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Conserved domains on  [gi|6320100|ref|NP_010180|]
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UDP-N-acetylglucosamine diphosphorylase [Saccharomyces cerevisiae S288C]

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 ...
 89-410 3.50e-170

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: 481.72  E-value: 3.50e-170
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100   89 NEYWRLGLEAIGKGEVAVILMAGGQGTRLGSSQPKGCYDIGLPSKKSLFQIQAEKLIRLQDM---VKDKKVEIPWYIMTS 165
Cdd:cd04193   1 KEWEEAGLKAIAEGKVAVLLLAGGQGTRLGFDGPKGMFPVGLPSKKSLFQLQAERILKLQELageASGKKVPIPWYIMTS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100  166 GPTRAATEAYFQEHNYFGLNKEQITFFNQGTLPAFDLTGKhFLMKDPVNLSQSPDGNGGLYRAIKENKLNEDFDRRGIKH 245
Cdd:cd04193  81 EATHEETRKFFKENNYFGLDPEQVHFFQQGMLPCVDFDGK-ILLEEKGKIAMAPNGNGGLYKALQTAGILEDMKKRGIKY 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100  246 VYMYCVDNVLSKIADPVFIGFAIKHGFELATKAVRKRDAHESVGLIATKNEKPCVIEYSEISNELAEAKDKDGLLKLRAG 325
Cdd:cd04193 160 IHVYSVDNILVKVADPVFIGFCISKGADVGAKVVRKRYPTEKVGVVVLVDGKPQVVEYSEISDELAEKRDADGELQYNAG 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100  326 NIVNHYYLVDLLKRDLDQWCENMPYHIAKKKIPAYDsVTGKYTKPTEPNGIKLEQFIFDVFDTVplNKFGCLEVDRCKEF 405
Cdd:cd04193 240 NIANHFFSLDFLEKAAEMEEPSLPYHIAKKKIPYVD-LEGGLVKPDEPNGIKLELFIFDVFPFA--KNFVCLEVDREEEF 316


                ....*
gi 6320100  406 SPLKN 410
Cdd:cd04193 317 SPLKN 321
 
Name Accession Description Interval E-value
UDPGlcNAc_PPase cd04193
UDPGlcNAc pyrophosphorylase catalayzes the synthesis of UDPGlcNAc; UDP-N-acetylglucosamine ...
 89-410 3.50e-170

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: 481.72  E-value: 3.50e-170
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100   89 NEYWRLGLEAIGKGEVAVILMAGGQGTRLGSSQPKGCYDIGLPSKKSLFQIQAEKLIRLQDM---VKDKKVEIPWYIMTS 165
Cdd:cd04193   1 KEWEEAGLKAIAEGKVAVLLLAGGQGTRLGFDGPKGMFPVGLPSKKSLFQLQAERILKLQELageASGKKVPIPWYIMTS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100  166 GPTRAATEAYFQEHNYFGLNKEQITFFNQGTLPAFDLTGKhFLMKDPVNLSQSPDGNGGLYRAIKENKLNEDFDRRGIKH 245
Cdd:cd04193  81 EATHEETRKFFKENNYFGLDPEQVHFFQQGMLPCVDFDGK-ILLEEKGKIAMAPNGNGGLYKALQTAGILEDMKKRGIKY 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100  246 VYMYCVDNVLSKIADPVFIGFAIKHGFELATKAVRKRDAHESVGLIATKNEKPCVIEYSEISNELAEAKDKDGLLKLRAG 325
Cdd:cd04193 160 IHVYSVDNILVKVADPVFIGFCISKGADVGAKVVRKRYPTEKVGVVVLVDGKPQVVEYSEISDELAEKRDADGELQYNAG 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100  326 NIVNHYYLVDLLKRDLDQWCENMPYHIAKKKIPAYDsVTGKYTKPTEPNGIKLEQFIFDVFDTVplNKFGCLEVDRCKEF 405
Cdd:cd04193 240 NIANHFFSLDFLEKAAEMEEPSLPYHIAKKKIPYVD-LEGGLVKPDEPNGIKLELFIFDVFPFA--KNFVCLEVDREEEF 316


                ....*
gi 6320100  406 SPLKN 410
Cdd:cd04193 317 SPLKN 321
PLN02435 PLN02435
probable UDP-N-acetylglucosamine pyrophosphorylase
 12-468 1.20e-120

probable UDP-N-acetylglucosamine pyrophosphorylase


Pssm-ID: 215238  Cd Length: 493  Bit Score: 361.88  E-value: 1.20e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100    12 GQSQLFHNWESLSRKDQEELLSNLEQISSKRspaklledCQNAIKFSLANSSKDTGVeISPLPPTSYESLIGNSKKENE- 90
Cdd:PLN02435  33 GQEDAFALWDELSPEERDLLVRDIESLDLPR--------IDRIIRCSLRSQGLPVPA-IEPVPENSVSTVEERTPEDREr 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100    91 YWRLGLEAIGKGEVAVILMAGGQGTRLGSSQPKGCYDIGLPSKKSLFQIQAEKLIRLQ-------DMVKDKKVEIPWYIM 163
Cdd:PLN02435 104 WWKMGLKAISEGKLAVVLLSGGQGTRLGSSDPKGCFNIGLPSGKSLFQLQAERILCVQrlaaqasSEGPGRPVTIHWYIM 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100   164 TSGPTRAATEAYFQEHNYFGLNKEQITFFNQGTLPAFDLTGKhFLMKDPVNLSQSPDGNGGLYRAIKENKLNEDFDRRGI 243
Cdd:PLN02435 184 TSPFTDEATRKFFESHKYFGLEADQVTFFQQGTLPCVSKDGK-FIMETPFKVAKAPDGNGGVYAALKSSRLLEDMASRGI 262

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100   244 KHVYMYCVDNVLSKIADPVFIGFAIKHGFELATKAVRKRDAHESVGLIAT--KNEKPCVIEYSEISNELAEAKDKD-GLL 320
Cdd:PLN02435 263 KYVDCYGVDNALVRVADPTFLGYFIDKGVASAAKVVRKAYPQEKVGVFVRrgKGGPLTVVEYSELDQAMASAINQQtGRL 342

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100   321 KLRAGNIVNHYYLVDLLKRDLDQWCENMPYHIAKKKIPAYDSVTgkytkptepNGIKLEQFIFDVFDTVPlnKFGCLEVD 400
Cdd:PLN02435 343 RYCWSNVCLHMFTLDFLNQVANGLEKDSIYHLAEKKIPSIHGYT---------MGLKLEQFIFDAFPYAP--STALFEVL 411

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6320100   401 RCKEFSPLKNGPGSKNDNPETSRLAYLKLGTSWLEDAGAIVKDGVL-----VEVSSKLSYAGENLSQF-KGKVF 468
Cdd:PLN02435 412 REEEFAPVKNANGSNFDTPESARLLVLRLHTRWVVAAGGFLTHSVPlyatgVEVSPLCSYAGENLEAIcRGRTF 485
QRI1 COG4284
UDP-N-acetylglucosamine pyrophosphorylase [Carbohydrate transport and metabolism];
10-414 8.00e-120

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


Pssm-ID: 443425  Cd Length: 402  Bit Score: 356.50  E-value: 8.00e-120
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100   10 EAGQSQLFHNWESLSRKDQEELLSNLEQISskrspAKLLEDCQNAIKFSLANSSKDTGVEISPLPPTSYESLIGNSKKEN 89
Cdd:COG4284   7 PHGQEHLLRFWDELSEAQQKMLEAQIEEID-----IDVFQHLYRQLVLAEGATGLIPESDIEPAPVTDLPLTDLDEVDRD 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100   90 EYWRLGLEAIGKGEVAVILMAGGQGTRLGSSQPKGCYDIGLPSKKSLFQIQAEKLIRLQdmvKDKKVEIPWYIMTSGPTR 169
Cdd:COG4284  82 RAEEAGEEALRAGKVAVILLAGGQGTRLGFDGPKGLLPVRPVKGKSLFDLIAEQVLAAR---RRYGVPLPLYIMTSFRTH 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100  170 AATEAYFQEHNYFGLNKEQITFFNQGTLPAFD-LTGKhFLMKDPVNLSQSPDGNGGLYRAIKENKLNEDFDRRGIKHVYM 248
Cdd:COG4284 159 EDTLAFLEEHDYFGLDGLPVHFFLQGMEPALDaDLGP-VLLPADPELELCPPGHGGIYTALLASGLLDKLLERGIRYLFV 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100  249 YCVDNVLSKIADPVFIGFAIKHGFELATKAVRKRDAHESVGLIATKNEKPCVIEYSEISNELAEAkdKDGLLKLRAGNIV 328
Cdd:COG4284 238 SNVDNPLGAVPDPAFAGWHAASGAPFTAKVVRRTPPDEKVGHLARVDGRLILREYSQLPDEEAEA--FTGELRHPYGNIN 315

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100  329 NHYYLVDLLKRDLDQWCENMPYHIAKKKIPAYDSVtgkyTKPTEPNGIKLEQFIFD---VFDtvplnKFGCLEVDRCKEF 405
Cdd:COG4284 316 NHWFDLDFLKRLLDERGLGLPLHRAEKKVDPLDES----GKPTSPNVIKFETFMFDaipLFD-----GAVAIEVDREERF 386


                ....*....
gi 6320100  406 SPLKNGPGS 414
Cdd:COG4284 387 APVKNTNGS 395
UDPGP pfam01704
UTP--glucose-1-phosphate uridylyltransferase; This family consists of UTP--glucose-1-phosphate ...
 69-410 1.45e-32

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: 128.02  E-value: 1.45e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100     69 EISPLPPTS---YESLiGNSKKENEywrlglEAIGKgeVAVILMAGGQGTRLGSSQPKGCYDIGlpSKKSLFQIQAEkli 145
Cdd:pfam01704  25 KIKPPPEEEivdYEDL-QEPEEEIK------ELLNK--LAVLKLNGGLGTSMGCVGPKSLIEVR--DGLTFLDLIVQ--- 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100    146 RLQDMVKDKKVEIPWYIMTSGPTRAATEAYFQehNYFGlNKEQITFFNQGTLPAFDLTGKHFLMK--DPVNLSQSPDGNG 223
Cdd:pfam01704  91 QIEHLNKKYNVDVPLVLMNSFNTDEDTKKIIR--KYKG-HKVDILTFNQSRYPRIDKDTLLPVPKsaDSDEEEWYPPGHG 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100    224 GLYRAIKENKLNEDFDRRGIKHVYMYCVDNvLSKIADPVFIGFAIKHGFELATKAVRKRDAHESVGLIATKNEKPCVIEY 303
Cdd:pfam01704 168 DLYESLYNSGLLDKLLAEGKEYLFVSNIDN-LGATVDLNILNYMVDNGAEFLMEVTDKTRADVKGGTLIEYDGKLRLLEI 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100    304 SEISNE-LAEAKDKDGLLKLRAGNIvnhyyLVDL--LKRDLDQwcENMPYHIA--KKKIPAYDSVtgkyTKPTEPNGIKL 378
Cdd:pfam01704 247 AQVPKEhVDEFKSIKKFKIFNTNNI-----WINLkaLKRVVEE--GELQLEIIvnKKTLDNGENV----IQLETAVGAAI 315

                         330       340       350
                  ....*....|....*....|....*....|..
gi 6320100    379 EQFifdvfdtvplNKFGCLEVDRcKEFSPLKN 410
Cdd:pfam01704 316 KNF----------KNAIGINVPR-SRFLPVKT 336
 
Name Accession Description Interval E-value
UDPGlcNAc_PPase cd04193
UDPGlcNAc pyrophosphorylase catalayzes the synthesis of UDPGlcNAc; UDP-N-acetylglucosamine ...
 89-410 3.50e-170

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: 481.72  E-value: 3.50e-170
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100   89 NEYWRLGLEAIGKGEVAVILMAGGQGTRLGSSQPKGCYDIGLPSKKSLFQIQAEKLIRLQDM---VKDKKVEIPWYIMTS 165
Cdd:cd04193   1 KEWEEAGLKAIAEGKVAVLLLAGGQGTRLGFDGPKGMFPVGLPSKKSLFQLQAERILKLQELageASGKKVPIPWYIMTS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100  166 GPTRAATEAYFQEHNYFGLNKEQITFFNQGTLPAFDLTGKhFLMKDPVNLSQSPDGNGGLYRAIKENKLNEDFDRRGIKH 245
Cdd:cd04193  81 EATHEETRKFFKENNYFGLDPEQVHFFQQGMLPCVDFDGK-ILLEEKGKIAMAPNGNGGLYKALQTAGILEDMKKRGIKY 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100  246 VYMYCVDNVLSKIADPVFIGFAIKHGFELATKAVRKRDAHESVGLIATKNEKPCVIEYSEISNELAEAKDKDGLLKLRAG 325
Cdd:cd04193 160 IHVYSVDNILVKVADPVFIGFCISKGADVGAKVVRKRYPTEKVGVVVLVDGKPQVVEYSEISDELAEKRDADGELQYNAG 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100  326 NIVNHYYLVDLLKRDLDQWCENMPYHIAKKKIPAYDsVTGKYTKPTEPNGIKLEQFIFDVFDTVplNKFGCLEVDRCKEF 405
Cdd:cd04193 240 NIANHFFSLDFLEKAAEMEEPSLPYHIAKKKIPYVD-LEGGLVKPDEPNGIKLELFIFDVFPFA--KNFVCLEVDREEEF 316


                ....*
gi 6320100  406 SPLKN 410
Cdd:cd04193 317 SPLKN 321
PLN02435 PLN02435
probable UDP-N-acetylglucosamine pyrophosphorylase
 12-468 1.20e-120

probable UDP-N-acetylglucosamine pyrophosphorylase


Pssm-ID: 215238  Cd Length: 493  Bit Score: 361.88  E-value: 1.20e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100    12 GQSQLFHNWESLSRKDQEELLSNLEQISSKRspaklledCQNAIKFSLANSSKDTGVeISPLPPTSYESLIGNSKKENE- 90
Cdd:PLN02435  33 GQEDAFALWDELSPEERDLLVRDIESLDLPR--------IDRIIRCSLRSQGLPVPA-IEPVPENSVSTVEERTPEDREr 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100    91 YWRLGLEAIGKGEVAVILMAGGQGTRLGSSQPKGCYDIGLPSKKSLFQIQAEKLIRLQ-------DMVKDKKVEIPWYIM 163
Cdd:PLN02435 104 WWKMGLKAISEGKLAVVLLSGGQGTRLGSSDPKGCFNIGLPSGKSLFQLQAERILCVQrlaaqasSEGPGRPVTIHWYIM 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100   164 TSGPTRAATEAYFQEHNYFGLNKEQITFFNQGTLPAFDLTGKhFLMKDPVNLSQSPDGNGGLYRAIKENKLNEDFDRRGI 243
Cdd:PLN02435 184 TSPFTDEATRKFFESHKYFGLEADQVTFFQQGTLPCVSKDGK-FIMETPFKVAKAPDGNGGVYAALKSSRLLEDMASRGI 262

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100   244 KHVYMYCVDNVLSKIADPVFIGFAIKHGFELATKAVRKRDAHESVGLIAT--KNEKPCVIEYSEISNELAEAKDKD-GLL 320
Cdd:PLN02435 263 KYVDCYGVDNALVRVADPTFLGYFIDKGVASAAKVVRKAYPQEKVGVFVRrgKGGPLTVVEYSELDQAMASAINQQtGRL 342

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100   321 KLRAGNIVNHYYLVDLLKRDLDQWCENMPYHIAKKKIPAYDSVTgkytkptepNGIKLEQFIFDVFDTVPlnKFGCLEVD 400
Cdd:PLN02435 343 RYCWSNVCLHMFTLDFLNQVANGLEKDSIYHLAEKKIPSIHGYT---------MGLKLEQFIFDAFPYAP--STALFEVL 411

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6320100   401 RCKEFSPLKNGPGSKNDNPETSRLAYLKLGTSWLEDAGAIVKDGVL-----VEVSSKLSYAGENLSQF-KGKVF 468
Cdd:PLN02435 412 REEEFAPVKNANGSNFDTPESARLLVLRLHTRWVVAAGGFLTHSVPlyatgVEVSPLCSYAGENLEAIcRGRTF 485
QRI1 COG4284
UDP-N-acetylglucosamine pyrophosphorylase [Carbohydrate transport and metabolism];
10-414 8.00e-120

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


Pssm-ID: 443425  Cd Length: 402  Bit Score: 356.50  E-value: 8.00e-120
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100   10 EAGQSQLFHNWESLSRKDQEELLSNLEQISskrspAKLLEDCQNAIKFSLANSSKDTGVEISPLPPTSYESLIGNSKKEN 89
Cdd:COG4284   7 PHGQEHLLRFWDELSEAQQKMLEAQIEEID-----IDVFQHLYRQLVLAEGATGLIPESDIEPAPVTDLPLTDLDEVDRD 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100   90 EYWRLGLEAIGKGEVAVILMAGGQGTRLGSSQPKGCYDIGLPSKKSLFQIQAEKLIRLQdmvKDKKVEIPWYIMTSGPTR 169
Cdd:COG4284  82 RAEEAGEEALRAGKVAVILLAGGQGTRLGFDGPKGLLPVRPVKGKSLFDLIAEQVLAAR---RRYGVPLPLYIMTSFRTH 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100  170 AATEAYFQEHNYFGLNKEQITFFNQGTLPAFD-LTGKhFLMKDPVNLSQSPDGNGGLYRAIKENKLNEDFDRRGIKHVYM 248
Cdd:COG4284 159 EDTLAFLEEHDYFGLDGLPVHFFLQGMEPALDaDLGP-VLLPADPELELCPPGHGGIYTALLASGLLDKLLERGIRYLFV 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100  249 YCVDNVLSKIADPVFIGFAIKHGFELATKAVRKRDAHESVGLIATKNEKPCVIEYSEISNELAEAkdKDGLLKLRAGNIV 328
Cdd:COG4284 238 SNVDNPLGAVPDPAFAGWHAASGAPFTAKVVRRTPPDEKVGHLARVDGRLILREYSQLPDEEAEA--FTGELRHPYGNIN 315

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100  329 NHYYLVDLLKRDLDQWCENMPYHIAKKKIPAYDSVtgkyTKPTEPNGIKLEQFIFD---VFDtvplnKFGCLEVDRCKEF 405
Cdd:COG4284 316 NHWFDLDFLKRLLDERGLGLPLHRAEKKVDPLDES----GKPTSPNVIKFETFMFDaipLFD-----GAVAIEVDREERF 386


                ....*....
gi 6320100  406 SPLKNGPGS 414
Cdd:COG4284 387 APVKNTNGS 395
PTZ00339 PTZ00339
UDP-N-acetylglucosamine pyrophosphorylase; Provisional
 1-467 5.62e-104

UDP-N-acetylglucosamine pyrophosphorylase; Provisional


Pssm-ID: 240368  Cd Length: 482  Bit Score: 318.61  E-value: 5.62e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100     1 MTDTKQLFI-EAGQSQLFHNWESLSRKDQEELLSNLEQISSKRSPAKLLEdcQNAIKFSLANSSKDTGVEISPLPPTSYE 79
Cdd:PTZ00339   5 LTGDGQDHLrEALKRRSEGEFTPLATQILSSLTNVDFKHRNAVLEPKLEE--YNAEAPVGIDIDSIHNCNIEPPNNNTFI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100    80 SLIGNSKKENEYWRLGLEAIGKGEVAVILMAGGQGTRLGSSQPKGCYDIGLPSKKSLFQIQAEKLIRLQDM-----VKDK 154
Cdd:PTZ00339  83 DIYEKEKERKELKESGLEIIKKGEVAVLILAGGLGTRLGSDKPKGLLECTPVKKKTLFQFHCEKVRRLEEMavavsGGGD 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100   155 KVEIPWYIMTSGPTRAATEAYFQEHNYFGLNKEQITFFNQGTLPAFDLTGKHFLMKDPVNLSQSPDGNGGLYRAIKENKL 234
Cdd:PTZ00339 163 DPTIYILVLTSSFNHDQTRQFLEENNFFGLDKEQVIFFKQSSLPCYDENTGRFIMSSQGSLCTAPGGNGDVFKALAKCSE 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100   235 NEDFDRRGIKHVYMYCVDNVLSKIADPVFIGFAIK-HGFELATKAVRKRDAhESVGLIATKNEKPCVIEYSEISNELAEA 313
Cdd:PTZ00339 243 LMDIVRKGIKYVQVISIDNILAKVLDPEFIGLASSfPAHDVLNKCVKREDD-ESVGVFCLKDYEWQVVEYTEINERILNN 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100   314 KDK-DGLLKLRAGNIVNHYYLVDLLKRDLDQWCEN-MPYHIAKKKIPAYDSVTgkytkpTEPNGIKLEQFIFDVFDTVpl 391
Cdd:PTZ00339 322 DELlTGELAFNYGNICSHIFSLDFLKKVAANRLYEsTPYHAARKKIPYINGPT------DKTMGIKLEAFIFDIFRYA-- 393

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100   392 NKFGCLEVDRCKEFSPLKNGPGSKNDNPETSRLAYLKLGTSWLEDAGAIVKDG-----VLVEVSSKLSYAGENLSQFKGK 466
Cdd:PTZ00339 394 KNVLILEVDREDEFAPIKNADGAAADTILNAQKLLLSLHTRWLEAALETVAGNpreglNLCEISPLVSYGGEGLFQYPGK 473


                 .
gi 6320100   467 V 467
Cdd:PTZ00339 474 K 474
UGPase_euk_like cd04180
Eukaryotic UGPase-like includes UDPase and UDPGlcNAc pyrophosphorylase enzymes; This family ...
 104-342 1.37e-53

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: 180.83  E-value: 1.37e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100  104 VAVILMAGGQGTRLGSSQPKGCYDIGLPSKKSLFQIQAEKLIRLQDmVKDKKVEIPWYIMTSGPTRAATEAYFQEHNyfg 183
Cdd:cd04180   1 VAVVLLAGGLGTRLGKDGPKSSTDVGLPSGQCFLQLIGEKILTLQE-IDLYSCKIPEQLMNSKYTHEKTQCYFEKIN--- 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100  184 LNKEQITFFNQGTLPAFDLTGKHFLMKDpVNLSQSPDGNGGLYRAIKENKLNEDFDRRGIKHVYMYCVDNVLSKIADPVF 263
Cdd:cd04180  77 QKNSYVITFMQGKLPLKNDDDARDPHNK-TKCHLFPCGHGDVVLALIHSGHLNKLLEKGYRYIHFIGVDNLLVKVADPLF 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100  264 IGFAIKHGFELATKAVRKRDAHESVG-LIATKNEKPCVIEYSEISNELAEAKDKDGL------LKLRAGNIVNHYYLVDL 336
Cdd:cd04180 156 IGIAIQNRKAINQKVVPKTRNEESGGyRIANINGRVQLLEYDQIKKLLKQKMVNNQIpkdiddAPFFLFNTNNLINFLVE 235


                ....*.
gi 6320100  337 LKRDLD 342
Cdd:cd04180 236 FKDRVD 241
UDPGP pfam01704
UTP--glucose-1-phosphate uridylyltransferase; This family consists of UTP--glucose-1-phosphate ...
 69-410 1.45e-32

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: 128.02  E-value: 1.45e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100     69 EISPLPPTS---YESLiGNSKKENEywrlglEAIGKgeVAVILMAGGQGTRLGSSQPKGCYDIGlpSKKSLFQIQAEkli 145
Cdd:pfam01704  25 KIKPPPEEEivdYEDL-QEPEEEIK------ELLNK--LAVLKLNGGLGTSMGCVGPKSLIEVR--DGLTFLDLIVQ--- 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100    146 RLQDMVKDKKVEIPWYIMTSGPTRAATEAYFQehNYFGlNKEQITFFNQGTLPAFDLTGKHFLMK--DPVNLSQSPDGNG 223
Cdd:pfam01704  91 QIEHLNKKYNVDVPLVLMNSFNTDEDTKKIIR--KYKG-HKVDILTFNQSRYPRIDKDTLLPVPKsaDSDEEEWYPPGHG 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100    224 GLYRAIKENKLNEDFDRRGIKHVYMYCVDNvLSKIADPVFIGFAIKHGFELATKAVRKRDAHESVGLIATKNEKPCVIEY 303
Cdd:pfam01704 168 DLYESLYNSGLLDKLLAEGKEYLFVSNIDN-LGATVDLNILNYMVDNGAEFLMEVTDKTRADVKGGTLIEYDGKLRLLEI 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100    304 SEISNE-LAEAKDKDGLLKLRAGNIvnhyyLVDL--LKRDLDQwcENMPYHIA--KKKIPAYDSVtgkyTKPTEPNGIKL 378
Cdd:pfam01704 247 AQVPKEhVDEFKSIKKFKIFNTNNI-----WINLkaLKRVVEE--GELQLEIIvnKKTLDNGENV----IQLETAVGAAI 315

                         330       340       350
                  ....*....|....*....|....*....|..
gi 6320100    379 EQFifdvfdtvplNKFGCLEVDRcKEFSPLKN 410
Cdd:pfam01704 316 KNF----------KNAIGINVPR-SRFLPVKT 336
UGGPase cd06424
UGGPase catalyzes the synthesis of UDP-Glucose/UDP-Galactose; UGGPase: UDP-Galactose/Glucose ...
 104-412 1.08e-22

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: 98.30  E-value: 1.08e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100  104 VAVILMAGGQGTRLGSSQPKgcydIGLP----SKKSLFQIQAEKLIRLQDMV-KDKKVEIPWYIMTSGPTRAATEAYFQE 178
Cdd:cd06424   1 AVFVLVAGGLGERLGYSGIK----IGLPveltTNTTYLQYYLNYIRAFQEASkKGEKMEIPFVIMTSDDTHSKTLKLLEE 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100  179 HNYFGLNKEQITFFNQGTLPAFDLTGKHFLM--KDPVNLSQSPDGNGGLYRAIKENKLNEDFDRRGIKHVYMYCVDNVLS 256
Cdd:cd06424  77 NNYFGLEKDQVHILKQEKVFCLIDNDAHLALdpDNTYSILTKPHGHGDVHTLLYNSGLLKKWIEAGYKWLVFFQDTNALA 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100  257 KIADPVFIGFAIKHGFELATKAVrKRDAHESVGLIA--TKNEKPCV---IEYSEISNEL-------AEAKDKDGlLKLRA 324
Cdd:cd06424 157 FKAIPAVLGVSATKSLDMNSLTV-PRKPKEAIGALCklTKNNGKSMtinVEYNQLDPLLrasgkddGDVDDKTG-FSPFP 234

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100  325 GNIVNHYYLVDLLKRDLDQWCENMPYHIAkkkiPAY-DSVTGKYTKPTepngiKLEQFIFDVFDTVPL-NKFGCLEVDRC 402
Cdd:cd06424 235 GNINQLVFSLGPYMDELEKTKGAIPEFIN----PKYkDATKTAFKSPT-----RLECMMQDIPLLFEEdYRVGFTVLDRW 305

                       330
                ....*....|
gi 6320100  403 KEFSPLKNGP 412
Cdd:cd06424 306 LCFSPVKNNL 315
PLN02830 PLN02830
UDP-sugar pyrophosphorylase
 9-449 3.59e-21

UDP-sugar pyrophosphorylase


Pssm-ID: 215444  Cd Length: 615  Bit Score: 96.68  E-value: 3.59e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100     9 IEAGQSQLFHNWESLSRKDQEE--LLSNLEQISSkRSPAKLLEDCQNAIKfsLANSSKDtGV----EISPLPPTSyESLI 82
Cdd:PLN02830  35 LELGQSHLFEHWPEPGVDDDDKrrLLEQVARLDE-SYPGGLAAYVSNAKE--LLADSKE-GVnpfeGWTPSVPEG-EVLE 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100    83 GNSKKENEYWRLGLEAIGKgeVAVILMAGGQGTRLGSSQPKgcydIGLPSK----KSLFQIQAEKLIRLQDMVKDKK--- 155
Cdd:PLN02830 110 YGSEEFVELEEAGLREAGN--AAFVLVAGGLGERLGYSGIK----VALPTEtatgTCYLQLYIESILALQERAKKRKakk 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100   156 -VEIPWYIMTSGPTRAATEAYFQEHNYFGLNKEQITFFNQGTLPAFDLTGKHFLMK--DPVNLSQSPDGNGGLYRAIKEN 232
Cdd:PLN02830 184 gRKIPLVIMTSDDTHARTLKLLERNDYFGMDPDQVTLLKQEKVACLMDNDARLALDpnDPYKIQTKPHGHGDVHALLYSS 263

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100   233 KLNEDFDRRGIKHVYMYCVDNVLSKIADPVFIGFAIKHGFELATKAVrKRDAHESVGLIA-----TKNEKPCVIEYSEIS 307
Cdd:PLN02830 264 GLLDKWLSAGKKWVVFFQDTNGLVFKAIPAALGVSATKGFDMNSLAV-PRKAKEAIGAIAklthkDGREMVINVEYNQLD 342

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100   308 NELAEAKDKDGLLKLRA------GNIvNHYYL-----VDLLKRDldqwcenmpyhiaKKKIPAYdsVTGKY---TKPTEP 373
Cdd:PLN02830 343 PLLRATGHPDGDVNDETgyspfpGNI-NQLILklgpyVKELAKT-------------GGVIEEF--VNPKYkdaTKTAFK 406

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100   374 NGIKLEQFIFDVFDTVPLN-KFGCLEVDRCKEFSPLKNGP---------GSKNDNPETSRLAYLKLGTSWLEDAGAIVKD 443
Cdd:PLN02830 407 SPTRLECMMQDYPKTLPPSaKVGFTVFDNWLAYSPVKNSPadgaakvpeGNPTHSATSGEMAIYGANCLILRKAGADVEE 486


                 ....*.
gi 6320100   444 GVLVEV 449
Cdd:PLN02830 487 PVEDVV 492
PLN02728 PLN02728
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
 97-123 4.03e-03

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase


Pssm-ID: 215387  Cd Length: 252  Bit Score: 38.94  E-value: 4.03e-03
                         10        20
                 ....*....|....*....|....*..
gi 6320100    97 EAIGKGEVAVILMAGGQGTRLGSSQPK 123
Cdd:PLN02728  18 AVVKEKSVSVILLAGGVGKRMGANMPK 44
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 104-123 4.25e-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: 38.66  E-value: 4.25e-03
                        10        20
                ....*....|....*....|
gi 6320100  104 VAVILMAGGQGTRLGSSQPK 123
Cdd:cd02516   1 VAAIILAAGSGSRMGADIPK 20
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 105-298 4.79e-03

NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; Nucleotidyltransferases transfer nucleotides onto phosphosugars. The enzyme family includes Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase. The products are activated sugars that are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides.


Pssm-ID: 133024 [Multi-domain]  Cd Length: 217  Bit Score: 38.33  E-value: 4.79e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100  105 AVILmAGGQGTRLG---SSQPKGCYDIGlpsKKSLFQIQAEKLIRLQDmvkdkkVEIpwyIMTSGPTRAATEAYFQEHNY 181
Cdd:cd04181   1 AVIL-AAGKGTRLRpltDTRPKPLLPIA---GKPILEYIIERLARAGI------DEI---ILVVGYLGEQIEEYFGDGSK 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320100  182 FGLNkeqITFFNQGTlpafdltgkhflmkdpvnlsqsPDGNGG-LYRAikENKLNEDfdrrgikHVYMYCVDNvLSKIAD 260
Cdd:cd04181  68 FGVN---IEYVVQEE----------------------PLGTAGaVRNA--EDFLGDD-------DFLVVNGDV-LTDLDL 112

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 6320100  261 PVFIGFAIKHGfELATKAVRKRDAHESVGLIATKN--------EKP 298
Cdd:cd04181 113 SELLRFHREKG-ADATIAVKEVEDPSRYGVVELDDdgrvtrfvEKP 157
 
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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