: 1.82e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591591  98 VVVKLNGGLGTSMGCKGPKSLIGVR--NENTFLDLTVQQI----EHLNKTYNTDVPLVLMNSFNTDEDTKKILQKYNHCR 171
Cdd:cd06424    2 VFVLVAGGLGERLGYSGIKIGLPVEltTNTTYLQYYLNYIrafqEASKKGEKMEIPFVIMTSDDTHSKTLKLLEENNYFG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591591 172 VK---IYTFNQSRYP-RINKESLLPIAKDVSYSGENTeawyPPGHGDIYASFYNSGLLDTFIEEGKEYIFVSNIDNLGAT 247
Cdd:cd06424   82 LEkdqVHILKQEKVFcLIDNDAHLALDPDNTYSILTK----PHGHGDVHTLLYNSGLLKKWIEAGYKWLVFFQDTNALAF 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591591 248 VDL-----------YILNHLMNPPngKRCEFVMEVTNKTRADVKGGTL-TQYEGKLRLVEIAQVPKAHVDEFKSVSKFKi 315
Cdd:cd06424  158 KAIpavlgvsatksLDMNSLTVPR--KPKEAIGALCKLTKNNGKSMTInVEYNQLDPLLRASGKDDGDVDDKTGFSPFP- 234
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 594591591 316 FNTNNLWISLGA-VKRLQEQNAIDMEIIvNPKTLD 349
Cdd:cd06424  235 GNINQLVFSLGPyMDELEKTKGAIPEFI-NPKYKD 268
UDPGlcNAc_PPase cd04193
UDPGlcNAc pyrophosphorylase catalayzes the synthesis of UDPGlcNAc; UDP-N-acetylglucosamine ...
79-243 1.07e-14

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: 74.95  E-value: 1.07e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591591  79 EKIKARGLpDNISSvlNKLVVVKLNGGLGTSMGCKGPKSL--IGVRNENTFLDLTVQQIEHLNK------TYNTDVPLVL 150
Cdd:cd04193    1 KEWEEAGL-KAIAE--GKVAVLLLAGGQGTRLGFDGPKGMfpVGLPSKKSLFQLQAERILKLQElageasGKKVPIPWYI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591591 151 MNSFNTDEDTKKILQKYNHCRVK---IYTFNQSryprinkesLLPIakdVSYSGE------NTEAWYPPGHGDIYASFYN 221
Cdd:cd04193   78 MTSEATHEETRKFFKENNYFGLDpeqVHFFQQG---------MLPC---VDFDGKilleekGKIAMAPNGNGGLYKALQT 145
                        170       180
                 ....*....|....*....|..
gi 594591591 222 SGLLDTFIEEGKEYIFVSNIDN 243
Cdd:cd04193  146 AGILEDMKKRGIKYIHVYSVDN 167
PLN02830 PLN02830
UDP-sugar pyrophosphorylase
77-349 4.79e-12

UDP-sugar pyrophosphorylase


Pssm-ID: 215444  Cd Length: 615  Bit Score: 68.17  E-value: 4.79e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591591  77 PYEKIKARGLPDnissvLNKLVVVKLNGGLGTSMGCKGPKslIGVRNENT----FLDLTVQQIEHLNKTYN-------TD 145
Cdd:PLN02830 114 EFVELEEAGLRE-----AGNAAFVLVAGGLGERLGYSGIK--VALPTETAtgtcYLQLYIESILALQERAKkrkakkgRK 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591591 146 VPLVLMNSFNTDEDTKKILQKYNH---CRVKIYTFNQSRYP-RINKESLLPIAKDVSYSGENTeawyPPGHGDIYASFYN 221
Cdd:PLN02830 187 IPLVIMTSDDTHARTLKLLERNDYfgmDPDQVTLLKQEKVAcLMDNDARLALDPNDPYKIQTK----PHGHGDVHALLYS 262
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591591 222 SGLLDTFIEEGKEYI----------FVSNIDNLGATVDL-YILNHLMNPPNGKrcEFVMEVTNKTRADvkGGTLTQyegk 290
Cdd:PLN02830 263 SGLLDKWLSAGKKWVvffqdtnglvFKAIPAALGVSATKgFDMNSLAVPRKAK--EAIGAIAKLTHKD--GREMVI---- 334
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 594591591 291 lrLVEIAQV---------PKAHVDEFKSVSKFKiFNTNNLWISLGA-VKRLQEQNAIdMEIIVNPKTLD 349
Cdd:PLN02830 335 --NVEYNQLdpllratghPDGDVNDETGYSPFP-GNINQLILKLGPyVKELAKTGGV-IEEFVNPKYKD 399
PTZ00339 PTZ00339
UDP-N-acetylglucosamine pyrophosphorylase; Provisional
99-317 3.53e-10

UDP-N-acetylglucosamine pyrophosphorylase; Provisional


Pssm-ID: 240368  Cd Length: 482  Bit Score: 62.07  E-value: 3.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591591  99 VVKLNGGLGTSMGCKGPKSL--IGVRNENTFLDLTVQQI---EHLNKTYN-----TDVPLVLMNSFNTDEDTKKILQKYN 168
Cdd:PTZ00339 109 VLILAGGLGTRLGSDKPKGLleCTPVKKKTLFQFHCEKVrrlEEMAVAVSgggddPTIYILVLTSSFNHDQTRQFLEENN 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591591 169 HCRVK---IYTFNQSRYPRINKESllpiaKDVSYSGENTEAWYPPGHGDIYASFYNSGLLDTFIEEGKEYIFVSNIDNLG 245
Cdd:PTZ00339 189 FFGLDkeqVIFFKQSSLPCYDENT-----GRFIMSSQGSLCTAPGGNGDVFKALAKCSELMDIVRKGIKYVQVISIDNIL 263
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 594591591 246 ATV-DLYILNHLMNPPngkrCEFVMEVTNKTRADVKGGTLTQYEGKLRLV---EIAQVPKAHVDEFKSVSKFKIFN 317
Cdd:PTZ00339 264 AKVlDPEFIGLASSFP----AHDVLNKCVKREDDESVGVFCLKDYEWQVVeytEINERILNNDELLTGELAFNYGN 335
PLN02435 PLN02435
probable UDP-N-acetylglucosamine pyrophosphorylase
68-243 4.74e-05

probable UDP-N-acetylglucosamine pyrophosphorylase


Pssm-ID: 215238  Cd Length: 493  Bit Score: 46.02  E-value: 4.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591591  68 QRPPEDSiqpyEKIKARGLpDNISSvlNKLVVVKLNGGLGTSMGCKGPKSL--IGVRNENTFLDLTVQQI--------EH 137
Cdd:PLN02435  95 ERTPEDR----ERWWKMGL-KAISE--GKLAVVLLSGGQGTRLGSSDPKGCfnIGLPSGKSLFQLQAERIlcvqrlaaQA 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591591 138 LNKTYNTDVPL--VLMNSFNTDEDTKKILQKYNHCRV---KIYTFNQSRYPRINK------ESLLPIAKDvsysgentea 206
Cdd:PLN02435 168 SSEGPGRPVTIhwYIMTSPFTDEATRKFFESHKYFGLeadQVTFFQQGTLPCVSKdgkfimETPFKVAKA---------- 237
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 594591591 207 wyPPGHGDIYASFYNSGLLDTFIEEGKEYIFVSNIDN 243
Cdd:PLN02435 238 --PDGNGGVYAALKSSRLLEDMASRGIKYVDCYGVDN 272
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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