|
Name |
Accession |
Description |
Interval |
E-value |
| UDPGlcNAc_PPase |
cd04193 |
UDPGlcNAc pyrophosphorylase catalayzes the synthesis of UDPGlcNAc; UDP-N-acetylglucosamine ... |
92-413 |
0e+00 |
|
UDPGlcNAc pyrophosphorylase catalayzes the synthesis of UDPGlcNAc; UDP-N-acetylglucosamine (UDPGlcNAc) pyrophosphorylase (UAP) (also named GlcNAc1P uridyltransferase), catalyzes the reversible conversion of UTP and GlcNAc1 to PPi and UDPGlcNAc. UDP-N-acetylglucosamine (UDPGlcNAc), the activated form of GlcNAc, is a key precursor of N- and O-linked glycosylations. It is essential for the synthesis of chitin (a major component of the fungal cell wall) and of the glycosylphosphatidylinositol (GPI) linker which anchors a variety of cell surface proteins to the plasma membrane. In bacteria, UDPGlcNAc represents an essential precursor for both peptidoglycan and lipopolysaccharide biosynthesis. Human UAP has two isoforms, resulting from alternative splicing of a single gene and differing by the presence or absence of 17 amino acids. UDPGlcNAc pyrophosphorylase shares significant sequence and structure conservation with UDPglucose pyrophosphorylase.
Pssm-ID: 133036 Cd Length: 323 Bit Score: 573.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817975 92 RWEEEGFRQISLNKVAVLLLAGGQGTRLGVTYPKGMYRVGLPSRKTLYQLQAERIRRVEQLAGERHGTRCTVPWYVMTSE 171
Cdd:cd04193 2 EWEEAGLKAIAEGKVAVLLLAGGQGTRLGFDGPKGMFPVGLPSKKSLFQLQAERILKLQELAGEASGKKVPIPWYIMTSE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817975 172 FTLGPTAEFFREHNFFHLDPANVVMFEQRLLPAVTFDGKVILERKDKVAMAPDGNGGLYCALEDHKILEDMERRGVEFVH 251
Cdd:cd04193 82 ATHEETRKFFKENNYFGLDPEQVHFFQQGMLPCVDFDGKILLEEKGKIAMAPNGNGGLYKALQTAGILEDMKKRGIKYIH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817975 252 VYCVDNILVRLADPVFIGFCVLQGADCGAKVVEKAYPEEPVGVVCQVDGVPQVVEYSEISPETAQLRASDGSLLYNAGNI 331
Cdd:cd04193 162 VYSVDNILVKVADPVFIGFCISKGADVGAKVVRKRYPTEKVGVVVLVDGKPQVVEYSEISDELAEKRDADGELQYNAGNI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817975 332 CNHFFTRGFLKAVTREFEPLLKPHVAVKKVPYVDEEGNLVKPLKPNGIKMEKFVFDVFRFAKNFAALEVLREEEFSPLKN 411
Cdd:cd04193 242 ANHFFSLDFLEKAAEMEEPSLPYHIAKKKIPYVDLEGGLVKPDEPNGIKLELFIFDVFPFAKNFVCLEVDREEEFSPLKN 321
|
..
gi 578817975 412 AE 413
Cdd:cd04193 322 AD 323
|
|
| PLN02435 |
PLN02435 |
probable UDP-N-acetylglucosamine pyrophosphorylase |
1-477 |
1.28e-125 |
|
probable UDP-N-acetylglucosamine pyrophosphorylase
Pssm-ID: 215238 Cd Length: 493 Bit Score: 375.75 E-value: 1.28e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817975 1 MASEQDVRARLQRAGQEHLLRFWAELAPEPRAALLAELALLEPEalreHCRRAAEACARPHGPPpdlAARLRPLPPERVG 80
Cdd:PLN02435 19 AAPPQALLERLKDYGQEDAFALWDELSPEERDLLVRDIESLDLP----RIDRIIRCSLRSQGLP---VPAIEPVPENSVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817975 81 RASRSDPETRRRWEEEGFRQISLNKVAVLLLAGGQGTRLGVTYPKGMYRVGLPSRKTLYQLQAERIRRVEQLA----GER 156
Cdd:PLN02435 92 TVEERTPEDRERWWKMGLKAISEGKLAVVLLSGGQGTRLGSSDPKGCFNIGLPSGKSLFQLQAERILCVQRLAaqasSEG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817975 157 HGTRCTVPWYVMTSEFTLGPTAEFFREHNFFHLDPANVVMFEQRLLPAVTFDGKVILERKDKVAMAPDGNGGLYCALEDH 236
Cdd:PLN02435 172 PGRPVTIHWYIMTSPFTDEATRKFFESHKYFGLEADQVTFFQQGTLPCVSKDGKFIMETPFKVAKAPDGNGGVYAALKSS 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817975 237 KILEDMERRGVEFVHVYCVDNILVRLADPVFIGFCVLQGADCGAKVVEKAYPEEPVGV-VCQVDGVP-QVVEYSEISPET 314
Cdd:PLN02435 252 RLLEDMASRGIKYVDCYGVDNALVRVADPTFLGYFIDKGVASAAKVVRKAYPQEKVGVfVRRGKGGPlTVVEYSELDQAM 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817975 315 A-QLRASDGSLLYNAGNICNHFFTRGFLKAVTREFEPLLKPHVAVKKVPYVDeeGNLVkplkpnGIKMEKFVFDVFRFAK 393
Cdd:PLN02435 332 AsAINQQTGRLRYCWSNVCLHMFTLDFLNQVANGLEKDSIYHLAEKKIPSIH--GYTM------GLKLEQFIFDAFPYAP 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817975 394 NFAALEVLREEEFSPLKNAEPADRDSPRTARQALLTQHYRWALRAGarfldahGAWLPELPsLPPNGdppaiCEISPLVS 473
Cdd:PLN02435 404 STALFEVLREEEFAPVKNANGSNFDTPESARLLVLRLHTRWVVAAG-------GFLTHSVP-LYATG-----VEVSPLCS 470
|
....
gi 578817975 474 YSGE 477
Cdd:PLN02435 471 YAGE 474
|
|
| QRI1 |
COG4284 |
UDP-N-acetylglucosamine pyrophosphorylase [Carbohydrate transport and metabolism]; |
10-420 |
3.00e-123 |
|
UDP-N-acetylglucosamine pyrophosphorylase [Carbohydrate transport and metabolism];
Pssm-ID: 443425 Cd Length: 402 Bit Score: 366.52 E-value: 3.00e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817975 10 RLQRAGQEHLLRFWAELAPEPRAALLAELALLEPEALrEHCRRAAEACARPHGPPPDlaARLRPLPPERVGRASRSDpET 89
Cdd:COG4284 4 KLEPHGQEHLLRFWDELSEAQQKMLEAQIEEIDIDVF-QHLYRQLVLAEGATGLIPE--SDIEPAPVTDLPLTDLDE-VD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817975 90 RRRWEEEGFRQISLNKVAVLLLAGGQGTRLGVTYPKGMYRVGLPSRKTLYQLQAERIRRveqlAGERHGTRctVPWYVMT 169
Cdd:COG4284 80 RDRAEEAGEEALRAGKVAVILLAGGQGTRLGFDGPKGLLPVRPVKGKSLFDLIAEQVLA----ARRRYGVP--LPLYIMT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817975 170 SEFTLGPTAEFFREHNFFHLDPANVVMFEQRLLPAV-TFDGKVILERKDKVAMAPDGNGGLYCALEDHKILEDMERRGVE 248
Cdd:COG4284 154 SFRTHEDTLAFLEEHDYFGLDGLPVHFFLQGMEPALdADLGPVLLPADPELELCPPGHGGIYTALLASGLLDKLLERGIR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817975 249 FVHVYCVDNILVRLADPVFIGFCVLQGADCGAKVVEKAYPEEPVGVVCQVDGVPQVVEYSEISPETAQlrASDGSLLYNA 328
Cdd:COG4284 234 YLFVSNVDNPLGAVPDPAFAGWHAASGAPFTAKVVRRTPPDEKVGHLARVDGRLILREYSQLPDEEAE--AFTGELRHPY 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817975 329 GNICNHFFTRGFLKAVTREFEPLLKPHVAVKKVPYVDEEGnlvKPLKPNGIKMEKFVFDVFRFAKNFAALEVLREEEFSP 408
Cdd:COG4284 312 GNINNHWFDLDFLKRLLDERGLGLPLHRAEKKVDPLDESG---KPTSPNVIKFETFMFDAIPLFDGAVAIEVDREERFAP 388
|
410
....*....|..
gi 578817975 409 LKNAEpaDRDSP 420
Cdd:COG4284 389 VKNTN--GSDSP 398
|
|
| UDPGP |
pfam01704 |
UTP--glucose-1-phosphate uridylyltransferase; This family consists of UTP--glucose-1-phosphate ... |
69-444 |
5.48e-72 |
|
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: 234.72 E-value: 5.48e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817975 69 ARLRPLPPER-VGRASRSDPEtrrrWEEEGFrqisLNKVAVLLLAGGQGTRLGVTYPKGMYRVGlpSRKTLYQLQAERIr 147
Cdd:pfam01704 24 DKIKPPPEEEiVDYEDLQEPE----EEIKEL----LNKLAVLKLNGGLGTSMGCVGPKSLIEVR--DGLTFLDLIVQQI- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817975 148 rvEQLageRHGTRCTVPWYVMTSEFTLGPTAEFFREHNFFHLDpanVVMFEQRLLPAVTFDGKVILERK---DKVAMAPD 224
Cdd:pfam01704 93 --EHL---NKKYNVDVPLVLMNSFNTDEDTKKIIRKYKGHKVD---ILTFNQSRYPRIDKDTLLPVPKSadsDEEEWYPP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817975 225 GNGGLYCALEDHKILEDMERRGVEFVHVYCVDNiLVRLADPVFIGFCVLQGADCGAKVVEKAYPEEPVGVVCQVDGVPQV 304
Cdd:pfam01704 165 GHGDLYESLYNSGLLDKLLAEGKEYLFVSNIDN-LGATVDLNILNYMVDNGAEFLMEVTDKTRADVKGGTLIEYDGKLRL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817975 305 VEYSEISPE-TAQLRASDGSLLYNAGNIcnhFFTrgfLKAVTREFE-PLLKPHVAVKKvPYVDEEGNLVKPLKPNGIKME 382
Cdd:pfam01704 244 LEIAQVPKEhVDEFKSIKKFKIFNTNNI---WIN---LKALKRVVEeGELQLEIIVNK-KTLDNGENVIQLETAVGAAIK 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578817975 383 KFvfdvfrfaKNFAALEVLReEEFSPLKnaepadrdsprTARQALLTQHYRWALRAGARFLD 444
Cdd:pfam01704 317 NF--------KNAIGINVPR-SRFLPVK-----------TTSDLLLVMSDLYVLNHGSLIMN 358
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| UDPGlcNAc_PPase |
cd04193 |
UDPGlcNAc pyrophosphorylase catalayzes the synthesis of UDPGlcNAc; UDP-N-acetylglucosamine ... |
92-413 |
0e+00 |
|
UDPGlcNAc pyrophosphorylase catalayzes the synthesis of UDPGlcNAc; UDP-N-acetylglucosamine (UDPGlcNAc) pyrophosphorylase (UAP) (also named GlcNAc1P uridyltransferase), catalyzes the reversible conversion of UTP and GlcNAc1 to PPi and UDPGlcNAc. UDP-N-acetylglucosamine (UDPGlcNAc), the activated form of GlcNAc, is a key precursor of N- and O-linked glycosylations. It is essential for the synthesis of chitin (a major component of the fungal cell wall) and of the glycosylphosphatidylinositol (GPI) linker which anchors a variety of cell surface proteins to the plasma membrane. In bacteria, UDPGlcNAc represents an essential precursor for both peptidoglycan and lipopolysaccharide biosynthesis. Human UAP has two isoforms, resulting from alternative splicing of a single gene and differing by the presence or absence of 17 amino acids. UDPGlcNAc pyrophosphorylase shares significant sequence and structure conservation with UDPglucose pyrophosphorylase.
Pssm-ID: 133036 Cd Length: 323 Bit Score: 573.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817975 92 RWEEEGFRQISLNKVAVLLLAGGQGTRLGVTYPKGMYRVGLPSRKTLYQLQAERIRRVEQLAGERHGTRCTVPWYVMTSE 171
Cdd:cd04193 2 EWEEAGLKAIAEGKVAVLLLAGGQGTRLGFDGPKGMFPVGLPSKKSLFQLQAERILKLQELAGEASGKKVPIPWYIMTSE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817975 172 FTLGPTAEFFREHNFFHLDPANVVMFEQRLLPAVTFDGKVILERKDKVAMAPDGNGGLYCALEDHKILEDMERRGVEFVH 251
Cdd:cd04193 82 ATHEETRKFFKENNYFGLDPEQVHFFQQGMLPCVDFDGKILLEEKGKIAMAPNGNGGLYKALQTAGILEDMKKRGIKYIH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817975 252 VYCVDNILVRLADPVFIGFCVLQGADCGAKVVEKAYPEEPVGVVCQVDGVPQVVEYSEISPETAQLRASDGSLLYNAGNI 331
Cdd:cd04193 162 VYSVDNILVKVADPVFIGFCISKGADVGAKVVRKRYPTEKVGVVVLVDGKPQVVEYSEISDELAEKRDADGELQYNAGNI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817975 332 CNHFFTRGFLKAVTREFEPLLKPHVAVKKVPYVDEEGNLVKPLKPNGIKMEKFVFDVFRFAKNFAALEVLREEEFSPLKN 411
Cdd:cd04193 242 ANHFFSLDFLEKAAEMEEPSLPYHIAKKKIPYVDLEGGLVKPDEPNGIKLELFIFDVFPFAKNFVCLEVDREEEFSPLKN 321
|
..
gi 578817975 412 AE 413
Cdd:cd04193 322 AD 323
|
|
| PLN02435 |
PLN02435 |
probable UDP-N-acetylglucosamine pyrophosphorylase |
1-477 |
1.28e-125 |
|
probable UDP-N-acetylglucosamine pyrophosphorylase
Pssm-ID: 215238 Cd Length: 493 Bit Score: 375.75 E-value: 1.28e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817975 1 MASEQDVRARLQRAGQEHLLRFWAELAPEPRAALLAELALLEPEalreHCRRAAEACARPHGPPpdlAARLRPLPPERVG 80
Cdd:PLN02435 19 AAPPQALLERLKDYGQEDAFALWDELSPEERDLLVRDIESLDLP----RIDRIIRCSLRSQGLP---VPAIEPVPENSVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817975 81 RASRSDPETRRRWEEEGFRQISLNKVAVLLLAGGQGTRLGVTYPKGMYRVGLPSRKTLYQLQAERIRRVEQLA----GER 156
Cdd:PLN02435 92 TVEERTPEDRERWWKMGLKAISEGKLAVVLLSGGQGTRLGSSDPKGCFNIGLPSGKSLFQLQAERILCVQRLAaqasSEG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817975 157 HGTRCTVPWYVMTSEFTLGPTAEFFREHNFFHLDPANVVMFEQRLLPAVTFDGKVILERKDKVAMAPDGNGGLYCALEDH 236
Cdd:PLN02435 172 PGRPVTIHWYIMTSPFTDEATRKFFESHKYFGLEADQVTFFQQGTLPCVSKDGKFIMETPFKVAKAPDGNGGVYAALKSS 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817975 237 KILEDMERRGVEFVHVYCVDNILVRLADPVFIGFCVLQGADCGAKVVEKAYPEEPVGV-VCQVDGVP-QVVEYSEISPET 314
Cdd:PLN02435 252 RLLEDMASRGIKYVDCYGVDNALVRVADPTFLGYFIDKGVASAAKVVRKAYPQEKVGVfVRRGKGGPlTVVEYSELDQAM 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817975 315 A-QLRASDGSLLYNAGNICNHFFTRGFLKAVTREFEPLLKPHVAVKKVPYVDeeGNLVkplkpnGIKMEKFVFDVFRFAK 393
Cdd:PLN02435 332 AsAINQQTGRLRYCWSNVCLHMFTLDFLNQVANGLEKDSIYHLAEKKIPSIH--GYTM------GLKLEQFIFDAFPYAP 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817975 394 NFAALEVLREEEFSPLKNAEPADRDSPRTARQALLTQHYRWALRAGarfldahGAWLPELPsLPPNGdppaiCEISPLVS 473
Cdd:PLN02435 404 STALFEVLREEEFAPVKNANGSNFDTPESARLLVLRLHTRWVVAAG-------GFLTHSVP-LYATG-----VEVSPLCS 470
|
....
gi 578817975 474 YSGE 477
Cdd:PLN02435 471 YAGE 474
|
|
| QRI1 |
COG4284 |
UDP-N-acetylglucosamine pyrophosphorylase [Carbohydrate transport and metabolism]; |
10-420 |
3.00e-123 |
|
UDP-N-acetylglucosamine pyrophosphorylase [Carbohydrate transport and metabolism];
Pssm-ID: 443425 Cd Length: 402 Bit Score: 366.52 E-value: 3.00e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817975 10 RLQRAGQEHLLRFWAELAPEPRAALLAELALLEPEALrEHCRRAAEACARPHGPPPDlaARLRPLPPERVGRASRSDpET 89
Cdd:COG4284 4 KLEPHGQEHLLRFWDELSEAQQKMLEAQIEEIDIDVF-QHLYRQLVLAEGATGLIPE--SDIEPAPVTDLPLTDLDE-VD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817975 90 RRRWEEEGFRQISLNKVAVLLLAGGQGTRLGVTYPKGMYRVGLPSRKTLYQLQAERIRRveqlAGERHGTRctVPWYVMT 169
Cdd:COG4284 80 RDRAEEAGEEALRAGKVAVILLAGGQGTRLGFDGPKGLLPVRPVKGKSLFDLIAEQVLA----ARRRYGVP--LPLYIMT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817975 170 SEFTLGPTAEFFREHNFFHLDPANVVMFEQRLLPAV-TFDGKVILERKDKVAMAPDGNGGLYCALEDHKILEDMERRGVE 248
Cdd:COG4284 154 SFRTHEDTLAFLEEHDYFGLDGLPVHFFLQGMEPALdADLGPVLLPADPELELCPPGHGGIYTALLASGLLDKLLERGIR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817975 249 FVHVYCVDNILVRLADPVFIGFCVLQGADCGAKVVEKAYPEEPVGVVCQVDGVPQVVEYSEISPETAQlrASDGSLLYNA 328
Cdd:COG4284 234 YLFVSNVDNPLGAVPDPAFAGWHAASGAPFTAKVVRRTPPDEKVGHLARVDGRLILREYSQLPDEEAE--AFTGELRHPY 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817975 329 GNICNHFFTRGFLKAVTREFEPLLKPHVAVKKVPYVDEEGnlvKPLKPNGIKMEKFVFDVFRFAKNFAALEVLREEEFSP 408
Cdd:COG4284 312 GNINNHWFDLDFLKRLLDERGLGLPLHRAEKKVDPLDESG---KPTSPNVIKFETFMFDAIPLFDGAVAIEVDREERFAP 388
|
410
....*....|..
gi 578817975 409 LKNAEpaDRDSP 420
Cdd:COG4284 389 VKNTN--GSDSP 398
|
|
| PTZ00339 |
PTZ00339 |
UDP-N-acetylglucosamine pyrophosphorylase; Provisional |
75-483 |
1.09e-107 |
|
UDP-N-acetylglucosamine pyrophosphorylase; Provisional
Pssm-ID: 240368 Cd Length: 482 Bit Score: 329.39 E-value: 1.09e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817975 75 PPERVGRASRSDPETRRRWEEEGFRQISLNKVAVLLLAGGQGTRLGVTYPKGMYRVGLPSRKTLYQLQAERIRRVEQLAG 154
Cdd:PTZ00339 76 PNNNTFIDIYEKEKERKELKESGLEIIKKGEVAVLILAGGLGTRLGSDKPKGLLECTPVKKKTLFQFHCEKVRRLEEMAV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817975 155 ERHGT--RCTVPWYVMTSEFTLGPTAEFFREHNFFHLDPANVVMFEQRLLPAVT-FDGKVILERKDKVAMAPDGNGGLYC 231
Cdd:PTZ00339 156 AVSGGgdDPTIYILVLTSSFNHDQTRQFLEENNFFGLDKEQVIFFKQSSLPCYDeNTGRFIMSSQGSLCTAPGGNGDVFK 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817975 232 ALEDHKILEDMERRGVEFVHVYCVDNILVRLADPVFIGFCVLQGADCGAKVVEKAYPEEPVGVVCQVDGVPQVVEYSEIS 311
Cdd:PTZ00339 236 ALAKCSELMDIVRKGIKYVQVISIDNILAKVLDPEFIGLASSFPAHDVLNKCVKREDDESVGVFCLKDYEWQVVEYTEIN 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817975 312 pETAQLRASD--GSLLYNAGNICNHFFTRGFLKAVTRE-FEPLLKPHVAVKKVPYVDEEGNlvkplKPNGIKMEKFVFDV 388
Cdd:PTZ00339 316 -ERILNNDELltGELAFNYGNICSHIFSLDFLKKVAANrLYESTPYHAARKKIPYINGPTD-----KTMGIKLEAFIFDI 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817975 389 FRFAKNFAALEVLREEEFSPLKNAEPADRDSPRTARQALLTQHYRWALRAGArfldahgawlpelpSLPPNGDPPAI-CE 467
Cdd:PTZ00339 390 FRYAKNVLILEVDREDEFAPIKNADGAAADTILNAQKLLLSLHTRWLEAALE--------------TVAGNPREGLNlCE 455
|
410
....*....|....*.
gi 578817975 468 ISPLVSYSGEVRAAHP 483
Cdd:PTZ00339 456 ISPLVSYGGEGLFQYP 471
|
|
| UGPase_euk_like |
cd04180 |
Eukaryotic UGPase-like includes UDPase and UDPGlcNAc pyrophosphorylase enzymes; This family ... |
106-411 |
4.99e-83 |
|
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: 258.25 E-value: 4.99e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817975 106 VAVLLLAGGQGTRLGVTYPKGMYRVGLPSRKTLYQLQAERIRRVEQLAGerhgTRCTVPWYVMTSEFTLGPTAEFFREHN 185
Cdd:cd04180 1 VAVVLLAGGLGTRLGKDGPKSSTDVGLPSGQCFLQLIGEKILTLQEIDL----YSCKIPEQLMNSKYTHEKTQCYFEKIN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817975 186 ffhLDPANVVMFEQRLLPAVTFDGKVILERKDKVAMAPDGNGGLYCALEDHKILEDMERRGVEFVHVYCVDNILVRLADP 265
Cdd:cd04180 77 ---QKNSYVITFMQGKLPLKNDDDARDPHNKTKCHLFPCGHGDVVLALIHSGHLNKLLEKGYRYIHFIGVDNLLVKVADP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817975 266 VFIGFCVLQGADCGAKVVEKAYPEEPVGVVCQVD-GVPQVVEYSEISPETAQLR------ASDGSLLYNAGNICNHFFTR 338
Cdd:cd04180 154 LFIGIAIQNRKAINQKVVPKTRNEESGGYRIANInGRVQLLEYDQIKKLLKQKMvnnqipKDIDDAPFFLFNTNNLINFL 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578817975 339 GFLKavtrefepllkphvavkkvpyvdeegnlvkplkpngikmeKFVFDVFRFAKNFAALEVLREEEFSPLKN 411
Cdd:cd04180 234 VEFK----------------------------------------DRVDDIIEFTDDIVGVMVHRAEEFAPVKN 266
|
|
| UDPGP |
pfam01704 |
UTP--glucose-1-phosphate uridylyltransferase; This family consists of UTP--glucose-1-phosphate ... |
69-444 |
5.48e-72 |
|
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: 234.72 E-value: 5.48e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817975 69 ARLRPLPPER-VGRASRSDPEtrrrWEEEGFrqisLNKVAVLLLAGGQGTRLGVTYPKGMYRVGlpSRKTLYQLQAERIr 147
Cdd:pfam01704 24 DKIKPPPEEEiVDYEDLQEPE----EEIKEL----LNKLAVLKLNGGLGTSMGCVGPKSLIEVR--DGLTFLDLIVQQI- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817975 148 rvEQLageRHGTRCTVPWYVMTSEFTLGPTAEFFREHNFFHLDpanVVMFEQRLLPAVTFDGKVILERK---DKVAMAPD 224
Cdd:pfam01704 93 --EHL---NKKYNVDVPLVLMNSFNTDEDTKKIIRKYKGHKVD---ILTFNQSRYPRIDKDTLLPVPKSadsDEEEWYPP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817975 225 GNGGLYCALEDHKILEDMERRGVEFVHVYCVDNiLVRLADPVFIGFCVLQGADCGAKVVEKAYPEEPVGVVCQVDGVPQV 304
Cdd:pfam01704 165 GHGDLYESLYNSGLLDKLLAEGKEYLFVSNIDN-LGATVDLNILNYMVDNGAEFLMEVTDKTRADVKGGTLIEYDGKLRL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817975 305 VEYSEISPE-TAQLRASDGSLLYNAGNIcnhFFTrgfLKAVTREFE-PLLKPHVAVKKvPYVDEEGNLVKPLKPNGIKME 382
Cdd:pfam01704 244 LEIAQVPKEhVDEFKSIKKFKIFNTNNI---WIN---LKALKRVVEeGELQLEIIVNK-KTLDNGENVIQLETAVGAAIK 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578817975 383 KFvfdvfrfaKNFAALEVLReEEFSPLKnaepadrdsprTARQALLTQHYRWALRAGARFLD 444
Cdd:pfam01704 317 NF--------KNAIGINVPR-SRFLPVK-----------TTSDLLLVMSDLYVLNHGSLIMN 358
|
|
| UGGPase |
cd06424 |
UGGPase catalyzes the synthesis of UDP-Glucose/UDP-Galactose; UGGPase: UDP-Galactose/Glucose ... |
106-312 |
6.66e-13 |
|
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: 69.41 E-value: 6.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817975 106 VAVLLLAGGQGTRLGVtypKGMyRVGLP----SRKTLYQLQAERIRRVEQLAGErhGTRCTVPWYVMTSEFTLGPTAEFF 181
Cdd:cd06424 1 AVFVLVAGGLGERLGY---SGI-KIGLPveltTNTTYLQYYLNYIRAFQEASKK--GEKMEIPFVIMTSDDTHSKTLKLL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817975 182 REHNFFHLDPANVVMFEQRLLPA-VTFDGKVILERKDKVAMA--PDGNGGLYCALEDHKILEDMERRGVEFVHVYCVDNI 258
Cdd:cd06424 75 EENNYFGLEKDQVHILKQEKVFClIDNDAHLALDPDNTYSILtkPHGHGDVHTLLYNSGLLKKWIEAGYKWLVFFQDTNA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 578817975 259 LVRLADPVFIGFCVLQGADCGAKVVEKAyPEEPVGVVCQ---VDGVPQV--VEYSEISP 312
Cdd:cd06424 155 LAFKAIPAVLGVSATKSLDMNSLTVPRK-PKEAIGALCKltkNNGKSMTinVEYNQLDP 212
|
|
| PLN02830 |
PLN02830 |
UDP-sugar pyrophosphorylase |
94-320 |
4.91e-09 |
|
UDP-sugar pyrophosphorylase
Pssm-ID: 215444 Cd Length: 615 Bit Score: 58.93 E-value: 4.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817975 94 EEEGFRQIslNKVAVLLLAGGQGTRLGVTYPKgmyrVGLPSRKT----LYQLQAERIRRVEQLA-GERHGTRCTVPWYVM 168
Cdd:PLN02830 119 EEAGLREA--GNAAFVLVAGGLGERLGYSGIK----VALPTETAtgtcYLQLYIESILALQERAkKRKAKKGRKIPLVIM 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817975 169 TSEFTLGPTAEFFREHNFFHLDPANVVMFEQRLLPAVT-FDGKVILERKD--KVAMAPDGNGGLYCALEDHKILEDMERR 245
Cdd:PLN02830 193 TSDDTHARTLKLLERNDYFGMDPDQVTLLKQEKVACLMdNDARLALDPNDpyKIQTKPHGHGDVHALLYSSGLLDKWLSA 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817975 246 GVEFVHVYCVDNILVRLADPVFIGFCVLQGADCGAKVV-EKAypEEPVGVVCQ---VDGVPQV--VEYSEISPetaQLRA 319
Cdd:PLN02830 273 GKKWVVFFQDTNGLVFKAIPAALGVSATKGFDMNSLAVpRKA--KEAIGAIAKlthKDGREMVinVEYNQLDP---LLRA 347
|
.
gi 578817975 320 S 320
Cdd:PLN02830 348 T 348
|
|
| UGPase_euk |
cd00897 |
Eukaryotic UGPase catalyses the synthesis of UDP-Glucose; UGPase (UDP-Glucose ... |
103-257 |
2.28e-07 |
|
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: 52.63 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817975 103 LNKVAVLLLAGGQGTRLGVTYPKGMyrVGLPSRKTLYQLQaerIRRVEQLaGERHGTRctVPWYVMTSEFTLGPTAEFFR 182
Cdd:cd00897 1 LNKLVVLKLNGGLGTSMGCTGPKSL--IEVRDGKTFLDLT---VQQIEHL-NKTYGVD--VPLVLMNSFNTDEDTKKILK 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578817975 183 EHNFFHLDpanVVMFEQRLLPAVTFDGKVILERK---DKVAMAPDGNGGLYCALEDHKILEDMERRGVEFVHVYCVDN 257
Cdd:cd00897 73 KYAGVNVD---IHTFNQSRYPRISKETLLPVPSWadsPDEEWYPPGHGDIFESLYNSGLLDTLLAQGKEYLFVSNIDN 147
|
|
| PLN02474 |
PLN02474 |
UTP--glucose-1-phosphate uridylyltransferase |
103-258 |
9.29e-06 |
|
UTP--glucose-1-phosphate uridylyltransferase
Pssm-ID: 178092 Cd Length: 469 Bit Score: 47.95 E-value: 9.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817975 103 LNKVAVLLLAGGQGTRLGVTYPKGMYRV--GLpsrkTLYQLQAERIRRVEQLAGerhgtrCTVPWYVMTSEFTLGPTAEF 180
Cdd:PLN02474 77 LDKLVVLKLNGGLGTTMGCTGPKSVIEVrnGL----TFLDLIVIQIENLNKKYG------CNVPLLLMNSFNTHDDTQKI 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817975 181 FREHNFFHLDpanVVMFEQRLLPAVTFDGKVILERK---DKVAMAPDGNGGLYCALEDHKILEDMERRGVEFVHVYCVDN 257
Cdd:PLN02474 147 VEKYTNSNIE---IHTFNQSQYPRVVADDFVPWPSKgktDKDGWYPPGHGDVFPSLMNSGKLDALLSQGKEYVFIANSDN 223
|
.
gi 578817975 258 I 258
Cdd:PLN02474 224 L 224
|
|
| CDP-ME_synthetase |
cd02516 |
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ... |
106-131 |
7.34e-03 |
|
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; 4-diphosphocytidyl-2-methyl-D-erythritol synthase (CDP-ME), also called 2C-methyl-d-erythritol 4-phosphate cytidylyltransferase catalyzes the third step in the alternative (non-mevalonate) pathway of Isopentenyl diphosphate (IPP) biosynthesis: the formation of 4-diphosphocytidyl-2C-methyl-D-erythritol from CTP and 2C-methyl-D-erythritol 4-phosphate. This mevalonate independent pathway that utilizes pyruvate and glyceraldehydes 3-phosphate as starting materials for production of IPP occurs in a variety of bacteria, archaea and plant cells, but is absent in mammals. Thus, CDP-ME synthetase is an attractive targets for the structure-based design of selective antibacterial, herbicidal and antimalarial drugs.
Pssm-ID: 133009 [Multi-domain] Cd Length: 218 Bit Score: 37.89 E-value: 7.34e-03
10 20
....*....|....*....|....*.
gi 578817975 106 VAVLLLAGGQGTRLGVTYPKGMYRVG 131
Cdd:cd02516 1 VAAIILAAGSGSRMGADIPKQFLELG 26
|
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|