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Conserved domains on  [gi|30520375|ref|NP_598567|]
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UDP-N-acetylhexosamine pyrophosphorylase isoform 2 [Mus musculus]

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
PubMed:  12691742|9445404|10521532
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 ...
 88-410 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: 590.35  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375  88 QAWESEGLSQISQNKVAVLLLAGGQGTRLGVSYPKGMYDVGLPSHKTLFQIQAERILKLQQLAEKHHGNKCTIPWYIMTS 167
Cdd:cd04193   1 KEWEEAGLKAIAEGKVAVLLLAGGQGTRLGFDGPKGMFPVGLPSKKSLFQLQAERILKLQELAGEASGKKVPIPWYIMTS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375 168 GRTMESTKEFFTKHKFFGLKKENVVFFQQGMLPAMSFDGKIILEEKNKVSMAPDGNGGLYRALAAQNIVEDMEQRGICSI 247
Cdd:cd04193  81 EATHEETRKFFKENNYFGLDPEQVHFFQQGMLPCVDFDGKILLEEKGKIAMAPNGNGGLYKALQTAGILEDMKKRGIKYI 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375 248 HVYCVDNILVKVADPRFIGFCIQKGADCGAKVVEKTNPTEPVGVVCRVDGVYQVVEYSEISLATAQRRSSDGRLLFNAGN 327
Cdd:cd04193 161 HVYSVDNILVKVADPVFIGFCISKGADVGAKVVRKRYPTEKVGVVVLVDGKPQVVEYSEISDELAEKRDADGELQYNAGN 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375 328 IANHFFTVPFLKDVVNVYEPQLQHHVAQKKIPYVDSQGHFIKPDKPNGIKMEKFVFDIFQFAKKFVVYEVLREDEFSPLK 407
Cdd:cd04193 241 IANHFFSLDFLEKAAEMEEPSLPYHIAKKKIPYVDLEGGLVKPDEPNGIKLELFIFDVFPFAKNFVCLEVDREEEFSPLK 320


                ...
gi 30520375 408 NAD 410
Cdd:cd04193 321 NAD 323
 
Name Accession Description Interval E-value
UDPGlcNAc_PPase cd04193
UDPGlcNAc pyrophosphorylase catalayzes the synthesis of UDPGlcNAc; UDP-N-acetylglucosamine ...
 88-410 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: 590.35  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375  88 QAWESEGLSQISQNKVAVLLLAGGQGTRLGVSYPKGMYDVGLPSHKTLFQIQAERILKLQQLAEKHHGNKCTIPWYIMTS 167
Cdd:cd04193   1 KEWEEAGLKAIAEGKVAVLLLAGGQGTRLGFDGPKGMFPVGLPSKKSLFQLQAERILKLQELAGEASGKKVPIPWYIMTS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375 168 GRTMESTKEFFTKHKFFGLKKENVVFFQQGMLPAMSFDGKIILEEKNKVSMAPDGNGGLYRALAAQNIVEDMEQRGICSI 247
Cdd:cd04193  81 EATHEETRKFFKENNYFGLDPEQVHFFQQGMLPCVDFDGKILLEEKGKIAMAPNGNGGLYKALQTAGILEDMKKRGIKYI 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375 248 HVYCVDNILVKVADPRFIGFCIQKGADCGAKVVEKTNPTEPVGVVCRVDGVYQVVEYSEISLATAQRRSSDGRLLFNAGN 327
Cdd:cd04193 161 HVYSVDNILVKVADPVFIGFCISKGADVGAKVVRKRYPTEKVGVVVLVDGKPQVVEYSEISDELAEKRDADGELQYNAGN 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375 328 IANHFFTVPFLKDVVNVYEPQLQHHVAQKKIPYVDSQGHFIKPDKPNGIKMEKFVFDIFQFAKKFVVYEVLREDEFSPLK 407
Cdd:cd04193 241 IANHFFSLDFLEKAAEMEEPSLPYHIAKKKIPYVDLEGGLVKPDEPNGIKLELFIFDVFPFAKNFVCLEVDREEEFSPLK 320


                ...
gi 30520375 408 NAD 410
Cdd:cd04193 321 NAD 323
PLN02435 PLN02435
probable UDP-N-acetylglucosamine pyrophosphorylase
 6-505 1.45e-140

probable UDP-N-acetylglucosamine pyrophosphorylase


Pssm-ID: 215238  Cd Length: 493  Bit Score: 414.27  E-value: 1.45e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375    6 LKQRLSQAGQEHLLQFWNELSEAQQVELYMELQAMNFEELNSFFRKAIGEfdrsshQEKVDARMEPVPRQVLGSAT-RDQ 84
Cdd:PLN02435  25 LLERLKDYGQEDAFALWDELSPEERDLLVRDIESLDLPRIDRIIRCSLRS------QGLPVPAIEPVPENSVSTVEeRTP 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375   85 EQLQAWESEGLSQISQNKVAVLLLAGGQGTRLGVSYPKGMYDVGLPSHKTLFQIQAERILKLQQLA----EKHHGNKCTI 160
Cdd:PLN02435  99 EDRERWWKMGLKAISEGKLAVVLLSGGQGTRLGSSDPKGCFNIGLPSGKSLFQLQAERILCVQRLAaqasSEGPGRPVTI 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375  161 PWYIMTSGRTMESTKEFFTKHKFFGLKKENVVFFQQGMLPAMSFDGKIILEEKNKVSMAPDGNGGLYRALAAQNIVEDME 240
Cdd:PLN02435 179 HWYIMTSPFTDEATRKFFESHKYFGLEADQVTFFQQGTLPCVSKDGKFIMETPFKVAKAPDGNGGVYAALKSSRLLEDMA 258

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375  241 QRGICSIHVYCVDNILVKVADPRFIGFCIQKGADCGAKVVEKTNPTEPVGVVCR--VDGVYQVVEYSEI--SLATAQRRS 316
Cdd:PLN02435 259 SRGIKYVDCYGVDNALVRVADPTFLGYFIDKGVASAAKVVRKAYPQEKVGVFVRrgKGGPLTVVEYSELdqAMASAINQQ 338

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375  317 SdGRLLFNAGNIANHFFTVPFLKDVVNVYEPQLQHHVAQKKIPYVDSQghfikpdkPNGIKMEKFVFDIFQFAKKFVVYE 396
Cdd:PLN02435 339 T-GRLRYCWSNVCLHMFTLDFLNQVANGLEKDSIYHLAEKKIPSIHGY--------TMGLKLEQFIFDAFPYAPSTALFE 409

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375  397 VLREDEFSPLKNADSQNgKDNPTTARHALMSLHHCWVLNAGGhFIdengsrLPAIPRATNGkseaitadvnhnlkdandv 476
Cdd:PLN02435 410 VLREEEFAPVKNANGSN-FDTPESARLLVLRLHTRWVVAAGG-FL------THSVPLYATG------------------- 462

                        490       500
                 ....*....|....*....|....*....
gi 30520375  477 piqCEISPLISYAGEGLEGYVADKEFHAP 505
Cdd:PLN02435 463 ---VEVSPLCSYAGENLEAICRGRTFHAP 488
QRI1 COG4284
UDP-N-acetylglucosamine pyrophosphorylase [Carbohydrate transport and metabolism];
6-418 5.25e-137

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


Pssm-ID: 443425  Cd Length: 402  Bit Score: 401.96  E-value: 5.25e-137
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375   6 LKQRLSQAGQEHLLQFWNELSEAQQVELYMELQAMNFEElnsfFRKAIGEFDRSSHQEKVDAR--MEPVPRQVLGSATRD 83
Cdd:COG4284   1 LIEKLEPHGQEHLLRFWDELSEAQQKMLEAQIEEIDIDV----FQHLYRQLVLAEGATGLIPEsdIEPAPVTDLPLTDLD 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375  84 QEQLQAWESEGLSQISQNKVAVLLLAGGQGTRLGVSYPKGMYDVGLPSHKTLFQIQAERILKlqqlAEKHHGnkCTIPWY 163
Cdd:COG4284  77 EVDRDRAEEAGEEALRAGKVAVILLAGGQGTRLGFDGPKGLLPVRPVKGKSLFDLIAEQVLA----ARRRYG--VPLPLY 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375 164 IMTSGRTMESTKEFFTKHKFFGLKKENVVFFQQGMLPAM-SFDGKIILEEKNKVSMAPDGNGGLYRALAAQNIVEDMEQR 242
Cdd:COG4284 151 IMTSFRTHEDTLAFLEEHDYFGLDGLPVHFFLQGMEPALdADLGPVLLPADPELELCPPGHGGIYTALLASGLLDKLLER 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375 243 GICSIHVYCVDNILVKVADPRFIGFCIQKGADCGAKVVEKTNPTEPVGVVCRVDGVYQVVEYSEisLATAQRRSSDGRLL 322
Cdd:COG4284 231 GIRYLFVSNVDNPLGAVPDPAFAGWHAASGAPFTAKVVRRTPPDEKVGHLARVDGRLILREYSQ--LPDEEAEAFTGELR 308

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375 323 FNAGNIANHFFTVPFLKDVVNVYEPQLQHHVAQKKIPYVDSQGhfiKPDKPNGIKMEKFVFDIFQFAKKFVVYEVLREDE 402
Cdd:COG4284 309 HPYGNINNHWFDLDFLKRLLDERGLGLPLHRAEKKVDPLDESG---KPTSPNVIKFETFMFDAIPLFDGAVAIEVDREER 385

                       410
                ....*....|....*.
gi 30520375 403 FSPLKNAdsqNGKDNP 418
Cdd:COG4284 386 FAPVKNT---NGSDSP 398
UDPGP pfam01704
UTP--glucose-1-phosphate uridylyltransferase; This family consists of UTP--glucose-1-phosphate ...
 45-471 8.93e-122

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: 363.37  E-value: 8.93e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375    45 LNSFFRKAIGEFDRSSHQEKVD-ARMEPVPRQVLgsatRDQEQLQA--WESEGLsqisQNKVAVLLLAGGQGTRLGVSYP 121
Cdd:pfam01704   1 LDGFFKLFSRYLSEKGKQEKIDwDKIKPPPEEEI----VDYEDLQEpeEEIKEL----LNKLAVLKLNGGLGTSMGCVGP 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375   122 KGMYDVGlpSHKTLFQIQAERILKLqqlaekHHGNKCTIPWYIMTSGRTMESTKEFFTKHKFfglKKENVVFFQQGMLPA 201
Cdd:pfam01704  73 KSLIEVR--DGLTFLDLIVQQIEHL------NKKYNVDVPLVLMNSFNTDEDTKKIIRKYKG---HKVDILTFNQSRYPR 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375   202 MSFDGKIILEEK---NKVSMAPDGNGGLYRALAAQNIVEDMEQRGICSIHVYCVDNiLVKVADPRFIGFCIQKGADCGAK 278
Cdd:pfam01704 142 IDKDTLLPVPKSadsDEEEWYPPGHGDLYESLYNSGLLDKLLAEGKEYLFVSNIDN-LGATVDLNILNYMVDNGAEFLME 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375   279 VVEKTNPTEPVGVVCRVDGVYQVVEYSEI-SLATAQRRSSDGRLLFNAGNIanhFFTVPFLKDVVNvyEPQLQHHVAQKK 357
Cdd:pfam01704 221 VTDKTRADVKGGTLIEYDGKLRLLEIAQVpKEHVDEFKSIKKFKIFNTNNI---WINLKALKRVVE--EGELQLEIIVNK 295

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375   358 iPYVDSQGHFIKPDKPNGIKMEKFvfdifqfaKKFVVYEVLReDEFSPLKNADSqngkdnpttarhALMSLHHCWVLNAG 437
Cdd:pfam01704 296 -KTLDNGENVIQLETAVGAAIKNF--------KNAIGINVPR-SRFLPVKTTSD------------LLLVMSDLYVLNHG 353

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 30520375   438 -------------------GHF--IDENGSRLPAIPRATNGKSEAITADV----NHNLK 471
Cdd:pfam01704 354 slimnpkrmfgtppvvllgDHFkkVDEFLKRFPSIPDLLELDHLTVSGDVtfgrNVTLK 412
 
Name Accession Description Interval E-value
UDPGlcNAc_PPase cd04193
UDPGlcNAc pyrophosphorylase catalayzes the synthesis of UDPGlcNAc; UDP-N-acetylglucosamine ...
 88-410 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: 590.35  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375  88 QAWESEGLSQISQNKVAVLLLAGGQGTRLGVSYPKGMYDVGLPSHKTLFQIQAERILKLQQLAEKHHGNKCTIPWYIMTS 167
Cdd:cd04193   1 KEWEEAGLKAIAEGKVAVLLLAGGQGTRLGFDGPKGMFPVGLPSKKSLFQLQAERILKLQELAGEASGKKVPIPWYIMTS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375 168 GRTMESTKEFFTKHKFFGLKKENVVFFQQGMLPAMSFDGKIILEEKNKVSMAPDGNGGLYRALAAQNIVEDMEQRGICSI 247
Cdd:cd04193  81 EATHEETRKFFKENNYFGLDPEQVHFFQQGMLPCVDFDGKILLEEKGKIAMAPNGNGGLYKALQTAGILEDMKKRGIKYI 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375 248 HVYCVDNILVKVADPRFIGFCIQKGADCGAKVVEKTNPTEPVGVVCRVDGVYQVVEYSEISLATAQRRSSDGRLLFNAGN 327
Cdd:cd04193 161 HVYSVDNILVKVADPVFIGFCISKGADVGAKVVRKRYPTEKVGVVVLVDGKPQVVEYSEISDELAEKRDADGELQYNAGN 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375 328 IANHFFTVPFLKDVVNVYEPQLQHHVAQKKIPYVDSQGHFIKPDKPNGIKMEKFVFDIFQFAKKFVVYEVLREDEFSPLK 407
Cdd:cd04193 241 IANHFFSLDFLEKAAEMEEPSLPYHIAKKKIPYVDLEGGLVKPDEPNGIKLELFIFDVFPFAKNFVCLEVDREEEFSPLK 320


                ...
gi 30520375 408 NAD 410
Cdd:cd04193 321 NAD 323
PLN02435 PLN02435
probable UDP-N-acetylglucosamine pyrophosphorylase
 6-505 1.45e-140

probable UDP-N-acetylglucosamine pyrophosphorylase


Pssm-ID: 215238  Cd Length: 493  Bit Score: 414.27  E-value: 1.45e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375    6 LKQRLSQAGQEHLLQFWNELSEAQQVELYMELQAMNFEELNSFFRKAIGEfdrsshQEKVDARMEPVPRQVLGSAT-RDQ 84
Cdd:PLN02435  25 LLERLKDYGQEDAFALWDELSPEERDLLVRDIESLDLPRIDRIIRCSLRS------QGLPVPAIEPVPENSVSTVEeRTP 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375   85 EQLQAWESEGLSQISQNKVAVLLLAGGQGTRLGVSYPKGMYDVGLPSHKTLFQIQAERILKLQQLA----EKHHGNKCTI 160
Cdd:PLN02435  99 EDRERWWKMGLKAISEGKLAVVLLSGGQGTRLGSSDPKGCFNIGLPSGKSLFQLQAERILCVQRLAaqasSEGPGRPVTI 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375  161 PWYIMTSGRTMESTKEFFTKHKFFGLKKENVVFFQQGMLPAMSFDGKIILEEKNKVSMAPDGNGGLYRALAAQNIVEDME 240
Cdd:PLN02435 179 HWYIMTSPFTDEATRKFFESHKYFGLEADQVTFFQQGTLPCVSKDGKFIMETPFKVAKAPDGNGGVYAALKSSRLLEDMA 258

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375  241 QRGICSIHVYCVDNILVKVADPRFIGFCIQKGADCGAKVVEKTNPTEPVGVVCR--VDGVYQVVEYSEI--SLATAQRRS 316
Cdd:PLN02435 259 SRGIKYVDCYGVDNALVRVADPTFLGYFIDKGVASAAKVVRKAYPQEKVGVFVRrgKGGPLTVVEYSELdqAMASAINQQ 338

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375  317 SdGRLLFNAGNIANHFFTVPFLKDVVNVYEPQLQHHVAQKKIPYVDSQghfikpdkPNGIKMEKFVFDIFQFAKKFVVYE 396
Cdd:PLN02435 339 T-GRLRYCWSNVCLHMFTLDFLNQVANGLEKDSIYHLAEKKIPSIHGY--------TMGLKLEQFIFDAFPYAPSTALFE 409

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375  397 VLREDEFSPLKNADSQNgKDNPTTARHALMSLHHCWVLNAGGhFIdengsrLPAIPRATNGkseaitadvnhnlkdandv 476
Cdd:PLN02435 410 VLREEEFAPVKNANGSN-FDTPESARLLVLRLHTRWVVAAGG-FL------THSVPLYATG------------------- 462

                        490       500
                 ....*....|....*....|....*....
gi 30520375  477 piqCEISPLISYAGEGLEGYVADKEFHAP 505
Cdd:PLN02435 463 ---VEVSPLCSYAGENLEAICRGRTFHAP 488
QRI1 COG4284
UDP-N-acetylglucosamine pyrophosphorylase [Carbohydrate transport and metabolism];
6-418 5.25e-137

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


Pssm-ID: 443425  Cd Length: 402  Bit Score: 401.96  E-value: 5.25e-137
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375   6 LKQRLSQAGQEHLLQFWNELSEAQQVELYMELQAMNFEElnsfFRKAIGEFDRSSHQEKVDAR--MEPVPRQVLGSATRD 83
Cdd:COG4284   1 LIEKLEPHGQEHLLRFWDELSEAQQKMLEAQIEEIDIDV----FQHLYRQLVLAEGATGLIPEsdIEPAPVTDLPLTDLD 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375  84 QEQLQAWESEGLSQISQNKVAVLLLAGGQGTRLGVSYPKGMYDVGLPSHKTLFQIQAERILKlqqlAEKHHGnkCTIPWY 163
Cdd:COG4284  77 EVDRDRAEEAGEEALRAGKVAVILLAGGQGTRLGFDGPKGLLPVRPVKGKSLFDLIAEQVLA----ARRRYG--VPLPLY 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375 164 IMTSGRTMESTKEFFTKHKFFGLKKENVVFFQQGMLPAM-SFDGKIILEEKNKVSMAPDGNGGLYRALAAQNIVEDMEQR 242
Cdd:COG4284 151 IMTSFRTHEDTLAFLEEHDYFGLDGLPVHFFLQGMEPALdADLGPVLLPADPELELCPPGHGGIYTALLASGLLDKLLER 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375 243 GICSIHVYCVDNILVKVADPRFIGFCIQKGADCGAKVVEKTNPTEPVGVVCRVDGVYQVVEYSEisLATAQRRSSDGRLL 322
Cdd:COG4284 231 GIRYLFVSNVDNPLGAVPDPAFAGWHAASGAPFTAKVVRRTPPDEKVGHLARVDGRLILREYSQ--LPDEEAEAFTGELR 308

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375 323 FNAGNIANHFFTVPFLKDVVNVYEPQLQHHVAQKKIPYVDSQGhfiKPDKPNGIKMEKFVFDIFQFAKKFVVYEVLREDE 402
Cdd:COG4284 309 HPYGNINNHWFDLDFLKRLLDERGLGLPLHRAEKKVDPLDESG---KPTSPNVIKFETFMFDAIPLFDGAVAIEVDREER 385

                       410
                ....*....|....*.
gi 30520375 403 FSPLKNAdsqNGKDNP 418
Cdd:COG4284 386 FAPVKNT---NGSDSP 398
UDPGP pfam01704
UTP--glucose-1-phosphate uridylyltransferase; This family consists of UTP--glucose-1-phosphate ...
 45-471 8.93e-122

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: 363.37  E-value: 8.93e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375    45 LNSFFRKAIGEFDRSSHQEKVD-ARMEPVPRQVLgsatRDQEQLQA--WESEGLsqisQNKVAVLLLAGGQGTRLGVSYP 121
Cdd:pfam01704   1 LDGFFKLFSRYLSEKGKQEKIDwDKIKPPPEEEI----VDYEDLQEpeEEIKEL----LNKLAVLKLNGGLGTSMGCVGP 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375   122 KGMYDVGlpSHKTLFQIQAERILKLqqlaekHHGNKCTIPWYIMTSGRTMESTKEFFTKHKFfglKKENVVFFQQGMLPA 201
Cdd:pfam01704  73 KSLIEVR--DGLTFLDLIVQQIEHL------NKKYNVDVPLVLMNSFNTDEDTKKIIRKYKG---HKVDILTFNQSRYPR 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375   202 MSFDGKIILEEK---NKVSMAPDGNGGLYRALAAQNIVEDMEQRGICSIHVYCVDNiLVKVADPRFIGFCIQKGADCGAK 278
Cdd:pfam01704 142 IDKDTLLPVPKSadsDEEEWYPPGHGDLYESLYNSGLLDKLLAEGKEYLFVSNIDN-LGATVDLNILNYMVDNGAEFLME 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375   279 VVEKTNPTEPVGVVCRVDGVYQVVEYSEI-SLATAQRRSSDGRLLFNAGNIanhFFTVPFLKDVVNvyEPQLQHHVAQKK 357
Cdd:pfam01704 221 VTDKTRADVKGGTLIEYDGKLRLLEIAQVpKEHVDEFKSIKKFKIFNTNNI---WINLKALKRVVE--EGELQLEIIVNK 295

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375   358 iPYVDSQGHFIKPDKPNGIKMEKFvfdifqfaKKFVVYEVLReDEFSPLKNADSqngkdnpttarhALMSLHHCWVLNAG 437
Cdd:pfam01704 296 -KTLDNGENVIQLETAVGAAIKNF--------KNAIGINVPR-SRFLPVKTTSD------------LLLVMSDLYVLNHG 353

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 30520375   438 -------------------GHF--IDENGSRLPAIPRATNGKSEAITADV----NHNLK 471
Cdd:pfam01704 354 slimnpkrmfgtppvvllgDHFkkVDEFLKRFPSIPDLLELDHLTVSGDVtfgrNVTLK 412
UGPase_euk_like cd04180
Eukaryotic UGPase-like includes UDPase and UDPGlcNAc pyrophosphorylase enzymes; This family ...
 103-408 2.04e-118

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: 349.55  E-value: 2.04e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375 103 VAVLLLAGGQGTRLGVSYPKGMYDVGLPSHKTLFQIQAERILKLQQLAEkhhgNKCTIPWYIMTSGRTMESTKEFFTKHK 182
Cdd:cd04180   1 VAVVLLAGGLGTRLGKDGPKSSTDVGLPSGQCFLQLIGEKILTLQEIDL----YSCKIPEQLMNSKYTHEKTQCYFEKIN 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375 183 ffgLKKENVVFFQQGMLPAMSFDGKIILEEKNKVSMAPDGNGGLYRALAAQNIVEDMEQRGICSIHVYCVDNILVKVADP 262
Cdd:cd04180  77 ---QKNSYVITFMQGKLPLKNDDDARDPHNKTKCHLFPCGHGDVVLALIHSGHLNKLLEKGYRYIHFIGVDNLLVKVADP 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375 263 RFIGFCIQKGADCGAKVVEKTNPTEPVGVVCRVD-GVYQVVEYSEISLATAQRR------SSDGRLLFNAGNIANHFFTV 335
Cdd:cd04180 154 LFIGIAIQNRKAINQKVVPKTRNEESGGYRIANInGRVQLLEYDQIKKLLKQKMvnnqipKDIDDAPFFLFNTNNLINFL 233

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30520375 336 PFLKDVVNvyepqlqhhvaqkkipyvdsqghfikpdkpngikmekfvfDIFQFAKKFVVYEVLREDEFSPLKN 408
Cdd:cd04180 234 VEFKDRVD----------------------------------------DIIEFTDDIVGVMVHRAEEFAPVKN 266
PTZ00339 PTZ00339
UDP-N-acetylglucosamine pyrophosphorylase; Provisional
 8-507 5.83e-116

UDP-N-acetylglucosamine pyrophosphorylase; Provisional


Pssm-ID: 240368  Cd Length: 482  Bit Score: 350.96  E-value: 5.83e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375    8 QRLSQAGQEHLLQFWNELSEAQQvelyMELQAMNFEELNSFFRKAIGEFDRSSHQEKVDAR-------------MEPVPR 74
Cdd:PTZ00339   3 KVLTGDGQDHLREALKRRSEGEF----TPLATQILSSLTNVDFKHRNAVLEPKLEEYNAEApvgididsihncnIEPPNN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375   75 QVLGSATRDQEQLQAWESEGLSQISQNKVAVLLLAGGQGTRLGVSYPKGMYDVGLPSHKTLFQIQAERILKLQQLAEKHH 154
Cdd:PTZ00339  79 NTFIDIYEKEKERKELKESGLEIIKKGEVAVLILAGGLGTRLGSDKPKGLLECTPVKKKTLFQFHCEKVRRLEEMAVAVS 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375  155 --GNKCTIPWYIMTSGRTMESTKEFFTKHKFFGLKKENVVFFQQGMLPAMS-FDGKIILEEKNKVSMAPDGNGGLYRALA 231
Cdd:PTZ00339 159 ggGDDPTIYILVLTSSFNHDQTRQFLEENNFFGLDKEQVIFFKQSSLPCYDeNTGRFIMSSQGSLCTAPGGNGDVFKALA 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375  232 AQNIVEDMEQRGICSIHVYCVDNILVKVADPRFIGFCIQKGADCGAKVVEKTNPTEPVGVVCRVDGVYQVVEYSEIS-LA 310
Cdd:PTZ00339 239 KCSELMDIVRKGIKYVQVISIDNILAKVLDPEFIGLASSFPAHDVLNKCVKREDDESVGVFCLKDYEWQVVEYTEINeRI 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375  311 TAQRRSSDGRLLFNAGNIANHFFTVPFLKDVVNVY-EPQLQHHVAQKKIPYVDSQGhfikpDKPNGIKMEKFVFDIFQFA 389
Cdd:PTZ00339 319 LNNDELLTGELAFNYGNICSHIFSLDFLKKVAANRlYESTPYHAARKKIPYINGPT-----DKTMGIKLEAFIFDIFRYA 393

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375  390 KKFVVYEVLREDEFSPLKNADSQNGkDNPTTARHALMSLHHCWVLNAGghfidengsrlpaIPRATNGKSEAitadvnhn 469
Cdd:PTZ00339 394 KNVLILEVDREDEFAPIKNADGAAA-DTILNAQKLLLSLHTRWLEAAL-------------ETVAGNPREGL-------- 451

                        490       500       510
                 ....*....|....*....|....*....|....*...
gi 30520375  470 lkdandvpIQCEISPLISYAGEGLEGYVADKEFHAPLI 507
Cdd:PTZ00339 452 --------NLCEISPLVSYGGEGLFQYPGKKILGLPEI 481
UGGPase cd06424
UGGPase catalyzes the synthesis of UDP-Glucose/UDP-Galactose; UGGPase: UDP-Galactose/Glucose ...
 103-294 1.60e-18

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: 86.36  E-value: 1.60e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375 103 VAVLLLAGGQGTRLGVSYPKGMYDVGLPSHKTLFQIQAERILKLQQLAEKHHGNKctIPWYIMTSGRTMESTKEFFTKHK 182
Cdd:cd06424   1 AVFVLVAGGLGERLGYSGIKIGLPVELTTNTTYLQYYLNYIRAFQEASKKGEKME--IPFVIMTSDDTHSKTLKLLEENN 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375 183 FFGLKKENVVFFQQGMLPAM-SFDGKIILEEKNKVSMA--PDGNGGLYRALAAQNIVEDMEQRGICSIHVYCVDNILVKV 259
Cdd:cd06424  79 YFGLEKDQVHILKQEKVFCLiDNDAHLALDPDNTYSILtkPHGHGDVHTLLYNSGLLKKWIEAGYKWLVFFQDTNALAFK 158

                       170       180       190
                ....*....|....*....|....*....|....*
gi 30520375 260 ADPRFIGFCIQKGADCGAKVVEKTnPTEPVGVVCR 294
Cdd:cd06424 159 AIPAVLGVSATKSLDMNSLTVPRK-PKEAIGALCK 192
PLN02830 PLN02830
UDP-sugar pyrophosphorylase
 4-224 2.04e-17

UDP-sugar pyrophosphorylase


Pssm-ID: 215444  Cd Length: 615  Bit Score: 85.51  E-value: 2.04e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375    4 NDLKQRLSQAGQEHLLQFWNELSEAQQVELYMELQAMNFEE-----LNSFFRKAIgEFDRSSHQEK--VDARMEPVPR-Q 75
Cdd:PLN02830  28 RALVRRLLELGQSHLFEHWPEPGVDDDDKRRLLEQVARLDEsypggLAAYVSNAK-ELLADSKEGVnpFEGWTPSVPEgE 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375   76 VLGSATRDQEQLqawESEGLSQIsqNKVAVLLLAGGQGTRLGVSYPKgmydVGLPSHKT----LFQIQAERILKLQQLAE 151
Cdd:PLN02830 107 VLEYGSEEFVEL---EEAGLREA--GNAAFVLVAGGLGERLGYSGIK----VALPTETAtgtcYLQLYIESILALQERAK 177

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30520375  152 KHHGNKCT-IPWYIMTSGRTMESTKEFFTKHKFFGLKKENVVFFQQGMLPAMS-FDGKIILEEKN--KVSMAPDGNG 224
Cdd:PLN02830 178 KRKAKKGRkIPLVIMTSDDTHARTLKLLERNDYFGMDPDQVTLLKQEKVACLMdNDARLALDPNDpyKIQTKPHGHG 254
UGPase_euk cd00897
Eukaryotic UGPase catalyses the synthesis of UDP-Glucose; UGPase (UDP-Glucose ...
 101-303 1.47e-08

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: 56.10  E-value: 1.47e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375 101 NKVAVLLLAGGQGTRLGVSYPKGMYDVglPSHKTLFQIQAERILKLQqlaeKHHGnkCTIPWYIMTSGRTMESTKEFFTK 180
Cdd:cd00897   2 NKLVVLKLNGGLGTSMGCTGPKSLIEV--RDGKTFLDLTVQQIEHLN----KTYG--VDVPLVLMNSFNTDEDTKKILKK 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375 181 hkfFGLKKENVVFFQQGMLPAMSFDGKIILEEK---NKVSMAPDGNGGLYRALAAQNIVEDMEQRGICSIHVYCVDNiLV 257
Cdd:cd00897  74 ---YAGVNVDIHTFNQSRYPRISKETLLPVPSWadsPDEEWYPPGHGDIFESLYNSGLLDTLLAQGKEYLFVSNIDN-LG 149

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 30520375 258 KVADPRFIGFCIQKGADCGAKVVEKTNPTEPVGVVCRVDGVYQVVE 303
Cdd:cd00897 150 ATVDLRILNHMVDNKAEYIMEVTDKTRADVKGGTLIQYEGKLRLLE 195
PLN02474 PLN02474
UTP--glucose-1-phosphate uridylyltransferase
 101-307 7.11e-04

UTP--glucose-1-phosphate uridylyltransferase


Pssm-ID: 178092  Cd Length: 469  Bit Score: 42.17  E-value: 7.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375  101 NKVAVLLLAGGQGTRLGVSYPKGMYDV--GLpSHKTLFQIQAERIlklqqlaekHHGNKCTIPWYIMTSGRTMESTKEFF 178
Cdd:PLN02474  78 DKLVVLKLNGGLGTTMGCTGPKSVIEVrnGL-TFLDLIVIQIENL---------NKKYGCNVPLLLMNSFNTHDDTQKIV 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520375  179 TKHKFFGLKkenVVFFQQGMLPAMSFDGKIILEEKNKVSMA---PDGNGGLYRALAAQNIVEDMEQRGICSIHVYCVDNi 255
Cdd:PLN02474 148 EKYTNSNIE---IHTFNQSQYPRVVADDFVPWPSKGKTDKDgwyPPGHGDVFPSLMNSGKLDALLSQGKEYVFIANSDN- 223

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 30520375  256 LVKVADPRFIGFCIQKGADCGAKVVEKTNPTEPVGVVCRVDGVYQVVEYSEI 307
Cdd:PLN02474 224 LGAIVDLKILNHLIQNKNEYCMEVTPKTLADVKGGTLISYEGKVQLLEIAQV 275
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 103-137 6.73e-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: 38.27  E-value: 6.73e-03
                        10        20        30
                ....*....|....*....|....*....|....*
gi 30520375 103 VAVLLLAGGQGTRLGVSYPKGMYDVGlpsHKTLFQ 137
Cdd:cd02516   1 VAAIILAAGSGSRMGADIPKQFLELG---GKPVLE 32
 
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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