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Conserved domains on  [gi|56312080|emb|CAI06725|]
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nucleotidyl transferase [Aromatoleum aromaticum EbN1]

Protein Classification

NDP-sugar synthase( domain architecture ID 11440233)

NDP-sugar synthase such as mannose-1-phosphate guanyltransferase and UTP--glucose-1-phosphate uridylyltransferase, which catalyzes the formation of UDP-glucose from UTP and glucose 1-phosphate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 2-226 1.44e-94

NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein s [Translation, ribosomal structure and biogenesis, Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 440821 [Multi-domain]  Cd Length: 238  Bit Score: 276.26  E-value: 1.44e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080   2 RAMILAAGRGERMRPLTDACPKPLLVAGGRPLIAWHLERLRMAGFTDVVINHAHLGTMIEAALGDGRQFGLHVAYSAETE 81
Cdd:COG1208   1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRFGVRITYVDEGE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080  82 ALETAGGVRQALALLGDAPFLVINGDVFCDADLAALRpvgAGLAATDDLAHLVMVPNPDHHPGGDFRLDGE-RLHR---- 156
Cdd:COG1208  81 PLGTGGALKRALPLLGDEPFLVLNGDILTDLDLAALL---AFHREKGADATLALVPVPDPSRYGVVELDGDgRVTRfvek 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 56312080 157 --DGEPRLTFSGIGVYRPALFAAVAAGTKAPLGPLLREAMDAGRVRGALHRGYWLDVGTPQRLAALDRHLRQ 226
Cdd:COG1208 158 peEPPSNLINAGIYVLEPEIFDYIPEGEPFDLEDLLPRLIAEGRVYGYVHDGYWLDIGTPEDLLEANALLLS 229
 
Name Accession Description Interval E-value
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 2-226 1.44e-94

NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein s [Translation, ribosomal structure and biogenesis, Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440821 [Multi-domain]  Cd Length: 238  Bit Score: 276.26  E-value: 1.44e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080   2 RAMILAAGRGERMRPLTDACPKPLLVAGGRPLIAWHLERLRMAGFTDVVINHAHLGTMIEAALGDGRQFGLHVAYSAETE 81
Cdd:COG1208   1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRFGVRITYVDEGE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080  82 ALETAGGVRQALALLGDAPFLVINGDVFCDADLAALRpvgAGLAATDDLAHLVMVPNPDHHPGGDFRLDGE-RLHR---- 156
Cdd:COG1208  81 PLGTGGALKRALPLLGDEPFLVLNGDILTDLDLAALL---AFHREKGADATLALVPVPDPSRYGVVELDGDgRVTRfvek 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 56312080 157 --DGEPRLTFSGIGVYRPALFAAVAAGTKAPLGPLLREAMDAGRVRGALHRGYWLDVGTPQRLAALDRHLRQ 226
Cdd:COG1208 158 peEPPSNLINAGIYVLEPEIFDYIPEGEPFDLEDLLPRLIAEGRVYGYVHDGYWLDIGTPEDLLEANALLLS 229
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 2-220 1.84e-82

NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.


Pssm-ID: 133044 [Multi-domain]  Cd Length: 221  Bit Score: 245.17  E-value: 1.84e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080   2 RAMILAAGRGERMRPLTDACPKPLLVAGGRPLIAWHLERLRMAGFTDVVINHAHLGTMIEAALGDgRQFGLHVAYSAE-T 80
Cdd:cd06422   1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHLGD-SRFGLRITISDEpD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080  81 EALETAGGVRQALALLGDAPFLVINGDVFCDADLAALRPVGAgLAATDDLAHLVMVPNPDHHPGGDFRLDGE-RLHRDGE 159
Cdd:cd06422  80 ELLETGGGIKKALPLLGDEPFLVVNGDILWDGDLAPLLLLHA-WRMDALLLLLPLVRNPGHNGVGDFSLDADgRLRRGGG 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 56312080 160 ---PRLTFSGIGVYRPALFAAVAAGtKAPLGPLLREAMDAGRVRGALHRGYWLDVGTPQRLAAL 220
Cdd:cd06422 159 gavAPFTFTGIQILSPELFAGIPPG-KFSLNPLWDRAIAAGRLFGLVYDGLWFDVGTPERLLAA 221
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 1-214 2.06e-36

UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The MJ_1101 protein from Methanococcus jannaschii has been characterized as the GlmU enzyme catalyzing the final two steps of UDP-GlcNAc biosynthesis. Many of the genes identified by this model are in proximity to the GlmS and GlmM genes and are also presumed to be GlmU. However, some archaeal genomes contain multiple closely-related homologs from this family and it is not clear what the substrate specificity is for each of them.


Pssm-ID: 274908 [Multi-domain]  Cd Length: 393  Bit Score: 131.95  E-value: 2.06e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080     1 MRAMILAAGRGERMRPLTDACPKPLLVAGGRPLIAWHLERLRMAGFTDVVINHAHLGTMIEAALGDGRQFGLHVAYSAET 80
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEKVREYFGDGSRGGVPIEYVVQE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080    81 EALETAGGVRQALALLGDaPFLVINGDVFCDADLaaLRpvgaGLAATDDLAHLVM-VPNPDHHpgGDFRLDGERLHR--- 156
Cdd:TIGR03992  81 EQLGTADALGSAKEYVDD-EFLVLNGDVLLDSDL--LE----RLIRAEAPAIAVVeVDDPSDY--GVVETDGGRVTGive 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 56312080   157 ---DGEPRLTFSGIGVYRPALFAAVAAGTKAPLGPL-----LREAMDAGRVRGALHRGYWLDVGTP 214
Cdd:TIGR03992 152 kpeNPPSNLINAGIYLFSPEIFELLEKTKLSPRGEYeltdaLQLLIDEGKVKAVELDGFWLDVGRP 217
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-217 2.78e-27

Nucleotidyl transferase; This family includes a wide range of enzymes which transfer nucleotides onto phosphosugars.


Pssm-ID: 425709 [Multi-domain]  Cd Length: 243  Bit Score: 104.26  E-value: 2.78e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080     2 RAMILAAGRGERMRPLTDACPKPL-LVAGGRPLIAWHLERLRMAGFTD-VVINHAHLGTMIEAALGDGRQFGLHVAYSAE 79
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLvPVGGKYPLIDYPLSRLANAGIREiIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080    80 TEALETAGGVRQALALLGD--APFLVINGDVFCDADLAAL----RPVGAGLAATddlahLVMVPNPDHHPGGDFRLDGE- 152
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDekSDVLVLGGDHIYRMDLEQAvkfhIEKAADATVT-----FGIVPVEPPTGYGVVEFDDNg 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080   153 RLHR-----DGEPRLTFSGIGVY--RPALFAAVAAGTKAP------LGPLLREAMDAGRVRGA-LHRGY-WLDVGTPQRL 217
Cdd:pfam00483 156 RVIRfvekpKLPKASNYASMGIYifNSGVLDFLAKYLEELkrgedeITDILPKALEDGKLAYAfIFKGYaWLDVGTWDSL 235
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 2-217 2.33e-11

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 62.00  E-value: 2.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080    2 RAMILAAGRGERMRPLTDACPKPLLVAGGRPLIAWHLERLRMAGFTDVVINHAHLGT-MIEAALGDGRQFGLHVAYSAET 80
Cdd:PRK15480   5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTpRFQQLLGDGSQWGLNLQYKVQP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080   81 ealeTAGGVRQALA-----LLGDAPFLVINGDVFCDADLAALR--PVGAGLAATDDLAHlvmVPNPDHHPGGDFRLDGER 153
Cdd:PRK15480  85 ----SPDGLAQAFIigeefIGGDDCALVLGDNIFYGHDLPKLMeaAVNKESGATVFAYH---VNDPERYGVVEFDQNGTA 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 56312080  154 L---HRDGEPRLTFSGIGVY-------RPALFAAVAAGTKAPLGPLLREAMDAGRVRGALH-RGY-WLDVGTPQRL 217
Cdd:PRK15480 158 IsleEKPLQPKSNYAVTGLYfydndvvEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMgRGYaWLDTGTHQSL 233
 
Name Accession Description Interval E-value
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 2-226 1.44e-94

NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein s [Translation, ribosomal structure and biogenesis, Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440821 [Multi-domain]  Cd Length: 238  Bit Score: 276.26  E-value: 1.44e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080   2 RAMILAAGRGERMRPLTDACPKPLLVAGGRPLIAWHLERLRMAGFTDVVINHAHLGTMIEAALGDGRQFGLHVAYSAETE 81
Cdd:COG1208   1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRFGVRITYVDEGE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080  82 ALETAGGVRQALALLGDAPFLVINGDVFCDADLAALRpvgAGLAATDDLAHLVMVPNPDHHPGGDFRLDGE-RLHR---- 156
Cdd:COG1208  81 PLGTGGALKRALPLLGDEPFLVLNGDILTDLDLAALL---AFHREKGADATLALVPVPDPSRYGVVELDGDgRVTRfvek 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 56312080 157 --DGEPRLTFSGIGVYRPALFAAVAAGTKAPLGPLLREAMDAGRVRGALHRGYWLDVGTPQRLAALDRHLRQ 226
Cdd:COG1208 158 peEPPSNLINAGIYVLEPEIFDYIPEGEPFDLEDLLPRLIAEGRVYGYVHDGYWLDIGTPEDLLEANALLLS 229
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 2-220 1.84e-82

NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.


Pssm-ID: 133044 [Multi-domain]  Cd Length: 221  Bit Score: 245.17  E-value: 1.84e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080   2 RAMILAAGRGERMRPLTDACPKPLLVAGGRPLIAWHLERLRMAGFTDVVINHAHLGTMIEAALGDgRQFGLHVAYSAE-T 80
Cdd:cd06422   1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHLGD-SRFGLRITISDEpD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080  81 EALETAGGVRQALALLGDAPFLVINGDVFCDADLAALRPVGAgLAATDDLAHLVMVPNPDHHPGGDFRLDGE-RLHRDGE 159
Cdd:cd06422  80 ELLETGGGIKKALPLLGDEPFLVVNGDILWDGDLAPLLLLHA-WRMDALLLLLPLVRNPGHNGVGDFSLDADgRLRRGGG 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 56312080 160 ---PRLTFSGIGVYRPALFAAVAAGtKAPLGPLLREAMDAGRVRGALHRGYWLDVGTPQRLAAL 220
Cdd:cd06422 159 gavAPFTFTGIQILSPELFAGIPPG-KFSLNPLWDRAIAAGRLFGLVYDGLWFDVGTPERLLAA 221
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 3-212 3.33e-54

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: 173.15  E-value: 3.33e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080   3 AMILAAGRGERMRPLTDACPKPLLVAGGRPLIAWHLERLRMAGFTDVVINHAHLGTMIEAALGDGRQFGLHVAYSAETEA 82
Cdd:cd04181   1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGSKFGVNIEYVVQEEP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080  83 LETAGGVRQALALLGDAPFLVINGDVFCDADLAAL--RPVGAGLAATddlahLVMVPNPDHHPGGDFRLDGE-RLHR--- 156
Cdd:cd04181  81 LGTAGAVRNAEDFLGDDDFLVVNGDVLTDLDLSELlrFHREKGADAT-----IAVKEVEDPSRYGVVELDDDgRVTRfve 155

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 56312080 157 ---DGEPRLTFSGIGVYRPALFAAVAAGTKAP---LGPLLREAMDAGRVRGALHRGYWLDVG 212
Cdd:cd04181 156 kptLPESNLANAGIYIFEPEILDYIPEILPRGedeLTDAIPLLIEEGKVYGYPVDGYWLDIG 217
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 3-221 5.54e-43

WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is involved in the biosynthesis, export or translocation of capsule. It is a subfamily of nucleotidyl transferases that transfer nucleotides onto phosphosugars.


Pssm-ID: 133065 [Multi-domain]  Cd Length: 223  Bit Score: 144.62  E-value: 5.54e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080   3 AMILAAGRGERMRPLTDACPKPLLVAGGRPLIAWHLERLRMAGFTDVVINHAHLGTMIEAALGDGRQFGLHVAYSAETEA 82
Cdd:cd06915   1 AVILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYLAEQIEEYFGDGYRGGIRIYYVIEPEP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080  83 LETAGGVRQALALLGDAPFLVINGDVFCDADLAALRpvgAGLAATDDLAHLVMVPNPDHHPGGDFRLDGERL-------H 155
Cdd:cd06915  81 LGTGGAIKNALPKLPEDQFLVLNGDTYFDVDLLALL---AALRASGADATMALRRVPDASRYGNVTVDGDGRviafvekG 157

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 56312080 156 RDGEPRLTFSGIGVYRPALFAAVAAGTKAPLGPLLREAMDAGRVRGALHRGYWLDVGTPQRLAALD 221
Cdd:cd06915 158 PGAAPGLINGGVYLLRKEILAEIPADAFSLEADVLPALVKRGRLYGFEVDGYFIDIGIPEDYARAQ 223
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 1-214 2.06e-36

UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The MJ_1101 protein from Methanococcus jannaschii has been characterized as the GlmU enzyme catalyzing the final two steps of UDP-GlcNAc biosynthesis. Many of the genes identified by this model are in proximity to the GlmS and GlmM genes and are also presumed to be GlmU. However, some archaeal genomes contain multiple closely-related homologs from this family and it is not clear what the substrate specificity is for each of them.


Pssm-ID: 274908 [Multi-domain]  Cd Length: 393  Bit Score: 131.95  E-value: 2.06e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080     1 MRAMILAAGRGERMRPLTDACPKPLLVAGGRPLIAWHLERLRMAGFTDVVINHAHLGTMIEAALGDGRQFGLHVAYSAET 80
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEKVREYFGDGSRGGVPIEYVVQE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080    81 EALETAGGVRQALALLGDaPFLVINGDVFCDADLaaLRpvgaGLAATDDLAHLVM-VPNPDHHpgGDFRLDGERLHR--- 156
Cdd:TIGR03992  81 EQLGTADALGSAKEYVDD-EFLVLNGDVLLDSDL--LE----RLIRAEAPAIAVVeVDDPSDY--GVVETDGGRVTGive 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 56312080   157 ---DGEPRLTFSGIGVYRPALFAAVAAGTKAPLGPL-----LREAMDAGRVRGALHRGYWLDVGTP 214
Cdd:TIGR03992 152 kpeNPPSNLINAGIYLFSPEIFELLEKTKLSPRGEYeltdaLQLLIDEGKVKAVELDGFWLDVGRP 217
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 1-224 1.47e-33

G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family is the long form of Glucose-1-phosphate thymidylyltransferase. Glucose-1-phosphate thymidylyltransferase catalyses the formation of dTDP-glucose, from dTTP and glucose 1-phosphate. It is the first enzyme in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme.There are two forms of Glucose-1-phosphate thymidylyltransferase in bacteria and archeae; short form and long form. The long form, which has an extra 50 amino acids c-terminal, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced.The long from enzymes also have a left-handed parallel helix domain at the c-terminus, whereas, th eshort form enzymes do not have this domain. The homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose.


Pssm-ID: 133032 [Multi-domain]  Cd Length: 236  Bit Score: 120.37  E-value: 1.47e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080   1 MRAMILAAGRGERMRPLTDACPKPLLVAGGRPLIAWHLERLRMAGFTDVVINHAHLGTMIEAALGDGRQFGLHVAYSAET 80
Cdd:cd04189   1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEALGDGSRFGVRITYILQE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080  81 EALETAGGVRQALALLGDAPFLVINGDVFCDADLAAL-RPVGAGLAAtddlAHLVMVPNPDHHPGGDFRLDGERLHRDGE 159
Cdd:cd04189  81 EPLGLAHAVLAARDFLGDEPFVVYLGDNLIQEGISPLvRDFLEEDAD----ASILLAEVEDPRRFGVAVVDDGRIVRLVE 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080 160 -PR-----LTFSGIGVYRPALFAAVAAgtkapLGPLLR---EAMDA--------GRVRGALHRGYWLDVGTPQRLAALDR 222
Cdd:cd04189 157 kPKeppsnLALVGVYAFTPAIFDAISR-----LKPSWRgelEITDAiqwlidrgRRVGYSIVTGWWKDTGTPEDLLEANR 231


                ..
gi 56312080 223 HL 224
Cdd:cd04189 232 LL 233
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 3-214 2.31e-33

NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.


Pssm-ID: 133048 [Multi-domain]  Cd Length: 220  Bit Score: 119.54  E-value: 2.31e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080   3 AMILAAGRGERMRPLTDACPKPLLVAGGRPLIAWHLERLRMAGFTDVVINHAHLGTMIEAALGDGRQFGLHVAYSAETEA 82
Cdd:cd06426   1 VVIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNYLAEMIEDYFGDGSKFGVNISYVREDKP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080  83 LETAGgvrqALALLG---DAPFLVINGDVFCDADLAALRpvgagLAATDDLAHLVMVPNPDHH--PGGDFRLDGERLHRD 157
Cdd:cd06426  81 LGTAG----ALSLLPekpTDPFLVMNGDILTNLNYEHLL-----DFHKENNADATVCVREYEVqvPYGVVETEGGRITSI 151

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 56312080 158 GE-PRLTF---SGIGVYRPALFAAVAAGTKAPLGPLLREAMDAGRVRGAL-HRGYWLDVGTP 214
Cdd:cd06426 152 EEkPTHSFlvnAGIYVLEPEVLDLIPKNEFFDMPDLIEKLIKEGKKVGVFpIHEYWLDIGRP 213
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-217 2.78e-27

Nucleotidyl transferase; This family includes a wide range of enzymes which transfer nucleotides onto phosphosugars.


Pssm-ID: 425709 [Multi-domain]  Cd Length: 243  Bit Score: 104.26  E-value: 2.78e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080     2 RAMILAAGRGERMRPLTDACPKPL-LVAGGRPLIAWHLERLRMAGFTD-VVINHAHLGTMIEAALGDGRQFGLHVAYSAE 79
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLvPVGGKYPLIDYPLSRLANAGIREiIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080    80 TEALETAGGVRQALALLGD--APFLVINGDVFCDADLAAL----RPVGAGLAATddlahLVMVPNPDHHPGGDFRLDGE- 152
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDekSDVLVLGGDHIYRMDLEQAvkfhIEKAADATVT-----FGIVPVEPPTGYGVVEFDDNg 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080   153 RLHR-----DGEPRLTFSGIGVY--RPALFAAVAAGTKAP------LGPLLREAMDAGRVRGA-LHRGY-WLDVGTPQRL 217
Cdd:pfam00483 156 RVIRfvekpKLPKASNYASMGIYifNSGVLDFLAKYLEELkrgedeITDILPKALEDGKLAYAfIFKGYaWLDVGTWDSL 235
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-217 1.26e-23

dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 95.93  E-value: 1.26e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080   1 MRAMILAAGRGERMRPLTDACPKPLLVAGGRPLIAWHLERLRMAGFTDV-VINHAHLGTMIEAALGDGRQFGLHVAYSAE 79
Cdd:COG1209   1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREIlIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080  80 TEALETAGGVRQALALLGDAPFLVINGDVFCDADL-------AALRPVGAGLAATDdlahlvmVPNPdhhpggdfrldgE 152
Cdd:COG1209  81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGlsellreAAARESGATIFGYK-------VEDP------------E 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080 153 R-----LHRDG----------EPRLTFSGIGVY--RPALFAAvAAGTKaplgP----------LLREAMDAGR-VRGALH 204
Cdd:COG1209 142 RygvveFDEDGrvvsleekpkEPKSNLAVTGLYfyDNDVVEI-AKNLK----PsargeleitdANQAYLERGKlVVELLG 216

                       250
                ....*....|....
gi 56312080 205 RGY-WLDVGTPQRL 217
Cdd:COG1209 217 RGFaWLDTGTHESL 230
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
2-225 1.27e-23

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 94.54  E-value: 1.27e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080   2 RAMILAAGRGERMRPLTDACPKPLLVAGGRPLIAWHLERLRMAGFTDVVINHAHLGTMIEAALgDGRQFGLHVAYSAETE 81
Cdd:COG1213   1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEAL-ARPGPDVTFVYNPDYD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080  82 ALETAGGVRQALALLGDaPFLVINGDVFCDAD-LAALrpvgagLAATDDLAHLVmvpNPDHHPGGDfrlDGERLHRDGEP 160
Cdd:COG1213  80 ETNNIYSLWLAREALDE-DFLLLNGDVVFDPAiLKRL------LASDGDIVLLV---DRKWEKPLD---EEVKVRVDEDG 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080 161 RLT----------FSG--IGVYR------PALFAAVAA-----GTKAPLGPLLREAMDAGRVRGAL--HRGYWLDVGTPQ 215
Cdd:COG1213 147 RIVeigkklppeeADGeyIGIFKfsaegaAALREALEAlidegGPNLYYEDALQELIDEGGPVKAVdiGGLPWVEIDTPE 226

                       250
                ....*....|
gi 56312080 216 RLAALDRHLR 225
Cdd:COG1213 227 DLERAEELFA 236
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 1-117 4.88e-21

N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose pyrophosphorylase (GTP: alpha-d-mannose-1-phosphate guanyltransferase) catalyzes the formation of GDP-d-mannose from GTP and alpha-d-mannose-1-Phosphate. It contains an N-terminal catalytic domain and a C-terminal Lefthanded-beta-Helix fold domain. GDP-d-mannose is the activated form of mannose for formation of cell wall lipoarabinomannan and various mannose-containing glycolipids and polysaccharides. The function of GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability. Repression of GDP-mannose pyrophosphorylase in yeast leads to phenotypes, such as cell lysis, defective cell wall, and failure of polarized growth and cell separation.


Pssm-ID: 133047 [Multi-domain]  Cd Length: 233  Bit Score: 87.65  E-value: 4.88e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080   1 MRAMILAAGRGERMRPLTDACPKPLLVAGGRPLIAWHLERLRMAGFTDVVINHAHLGTMIEAALGDGRQ-FGLHVAYSAE 79
Cdd:cd06425   1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYRPEDMVPFLKEYEKkLGIKITFSIE 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 56312080  80 TEALETAGGVRQALALLG--DAPFLVINGDVFCDADLAAL 117
Cdd:cd06425  81 TEPLGTAGPLALARDLLGddDEPFFVLNSDVICDFPLAEL 120
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 3-199 1.55e-20

Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family contains proteins similar to prokaryotic phosphocholine (P-cho) cytidylyltransferases. Phosphocholine (PC) cytidylyltransferases catalyze the transfer of a cytidine monophosphate from CTP to phosphocholine to form CDP-choline. PC is the most abundant phospholipid in eukaryotic membranes and it is also important in prokaryotic membranes. For pathogenic prokaryotes, the cell surface PC facilitates the interaction with host surface and induces attachment and invasion. In addition cell wall PC serves as scaffold for a group of choline-binding proteins that are secreted from the cells. Phosphocholine (PC) cytidylyltransferase is a key enzyme in the prokaryotic choline metabolism pathway. It has been hypothesized to consist of a choline transport system, a choline kinase, CTP:phosphocholine cytidylyltransferase, and a choline phosphotransferase that transfers P-Cho from CDP-Cho to either lipoteichoic acid or lipopolysaccharide.


Pssm-ID: 133014 [Multi-domain]  Cd Length: 229  Bit Score: 86.13  E-value: 1.55e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080   3 AMILAAGRGERMRPLTDACPKPLLVAGGRPLIAWHLERLRMAGFTDVVINHAHLGTMIEAALgdGRQFGLHVAYSAETEA 82
Cdd:cd02523   1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELL--KKYPNIKFVYNPDYAE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080  83 LETAGGVRQALALLGDaPFLVINGDVFCDAD-----LAALRPVGAGLAATDDLAHLVMVpnpDHHPGGDFRLD-GERLHR 156
Cdd:cd02523  79 TNNIYSLYLARDFLDE-DFLLLEGDVVFDPSilerlLSSPADNAILVDKKTKEWEDEYV---KDLDDAGVLLGiISKAKN 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 56312080 157 DGEPRLTFSGIGVYRPALFAAVAagtkaplgPLLREAMDAGRV 199
Cdd:cd02523 155 LEEIQGEYVGISKFSPEDADRLA--------EALEELIEAGRV 189
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 1-117 1.21e-18

G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is the short form of glucose-1-phosphate thymidylyltransferase. Glucose-1-phosphate thymidylyltransferase catalyses the formation of dTDP-glucose, from dTTP and glucose 1-phosphate. It is the first enzyme in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme.There are two forms of Glucose-1-phosphate thymidylyltransferase in bacteria and archeae; short form and long form. The homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose. The long form, which has an extra 50 amino acids c-terminal, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced.


Pssm-ID: 133019 [Multi-domain]  Cd Length: 240  Bit Score: 81.47  E-value: 1.21e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080   1 MRAMILAAGRGERMRPLTDACPKPLLVAGGRPLIAWHLERLRMAGFTDVVI--NHAHLGTMIEaALGDGRQFGLHVAYSA 78
Cdd:cd02538   1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIisTPEDLPLFKE-LLGDGSDLGIRITYAV 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 56312080  79 EtealETAGGVRQALAL----LGDAPFLVINGD-VFCDADLAAL 117
Cdd:cd02538  80 Q----PKPGGLAQAFIIgeefIGDDPVCLILGDnIFYGQGLSPI 119
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 3-117 7.57e-14

The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; N-terminal domain of eEIF-2B epsilon and gamma, subunits of eukaryotic translation initiators, is a subfamily of glycosyltranferase 2 and is predicted to have glycosyltranferase activity. eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit epsilon shares sequence similarity with gamma subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.


Pssm-ID: 133001 [Multi-domain]  Cd Length: 216  Bit Score: 68.05  E-value: 7.57e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080   3 AMILAAGRGERMRPLTDACPKPLLVAGGRPLIAWHLERLRMAGFTDVVI---NHA-----HLGTMIEAALGDGRQfgLHV 74
Cdd:cd02507   3 AVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVvccEHSqaiieHLLKSKWSSLSSKMI--VDV 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 56312080  75 AYSAETEALETAGGVRQALALL-GDapFLVINGDVFCDADLAAL 117
Cdd:cd02507  81 ITSDLCESAGDALRLRDIRGLIrSD--FLLLSCDLVSNIPLSEL 122
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 1-117 4.51e-13

The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; N-terminal domain of gamma subunit of the eukaryotic translation initiation factor 2B (eIF-2B): eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit gamma shares sequence similarity with epsilon subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.


Pssm-ID: 133041 [Multi-domain]  Cd Length: 214  Bit Score: 65.76  E-value: 4.51e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080   1 MRAMILAAGRGERMRPLTDACPKPLLVAGGRPLIAWHLERLRMAGFTDVVI-----NHAHLGTMIEAALGDGRQFgLHVA 75
Cdd:cd04198   1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVvvpeeEQAEISTYLRSFPLNLKQK-LDEV 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 56312080  76 YSAETEALETAGGVRQALA-LLGDapFLVINGDVFCDADLAAL 117
Cdd:cd04198  80 TIVLDEDMGTADSLRHIRKkIKKD--FLVLSCDLITDLPLIEL 120
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 3-117 5.29e-13

N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose pyrophosphorylase; N-terminal domain of the M1P-guanylyltransferase A-isoform like proteins: The proteins of this family are likely to be a isoform of GDP-mannose pyrophosphorylase. Their sequences are highly conserved with mannose-1-phosphate guanyltransferase, but generally about 40-60 bases longer. GDP-mannose pyrophosphorylase (GTP: alpha-d-mannose-1-phosphate guanyltransferase) catalyzes the formation of GDP-d-mannose from GTP and alpha-d-mannose-1-Phosphate. It contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain. GDP-d-mannose is the activated form of mannose for formation of cell wall lipoarabinomannan and various mannose-containing glycolipids and polysaccharides. The function of GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability. Repression of GDP-mannose pyrophosphorylase in yeast leads to phenotypes including cell lysis, defective cell wall, and failure of polarized growth and cell separation.


Pssm-ID: 133050 [Multi-domain]  Cd Length: 257  Bit Score: 66.12  E-value: 5.29e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080   3 AMILAAG--RGERMRPLTDACPKPLLVAGGRPLIAWHLERL-RMAGFTDVVInhahLGTMIEAALGD-----GRQFGLHV 74
Cdd:cd06428   1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACaKVPDLKEVLL----IGFYPESVFSDfisdaQQEFNVPI 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 56312080  75 AYSAETEALETAGGV---RQalALLGDAP--FLVINGDVFCDADLAAL 117
Cdd:cd06428  77 RYLQEYKPLGTAGGLyhfRD--QILAGNPsaFFVLNADVCCDFPLQEL 122
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 3-108 1.18e-11

Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 63.51  E-value: 1.18e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080   3 AMILAAGRGERMRpltDACPKPLLVAGGRPLIAWHLERLRMAGFTDVVINHAHLGTMIEAALGDgrqFGLHVAYsaETEA 82
Cdd:COG1207   5 VVILAAGKGTRMK---SKLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVRAALAD---LDVEFVL--QEEQ 76

                        90       100
                ....*....|....*....|....*...
gi 56312080  83 LETAGGVRQALALLG--DAPFLVINGDV 108
Cdd:COG1207  77 LGTGHAVQQALPALPgdDGTVLVLYGDV 104
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 2-217 2.33e-11

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 62.00  E-value: 2.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080    2 RAMILAAGRGERMRPLTDACPKPLLVAGGRPLIAWHLERLRMAGFTDVVINHAHLGT-MIEAALGDGRQFGLHVAYSAET 80
Cdd:PRK15480   5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTpRFQQLLGDGSQWGLNLQYKVQP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080   81 ealeTAGGVRQALA-----LLGDAPFLVINGDVFCDADLAALR--PVGAGLAATDDLAHlvmVPNPDHHPGGDFRLDGER 153
Cdd:PRK15480  85 ----SPDGLAQAFIigeefIGGDDCALVLGDNIFYGHDLPKLMeaAVNKESGATVFAYH---VNDPERYGVVEFDQNGTA 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 56312080  154 L---HRDGEPRLTFSGIGVY-------RPALFAAVAAGTKAPLGPLLREAMDAGRVRGALH-RGY-WLDVGTPQRL 217
Cdd:PRK15480 158 IsleEKPLQPKSNYAVTGLYfydndvvEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMgRGYaWLDTGTHQSL 233
LicC COG4750
CTP:phosphocholine cytidylyltransferase LicC [Cell wall/membrane/envelope biogenesis, Lipid ...
 1-51 6.09e-11

CTP:phosphocholine cytidylyltransferase LicC [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism];


Pssm-ID: 443784 [Multi-domain]  Cd Length: 228  Bit Score: 59.84  E-value: 6.09e-11
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 56312080   1 MRAMILAAGRGERMRPLTDACPKPLLVAGGRPLIAWHLERLRMAGFTDVVI 51
Cdd:COG4750   1 MNAIILAAGLGSRFAPITYETPKGLLKVNGEPLIERQIRQLHEAGITDITV 51
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 3-108 1.67e-10

N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate uridyltransferase (GlmU). GlmU is an essential bacterial enzyme with both an acetyltransferase and an uridyltransferase activity which have been mapped to the C-terminal and N-terminal domains, respectively. This family represents the N-terminal uridyltransferase. GlmU performs the last two steps in the synthesis of UDP-N-acetylglucosamine (UDP-GlcNAc), which is an essential precursor in both the peptidoglycan and the lipopolysaccharide metabolic pathways in Gram-positive and Gram-negative bacteria, respectively.


Pssm-ID: 133020 [Multi-domain]  Cd Length: 229  Bit Score: 58.68  E-value: 1.67e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080   3 AMILAAGRGERMRpltDACPKPLLVAGGRPLIAWHLERLRMAGFTDVVINHAHLGTMIEAALGDgrqFGLHVAYsaETEA 82
Cdd:cd02540   1 AVILAAGKGTRMK---SDLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVKKALAN---PNVEFVL--QEEQ 72

                        90       100
                ....*....|....*....|....*...
gi 56312080  83 LETAGGVRQALALLGD--APFLVINGDV 108
Cdd:cd02540  73 LGTGHAVKQALPALKDfeGDVLVLYGDV 100
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 1-102 7.87e-09

bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase; Provisional


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 54.99  E-value: 7.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080    1 MRAMILAAGRGERMRpltDACPKPLLVAGGRPLIAWHLERLRMAGFTDVVINHAHLGTMIEAAL-GDG-------RQFGL 72
Cdd:PRK14358   8 LDVVILAAGQGTRMK---SALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGAEQVEAALqGSGvafarqeQQLGT 84

                         90       100       110
                 ....*....|....*....|....*....|
gi 56312080   73 HVAYSAETEALETAGGvrQALALLGDAPFL 102
Cdd:PRK14358  85 GDAFLSGASALTEGDA--DILVLYGDTPLL 112
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-156 2.11e-07

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 50.63  E-value: 2.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080    3 AMILAAGRGERMRpltDACPKPLLVAGGRPLIAWHLERLRMAGFTDVVINHAHLGTMIEAALgdgRQFGLHVAYSAETEA 82
Cdd:PRK14353   8 AIILAAGEGTRMK---SSLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGPGAEAVAAAA---AKIAPDAEIFVQKER 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080   83 LETAGGVRQALALL--GDAPFLVINGDV--FCDADLAALRpvgAGLAATDDLAHLVMVPnPDhhPGGDFRL--DGERLHR 156
Cdd:PRK14353  82 LGTAHAVLAAREALagGYGDVLVLYGDTplITAETLARLR---ERLADGADVVVLGFRA-AD--PTGYGRLivKGGRLVA 155
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-107 2.95e-07

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 50.22  E-value: 2.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080    3 AMILAAGRGERMRpltDACPKPLLVAGGRPLIAWHLERLRMAGFTDVVINHAHLGTMIEAALGDGrqfglhVAYSAETEA 82
Cdd:PRK14354   5 AIILAAGKGTRMK---SKLPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVGHGAEEVKEVLGDR------SEFALQEEQ 75

                         90       100
                 ....*....|....*....|....*..
gi 56312080   83 LETAGGVRQALALLGDAP--FLVINGD 107
Cdd:PRK14354  76 LGTGHAVMQAEEFLADKEgtTLVICGD 102
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
 3-117 6.40e-07

G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; Alpha-D-Glucose-1-phosphate Cytidylyltransferase catalyzes the production of CDP-D-Glucose from alpha-D-Glucose-1-phosphate and MgCTP as substrate. CDP-D-Glucose is the precursor for synthesizing four of the five naturally occurring 3,6-dideoxy sugars-abequose (3,6-dideoxy-D-Xylo-hexose), ascarylose (3,6-dideoxy-L-arabino-hexose), paratose (3,6-dideoxy-D-ribohexose), and tyvelose (3,6-dideoxy-D-arabino-hexose. Deoxysugars are ubiquitous in nature where they function in a variety of biological processes, including cell adhesion, immune response, determination of ABO blood groups, fertilization, antibiotic function, and microbial pathogenicity.


Pssm-ID: 133015 [Multi-domain]  Cd Length: 253  Bit Score: 48.72  E-value: 6.40e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080   3 AMILAAGRGERMRPLTDACPKPLLVAGGRPLIaWHLERLRMA-GFTDVVINHAHLGTMI-------EAALGD------GR 68
Cdd:cd02524   1 VVILAGGLGTRLSEETELKPKPMVEIGGRPIL-WHIMKIYSHyGHNDFILCLGYKGHVIkeyflnyFLHNSDvtidlgTN 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 56312080  69 QFGLHVAYS-------AET-EALETAGGVRQALALLGDA-PFLVINGDVFCDADLAAL 117
Cdd:cd02524  80 RIELHNSDIedwkvtlVDTgLNTMTGGRLKRVRRYLGDDeTFMLTYGDGVSDVNINAL 137
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 1-113 8.58e-07

Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose Pyrophosphorylase (UGPase) 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. UGPase is found in both prokaryotes and eukaryotes, although prokaryotic and eukaryotic forms of UGPase catalyze the same reaction, they share low sequence similarity.


Pssm-ID: 133021 [Multi-domain]  Cd Length: 267  Bit Score: 48.30  E-value: 8.58e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080   1 MRAMILAAGRGERMRPLTDACPKPLLVAGGRPLIAWHLERLRMAGFTDVVI----------NHAHLGTMIEAALgdgRQF 70
Cdd:cd02541   1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIvtgrgkraieDHFDRSYELEETL---EKK 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 56312080  71 GLH--VAYSAETEALETAGGVRQALAL-LGDA-----------PFLVINGDVFCDAD 113
Cdd:cd02541  78 GKTdlLEEVRIISDLANIHYVRQKEPLgLGHAvlcakpfigdePFAVLLGDDLIDSK 134
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
 5-116 8.99e-07

GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; GT2_BcbE_like: The bcbE gene is one of the genes in the capsule biosynthetic locus of Pasteurella multocida. Its deducted product is likely involved in the biosynthesis of the polysaccharide capsule, which is found on surface of a wide range of bacteria. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.


Pssm-ID: 133026 [Multi-domain]  Cd Length: 231  Bit Score: 48.02  E-value: 8.99e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080   5 ILAAGRGERMRPLTDACPKPLLVAGGRPLIAWHLERLRMAG---FTDVV----INHAHLGTMIEAALGDGRQfglhVAYS 77
Cdd:cd04183   3 IPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEWVIESLAKIFdsrFIFICrdehNTKFHLDESLKLLAPNATV----VELD 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 56312080  78 AETE-ALETAGGVRQALAllGDAPFLVINGDVFCDADLAA 116
Cdd:cd04183  79 GETLgAACTVLLAADLID--NDDPLLIFNCDQIVESDLLA 116
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 3-102 2.09e-06

MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine dinucleotide biosynthesis protein A). The family also includes a wide range of other NTP transferase domain.


Pssm-ID: 463715 [Multi-domain]  Cd Length: 159  Bit Score: 46.03  E-value: 2.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080     3 AMILAAGRGERMRPltdacPKPLLVAGGRPLIAWHLERLRMAgFTDVVINHAHlgtmiEAALGDGRQFGLHVAYSAETE- 81
Cdd:pfam12804   1 AVILAGGRSSRMGG-----DKALLPLGGKPLLERVLERLRPA-GDEVVVVAND-----EEVLAALAGLGVPVVPDPDPGq 69

                          90       100
                  ....*....|....*....|....*....
gi 56312080    82 --------ALETAGGVRQALALLGDAPFL 102
Cdd:pfam12804  70 gplagllaALRAAPGADAVLVLACDMPFL 98
ispD TIGR00453
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ...
 3-104 2.35e-06

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase, the IspD protein of the deoxyxylulose pathway of IPP biosynthesis. In about twenty percent of bacterial genomes, this protein occurs as IspDF, a bifunctional fusion protein. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 213532  Cd Length: 217  Bit Score: 46.90  E-value: 2.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080     3 AMILAAGRGERMRPltdACPKPLLVAGGRPLIAWHLERLRMAGFTDVVInhahlgtmIEAALGDGRQFGLHVAYSAETEA 82
Cdd:TIGR00453   2 AVIPAAGRGTRFGS---GVPKQYLELGGRPLLEHALDAFLAHPAIDEVV--------VVVSPDDTEFFQKYLVARAVPKI 70

                          90       100
                  ....*....|....*....|....*.
gi 56312080    83 L----ETAGGVRQALALLGDAPFLVI 104
Cdd:TIGR00453  71 VaggdTRQDSVRNGLKALKDAEFVLV 96
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
3-102 5.29e-06

CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 45.54  E-value: 5.29e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080   3 AMILAAGRGERMrpltdACPKPLLVAGGRPLIAWHLERLRMAGFTDVVINHAHLGTMIEAALgdgRQFGLHVAYSAETE- 81
Cdd:COG2068   6 AIILAAGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADAEEVAAAL---AGLGVRVVVNPDWEe 77

                        90       100       110
                ....*....|....*....|....*....|
gi 56312080  82 --------ALETA-GGVRQALALLGDAPFL 102
Cdd:COG2068  78 gmssslraGLAALpADADAVLVLLGDQPLV 107
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 5-127 1.98e-05

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440824  Cd Length: 224  Bit Score: 43.97  E-value: 1.98e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080   5 ILAAGRGERMRpltDACPKPLLVAGGRPLIAWHLERLRMAGFTD---VVINHAHLGTMIEAALGDGRQFGLHVAysaete 81
Cdd:COG1211   2 IPAAGSGSRMG---AGIPKQFLPLGGKPVLEHTLEAFLAHPRIDeivVVVPPDDIEYFEELLAKYGIDKPVRVV------ 72

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 56312080  82 aletAGG------VRQALALLGDAPFLV---------INGDVFCDAdLAALRPVGAGLAAT 127
Cdd:COG1211  73 ----AGGatrqdsVRNGLEALPDDDDWVlvhdaarplVSPELIDRV-IEAAREYGAAIPAL 128
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-108 2.73e-05

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 44.35  E-value: 2.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080    3 AMILAAGRGERMRpltDACPKPLLVAGGRPLIAWHLERLRMAGFTDVVINHAHLGTMIEAALGDGRQfglhVAYSAETEA 82
Cdd:PRK14355   6 AIILAAGKGTRMK---SDLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHFAGDGD----VSFALQEEQ 78

                         90       100
                 ....*....|....*....|....*...
gi 56312080   83 LETAGGVRQALALL--GDAPFLVINGDV 108
Cdd:PRK14355  79 LGTGHAVACAAPALdgFSGTVLILCGDV 106
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 3-51 3.50e-05

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: 43.28  E-value: 3.50e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 56312080   3 AMILAAGRGERMRPltdACPKPLLVAGGRPLIAWHLERL-RMAGFTDVVI 51
Cdd:cd02516   3 AIILAAGSGSRMGA---DIPKQFLELGGKPVLEHTLEAFlAHPAIDEIVV 49
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
3-51 5.04e-05

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 42.81  E-value: 5.04e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 56312080    3 AMILAAGRGERMRPltdACPKPLLVAGGRPLIAWHLERLRMAGFTDVVI 51
Cdd:PRK00155   6 AIIPAAGKGSRMGA---DRPKQYLPLGGKPILEHTLEAFLAHPRIDEII 51
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 3-102 8.23e-05

GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133025 [Multi-domain]  Cd Length: 186  Bit Score: 41.78  E-value: 8.23e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080   3 AMILAAGRGERMRPltdacPKPLLVAGGRPLIAWHLERLRMAGFTDVVINHAHLGTMIEAALGDGRQFGLHVAYSAE--- 79
Cdd:cd04182   3 AIILAAGRSSRMGG-----NKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALAGLPVVVVINPDWEEgms 77

                        90       100
                ....*....|....*....|....*....
gi 56312080  80 ------TEALetAGGVRQALALLGDAPFL 102
Cdd:cd04182  78 sslaagLEAL--PADADAVLILLADQPLV 104
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
2-111 9.41e-05

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 42.59  E-value: 9.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080    2 RAMILAAGRGERMRPLTDACPKPLLVAGGRPLIAWHLERLRMAGFTDVVI----------NHAHLGTMIEAALGDGRQFG 71
Cdd:PRK13389  10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLvthssknsieNHFDTSFELEAMLEKRVKRQ 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 56312080   72 LHVAYSAETEALETAGGVRQALA------------LLGDAPFLVINGDVFCD 111
Cdd:PRK13389  90 LLDEVQSICPPHVTIMQVRQGLAkglghavlcahpVVGDEPVAVILPDVILD 141
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
1-126 1.23e-04

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 42.18  E-value: 1.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080    1 MRAMILAAGRGERMRPLTDACPKPLLVAGGRPLIAWHLERLRMAGFTDVV-INHA-------HLGTMIE-AALGDGRqfg 71
Cdd:PRK10122   4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVlVTHAsknavenHFDTSYElESLLEQR--- 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 56312080   72 LHVAYSAETEALETAG----GVRQALAL------------LGDAPFLVINGDVFCDAdlAALRPVGAGLAA 126
Cdd:PRK10122  81 VKRQLLAEVQSICPPGvtimNVRQGQPLglghsilcarpaIGDNPFVVVLPDVVIDD--ASADPLRYNLAA 149
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
 1-103 1.84e-04

GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate guanylyltransferase, also called GDP-mannose pyrophosphorylase (GDP-MP), catalyzes the formation of GDP-Mannose from mannose-1-phosphate and GTP. Mannose is a key monosaccharide for glycosylation of proteins and lipids. GDP-Mannose is the activated donor for mannosylation of various biomolecules. This enzyme is known to be bifunctional, as both mannose-6-phosphate isomerase and mannose-1-phosphate guanylyltransferase. This CD covers the N-terminal GDP-mannose-1-phosphate guanylyltransferase domain, whereas the isomerase function is located at the C-terminal half. GDP-MP is a member of the nucleotidyltransferase family of enzymes.


Pssm-ID: 133003 [Multi-domain]  Cd Length: 274  Bit Score: 41.41  E-value: 1.84e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080   1 MRAMILAAGRGERMRPL-TDACPKPLL-VAGGRPLIAWHLERLRMAGFTD---VVINHAHLGTMIEAAlgdgRQFGLHVA 75
Cdd:cd02509   1 IYPVILAGGSGTRLWPLsRESYPKQFLkLFGDKSLLQQTLDRLKGLVPPDrilVVTNEEYRFLVREQL----PEGLPEEN 76

                        90       100       110
                ....*....|....*....|....*....|....
gi 56312080  76 YSAETEALETAGGVrqALALL------GDAPFLV 103
Cdd:cd02509  77 IILEPEGRNTAPAI--ALAALylakrdPDAVLLV 108
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 6-110 2.76e-04

GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP:adenosylcobinamide-phosphate guanylyltransferase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441867 [Multi-domain]  Cd Length: 185  Bit Score: 40.26  E-value: 2.76e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080   6 LAAGRGERMrpltDACPKPLLVAGGRPLIAWHLERLRMAGFTD--VVINHAHLGTmieAALGDGRQFglhvaysaetEAL 83
Cdd:COG2266   1 MAGGKGTRL----GGGEKPLLEICGKPMIDRVIDALEESCIDKiyVAVSPNTPKT---REYLKERGV----------EVI 63

                        90       100       110
                ....*....|....*....|....*....|..
gi 56312080  84 ETAGG-----VRQALALLGDaPFLVINGDVFC 110
Cdd:COG2266  64 ETPGEgyvedLNEALESISG-PVLVVPADLPL 94
ispDF PRK09382
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ...
 3-51 4.19e-04

bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase protein; Provisional


Pssm-ID: 236492 [Multi-domain]  Cd Length: 378  Bit Score: 40.60  E-value: 4.19e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 56312080    3 AMILAAGRGERMRPltdACPKPLLVAGGRPLIAWHLERL-RMAGFTDVVI 51
Cdd:PRK09382   8 LVIVAAGRSTRFSA---EVKKQWLRIGGKPLWLHVLENLsSAPAFKEIVV 54
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 3-24 6.78e-04

Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate transport and metabolism];


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 40.06  E-value: 6.78e-04
                        10        20
                ....*....|....*....|..
gi 56312080   3 AMILAAGRGERMRPLTDACPKP 24
Cdd:COG0448   4 AIILAGGRGSRLGPLTKDRAKP 25
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 1-52 6.89e-04

MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme molybdopterin-guanine dinucleotide biosynthesis protein A (MobA). All mononuclear molybdoenzymes bind molybdenum in complex with an organic cofactor termed molybdopterin (MPT). In many bacteria, including Escherichia coli, molybdopterin can be further modified by attachment of a GMP group to the terminal phosphate of molybdopterin to form molybdopterin guanine dinucleotide (MGD). This GMP attachment step is catalyzed by MobA, by linking a guanosine 5'-phosphate to MPT forming molybdopterin guanine dinucleotide. This reaction requires GTP, MgCl2, and the MPT form of the cofactor. It is a reaction unique to prokaryotes, and therefore may represent a potential drug target.


Pssm-ID: 133000 [Multi-domain]  Cd Length: 181  Bit Score: 39.10  E-value: 6.89e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 56312080   1 MRAMILAAGRGERMrpltdACPKPLLVAGGRPLIAWHLERLRMAgFTDVVIN 52
Cdd:cd02503   1 ITGVILAGGKSRRM-----GGDKALLELGGKPLLEHVLERLKPL-VDEVVIS 46
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 3-52 7.00e-04

Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; Molybdopterin-guanine dinucleotide biosynthesis protein A is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 440509 [Multi-domain]  Cd Length: 188  Bit Score: 39.41  E-value: 7.00e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 56312080   3 AMILAAGRGERMrpltdACPKPLLVAGGRPLIAWHLERLRMAgFTDVVIN 52
Cdd:COG0746   7 GVILAGGRSRRM-----GQDKALLPLGGRPLLERVLERLRPQ-VDEVVIV 50
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
 3-30 1.98e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 38.67  E-value: 1.98e-03
                         10        20
                 ....*....|....*....|....*...
gi 56312080    3 AMILAAGRGERMRPLTDACPKPLLVAGG 30
Cdd:PRK00725  18 ALILAGGRGSRLKELTDKRAKPAVYFGG 45
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-107 2.17e-03

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 38.55  E-value: 2.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080    3 AMILAAGRGERMRplTDAcPKPLLVAGGRPLIAWHLERLRMAGFTDVVINHAHLGTMIEAALGDgrqfgLHVAYSAETEA 82
Cdd:PRK14356   8 ALILAAGKGTRMH--SDK-PKVLQTLLGEPMLRFVYRALRPLFGDNVWTVVGHRADMVRAAFPD-----EDARFVLQEQQ 79

                         90       100
                 ....*....|....*....|....*...
gi 56312080   83 LETAGGVRQALALLGDAPF---LVINGD 107
Cdd:PRK14356  80 LGTGHALQCAWPSLTAAGLdrvLVVNGD 107
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
 3-31 4.02e-03

ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ADP-glucose pyrophosphorylase (glucose-1-phosphate adenylyltransferase) catalyzes a very important step in the biosynthesis of alpha 1,4-glucans (glycogen or starch) in bacteria and plants: synthesis of the activated glucosyl donor, ADP-glucose, from glucose-1-phosphate and ATP. ADP-glucose pyrophosphorylase is a tetrameric allosterically regulated enzyme. While a homotetramer in bacteria, in plant chloroplasts and amyloplasts, it is a heterotetramer of two different, yet evolutionary related, subunits. There are a number of conserved regions in the sequence of bacterial and plant ADP-glucose pyrophosphorylase subunits. It is a subfamily of a very diverse glycosy transferase family 2.


Pssm-ID: 133002 [Multi-domain]  Cd Length: 200  Bit Score: 37.14  E-value: 4.02e-03
                        10        20
                ....*....|....*....|....*....
gi 56312080   3 AMILAAGRGERMRPLTDACPKPLLVAGGR 31
Cdd:cd02508   1 AIILAGGEGTRLSPLTKKRAKPAVPFGGR 29
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 5-108 4.75e-03

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 37.60  E-value: 4.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080    5 ILAAGRGERMRpltDACPKPLLVAGGRPLIAWHLE---------RLRMAGftdvvinhaHLGTMIEAALGDgrQFGLHva 75
Cdd:PRK14360   6 ILAAGKGTRMK---SSLPKVLHPLGGKSLVERVLDsceelkpdrRLVIVG---------HQAEEVEQSLAH--LPGLE-- 69

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 56312080   76 YSAETEALETAGGVRQALALL----GDapFLVINGDV 108
Cdd:PRK14360  70 FVEQQPQLGTGHAVQQLLPVLkgfeGD--LLVLNGDV 104
mobA PRK00317
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
 1-52 7.37e-03

molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed


Pssm-ID: 234725 [Multi-domain]  Cd Length: 193  Bit Score: 36.32  E-value: 7.37e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 56312080    1 MRAMILAAGRGERMrpltDACPKPLLVAGGRPLIAWHLERLRmAGFTDVVIN 52
Cdd:PRK00317   4 ITGVILAGGRSRRM----GGVDKGLQELNGKPLIQHVIERLA-PQVDEIVIN 50
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-102 7.88e-03

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 37.05  E-value: 7.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56312080    1 MRAMILAAGRGERMRpltDACPKPLLVAGGRPLIAWHLER-LRMAGFTDVVINHAHlgTMIEAALGDgrqfglHVAYSAE 79
Cdd:PRK14357   1 MRALVLAAGKGTRMK---SKIPKVLHKISGKPMINWVIDTaKKVAQKVGVVLGHEA--ELVKKLLPE------WVKIFLQ 69

                         90       100       110
                 ....*....|....*....|....*....|...
gi 56312080   80 TEALETAGGVRQA----------LALLGDAPFL 102
Cdd:PRK14357  70 EEQLGTAHAVMCArdfiepgddlLILYGDVPLI 102
 
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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