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Conserved domains on  [gi|767958689|ref|XP_011517484|]
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UDP-N-acetylhexosamine pyrophosphorylase-like protein 1 isoform X3 [Homo sapiens]

Protein Classification

UDPGP type 1 family protein( domain architecture ID 10135883)

UDPGP type 1 family protein such as human UDP-N-acetylhexosamine pyrophosphorylase that catalyzes the last step in biosynthesis of uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc) by converting UTP and glucosamine 1-phosphate (GlcNAc-1-P) to the sugar nucleotide

EC:  2.7.-.-
Gene Ontology:  GO:0016772
SCOP:  4000691|3000077

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
UDPGlcNAc_PPase cd04193
UDPGlcNAc pyrophosphorylase catalayzes the synthesis of UDPGlcNAc; UDP-N-acetylglucosamine ...
1-246 3.84e-151

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: 427.79  E-value: 3.84e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958689   1 MTSEFTLGPTAEFFREHNFFHLDPANVVMFEQRLLPAVTFDGKVILERKDKVAMAPDGNGGLYCALEDHKILEDMERRGV 80
Cdd:cd04193   78 MTSEATHEETRKFFKENNYFGLDPEQVHFFQQGMLPCVDFDGKILLEEKGKIAMAPNGNGGLYKALQTAGILEDMKKRGI 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958689  81 EFVHVYCVDNILVRLADPVFIGFCVLQGADCGAKVVEKAYPEEPVGVVCQVDGVPQVVEYSEISPETAQLRASDGSLLYN 160
Cdd:cd04193  158 KYIHVYSVDNILVKVADPVFIGFCISKGADVGAKVVRKRYPTEKVGVVVLVDGKPQVVEYSEISDELAEKRDADGELQYN 237
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958689 161 AGNICNHFFTRGFLKAVTREFEPLLKPHVAVKKVPYVDEEGNLVKPLKPNGIKMEKFVFDVFRFAKNFAALEVLREEEFS 240
Cdd:cd04193  238 AGNIANHFFSLDFLEKAAEMEEPSLPYHIAKKKIPYVDLEGGLVKPDEPNGIKLELFIFDVFPFAKNFVCLEVDREEEFS 317

                 ....*.
gi 767958689 241 PLKNAE 246
Cdd:cd04193  318 PLKNAD 323
 
Name Accession Description Interval E-value
UDPGlcNAc_PPase cd04193
UDPGlcNAc pyrophosphorylase catalayzes the synthesis of UDPGlcNAc; UDP-N-acetylglucosamine ...
1-246 3.84e-151

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: 427.79  E-value: 3.84e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958689   1 MTSEFTLGPTAEFFREHNFFHLDPANVVMFEQRLLPAVTFDGKVILERKDKVAMAPDGNGGLYCALEDHKILEDMERRGV 80
Cdd:cd04193   78 MTSEATHEETRKFFKENNYFGLDPEQVHFFQQGMLPCVDFDGKILLEEKGKIAMAPNGNGGLYKALQTAGILEDMKKRGI 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958689  81 EFVHVYCVDNILVRLADPVFIGFCVLQGADCGAKVVEKAYPEEPVGVVCQVDGVPQVVEYSEISPETAQLRASDGSLLYN 160
Cdd:cd04193  158 KYIHVYSVDNILVKVADPVFIGFCISKGADVGAKVVRKRYPTEKVGVVVLVDGKPQVVEYSEISDELAEKRDADGELQYN 237
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958689 161 AGNICNHFFTRGFLKAVTREFEPLLKPHVAVKKVPYVDEEGNLVKPLKPNGIKMEKFVFDVFRFAKNFAALEVLREEEFS 240
Cdd:cd04193  238 AGNIANHFFSLDFLEKAAEMEEPSLPYHIAKKKIPYVDLEGGLVKPDEPNGIKLELFIFDVFPFAKNFVCLEVDREEEFS 317

                 ....*.
gi 767958689 241 PLKNAE 246
Cdd:cd04193  318 PLKNAD 323
QRI1 COG4284
UDP-N-acetylglucosamine pyrophosphorylase [Carbohydrate transport and metabolism];
1-253 1.17e-87

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


Pssm-ID: 443425  Cd Length: 402  Bit Score: 269.06  E-value: 1.17e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958689   1 MTSEFTLGPTAEFFREHNFFHLDPANVVMFEQRLLPAV-TFDGKVILERKDKVAMAPDGNGGLYCALEDHKILEDMERRG 79
Cdd:COG4284  152 MTSFRTHEDTLAFLEEHDYFGLDGLPVHFFLQGMEPALdADLGPVLLPADPELELCPPGHGGIYTALLASGLLDKLLERG 231
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958689  80 VEFVHVYCVDNILVRLADPVFIGFCVLQGADCGAKVVEKAYPEEPVGVVCQVDGVPQVVEYSEISPETAQlrASDGSLLY 159
Cdd:COG4284  232 IRYLFVSNVDNPLGAVPDPAFAGWHAASGAPFTAKVVRRTPPDEKVGHLARVDGRLILREYSQLPDEEAE--AFTGELRH 309
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958689 160 NAGNICNHFFTRGFLKAVTREFEPLLKPHVAVKKVPYVDEEGnlvKPLKPNGIKMEKFVFDVFRFAKNFAALEVLREEEF 239
Cdd:COG4284  310 PYGNINNHWFDLDFLKRLLDERGLGLPLHRAEKKVDPLDESG---KPTSPNVIKFETFMFDAIPLFDGAVAIEVDREERF 386
                        250
                 ....*....|....
gi 767958689 240 SPLKNAEpaDRDSP 253
Cdd:COG4284  387 APVKNTN--GSDSP 398
PLN02435 PLN02435
probable UDP-N-acetylglucosamine pyrophosphorylase
1-310 4.85e-85

probable UDP-N-acetylglucosamine pyrophosphorylase


Pssm-ID: 215238  Cd Length: 493  Bit Score: 265.58  E-value: 4.85e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958689   1 MTSEFTLGPTAEFFREHNFFHLDPANVVMFEQRLLPAVTFDGKVILERKDKVAMAPDGNGGLYCALEDHKILEDMERRGV 80
Cdd:PLN02435 183 MTSPFTDEATRKFFESHKYFGLEADQVTFFQQGTLPCVSKDGKFIMETPFKVAKAPDGNGGVYAALKSSRLLEDMASRGI 262
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958689  81 EFVHVYCVDNILVRLADPVFIGFCVLQGADCGAKVVEKAYPEEPVGV-VCQVDGVP-QVVEYSEISPETA-QLRASDGSL 157
Cdd:PLN02435 263 KYVDCYGVDNALVRVADPTFLGYFIDKGVASAAKVVRKAYPQEKVGVfVRRGKGGPlTVVEYSELDQAMAsAINQQTGRL 342
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958689 158 LYNAGNICNHFFTRGFLKAVTREFEPLLKPHVAVKKVPYVDeeGNLVkplkpnGIKMEKFVFDVFRFAKNFAALEVLREE 237
Cdd:PLN02435 343 RYCWSNVCLHMFTLDFLNQVANGLEKDSIYHLAEKKIPSIH--GYTM------GLKLEQFIFDAFPYAPSTALFEVLREE 414
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767958689 238 EFSPLKNAEPADRDSPRTARQALLTQHYRWALRAGarfldahGAWLPELPsLPPNGdppaiCEISPLVSYSGE 310
Cdd:PLN02435 415 EFAPVKNANGSNFDTPESARLLVLRLHTRWVVAAG-------GFLTHSVP-LYATG-----VEVSPLCSYAGE 474
UDPGP pfam01704
UTP--glucose-1-phosphate uridylyltransferase; This family consists of UTP--glucose-1-phosphate ...
1-277 1.72e-49

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: 170.77  E-value: 1.72e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958689    1 MTSEFTLGPTAEFFREHNFFHLDpanVVMFEQRLLPAVTFDGKVILERK---DKVAMAPDGNGGLYCALEDHKILEDMER 77
Cdd:pfam01704 108 MNSFNTDEDTKKIIRKYKGHKVD---ILTFNQSRYPRIDKDTLLPVPKSadsDEEEWYPPGHGDLYESLYNSGLLDKLLA 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958689   78 RGVEFVHVYCVDNiLVRLADPVFIGFCVLQGADCGAKVVEKAYPEEPVGVVCQVDGVPQVVEYSEISPE-TAQLRASDGS 156
Cdd:pfam01704 185 EGKEYLFVSNIDN-LGATVDLNILNYMVDNGAEFLMEVTDKTRADVKGGTLIEYDGKLRLLEIAQVPKEhVDEFKSIKKF 263
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958689  157 LLYNAGNIcnhFFTrgfLKAVTREFE-PLLKPHVAVKKvPYVDEEGNLVKPLKPNGIKMEKFvfdvfrfaKNFAALEVLR 235
Cdd:pfam01704 264 KIFNTNNI---WIN---LKALKRVVEeGELQLEIIVNK-KTLDNGENVIQLETAVGAAIKNF--------KNAIGINVPR 328
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 767958689  236 eEEFSPLKnaepadrdsprTARQALLTQHYRWALRAGARFLD 277
Cdd:pfam01704 329 -SRFLPVK-----------TTSDLLLVMSDLYVLNHGSLIMN 358
 
Name Accession Description Interval E-value
UDPGlcNAc_PPase cd04193
UDPGlcNAc pyrophosphorylase catalayzes the synthesis of UDPGlcNAc; UDP-N-acetylglucosamine ...
1-246 3.84e-151

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: 427.79  E-value: 3.84e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958689   1 MTSEFTLGPTAEFFREHNFFHLDPANVVMFEQRLLPAVTFDGKVILERKDKVAMAPDGNGGLYCALEDHKILEDMERRGV 80
Cdd:cd04193   78 MTSEATHEETRKFFKENNYFGLDPEQVHFFQQGMLPCVDFDGKILLEEKGKIAMAPNGNGGLYKALQTAGILEDMKKRGI 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958689  81 EFVHVYCVDNILVRLADPVFIGFCVLQGADCGAKVVEKAYPEEPVGVVCQVDGVPQVVEYSEISPETAQLRASDGSLLYN 160
Cdd:cd04193  158 KYIHVYSVDNILVKVADPVFIGFCISKGADVGAKVVRKRYPTEKVGVVVLVDGKPQVVEYSEISDELAEKRDADGELQYN 237
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958689 161 AGNICNHFFTRGFLKAVTREFEPLLKPHVAVKKVPYVDEEGNLVKPLKPNGIKMEKFVFDVFRFAKNFAALEVLREEEFS 240
Cdd:cd04193  238 AGNIANHFFSLDFLEKAAEMEEPSLPYHIAKKKIPYVDLEGGLVKPDEPNGIKLELFIFDVFPFAKNFVCLEVDREEEFS 317

                 ....*.
gi 767958689 241 PLKNAE 246
Cdd:cd04193  318 PLKNAD 323
QRI1 COG4284
UDP-N-acetylglucosamine pyrophosphorylase [Carbohydrate transport and metabolism];
1-253 1.17e-87

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


Pssm-ID: 443425  Cd Length: 402  Bit Score: 269.06  E-value: 1.17e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958689   1 MTSEFTLGPTAEFFREHNFFHLDPANVVMFEQRLLPAV-TFDGKVILERKDKVAMAPDGNGGLYCALEDHKILEDMERRG 79
Cdd:COG4284  152 MTSFRTHEDTLAFLEEHDYFGLDGLPVHFFLQGMEPALdADLGPVLLPADPELELCPPGHGGIYTALLASGLLDKLLERG 231
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958689  80 VEFVHVYCVDNILVRLADPVFIGFCVLQGADCGAKVVEKAYPEEPVGVVCQVDGVPQVVEYSEISPETAQlrASDGSLLY 159
Cdd:COG4284  232 IRYLFVSNVDNPLGAVPDPAFAGWHAASGAPFTAKVVRRTPPDEKVGHLARVDGRLILREYSQLPDEEAE--AFTGELRH 309
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958689 160 NAGNICNHFFTRGFLKAVTREFEPLLKPHVAVKKVPYVDEEGnlvKPLKPNGIKMEKFVFDVFRFAKNFAALEVLREEEF 239
Cdd:COG4284  310 PYGNINNHWFDLDFLKRLLDERGLGLPLHRAEKKVDPLDESG---KPTSPNVIKFETFMFDAIPLFDGAVAIEVDREERF 386
                        250
                 ....*....|....
gi 767958689 240 SPLKNAEpaDRDSP 253
Cdd:COG4284  387 APVKNTN--GSDSP 398
PLN02435 PLN02435
probable UDP-N-acetylglucosamine pyrophosphorylase
1-310 4.85e-85

probable UDP-N-acetylglucosamine pyrophosphorylase


Pssm-ID: 215238  Cd Length: 493  Bit Score: 265.58  E-value: 4.85e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958689   1 MTSEFTLGPTAEFFREHNFFHLDPANVVMFEQRLLPAVTFDGKVILERKDKVAMAPDGNGGLYCALEDHKILEDMERRGV 80
Cdd:PLN02435 183 MTSPFTDEATRKFFESHKYFGLEADQVTFFQQGTLPCVSKDGKFIMETPFKVAKAPDGNGGVYAALKSSRLLEDMASRGI 262
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958689  81 EFVHVYCVDNILVRLADPVFIGFCVLQGADCGAKVVEKAYPEEPVGV-VCQVDGVP-QVVEYSEISPETA-QLRASDGSL 157
Cdd:PLN02435 263 KYVDCYGVDNALVRVADPTFLGYFIDKGVASAAKVVRKAYPQEKVGVfVRRGKGGPlTVVEYSELDQAMAsAINQQTGRL 342
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958689 158 LYNAGNICNHFFTRGFLKAVTREFEPLLKPHVAVKKVPYVDeeGNLVkplkpnGIKMEKFVFDVFRFAKNFAALEVLREE 237
Cdd:PLN02435 343 RYCWSNVCLHMFTLDFLNQVANGLEKDSIYHLAEKKIPSIH--GYTM------GLKLEQFIFDAFPYAPSTALFEVLREE 414
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767958689 238 EFSPLKNAEPADRDSPRTARQALLTQHYRWALRAGarfldahGAWLPELPsLPPNGdppaiCEISPLVSYSGE 310
Cdd:PLN02435 415 EFAPVKNANGSNFDTPESARLLVLRLHTRWVVAAG-------GFLTHSVP-LYATG-----VEVSPLCSYAGE 474
PTZ00339 PTZ00339
UDP-N-acetylglucosamine pyrophosphorylase; Provisional
1-316 2.81e-82

UDP-N-acetylglucosamine pyrophosphorylase; Provisional


Pssm-ID: 240368  Cd Length: 482  Bit Score: 257.75  E-value: 2.81e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958689   1 MTSEFTLGPTAEFFREHNFFHLDPANVVMFEQRLLPAVT-FDGKVILERKDKVAMAPDGNGGLYCALEDHKILEDMERRG 79
Cdd:PTZ00339 171 LTSSFNHDQTRQFLEENNFFGLDKEQVIFFKQSSLPCYDeNTGRFIMSSQGSLCTAPGGNGDVFKALAKCSELMDIVRKG 250
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958689  80 VEFVHVYCVDNILVRLADPVFIGFCVLQGADCGAKVVEKAYPEEPVGVVCQVDGVPQVVEYSEISpETAQLRASD--GSL 157
Cdd:PTZ00339 251 IKYVQVISIDNILAKVLDPEFIGLASSFPAHDVLNKCVKREDDESVGVFCLKDYEWQVVEYTEIN-ERILNNDELltGEL 329
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958689 158 LYNAGNICNHFFTRGFLKAVTRE-FEPLLKPHVAVKKVPYVDEEGNlvkplKPNGIKMEKFVFDVFRFAKNFAALEVLRE 236
Cdd:PTZ00339 330 AFNYGNICSHIFSLDFLKKVAANrLYESTPYHAARKKIPYINGPTD-----KTMGIKLEAFIFDIFRYAKNVLILEVDRE 404
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958689 237 EEFSPLKNAEPADRDSPRTARQALLTQHYRWALRAGArfldahgawlpelpSLPPNGDPPAI-CEISPLVSYSGEVRAAH 315
Cdd:PTZ00339 405 DEFAPIKNADGAAADTILNAQKLLLSLHTRWLEAALE--------------TVAGNPREGLNlCEISPLVSYGGEGLFQY 470

                 .
gi 767958689 316 P 316
Cdd:PTZ00339 471 P 471
UGPase_euk_like cd04180
Eukaryotic UGPase-like includes UDPase and UDPGlcNAc pyrophosphorylase enzymes; This family ...
1-244 9.75e-58

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: 187.76  E-value: 9.75e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958689   1 MTSEFTLGPTAEFFREHNffhLDPANVVMFEQRLLPAVTFDGKVILERKDKVAMAPDGNGGLYCALEDHKILEDMERRGV 80
Cdd:cd04180   59 MNSKYTHEKTQCYFEKIN---QKNSYVITFMQGKLPLKNDDDARDPHNKTKCHLFPCGHGDVVLALIHSGHLNKLLEKGY 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958689  81 EFVHVYCVDNILVRLADPVFIGFCVLQGADCGAKVVEKAYPEEPVGVVCQVD-GVPQVVEYSEISPETAQLR------AS 153
Cdd:cd04180  136 RYIHFIGVDNLLVKVADPLFIGIAIQNRKAINQKVVPKTRNEESGGYRIANInGRVQLLEYDQIKKLLKQKMvnnqipKD 215
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958689 154 DGSLLYNAGNICNHFFTRGFLKavtrefepllkphvavkkvpyvdeegnlvkplkpngikmeKFVFDVFRFAKNFAALEV 233
Cdd:cd04180  216 IDDAPFFLFNTNNLINFLVEFK----------------------------------------DRVDDIIEFTDDIVGVMV 255
                        250
                 ....*....|.
gi 767958689 234 LREEEFSPLKN 244
Cdd:cd04180  256 HRAEEFAPVKN 266
UDPGP pfam01704
UTP--glucose-1-phosphate uridylyltransferase; This family consists of UTP--glucose-1-phosphate ...
1-277 1.72e-49

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: 170.77  E-value: 1.72e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958689    1 MTSEFTLGPTAEFFREHNFFHLDpanVVMFEQRLLPAVTFDGKVILERK---DKVAMAPDGNGGLYCALEDHKILEDMER 77
Cdd:pfam01704 108 MNSFNTDEDTKKIIRKYKGHKVD---ILTFNQSRYPRIDKDTLLPVPKSadsDEEEWYPPGHGDLYESLYNSGLLDKLLA 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958689   78 RGVEFVHVYCVDNiLVRLADPVFIGFCVLQGADCGAKVVEKAYPEEPVGVVCQVDGVPQVVEYSEISPE-TAQLRASDGS 156
Cdd:pfam01704 185 EGKEYLFVSNIDN-LGATVDLNILNYMVDNGAEFLMEVTDKTRADVKGGTLIEYDGKLRLLEIAQVPKEhVDEFKSIKKF 263
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958689  157 LLYNAGNIcnhFFTrgfLKAVTREFE-PLLKPHVAVKKvPYVDEEGNLVKPLKPNGIKMEKFvfdvfrfaKNFAALEVLR 235
Cdd:pfam01704 264 KIFNTNNI---WIN---LKALKRVVEeGELQLEIIVNK-KTLDNGENVIQLETAVGAAIKNF--------KNAIGINVPR 328
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 767958689  236 eEEFSPLKnaepadrdsprTARQALLTQHYRWALRAGARFLD 277
Cdd:pfam01704 329 -SRFLPVK-----------TTSDLLLVMSDLYVLNHGSLIMN 358
 
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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