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Conserved domains on  [gi|1798182223|ref|NP_001364458|]
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UTP--glucose-1-phosphate uridylyltransferase isoform c [Homo sapiens]

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 ...
1-353 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: 680.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798182223   1 MGCKGPKSLIGVRNENTFLDLTVQQIEHLNKTYNTDVPLVLMNSFNTDEDTKKILQKYNHCRVKIYTFNQSRYPRINKES 80
Cdd:pfam01704  67 MGCVGPKSLIEVRDGLTFLDLIVQQIEHLNKKYNVDVPLVLMNSFNTDEDTKKIIRKYKGHKVDILTFNQSRYPRIDKDT 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798182223  81 LLPVAKDvsySGENTEAWYPPGHGDIYASFYNSGLLDTFIGEGKEYIFVSNIDNLGATVDLYILNHLMNppngKRCEFVM 160
Cdd:pfam01704 147 LLPVPKS---ADSDEEEWYPPGHGDLYESLYNSGLLDKLLAEGKEYLFVSNIDNLGATVDLNILNYMVD----NGAEFLM 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798182223 161 EVTNKTRADVKGGTLTQYEGKLRLVEIAQVPKAHVDEFKSVSKFKIFNTNNLWISLAAVKRLQEQNAIDMEIIVNAKTLD 240
Cdd:pfam01704 220 EVTDKTRADVKGGTLIEYDGKLRLLEIAQVPKEHVDEFKSIKKFKIFNTNNIWINLKALKRVVEEGELQLEIIVNKKTLD 299
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798182223 241 GGLNVIQLETAVGAAIKSFENSLGINVPRSRFLPVKTTSDLLLVMSNLYSLNAGSLTMSEKREFPTVPLVKLGSSFTKVQ 320
Cdd:pfam01704 300 NGENVIQLETAVGAAIKNFKNAIGINVPRSRFLPVKTTSDLLLVMSDLYVLNHGSLIMNPKRMFGTPPVVLLGDHFKKVD 379
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1798182223 321 DYLRRFESIPDMLELDHLTVSGDVTFGKNVSLK 353
Cdd:pfam01704 380 EFLKRFPSIPDLLELDHLTVSGDVTFGRNVTLK 412
 
Name Accession Description Interval E-value
UDPGP pfam01704
UTP--glucose-1-phosphate uridylyltransferase; This family consists of UTP--glucose-1-phosphate ...
1-353 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: 680.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798182223   1 MGCKGPKSLIGVRNENTFLDLTVQQIEHLNKTYNTDVPLVLMNSFNTDEDTKKILQKYNHCRVKIYTFNQSRYPRINKES 80
Cdd:pfam01704  67 MGCVGPKSLIEVRDGLTFLDLIVQQIEHLNKKYNVDVPLVLMNSFNTDEDTKKIIRKYKGHKVDILTFNQSRYPRIDKDT 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798182223  81 LLPVAKDvsySGENTEAWYPPGHGDIYASFYNSGLLDTFIGEGKEYIFVSNIDNLGATVDLYILNHLMNppngKRCEFVM 160
Cdd:pfam01704 147 LLPVPKS---ADSDEEEWYPPGHGDLYESLYNSGLLDKLLAEGKEYLFVSNIDNLGATVDLNILNYMVD----NGAEFLM 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798182223 161 EVTNKTRADVKGGTLTQYEGKLRLVEIAQVPKAHVDEFKSVSKFKIFNTNNLWISLAAVKRLQEQNAIDMEIIVNAKTLD 240
Cdd:pfam01704 220 EVTDKTRADVKGGTLIEYDGKLRLLEIAQVPKEHVDEFKSIKKFKIFNTNNIWINLKALKRVVEEGELQLEIIVNKKTLD 299
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798182223 241 GGLNVIQLETAVGAAIKSFENSLGINVPRSRFLPVKTTSDLLLVMSNLYSLNAGSLTMSEKREFPTVPLVKLGSSFTKVQ 320
Cdd:pfam01704 300 NGENVIQLETAVGAAIKNFKNAIGINVPRSRFLPVKTTSDLLLVMSDLYVLNHGSLIMNPKRMFGTPPVVLLGDHFKKVD 379
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1798182223 321 DYLRRFESIPDMLELDHLTVSGDVTFGKNVSLK 353
Cdd:pfam01704 380 EFLKRFPSIPDLLELDHLTVSGDVTFGRNVTLK 412
UGPase_euk cd00897
Eukaryotic UGPase catalyses the synthesis of UDP-Glucose; UGPase (UDP-Glucose ...
1-291 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: 574.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798182223   1 MGCKGPKSLIGVRNENTFLDLTVQQIEHLNKTYNTDVPLVLMNSFNTDEDTKKILQKYNHCRVKIYTFNQSRYPRINKES 80
Cdd:cd00897    17 MGCTGPKSLIEVRDGKTFLDLTVQQIEHLNKTYGVDVPLVLMNSFNTDEDTKKILKKYAGVNVDIHTFNQSRYPRISKET 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798182223  81 LLPVAkdvSYSGENTEAWYPPGHGDIYASFYNSGLLDTFIGEGKEYIFVSNIDNLGATVDLYILNHLMNPPngkrCEFVM 160
Cdd:cd00897    97 LLPVP---SWADSPDEEWYPPGHGDIFESLYNSGLLDTLLAQGKEYLFVSNIDNLGATVDLRILNHMVDNK----AEYIM 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798182223 161 EVTNKTRADVKGGTLTQYEGKLRLVEIAQVPKAHVDEFKSVSKFKIFNTNNLWISLAAVKRLQEQNAIDMEIIVNAKTLD 240
Cdd:cd00897   170 EVTDKTRADVKGGTLIQYEGKLRLLEIAQVPKEHVDEFKSIKKFKIFNTNNLWVNLKAVKRVVEENALDLEIIVNPKTVD 249
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1798182223 241 GGLNVIQLETAVGAAIKSFENSLGINVPRSRFLPVKTTSDLLLVMSNLYSL 291
Cdd:cd00897   250 GGLNVIQLETAVGAAIKNFDNALGVNVPRSRFLPVKTTSDLLLVRSDLYSL 300
PLN02474 PLN02474
UTP--glucose-1-phosphate uridylyltransferase
1-381 2.82e-173

UTP--glucose-1-phosphate uridylyltransferase


Pssm-ID: 178092  Cd Length: 469  Bit Score: 491.70  E-value: 2.82e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798182223   1 MGCKGPKSLIGVRNENTFLDLTVQQIEHLNKTYNTDVPLVLMNSFNTDEDTKKILQKYNHCRVKIYTFNQSRYPRINKES 80
Cdd:PLN02474   93 MGCTGPKSVIEVRNGLTFLDLIVIQIENLNKKYGCNVPLLLMNSFNTHDDTQKIVEKYTNSNIEIHTFNQSQYPRVVADD 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798182223  81 LLPVAkdvSYSGENTEAWYPPGHGDIYASFYNSGLLDTFIGEGKEYIFVSNIDNLGATVDLYILNHLMNPPNgkrcEFVM 160
Cdd:PLN02474  173 FVPWP---SKGKTDKDGWYPPGHGDVFPSLMNSGKLDALLSQGKEYVFIANSDNLGAIVDLKILNHLIQNKN----EYCM 245
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798182223 161 EVTNKTRADVKGGTLTQYEGKLRLVEIAQVPKAHVDEFKSVSKFKIFNTNNLWISLAAVKRLQEQNAIDMEIIVNAKTLD 240
Cdd:PLN02474  246 EVTPKTLADVKGGTLISYEGKVQLLEIAQVPDEHVNEFKSIEKFKIFNTNNLWVNLKAIKRLVEADALKMEIIPNPKEVD 325
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798182223 241 GgLNVIQLETAVGAAIKSFENSLGINVPRSRFLPVKTTSDLLLVMSNLYSLNAGSLTMSEKREFPTVPLVKLGSSFTKVQ 320
Cdd:PLN02474  326 G-VKVLQLETAAGAAIRFFDNAIGINVPRSRFLPVKATSDLLLVQSDLYTLVDGFVIRNKARTNPSNPSIELGPEFKKVA 404
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1798182223 321 DYLRRFESIPDMLELDHLTVSGDVTFGKNVSLKGTVIIIANHGDRIDIPPGAVLENKIVSG 381
Cdd:PLN02474  405 NFLSRFKSIPSIVELDSLKVSGDVWFGSGIVLKGKVTITAKSGVKLEIPDGAVLENKDING 465
QRI1 COG4284
UDP-N-acetylglucosamine pyrophosphorylase [Carbohydrate transport and metabolism];
1-280 1.15e-78

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


Pssm-ID: 443425  Cd Length: 402  Bit Score: 247.49  E-value: 1.15e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798182223   1 MGCKGPKSL--IGVRNENTFLDLTVQQIEHLNKTYNTDVPLVLMNSFNTDEDTKKILQKYNHCRV---KIYTFNQSRYPR 75
Cdd:COG4284   109 LGFDGPKGLlpVRPVKGKSLFDLIAEQVLAARRRYGVPLPLYIMTSFRTHEDTLAFLEEHDYFGLdglPVHFFLQGMEPA 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798182223  76 INKE--SLLPVAKDvsysgenTEAWYPPGHGDIYASFYNSGLLDTFIGEGKEYIFVSNIDN-LGATVDLYIL-NHLMnpp 151
Cdd:COG4284   189 LDADlgPVLLPADP-------ELELCPPGHGGIYTALLASGLLDKLLERGIRYLFVSNVDNpLGAVPDPAFAgWHAA--- 258
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798182223 152 ngKRCEFVMEVTNKTRADVKGGTLTQYEGKLRLVEIAQVPKAHVDEFKSVSKFKIFNTNNLWISLAAVKRLQEQNAIDME 231
Cdd:COG4284   259 --SGAPFTAKVVRRTPPDEKVGHLARVDGRLILREYSQLPDEEAEAFTGELRHPYGNINNHWFDLDFLKRLLDERGLGLP 336
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1798182223 232 IIVNAKTLD----GGL----NVIQLETAVGAAIKSFENSLGINVPR-SRFLPVKTTSD 280
Cdd:COG4284   337 LHRAEKKVDpldeSGKptspNVIKFETFMFDAIPLFDGAVAIEVDReERFAPVKNTNG 394
 
Name Accession Description Interval E-value
UDPGP pfam01704
UTP--glucose-1-phosphate uridylyltransferase; This family consists of UTP--glucose-1-phosphate ...
1-353 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: 680.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798182223   1 MGCKGPKSLIGVRNENTFLDLTVQQIEHLNKTYNTDVPLVLMNSFNTDEDTKKILQKYNHCRVKIYTFNQSRYPRINKES 80
Cdd:pfam01704  67 MGCVGPKSLIEVRDGLTFLDLIVQQIEHLNKKYNVDVPLVLMNSFNTDEDTKKIIRKYKGHKVDILTFNQSRYPRIDKDT 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798182223  81 LLPVAKDvsySGENTEAWYPPGHGDIYASFYNSGLLDTFIGEGKEYIFVSNIDNLGATVDLYILNHLMNppngKRCEFVM 160
Cdd:pfam01704 147 LLPVPKS---ADSDEEEWYPPGHGDLYESLYNSGLLDKLLAEGKEYLFVSNIDNLGATVDLNILNYMVD----NGAEFLM 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798182223 161 EVTNKTRADVKGGTLTQYEGKLRLVEIAQVPKAHVDEFKSVSKFKIFNTNNLWISLAAVKRLQEQNAIDMEIIVNAKTLD 240
Cdd:pfam01704 220 EVTDKTRADVKGGTLIEYDGKLRLLEIAQVPKEHVDEFKSIKKFKIFNTNNIWINLKALKRVVEEGELQLEIIVNKKTLD 299
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798182223 241 GGLNVIQLETAVGAAIKSFENSLGINVPRSRFLPVKTTSDLLLVMSNLYSLNAGSLTMSEKREFPTVPLVKLGSSFTKVQ 320
Cdd:pfam01704 300 NGENVIQLETAVGAAIKNFKNAIGINVPRSRFLPVKTTSDLLLVMSDLYVLNHGSLIMNPKRMFGTPPVVLLGDHFKKVD 379
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1798182223 321 DYLRRFESIPDMLELDHLTVSGDVTFGKNVSLK 353
Cdd:pfam01704 380 EFLKRFPSIPDLLELDHLTVSGDVTFGRNVTLK 412
UGPase_euk cd00897
Eukaryotic UGPase catalyses the synthesis of UDP-Glucose; UGPase (UDP-Glucose ...
1-291 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: 574.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798182223   1 MGCKGPKSLIGVRNENTFLDLTVQQIEHLNKTYNTDVPLVLMNSFNTDEDTKKILQKYNHCRVKIYTFNQSRYPRINKES 80
Cdd:cd00897    17 MGCTGPKSLIEVRDGKTFLDLTVQQIEHLNKTYGVDVPLVLMNSFNTDEDTKKILKKYAGVNVDIHTFNQSRYPRISKET 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798182223  81 LLPVAkdvSYSGENTEAWYPPGHGDIYASFYNSGLLDTFIGEGKEYIFVSNIDNLGATVDLYILNHLMNPPngkrCEFVM 160
Cdd:cd00897    97 LLPVP---SWADSPDEEWYPPGHGDIFESLYNSGLLDTLLAQGKEYLFVSNIDNLGATVDLRILNHMVDNK----AEYIM 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798182223 161 EVTNKTRADVKGGTLTQYEGKLRLVEIAQVPKAHVDEFKSVSKFKIFNTNNLWISLAAVKRLQEQNAIDMEIIVNAKTLD 240
Cdd:cd00897   170 EVTDKTRADVKGGTLIQYEGKLRLLEIAQVPKEHVDEFKSIKKFKIFNTNNLWVNLKAVKRVVEENALDLEIIVNPKTVD 249
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1798182223 241 GGLNVIQLETAVGAAIKSFENSLGINVPRSRFLPVKTTSDLLLVMSNLYSL 291
Cdd:cd00897   250 GGLNVIQLETAVGAAIKNFDNALGVNVPRSRFLPVKTTSDLLLVRSDLYSL 300
PLN02474 PLN02474
UTP--glucose-1-phosphate uridylyltransferase
1-381 2.82e-173

UTP--glucose-1-phosphate uridylyltransferase


Pssm-ID: 178092  Cd Length: 469  Bit Score: 491.70  E-value: 2.82e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798182223   1 MGCKGPKSLIGVRNENTFLDLTVQQIEHLNKTYNTDVPLVLMNSFNTDEDTKKILQKYNHCRVKIYTFNQSRYPRINKES 80
Cdd:PLN02474   93 MGCTGPKSVIEVRNGLTFLDLIVIQIENLNKKYGCNVPLLLMNSFNTHDDTQKIVEKYTNSNIEIHTFNQSQYPRVVADD 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798182223  81 LLPVAkdvSYSGENTEAWYPPGHGDIYASFYNSGLLDTFIGEGKEYIFVSNIDNLGATVDLYILNHLMNPPNgkrcEFVM 160
Cdd:PLN02474  173 FVPWP---SKGKTDKDGWYPPGHGDVFPSLMNSGKLDALLSQGKEYVFIANSDNLGAIVDLKILNHLIQNKN----EYCM 245
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798182223 161 EVTNKTRADVKGGTLTQYEGKLRLVEIAQVPKAHVDEFKSVSKFKIFNTNNLWISLAAVKRLQEQNAIDMEIIVNAKTLD 240
Cdd:PLN02474  246 EVTPKTLADVKGGTLISYEGKVQLLEIAQVPDEHVNEFKSIEKFKIFNTNNLWVNLKAIKRLVEADALKMEIIPNPKEVD 325
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798182223 241 GgLNVIQLETAVGAAIKSFENSLGINVPRSRFLPVKTTSDLLLVMSNLYSLNAGSLTMSEKREFPTVPLVKLGSSFTKVQ 320
Cdd:PLN02474  326 G-VKVLQLETAAGAAIRFFDNAIGINVPRSRFLPVKATSDLLLVQSDLYTLVDGFVIRNKARTNPSNPSIELGPEFKKVA 404
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1798182223 321 DYLRRFESIPDMLELDHLTVSGDVTFGKNVSLKGTVIIIANHGDRIDIPPGAVLENKIVSG 381
Cdd:PLN02474  405 NFLSRFKSIPSIVELDSLKVSGDVWFGSGIVLKGKVTITAKSGVKLEIPDGAVLENKDING 465
QRI1 COG4284
UDP-N-acetylglucosamine pyrophosphorylase [Carbohydrate transport and metabolism];
1-280 1.15e-78

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


Pssm-ID: 443425  Cd Length: 402  Bit Score: 247.49  E-value: 1.15e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798182223   1 MGCKGPKSL--IGVRNENTFLDLTVQQIEHLNKTYNTDVPLVLMNSFNTDEDTKKILQKYNHCRV---KIYTFNQSRYPR 75
Cdd:COG4284   109 LGFDGPKGLlpVRPVKGKSLFDLIAEQVLAARRRYGVPLPLYIMTSFRTHEDTLAFLEEHDYFGLdglPVHFFLQGMEPA 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798182223  76 INKE--SLLPVAKDvsysgenTEAWYPPGHGDIYASFYNSGLLDTFIGEGKEYIFVSNIDN-LGATVDLYIL-NHLMnpp 151
Cdd:COG4284   189 LDADlgPVLLPADP-------ELELCPPGHGGIYTALLASGLLDKLLERGIRYLFVSNVDNpLGAVPDPAFAgWHAA--- 258
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798182223 152 ngKRCEFVMEVTNKTRADVKGGTLTQYEGKLRLVEIAQVPKAHVDEFKSVSKFKIFNTNNLWISLAAVKRLQEQNAIDME 231
Cdd:COG4284   259 --SGAPFTAKVVRRTPPDEKVGHLARVDGRLILREYSQLPDEEAEAFTGELRHPYGNINNHWFDLDFLKRLLDERGLGLP 336
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1798182223 232 IIVNAKTLD----GGL----NVIQLETAVGAAIKSFENSLGINVPR-SRFLPVKTTSD 280
Cdd:COG4284   337 LHRAEKKVDpldeSGKptspNVIKFETFMFDAIPLFDGAVAIEVDReERFAPVKNTNG 394
UGPase_euk_like cd04180
Eukaryotic UGPase-like includes UDPase and UDPGlcNAc pyrophosphorylase enzymes; This family ...
1-276 1.34e-55

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: 183.91  E-value: 1.34e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798182223   1 MGCKGPKSLIGVRNEN--TFLDLTVQQIEHLNKTYNT--DVPLVLMNSFNTDEDTKKILQKYNHCRVKIYTFNQSRYPRI 76
Cdd:cd04180    14 LGKDGPKSSTDVGLPSgqCFLQLIGEKILTLQEIDLYscKIPEQLMNSKYTHEKTQCYFEKINQKNSYVITFMQGKLPLK 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798182223  77 NKESLlpvakdVSYSGENTEAWYPPGHGDIYASFYNSGLLDTFIGEGKEYIFVSNIDNLGATV-DLYILNHLMNppngKR 155
Cdd:cd04180    94 NDDDA------RDPHNKTKCHLFPCGHGDVVLALIHSGHLNKLLEKGYRYIHFIGVDNLLVKVaDPLFIGIAIQ----NR 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798182223 156 CEFVMEVTNKTRADVKGGTLTQYE-GKLRLVEIAQVPKAHVDE--------FKSVSKFKIFNTNNLWISLAAVKRLqeqn 226
Cdd:cd04180   164 KAINQKVVPKTRNEESGGYRIANInGRVQLLEYDQIKKLLKQKmvnnqipkDIDDAPFFLFNTNNLINFLVEFKDR---- 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1798182223 227 aidmeiivnaktldgglnviqletaVGAAIKSFENSLGINVPRS-RFLPVK 276
Cdd:cd04180   240 -------------------------VDDIIEFTDDIVGVMVHRAeEFAPVK 265
UGGPase cd06424
UGGPase catalyzes the synthesis of UDP-Glucose/UDP-Galactose; UGGPase: UDP-Galactose/Glucose ...
15-240 8.60e-12

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: 65.56  E-value: 8.60e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798182223  15 ENTFLDLTVQQI----EHLNKTYNTDVPLVLMNSFNTDEDTKKILQKYNHCRVK---IYTFNQSRYP-RINKESLLPVAK 86
Cdd:cd06424    30 NTTYLQYYLNYIrafqEASKKGEKMEIPFVIMTSDDTHSKTLKLLEENNYFGLEkdqVHILKQEKVFcLIDNDAHLALDP 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798182223  87 DVSYSGENTeawyPPGHGDIYASFYNSGLLDTFIGEGKEYIFVSNIDNLGATVDL-----------YILNHLMNPPngKR 155
Cdd:cd06424   110 DNTYSILTK----PHGHGDVHTLLYNSGLLKKWIEAGYKWLVFFQDTNALAFKAIpavlgvsatksLDMNSLTVPR--KP 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798182223 156 CEFVMEVTNKTRADVKGGTL-TQYEGKLRLVEIAQVPKAHVDEFKSVSKFKiFNTNNLWISLAA-VKRLQEQNAIDMEII 233
Cdd:cd06424   184 KEAIGALCKLTKNNGKSMTInVEYNQLDPLLRASGKDDGDVDDKTGFSPFP-GNINQLVFSLGPyMDELEKTKGAIPEFI 262

                  ....*..
gi 1798182223 234 vNAKTLD 240
Cdd:cd06424   263 -NPKYKD 268
UDPGlcNAc_PPase cd04193
UDPGlcNAc pyrophosphorylase catalayzes the synthesis of UDPGlcNAc; UDP-N-acetylglucosamine ...
1-134 2.05e-09

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: 58.39  E-value: 2.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798182223   1 MGCKGPKSL--IGVRNENTFLDLTVQQIEHLNK------TYNTDVPLVLMNSFNTDEDTKKILQKYNHCRVK---IYTFN 69
Cdd:cd04193    29 LGFDGPKGMfpVGLPSKKSLFQLQAERILKLQElageasGKKVPIPWYIMTSEATHEETRKFFKENNYFGLDpeqVHFFQ 108
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1798182223  70 QSryprinkesLLPVakdVSYSGE------NTEAWYPPGHGDIYASFYNSGLLDTFIGEGKEYIFVSNIDN 134
Cdd:cd04193   109 QG---------MLPC---VDFDGKilleekGKIAMAPNGNGGLYKALQTAGILEDMKKRGIKYIHVYSVDN 167
PLN02830 PLN02830
UDP-sugar pyrophosphorylase
18-240 1.39e-07

UDP-sugar pyrophosphorylase


Pssm-ID: 215444  Cd Length: 615  Bit Score: 53.54  E-value: 1.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798182223  18 FLDLTVQQIEHLNKTYN-------TDVPLVLMNSFNTDEDTKKILQKYNH---CRVKIYTFNQSRYP-RINKESLLPVAK 86
Cdd:PLN02830  161 YLQLYIESILALQERAKkrkakkgRKIPLVIMTSDDTHARTLKLLERNDYfgmDPDQVTLLKQEKVAcLMDNDARLALDP 240
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798182223  87 DVSYSGENTeawyPPGHGDIYASFYNSGLLDTFIGEGKEYI----------FVSNIDNLGATVDL-YILNHLMNPPNGKr 155
Cdd:PLN02830  241 NDPYKIQTK----PHGHGDVHALLYSSGLLDKWLSAGKKWVvffqdtnglvFKAIPAALGVSATKgFDMNSLAVPRKAK- 315
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798182223 156 cEFVMEVTNKTRADvkGGTLTQyegklrLVEIAQV---------PKAHVDEFKSVSKFKiFNTNNLWISLAA-VKRLQEQ 225
Cdd:PLN02830  316 -EAIGAIAKLTHKD--GREMVI------NVEYNQLdpllratghPDGDVNDETGYSPFP-GNINQLILKLGPyVKELAKT 385
                         250
                  ....*....|....*
gi 1798182223 226 NAIdMEIIVNAKTLD 240
Cdd:PLN02830  386 GGV-IEEFVNPKYKD 399
PTZ00339 PTZ00339
UDP-N-acetylglucosamine pyrophosphorylase; Provisional
1-208 3.65e-06

UDP-N-acetylglucosamine pyrophosphorylase; Provisional


Pssm-ID: 240368  Cd Length: 482  Bit Score: 48.58  E-value: 3.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798182223   1 MGCKGPKSL--IGVRNENTFLDLTVQQI---EHLNKTYN-----TDVPLVLMNSFNTDEDTKKILQKYNHCRVK---IYT 67
Cdd:PTZ00339  120 LGSDKPKGLleCTPVKKKTLFQFHCEKVrrlEEMAVAVSgggddPTIYILVLTSSFNHDQTRQFLEENNFFGLDkeqVIF 199
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798182223  68 FNQSRYPRINKESllpvaKDVSYSGENTEAWYPPGHGDIYASFYNSGLLDTFIGEGKEYIFVSNIDNLGATV-DLYILNH 146
Cdd:PTZ00339  200 FKQSSLPCYDENT-----GRFIMSSQGSLCTAPGGNGDVFKALAKCSELMDIVRKGIKYVQVISIDNILAKVlDPEFIGL 274
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1798182223 147 LMNPPngkrCEFVMEVTNKTRADVKGGTLTQYEGKLRLV---EIAQVPKAHVDEFKSVSKFKIFN 208
Cdd:PTZ00339  275 ASSFP----AHDVLNKCVKREDDESVGVFCLKDYEWQVVeytEINERILNNDELLTGELAFNYGN 335
 
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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