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Conserved domains on  [gi|578817975|ref|XP_006717380|]
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UDP-N-acetylhexosamine pyrophosphorylase-like protein 1 isoform X2 [Homo sapiens]

Protein Classification

UDPGP type 1 family protein( domain architecture ID 10135883)

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

EC:  2.7.-.-
Gene Ontology:  GO:0016772
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 ...
 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
 
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
 
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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