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Conserved domains on  [gi|1743150800|ref|XP_030679904|]
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UDP-N-acetylhexosamine pyrophosphorylase isoform X2 [Nomascus leucogenys]

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: 596.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800  88 QSWESEGLFQISQNKVAVLLLAGGQGTRLGVAYPKGMYDVGLPSRKTLFQIQAERILKLQQVAEKYYGNKCIIPWYIMTS 167
Cdd:cd04193     1 KEWEEAGLKAIAEGKVAVLLLAGGQGTRLGFDGPKGMFPVGLPSKKSLFQLQAERILKLQELAGEASGKKVPIPWYIMTS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800 168 GRTMESTKEFFTKHKYFGLKKENVIFFQQGMLPAMSFDGKIILEEKNKVSMAPDGNGGLYRALAAQNIVEDMEQRGIWSI 247
Cdd:cd04193    81 EATHEETRKFFKENNYFGLDPEQVHFFQQGMLPCVDFDGKILLEEKGKIAMAPNGNGGLYKALQTAGILEDMKKRGIKYI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800 248 HVYCVDNILVKVADPRFIGFCIQKGADCGAKVVEKTNPTEPVGVVCRVDGVYQVVEYSEISLATAQKRSSDGRLLFNAGN 327
Cdd:cd04193   161 HVYSVDNILVKVADPVFIGFCISKGADVGAKVVRKRYPTEKVGVVVLVDGKPQVVEYSEISDELAEKRDADGELQYNAGN 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800 328 IANHFFTVPFLRDVVNVYEPQLQHHVAQKKIPYVDTQGQLIKPDKPNGIKMEKFVFDIFQFAKKFVVYEVLREDEFSPLK 407
Cdd:cd04193   241 IANHFFSLDFLEKAAEMEEPSLPYHIAKKKIPYVDLEGGLVKPDEPNGIKLELFIFDVFPFAKNFVCLEVDREEEFSPLK 320


                  ...
gi 1743150800 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: 596.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800  88 QSWESEGLFQISQNKVAVLLLAGGQGTRLGVAYPKGMYDVGLPSRKTLFQIQAERILKLQQVAEKYYGNKCIIPWYIMTS 167
Cdd:cd04193     1 KEWEEAGLKAIAEGKVAVLLLAGGQGTRLGFDGPKGMFPVGLPSKKSLFQLQAERILKLQELAGEASGKKVPIPWYIMTS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800 168 GRTMESTKEFFTKHKYFGLKKENVIFFQQGMLPAMSFDGKIILEEKNKVSMAPDGNGGLYRALAAQNIVEDMEQRGIWSI 247
Cdd:cd04193    81 EATHEETRKFFKENNYFGLDPEQVHFFQQGMLPCVDFDGKILLEEKGKIAMAPNGNGGLYKALQTAGILEDMKKRGIKYI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800 248 HVYCVDNILVKVADPRFIGFCIQKGADCGAKVVEKTNPTEPVGVVCRVDGVYQVVEYSEISLATAQKRSSDGRLLFNAGN 327
Cdd:cd04193   161 HVYSVDNILVKVADPVFIGFCISKGADVGAKVVRKRYPTEKVGVVVLVDGKPQVVEYSEISDELAEKRDADGELQYNAGN 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800 328 IANHFFTVPFLRDVVNVYEPQLQHHVAQKKIPYVDTQGQLIKPDKPNGIKMEKFVFDIFQFAKKFVVYEVLREDEFSPLK 407
Cdd:cd04193   241 IANHFFSLDFLEKAAEMEEPSLPYHIAKKKIPYVDLEGGLVKPDEPNGIKLELFIFDVFPFAKNFVCLEVDREEEFSPLK 320


                  ...
gi 1743150800 408 NAD 410
Cdd:cd04193   321 NAD 323
PLN02435 PLN02435
probable UDP-N-acetylglucosamine pyrophosphorylase
 10-489 1.15e-137

probable UDP-N-acetylglucosamine pyrophosphorylase


Pssm-ID: 215238  Cd Length: 493  Bit Score: 406.56  E-value: 1.15e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800  10 LSKAGQEHLLRYWNELEEAQQVELYAELQAMNFEELNFFFQKAIEGfnqsshQKNVDARMEPVPREVLGSAT-RDQDQLQ 88
Cdd:PLN02435   29 LKDYGQEDAFALWDELSPEERDLLVRDIESLDLPRIDRIIRCSLRS------QGLPVPAIEPVPENSVSTVEeRTPEDRE 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800  89 SWESEGLFQISQNKVAVLLLAGGQGTRLGVAYPKGMYDVGLPSRKTLFQIQAERILKLQ----QVAEKYYGNKCIIPWYI 164
Cdd:PLN02435  103 RWWKMGLKAISEGKLAVVLLSGGQGTRLGSSDPKGCFNIGLPSGKSLFQLQAERILCVQrlaaQASSEGPGRPVTIHWYI 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800 165 MTSGRTMESTKEFFTKHKYFGLKKENVIFFQQGMLPAMSFDGKIILEEKNKVSMAPDGNGGLYRALAAQNIVEDMEQRGI 244
Cdd:PLN02435  183 MTSPFTDEATRKFFESHKYFGLEADQVTFFQQGTLPCVSKDGKFIMETPFKVAKAPDGNGGVYAALKSSRLLEDMASRGI 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800 245 WSIHVYCVDNILVKVADPRFIGFCIQKGADCGAKVVEKTNPTEPVGVVCR--VDGVYQVVEYSEI--SLATAQKRSSdGR 320
Cdd:PLN02435  263 KYVDCYGVDNALVRVADPTFLGYFIDKGVASAAKVVRKAYPQEKVGVFVRrgKGGPLTVVEYSELdqAMASAINQQT-GR 341

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800 321 LLFNAGNIANHFFTVPFLRDVVNVYEPQLQHHVAQKKIPYVDTQGQlikpdkpnGIKMEKFVFDIFQFAKKFVVYEVLRE 400
Cdd:PLN02435  342 LRYCWSNVCLHMFTLDFLNQVANGLEKDSIYHLAEKKIPSIHGYTM--------GLKLEQFIFDAFPYAPSTALFEVLRE 413

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800 401 DEFSPLKNADSQNgKDNPTTARHALMSLHHCWVLNAGGhFIdengsrlpaiprlkdANDVPIQ---CEISPLISYAGEGL 477
Cdd:PLN02435  414 EEFAPVKNANGSN-FDTPESARLLVLRLHTRWVVAAGG-FL---------------THSVPLYatgVEVSPLCSYAGENL 476

                         490
                  ....*....|..
gi 1743150800 478 ESYVADKEFHAP 489
Cdd:PLN02435  477 EAICRGRTFHAP 488
QRI1 COG4284
UDP-N-acetylglucosamine pyrophosphorylase [Carbohydrate transport and metabolism];
6-418 9.92e-136

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


Pssm-ID: 443425  Cd Length: 402  Bit Score: 398.10  E-value: 9.92e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800   6 LKLTLSKAGQEHLLRYWNELEEAQQVELYAELQAMNFEELNFFFQKAIEGFNQSShqKNVDARMEPVPREVLGSATRDQD 85
Cdd:COG4284     1 LIEKLEPHGQEHLLRFWDELSEAQQKMLEAQIEEIDIDVFQHLYRQLVLAEGATG--LIPESDIEPAPVTDLPLTDLDEV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800  86 QLQSWESEGLFQISQNKVAVLLLAGGQGTRLGVAYPKGMYDVGLPSRKTLFQIQAERILKlqqvAEKYYGnkCIIPWYIM 165
Cdd:COG4284    79 DRDRAEEAGEEALRAGKVAVILLAGGQGTRLGFDGPKGLLPVRPVKGKSLFDLIAEQVLA----ARRRYG--VPLPLYIM 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800 166 TSGRTMESTKEFFTKHKYFGLKKENVIFFQQGMLPAM-SFDGKIILEEKNKVSMAPDGNGGLYRALAAQNIVEDMEQRGI 244
Cdd:COG4284   153 TSFRTHEDTLAFLEEHDYFGLDGLPVHFFLQGMEPALdADLGPVLLPADPELELCPPGHGGIYTALLASGLLDKLLERGI 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800 245 WSIHVYCVDNILVKVADPRFIGFCIQKGADCGAKVVEKTNPTEPVGVVCRVDGVYQVVEYSEisLATAQKRSSDGRLLFN 324
Cdd:COG4284   233 RYLFVSNVDNPLGAVPDPAFAGWHAASGAPFTAKVVRRTPPDEKVGHLARVDGRLILREYSQ--LPDEEAEAFTGELRHP 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800 325 AGNIANHFFTVPFLRDVVNVYEPQLQHHVAQKKIPYVDTQGqliKPDKPNGIKMEKFVFDIFQFAKKFVVYEVLREDEFS 404
Cdd:COG4284   311 YGNINNHWFDLDFLKRLLDERGLGLPLHRAEKKVDPLDESG---KPTSPNVIKFETFMFDAIPLFDGAVAIEVDREERFA 387

                         410
                  ....*....|....
gi 1743150800 405 PLKNAdsqNGKDNP 418
Cdd:COG4284   388 PVKNT---NGSDSP 398
UDPGP pfam01704
UTP--glucose-1-phosphate uridylyltransferase; This family consists of UTP--glucose-1-phosphate ...
 45-466 1.47e-124

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: 369.92  E-value: 1.47e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800  45 LNFFFQKAIEGFNQSSHQKNVD-ARMEPVPREVLgsatRDQDQLQS--WESEGLFqisqNKVAVLLLAGGQGTRLGVAYP 121
Cdd:pfam01704   1 LDGFFKLFSRYLSEKGKQEKIDwDKIKPPPEEEI----VDYEDLQEpeEEIKELL----NKLAVLKLNGGLGTSMGCVGP 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800 122 KGMYDVGlpSRKTLFQIQAERILKLQQvaeKYygnKCIIPWYIMTSGRTMESTKEFFTKhkYFGlKKENVIFFQQGMLPA 201
Cdd:pfam01704  73 KSLIEVR--DGLTFLDLIVQQIEHLNK---KY---NVDVPLVLMNSFNTDEDTKKIIRK--YKG-HKVDILTFNQSRYPR 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800 202 MSFDGKIILEEK---NKVSMAPDGNGGLYRALAAQNIVEDMEQRGIWSIHVYCVDNiLVKVADPRFIGFCIQKGADCGAK 278
Cdd:pfam01704 142 IDKDTLLPVPKSadsDEEEWYPPGHGDLYESLYNSGLLDKLLAEGKEYLFVSNIDN-LGATVDLNILNYMVDNGAEFLME 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800 279 VVEKTNPTEPVGVVCRVDGVYQVVEYSEI-SLATAQKRSSDGRLLFNAGNIanhFFTVPFLRDVVNvyEPQLQHHVAQKK 357
Cdd:pfam01704 221 VTDKTRADVKGGTLIEYDGKLRLLEIAQVpKEHVDEFKSIKKFKIFNTNNI---WINLKALKRVVE--EGELQLEIIVNK 295

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800 358 iPYVDTQGQLIKPDKPNGIKMEKFvfdifqfaKKFVVYEVLReDEFSPLKNADSqngkdnpttarhALMSLHHCWVLNAG 437
Cdd:pfam01704 296 -KTLDNGENVIQLETAVGAAIKNF--------KNAIGINVPR-SRFLPVKTTSD------------LLLVMSDLYVLNHG 353

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 1743150800 438 -------------------GHF--IDENGSRLPAIPRLKDANDVPIQCEI 466
Cdd:pfam01704 354 slimnpkrmfgtppvvllgDHFkkVDEFLKRFPSIPDLLELDHLTVSGDV 403
 
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: 596.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800  88 QSWESEGLFQISQNKVAVLLLAGGQGTRLGVAYPKGMYDVGLPSRKTLFQIQAERILKLQQVAEKYYGNKCIIPWYIMTS 167
Cdd:cd04193     1 KEWEEAGLKAIAEGKVAVLLLAGGQGTRLGFDGPKGMFPVGLPSKKSLFQLQAERILKLQELAGEASGKKVPIPWYIMTS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800 168 GRTMESTKEFFTKHKYFGLKKENVIFFQQGMLPAMSFDGKIILEEKNKVSMAPDGNGGLYRALAAQNIVEDMEQRGIWSI 247
Cdd:cd04193    81 EATHEETRKFFKENNYFGLDPEQVHFFQQGMLPCVDFDGKILLEEKGKIAMAPNGNGGLYKALQTAGILEDMKKRGIKYI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800 248 HVYCVDNILVKVADPRFIGFCIQKGADCGAKVVEKTNPTEPVGVVCRVDGVYQVVEYSEISLATAQKRSSDGRLLFNAGN 327
Cdd:cd04193   161 HVYSVDNILVKVADPVFIGFCISKGADVGAKVVRKRYPTEKVGVVVLVDGKPQVVEYSEISDELAEKRDADGELQYNAGN 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800 328 IANHFFTVPFLRDVVNVYEPQLQHHVAQKKIPYVDTQGQLIKPDKPNGIKMEKFVFDIFQFAKKFVVYEVLREDEFSPLK 407
Cdd:cd04193   241 IANHFFSLDFLEKAAEMEEPSLPYHIAKKKIPYVDLEGGLVKPDEPNGIKLELFIFDVFPFAKNFVCLEVDREEEFSPLK 320


                  ...
gi 1743150800 408 NAD 410
Cdd:cd04193   321 NAD 323
PLN02435 PLN02435
probable UDP-N-acetylglucosamine pyrophosphorylase
 10-489 1.15e-137

probable UDP-N-acetylglucosamine pyrophosphorylase


Pssm-ID: 215238  Cd Length: 493  Bit Score: 406.56  E-value: 1.15e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800  10 LSKAGQEHLLRYWNELEEAQQVELYAELQAMNFEELNFFFQKAIEGfnqsshQKNVDARMEPVPREVLGSAT-RDQDQLQ 88
Cdd:PLN02435   29 LKDYGQEDAFALWDELSPEERDLLVRDIESLDLPRIDRIIRCSLRS------QGLPVPAIEPVPENSVSTVEeRTPEDRE 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800  89 SWESEGLFQISQNKVAVLLLAGGQGTRLGVAYPKGMYDVGLPSRKTLFQIQAERILKLQ----QVAEKYYGNKCIIPWYI 164
Cdd:PLN02435  103 RWWKMGLKAISEGKLAVVLLSGGQGTRLGSSDPKGCFNIGLPSGKSLFQLQAERILCVQrlaaQASSEGPGRPVTIHWYI 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800 165 MTSGRTMESTKEFFTKHKYFGLKKENVIFFQQGMLPAMSFDGKIILEEKNKVSMAPDGNGGLYRALAAQNIVEDMEQRGI 244
Cdd:PLN02435  183 MTSPFTDEATRKFFESHKYFGLEADQVTFFQQGTLPCVSKDGKFIMETPFKVAKAPDGNGGVYAALKSSRLLEDMASRGI 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800 245 WSIHVYCVDNILVKVADPRFIGFCIQKGADCGAKVVEKTNPTEPVGVVCR--VDGVYQVVEYSEI--SLATAQKRSSdGR 320
Cdd:PLN02435  263 KYVDCYGVDNALVRVADPTFLGYFIDKGVASAAKVVRKAYPQEKVGVFVRrgKGGPLTVVEYSELdqAMASAINQQT-GR 341

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800 321 LLFNAGNIANHFFTVPFLRDVVNVYEPQLQHHVAQKKIPYVDTQGQlikpdkpnGIKMEKFVFDIFQFAKKFVVYEVLRE 400
Cdd:PLN02435  342 LRYCWSNVCLHMFTLDFLNQVANGLEKDSIYHLAEKKIPSIHGYTM--------GLKLEQFIFDAFPYAPSTALFEVLRE 413

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800 401 DEFSPLKNADSQNgKDNPTTARHALMSLHHCWVLNAGGhFIdengsrlpaiprlkdANDVPIQ---CEISPLISYAGEGL 477
Cdd:PLN02435  414 EEFAPVKNANGSN-FDTPESARLLVLRLHTRWVVAAGG-FL---------------THSVPLYatgVEVSPLCSYAGENL 476

                         490
                  ....*....|..
gi 1743150800 478 ESYVADKEFHAP 489
Cdd:PLN02435  477 EAICRGRTFHAP 488
QRI1 COG4284
UDP-N-acetylglucosamine pyrophosphorylase [Carbohydrate transport and metabolism];
6-418 9.92e-136

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


Pssm-ID: 443425  Cd Length: 402  Bit Score: 398.10  E-value: 9.92e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800   6 LKLTLSKAGQEHLLRYWNELEEAQQVELYAELQAMNFEELNFFFQKAIEGFNQSShqKNVDARMEPVPREVLGSATRDQD 85
Cdd:COG4284     1 LIEKLEPHGQEHLLRFWDELSEAQQKMLEAQIEEIDIDVFQHLYRQLVLAEGATG--LIPESDIEPAPVTDLPLTDLDEV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800  86 QLQSWESEGLFQISQNKVAVLLLAGGQGTRLGVAYPKGMYDVGLPSRKTLFQIQAERILKlqqvAEKYYGnkCIIPWYIM 165
Cdd:COG4284    79 DRDRAEEAGEEALRAGKVAVILLAGGQGTRLGFDGPKGLLPVRPVKGKSLFDLIAEQVLA----ARRRYG--VPLPLYIM 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800 166 TSGRTMESTKEFFTKHKYFGLKKENVIFFQQGMLPAM-SFDGKIILEEKNKVSMAPDGNGGLYRALAAQNIVEDMEQRGI 244
Cdd:COG4284   153 TSFRTHEDTLAFLEEHDYFGLDGLPVHFFLQGMEPALdADLGPVLLPADPELELCPPGHGGIYTALLASGLLDKLLERGI 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800 245 WSIHVYCVDNILVKVADPRFIGFCIQKGADCGAKVVEKTNPTEPVGVVCRVDGVYQVVEYSEisLATAQKRSSDGRLLFN 324
Cdd:COG4284   233 RYLFVSNVDNPLGAVPDPAFAGWHAASGAPFTAKVVRRTPPDEKVGHLARVDGRLILREYSQ--LPDEEAEAFTGELRHP 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800 325 AGNIANHFFTVPFLRDVVNVYEPQLQHHVAQKKIPYVDTQGqliKPDKPNGIKMEKFVFDIFQFAKKFVVYEVLREDEFS 404
Cdd:COG4284   311 YGNINNHWFDLDFLKRLLDERGLGLPLHRAEKKVDPLDESG---KPTSPNVIKFETFMFDAIPLFDGAVAIEVDREERFA 387

                         410
                  ....*....|....
gi 1743150800 405 PLKNAdsqNGKDNP 418
Cdd:COG4284   388 PVKNT---NGSDSP 398
UDPGP pfam01704
UTP--glucose-1-phosphate uridylyltransferase; This family consists of UTP--glucose-1-phosphate ...
 45-466 1.47e-124

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: 369.92  E-value: 1.47e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800  45 LNFFFQKAIEGFNQSSHQKNVD-ARMEPVPREVLgsatRDQDQLQS--WESEGLFqisqNKVAVLLLAGGQGTRLGVAYP 121
Cdd:pfam01704   1 LDGFFKLFSRYLSEKGKQEKIDwDKIKPPPEEEI----VDYEDLQEpeEEIKELL----NKLAVLKLNGGLGTSMGCVGP 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800 122 KGMYDVGlpSRKTLFQIQAERILKLQQvaeKYygnKCIIPWYIMTSGRTMESTKEFFTKhkYFGlKKENVIFFQQGMLPA 201
Cdd:pfam01704  73 KSLIEVR--DGLTFLDLIVQQIEHLNK---KY---NVDVPLVLMNSFNTDEDTKKIIRK--YKG-HKVDILTFNQSRYPR 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800 202 MSFDGKIILEEK---NKVSMAPDGNGGLYRALAAQNIVEDMEQRGIWSIHVYCVDNiLVKVADPRFIGFCIQKGADCGAK 278
Cdd:pfam01704 142 IDKDTLLPVPKSadsDEEEWYPPGHGDLYESLYNSGLLDKLLAEGKEYLFVSNIDN-LGATVDLNILNYMVDNGAEFLME 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800 279 VVEKTNPTEPVGVVCRVDGVYQVVEYSEI-SLATAQKRSSDGRLLFNAGNIanhFFTVPFLRDVVNvyEPQLQHHVAQKK 357
Cdd:pfam01704 221 VTDKTRADVKGGTLIEYDGKLRLLEIAQVpKEHVDEFKSIKKFKIFNTNNI---WINLKALKRVVE--EGELQLEIIVNK 295

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800 358 iPYVDTQGQLIKPDKPNGIKMEKFvfdifqfaKKFVVYEVLReDEFSPLKNADSqngkdnpttarhALMSLHHCWVLNAG 437
Cdd:pfam01704 296 -KTLDNGENVIQLETAVGAAIKNF--------KNAIGINVPR-SRFLPVKTTSD------------LLLVMSDLYVLNHG 353

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 1743150800 438 -------------------GHF--IDENGSRLPAIPRLKDANDVPIQCEI 466
Cdd:pfam01704 354 slimnpkrmfgtppvvllgDHFkkVDEFLKRFPSIPDLLELDHLTVSGDV 403
UGPase_euk_like cd04180
Eukaryotic UGPase-like includes UDPase and UDPGlcNAc pyrophosphorylase enzymes; This family ...
 103-408 3.63e-123

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: 361.10  E-value: 3.63e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800 103 VAVLLLAGGQGTRLGVAYPKGMYDVGLPSRKTLFQIQAERILKLQQVAEkyygNKCIIPWYIMTSGRTMESTKEFFTKHK 182
Cdd:cd04180     1 VAVVLLAGGLGTRLGKDGPKSSTDVGLPSGQCFLQLIGEKILTLQEIDL----YSCKIPEQLMNSKYTHEKTQCYFEKIN 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800 183 yfgLKKENVIFFQQGMLPAMSFDGKIILEEKNKVSMAPDGNGGLYRALAAQNIVEDMEQRGIWSIHVYCVDNILVKVADP 262
Cdd:cd04180    77 ---QKNSYVITFMQGKLPLKNDDDARDPHNKTKCHLFPCGHGDVVLALIHSGHLNKLLEKGYRYIHFIGVDNLLVKVADP 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800 263 RFIGFCIQKGADCGAKVVEKTNPTEPVGVVCRVD-GVYQVVEYSEISLATAQKR------SSDGRLLFNAGNIANHFFTV 335
Cdd:cd04180   154 LFIGIAIQNRKAINQKVVPKTRNEESGGYRIANInGRVQLLEYDQIKKLLKQKMvnnqipKDIDDAPFFLFNTNNLINFL 233

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1743150800 336 PFLRDVVNvyepqlqhhvaqkkipyvdtqgqlikpdkpngikmekfvfDIFQFAKKFVVYEVLREDEFSPLKN 408
Cdd:cd04180   234 VEFKDRVD----------------------------------------DIIEFTDDIVGVMVHRAEEFAPVKN 266
PTZ00339 PTZ00339
UDP-N-acetylglucosamine pyrophosphorylase; Provisional
 10-491 7.61e-117

UDP-N-acetylglucosamine pyrophosphorylase; Provisional


Pssm-ID: 240368  Cd Length: 482  Bit Score: 352.51  E-value: 7.61e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800  10 LSKAGQEHLLRYWNELEE-------AQQVELYAELQAMNFEE-----LNFFFQKAIEGFNQSSHQKNVdarMEPVPREVL 77
Cdd:PTZ00339    5 LTGDGQDHLREALKRRSEgeftplaTQILSSLTNVDFKHRNAvlepkLEEYNAEAPVGIDIDSIHNCN---IEPPNNNTF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800  78 GSATRDQDQLQSWESEGLFQISQNKVAVLLLAGGQGTRLGVAYPKGMYDVGLPSRKTLFQIQAERILKLQQVAEKYY--G 155
Cdd:PTZ00339   82 IDIYEKEKERKELKESGLEIIKKGEVAVLILAGGLGTRLGSDKPKGLLECTPVKKKTLFQFHCEKVRRLEEMAVAVSggG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800 156 NKCIIPWYIMTSGRTMESTKEFFTKHKYFGLKKENVIFFQQGMLPAMS-FDGKIILEEKNKVSMAPDGNGGLYRALAAQN 234
Cdd:PTZ00339  162 DDPTIYILVLTSSFNHDQTRQFLEENNFFGLDKEQVIFFKQSSLPCYDeNTGRFIMSSQGSLCTAPGGNGDVFKALAKCS 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800 235 IVEDMEQRGIWSIHVYCVDNILVKVADPRFIGFCIQKGADCGAKVVEKTNPTEPVGVVCRVDGVYQVVEYSEIS-LATAQ 313
Cdd:PTZ00339  242 ELMDIVRKGIKYVQVISIDNILAKVLDPEFIGLASSFPAHDVLNKCVKREDDESVGVFCLKDYEWQVVEYTEINeRILNN 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800 314 KRSSDGRLLFNAGNIANHFFTVPFLRDVVNVY-EPQLQHHVAQKKIPYVDtqgqlIKPDKPNGIKMEKFVFDIFQFAKKF 392
Cdd:PTZ00339  322 DELLTGELAFNYGNICSHIFSLDFLKKVAANRlYESTPYHAARKKIPYIN-----GPTDKTMGIKLEAFIFDIFRYAKNV 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800 393 VVYEVLREDEFSPLKNADSQNGkDNPTTARHALMSLHHCWVLNAGGHFIDENGSRLpaiprlkdandvpIQCEISPLISY 472
Cdd:PTZ00339  397 LILEVDREDEFAPIKNADGAAA-DTILNAQKLLLSLHTRWLEAALETVAGNPREGL-------------NLCEISPLVSY 462

                         490
                  ....*....|....*....
gi 1743150800 473 AGEGLESYVADKEFHAPLI 491
Cdd:PTZ00339  463 GGEGLFQYPGKKILGLPEI 481
UGGPase cd06424
UGGPase catalyzes the synthesis of UDP-Glucose/UDP-Galactose; UGGPase: UDP-Galactose/Glucose ...
 103-294 7.63e-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: 84.43  E-value: 7.63e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800 103 VAVLLLAGGQGTRLGVAYPKGMYDVGLPSRKTLFQIQAERILKLQQVAEKYYGNKciIPWYIMTSGRTMESTKEFFTKHK 182
Cdd:cd06424     1 AVFVLVAGGLGERLGYSGIKIGLPVELTTNTTYLQYYLNYIRAFQEASKKGEKME--IPFVIMTSDDTHSKTLKLLEENN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800 183 YFGLKKENVIFFQQGMLPAM-SFDGKIILEEKNKVSMA--PDGNGGLYRALAAQNIVEDMEQRGIWSIHVYCVDNILVKV 259
Cdd:cd06424    79 YFGLEKDQVHILKQEKVFCLiDNDAHLALDPDNTYSILtkPHGHGDVHTLLYNSGLLKKWIEAGYKWLVFFQDTNALAFK 158

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1743150800 260 ADPRFIGFCIQKGADCGAKVVEKTnPTEPVGVVCR 294
Cdd:cd06424   159 AIPAVLGVSATKSLDMNSLTVPRK-PKEAIGALCK 192
PLN02830 PLN02830
UDP-sugar pyrophosphorylase
 9-224 5.60e-17

UDP-sugar pyrophosphorylase


Pssm-ID: 215444  Cd Length: 615  Bit Score: 83.97  E-value: 5.60e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800   9 TLSKAGQEHLLRYWNE--LEEAQQVELYAELQAMNFEE---LNFFFQKAIEGFNQSSHQKNVDARMEP-VPR-EVLGSAT 81
Cdd:PLN02830   33 RLLELGQSHLFEHWPEpgVDDDDKRRLLEQVARLDESYpggLAAYVSNAKELLADSKEGVNPFEGWTPsVPEgEVLEYGS 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800  82 rdqDQLQSWESEGLFQIsqNKVAVLLLAGGQGTRLGVAYPKgmydVGLPSRKT----LFQIQAERILKLQQVAEKYYGNK 157
Cdd:PLN02830  113 ---EEFVELEEAGLREA--GNAAFVLVAGGLGERLGYSGIK----VALPTETAtgtcYLQLYIESILALQERAKKRKAKK 183

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1743150800 158 CI-IPWYIMTSGRTMESTKEFFTKHKYFGLKKENVIFFQQGMLPAMS-FDGKIILEEKN--KVSMAPDGNG 224
Cdd:PLN02830  184 GRkIPLVIMTSDDTHARTLKLLERNDYFGMDPDQVTLLKQEKVACLMdNDARLALDPNDpyKIQTKPHGHG 254
UGPase_euk cd00897
Eukaryotic UGPase catalyses the synthesis of UDP-Glucose; UGPase (UDP-Glucose ...
 101-303 6.87e-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: 54.17  E-value: 6.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800 101 NKVAVLLLAGGQGTRLGVAYPKGMYDVglPSRKTLFQIQAERILKLQQvaeKYYGNkciIPWYIMTSGRTMESTKEFFTK 180
Cdd:cd00897     2 NKLVVLKLNGGLGTSMGCTGPKSLIEV--RDGKTFLDLTVQQIEHLNK---TYGVD---VPLVLMNSFNTDEDTKKILKK 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800 181 HKYFglkKENVIFFQQGMLPAMSFDGKIILEEK---NKVSMAPDGNGGLYRALAAQNIVEDMEQRGIWSIHVYCVDNiLV 257
Cdd:cd00897    74 YAGV---NVDIHTFNQSRYPRISKETLLPVPSWadsPDEEWYPPGHGDIFESLYNSGLLDTLLAQGKEYLFVSNIDN-LG 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1743150800 258 KVADPRFIGFCIQKGADCGAKVVEKTNPTEPVGVVCRVDGVYQVVE 303
Cdd:cd00897   150 ATVDLRILNHMVDNKAEYIMEVTDKTRADVKGGTLIQYEGKLRLLE 195
PLN02474 PLN02474
UTP--glucose-1-phosphate uridylyltransferase
 101-328 2.46e-04

UTP--glucose-1-phosphate uridylyltransferase


Pssm-ID: 178092  Cd Length: 469  Bit Score: 43.71  E-value: 2.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800 101 NKVAVLLLAGGQGTRLGVAYPKGMYDV--GLpSRKTLFQIQAERIlklqqvaEKYYGnkCIIPWYIMTSGRTMESTKEFF 178
Cdd:PLN02474   78 DKLVVLKLNGGLGTTMGCTGPKSVIEVrnGL-TFLDLIVIQIENL-------NKKYG--CNVPLLLMNSFNTHDDTQKIV 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743150800 179 TKHKYFGLKkenVIFFQQGMLPAMSFDGKIILEEKNKVSMA---PDGNGGLYRALAAQNIVEDMEQRGIWSIHVYCVDNi 255
Cdd:PLN02474  148 EKYTNSNIE---IHTFNQSQYPRVVADDFVPWPSKGKTDKDgwyPPGHGDVFPSLMNSGKLDALLSQGKEYVFIANSDN- 223

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1743150800 256 LVKVADPRFIGFCIQKGADCGAKVVEKTNPTEPVGVVCRVDGVYQVVEYSEISLATAQK-RSSDGRLLFNAGNI 328
Cdd:PLN02474  224 LGAIVDLKILNHLIQNKNEYCMEVTPKTLADVKGGTLISYEGKVQLLEIAQVPDEHVNEfKSIEKFKIFNTNNL 297
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 103-122 9.65e-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: 37.50  E-value: 9.65e-03
                          10        20
                  ....*....|....*....|
gi 1743150800 103 VAVLLLAGGQGTRLGVAYPK 122
Cdd:cd02516     1 VAAIILAAGSGSRMGADIPK 20
 
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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