NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|256796963|gb|ACV27619|]
View 

Nucleotidyl transferase [Kangiella koreensis DSM 16069]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 2-222 8.38e-102

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: 294.75  E-value: 8.38e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963   2 KAMILAAGRGERMRPLTDERPKPLLKVNGKALIEWHIEALKEAGISDIIINTSWLGELIPEYLGDGAYWGVNLSFSPEEQ 81
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRFGVRITYVDEGE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963  82 ALETAGGIRKALDFFENEPFIVVNGDVWTDIDYTGIAKAPESS---AHIVLVPNPEHHPEGDFCVTEGGKVKS------E 152
Cdd:COG1208   81 PLGTGGALKRALPLLGDEPFLVLNGDILTDLDLAALLAFHREKgadATLALVPVPDPSRYGVVELDGDGRVTRfvekpeE 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963 153 GEPKLTFSGIGVYQPKVFADLPEDEAIPLGPILRQLMEQDDVTYELYQGRWHDIGTPERLQSLNESFQRK 222
Cdd:COG1208  161 PPSNLINAGIYVLEPEIFDYIPEGEPFDLEDLLPRLIAEGRVYGYVHDGYWLDIGTPEDLLEANALLLSG 230
 
Name Accession Description Interval E-value
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 2-222 8.38e-102

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: 294.75  E-value: 8.38e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963   2 KAMILAAGRGERMRPLTDERPKPLLKVNGKALIEWHIEALKEAGISDIIINTSWLGELIPEYLGDGAYWGVNLSFSPEEQ 81
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRFGVRITYVDEGE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963  82 ALETAGGIRKALDFFENEPFIVVNGDVWTDIDYTGIAKAPESS---AHIVLVPNPEHHPEGDFCVTEGGKVKS------E 152
Cdd:COG1208   81 PLGTGGALKRALPLLGDEPFLVLNGDILTDLDLAALLAFHREKgadATLALVPVPDPSRYGVVELDGDGRVTRfvekpeE 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963 153 GEPKLTFSGIGVYQPKVFADLPEDEAIPLGPILRQLMEQDDVTYELYQGRWHDIGTPERLQSLNESFQRK 222
Cdd:COG1208  161 PPSNLINAGIYVLEPEIFDYIPEGEPFDLEDLLPRLIAEGRVYGYVHDGYWLDIGTPEDLLEANALLLSG 230
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 2-215 2.49e-92

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: 270.21  E-value: 2.49e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963   2 KAMILAAGRGERMRPLTDERPKPLLKVNGKALIEWHIEALKEAGISDIIINTSWLGELIPEYLGDgAYWGVNLSFSPEE- 80
Cdd:cd06422    1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHLGD-SRFGLRITISDEPd 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963  81 QALETAGGIRKALDFFENEPFIVVNGDVWTDIDYTG-----IAKAPESSAHIVLVPNPEHHPEGDFCVTEGGKVKSEGE- 154
Cdd:cd06422   80 ELLETGGGIKKALPLLGDEPFLVVNGDILWDGDLAPllllhAWRMDALLLLLPLVRNPGHNGVGDFSLDADGRLRRGGGg 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 256796963 155 --PKLTFSGIGVYQPKVFADLPEdEAIPLGPILRQLMEQDDVTYELYQGRWHDIGTPERLQSL 215
Cdd:cd06422  160 avAPFTFTGIQILSPELFAGIPP-GKFSLNPLWDRAIAAGRLFGLVYDGLWFDVGTPERLLAA 221
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 1-225 7.77e-49

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: 164.30  E-value: 7.77e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963    1 MKAMILAAGRGERMRPLTDERPKPLLKVNGKALIEWHIEALKEAGISDIIINTSWLGELIPEYLGDGAYWGVNLSFSPEE 80
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEKVREYFGDGSRGGVPIEYVVQE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963   81 QALETAGGIRKALDFFEnEPFIVVNGDVWTDID-YTGIAKAPESSAHIVLVPNPEhhpegDFCV--TEGGKV-----KSE 152
Cdd:TIGR03992  81 EQLGTADALGSAKEYVD-DEFLVLNGDVLLDSDlLERLIRAEAPAIAVVEVDDPS-----DYGVveTDGGRVtgiveKPE 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963  153 GEP-KLTFSGIGVYQPKVFADLpedEAIPLGP--------ILRQLMEQDDVTYELYQGRWHDIGTPERLQSLNESFQRKL 223
Cdd:TIGR03992 155 NPPsNLINAGIYLFSPEIFELL---EKTKLSPrgeyeltdALQLLIDEGKVKAVELDGFWLDVGRPWDLLDANEALLDNL 231


                  ..
gi 256796963  224 KT 225
Cdd:TIGR03992 232 EP 233
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-212 4.65e-31

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: 114.27  E-value: 4.65e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963    2 KAMILAAGRGERMRPLTDERPKPL-LKVNGKALIEWHIEALKEAGISDII-INTSWLGELIPEYLGDGAYWGVNLSFSPE 79
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLvPVGGKYPLIDYPLSRLANAGIREIIvILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963   80 EQALETAGGIRKALDFFENE--PFIVVNGDVWTDIDYT-----GIAKAPESSAHIVLVPnpeHHPEGDFCVTE---GGKV 149
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEksDVLVLGGDHIYRMDLEqavkfHIEKAADATVTFGIVP---VEPPTGYGVVEfddNGRV 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 256796963  150 -----KSEGEPKLTFSGIGVY--QPKVFADLPED------EAIPLGPILRQLMEQDDVTYElYQGR---WHDIGTPERL 212
Cdd:pfam00483 158 irfveKPKLPKASNYASMGIYifNSGVLDFLAKYleelkrGEDEITDILPKALEDGKLAYA-FIFKgyaWLDVGTWDSL 235
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-107 7.61e-10

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 57.92  E-value: 7.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963   3 AMILAAGRGERMRpltDERPKPLLKVNGKALIEWHIEALKEAGISDIIINTSWLGELIPEYLGDGAywgvnlSFSPEEQA 82
Cdd:PRK14354   5 AIILAAGKGTRMK---SKLPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVGHGAEEVKEVLGDRS------EFALQEEQ 75

                         90       100
                 ....*....|....*....|....*..
gi 256796963  83 LETAGGIRKALDFFENEP--FIVVNGD 107
Cdd:PRK14354  76 LGTGHAVMQAEEFLADKEgtTLVICGD 102
 
Name Accession Description Interval E-value
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 2-222 8.38e-102

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: 294.75  E-value: 8.38e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963   2 KAMILAAGRGERMRPLTDERPKPLLKVNGKALIEWHIEALKEAGISDIIINTSWLGELIPEYLGDGAYWGVNLSFSPEEQ 81
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRFGVRITYVDEGE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963  82 ALETAGGIRKALDFFENEPFIVVNGDVWTDIDYTGIAKAPESS---AHIVLVPNPEHHPEGDFCVTEGGKVKS------E 152
Cdd:COG1208   81 PLGTGGALKRALPLLGDEPFLVLNGDILTDLDLAALLAFHREKgadATLALVPVPDPSRYGVVELDGDGRVTRfvekpeE 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963 153 GEPKLTFSGIGVYQPKVFADLPEDEAIPLGPILRQLMEQDDVTYELYQGRWHDIGTPERLQSLNESFQRK 222
Cdd:COG1208  161 PPSNLINAGIYVLEPEIFDYIPEGEPFDLEDLLPRLIAEGRVYGYVHDGYWLDIGTPEDLLEANALLLSG 230
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 2-215 2.49e-92

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: 270.21  E-value: 2.49e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963   2 KAMILAAGRGERMRPLTDERPKPLLKVNGKALIEWHIEALKEAGISDIIINTSWLGELIPEYLGDgAYWGVNLSFSPEE- 80
Cdd:cd06422    1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHLGD-SRFGLRITISDEPd 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963  81 QALETAGGIRKALDFFENEPFIVVNGDVWTDIDYTG-----IAKAPESSAHIVLVPNPEHHPEGDFCVTEGGKVKSEGE- 154
Cdd:cd06422   80 ELLETGGGIKKALPLLGDEPFLVVNGDILWDGDLAPllllhAWRMDALLLLLPLVRNPGHNGVGDFSLDADGRLRRGGGg 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 256796963 155 --PKLTFSGIGVYQPKVFADLPEdEAIPLGPILRQLMEQDDVTYELYQGRWHDIGTPERLQSL 215
Cdd:cd06422  160 avAPFTFTGIQILSPELFAGIPP-GKFSLNPLWDRAIAAGRLFGLVYDGLWFDVGTPERLLAA 221
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 3-207 5.75e-60

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: 187.79  E-value: 5.75e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963   3 AMILAAGRGERMRPLTDERPKPLLKVNGKALIEWHIEALKEAGISDIIINTSWLGELIPEYLGDGAYWGVNLSFSPEEQA 82
Cdd:cd04181    1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGSKFGVNIEYVVQEEP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963  83 LETAGGIRKALDFFENEPFIVVNGDVWTDIDYTGIAKAPESSAHIVLVPNPEHHPEGDF--CVTEG-GKVK------SEG 153
Cdd:cd04181   81 LGTAGAVRNAEDFLGDDDFLVVNGDVLTDLDLSELLRFHREKGADATIAVKEVEDPSRYgvVELDDdGRVTrfvekpTLP 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 256796963 154 EPKLTFSGIGVYQPKVFADLPEDEAIP---LGPILRQLMEQDDVTYELYQGRWHDIG 207
Cdd:cd04181  161 ESNLANAGIYIFEPEILDYIPEILPRGedeLTDAIPLLIEEGKVYGYPVDGYWLDIG 217
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 1-225 7.77e-49

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: 164.30  E-value: 7.77e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963    1 MKAMILAAGRGERMRPLTDERPKPLLKVNGKALIEWHIEALKEAGISDIIINTSWLGELIPEYLGDGAYWGVNLSFSPEE 80
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEKVREYFGDGSRGGVPIEYVVQE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963   81 QALETAGGIRKALDFFEnEPFIVVNGDVWTDID-YTGIAKAPESSAHIVLVPNPEhhpegDFCV--TEGGKV-----KSE 152
Cdd:TIGR03992  81 EQLGTADALGSAKEYVD-DEFLVLNGDVLLDSDlLERLIRAEAPAIAVVEVDDPS-----DYGVveTDGGRVtgiveKPE 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963  153 GEP-KLTFSGIGVYQPKVFADLpedEAIPLGP--------ILRQLMEQDDVTYELYQGRWHDIGTPERLQSLNESFQRKL 223
Cdd:TIGR03992 155 NPPsNLINAGIYLFSPEIFELL---EKTKLSPrgeyeltdALQLLIDEGKVKAVELDGFWLDVGRPWDLLDANEALLDNL 231


                  ..
gi 256796963  224 KT 225
Cdd:TIGR03992 232 EP 233
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 3-213 3.01e-45

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: 150.40  E-value: 3.01e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963   3 AMILAAGRGERMRPLTDERPKPLLKVNGKALIEWHIEALKEAGISDIIINTSWLGELIPEYLGDGAYWGVNLSFSPEEQA 82
Cdd:cd06915    1 AVILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYLAEQIEEYFGDGYRGGIRIYYVIEPEP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963  83 LETAGGIRKALDFFENEPFIVVNGDVWTDIDYTGIAKA---PESSAHIVLVPNPEHHPEGDFCVTEGGKV------KSEG 153
Cdd:cd06915   81 LGTGGAIKNALPKLPEDQFLVLNGDTYFDVDLLALLAAlraSGADATMALRRVPDASRYGNVTVDGDGRViafvekGPGA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963 154 EPKLTFSGIGVYQPKVFADLPEDEAIPLGPILRQLMEQDDVTYELYQGRWHDIGTPERLQ 213
Cdd:cd06915  161 APGLINGGVYLLRKEILAEIPADAFSLEADVLPALVKRGRLYGFEVDGYFIDIGIPEDYA 220
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 1-217 2.51e-42

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: 143.09  E-value: 2.51e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963   1 MKAMILAAGRGERMRPLTDERPKPLLKVNGKALIEWHIEALKEAGISDIIINTSWLGELIPEYLGDGAYWGVNLSFSPEE 80
Cdd:cd04189    1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEALGDGSRFGVRITYILQE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963  81 QALETAGGIRKALDFFENEPFIVVNGDVWTDIDYTGIAK---APESSAHIVL--VPNPEHHpegDFCVTEGGKV-----K 150
Cdd:cd04189   81 EPLGLAHAVLAARDFLGDEPFVVYLGDNLIQEGISPLVRdflEEDADASILLaeVEDPRRF---GVAVVDDGRIvrlveK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963 151 SEgEPKLTFSGIGVY--QPKVFadlpedEAIP-LGPILR---------QLMEQD--DVTYELYQGRWHDIGTPERLQSLN 216
Cdd:cd04189  158 PK-EPPSNLALVGVYafTPAIF------DAISrLKPSWRgeleitdaiQWLIDRgrRVGYSIVTGWWKDTGTPEDLLEAN 230


                 .
gi 256796963 217 E 217
Cdd:cd04189  231 R 231
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 3-216 1.22e-41

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: 141.11  E-value: 1.22e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963   3 AMILAAGRGERMRPLTDERPKPLLKVNGKALIEWHIEALKEAGISDIIINTSWLGELIPEYLGDGAYWGVNLSFSPEEQA 82
Cdd:cd06426    1 VVIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNYLAEMIEDYFGDGSKFGVNISYVREDKP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963  83 LETAGGIrKALDFFENEPFIVVNGDVWTDIDYTGIAKapessAHIvlvpnpEHHPEGDFCV-------------TEGGKV 149
Cdd:cd06426   81 LGTAGAL-SLLPEKPTDPFLVMNGDILTNLNYEHLLD-----FHK------ENNADATVCVreyevqvpygvveTEGGRI 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 256796963 150 KS-EGEPKLTF---SGIGVYQPKVFADLPEDEAIPLGPILRQLMEQDD--VTYELYqGRWHDIGTPERLQSLN 216
Cdd:cd06426  149 TSiEEKPTHSFlvnAGIYVLEPEVLDLIPKNEFFDMPDLIEKLIKEGKkvGVFPIH-EYWLDIGRPEDYEKAN 220
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 3-213 1.26e-33

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: 120.41  E-value: 1.26e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963   3 AMILAAGRGERMRPLTDERPKPLLKVNGKALIEWHIEALKEAGISDIIINTSWLGELIPEYLGDgaYWGVNLSFSPEEQA 82
Cdd:cd02523    1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKK--YPNIKFVYNPDYAE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963  83 LETAGGIRKALDFFeNEPFIVVNGDVWtdIDYTGIAKAPESSAHIVLVPNP----------EHHPEGDFCVTEGGKVKSE 152
Cdd:cd02523   79 TNNIYSLYLARDFL-DEDFLLLEGDVV--FDPSILERLLSSPADNAILVDKktkewedeyvKDLDDAGVLLGIISKAKNL 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 256796963 153 GEPKLTFSGIGVYQPKVFADLPE--DEAIPLGP-------ILRQLMEQDDVTYELYQ-GRWHDIGTPERLQ 213
Cdd:cd02523  156 EEIQGEYVGISKFSPEDADRLAEalEELIEAGRvnlyyedALQRLISEEGVKVKDISdGFWYEIDDLEDLE 226
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-212 4.65e-31

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: 114.27  E-value: 4.65e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963    2 KAMILAAGRGERMRPLTDERPKPL-LKVNGKALIEWHIEALKEAGISDII-INTSWLGELIPEYLGDGAYWGVNLSFSPE 79
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLvPVGGKYPLIDYPLSRLANAGIREIIvILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963   80 EQALETAGGIRKALDFFENE--PFIVVNGDVWTDIDYT-----GIAKAPESSAHIVLVPnpeHHPEGDFCVTE---GGKV 149
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEksDVLVLGGDHIYRMDLEqavkfHIEKAADATVTFGIVP---VEPPTGYGVVEfddNGRV 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 256796963  150 -----KSEGEPKLTFSGIGVY--QPKVFADLPED------EAIPLGPILRQLMEQDDVTYElYQGR---WHDIGTPERL 212
Cdd:pfam00483 158 irfveKPKLPKASNYASMGIYifNSGVLDFLAKYleelkrGEDEITDILPKALEDGKLAYA-FIFKgyaWLDVGTWDSL 235
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
2-108 2.21e-29

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 109.56  E-value: 2.21e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963   2 KAMILAAGRGERMRPLTDERPKPLLKVNGKALIEWHIEALKEAGISDIIINTSWLGELIPEYLGDGaYWGVNLSFSPEEQ 81
Cdd:COG1213    1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEALARP-GPDVTFVYNPDYD 79

                         90       100
                 ....*....|....*....|....*..
gi 256796963  82 ALETAGGIRKALDFFeNEPFIVVNGDV 108
Cdd:COG1213   80 ETNNIYSLWLAREAL-DEDFLLLNGDV 105
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-227 3.21e-28

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 107.87  E-value: 3.21e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963   1 MKAMILAAGRGERMRPLTDERPKPLLKVNGKALIEWHIEALKEAGISDI-IINTSWLGELIPEYLGDGAYWGVNLSFSPE 79
Cdd:COG1209    1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREIlIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963  80 EQALETAGGIRKALDFFENEPFIVVNGDvwTDIDYTGI------AKAPESSAHIVL--VPNPEHhpegdFCVTE---GGK 148
Cdd:COG1209   81 PEPLGLAHAFIIAEDFIGGDPVALVLGD--NIFYGDGLsellreAAARESGATIFGykVEDPER-----YGVVEfdeDGR 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963 149 VKS--E--GEPKLTFSGIGVY--QPKVFadlpeDEAIPLGP----------ILRQLMEQDD-VTYELYQGR-WHDIGTPE 210
Cdd:COG1209  154 VVSleEkpKEPKSNLAVTGLYfyDNDVV-----EIAKNLKPsargeleitdANQAYLERGKlVVELLGRGFaWLDTGTHE 228

                        250
                 ....*....|....*..
gi 256796963 211 RLQSLNesfqRKLKTIE 227
Cdd:COG1209  229 SLLEAN----RFVLTIE 241
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 1-111 1.80e-24

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: 96.90  E-value: 1.80e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963   1 MKAMILAAGRGERMRPLTDERPKPLLKVNGKALIEWHIEALKEAGISDIIINTSWLGELIPEYLGD-GAYWGVNLSFSPE 79
Cdd:cd06425    1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYRPEDMVPFLKEyEKKLGIKITFSIE 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 256796963  80 EQALETAGGIRKALDFFE--NEPFIVVNGDVWTD 111
Cdd:cd06425   81 TEPLGTAGPLALARDLLGddDEPFFVLNSDVICD 114
LicC COG4750
CTP:phosphocholine cytidylyltransferase LicC [Cell wall/membrane/envelope biogenesis, Lipid ...
 1-109 1.71e-23

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


Pssm-ID: 443784 [Multi-domain]  Cd Length: 228  Bit Score: 94.13  E-value: 1.71e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963   1 MKAMILAAGRGERMRPLTDERPKPLLKVNGKALIEWHIEALKEAGISDIIINTSWLGELIpEYLGDGayWGVNLSFSPEE 80
Cdd:COG4750    1 MNAIILAAGLGSRFAPITYETPKGLLKVNGEPLIERQIRQLHEAGITDITVVVGYLKEQF-EYLEDK--YGVKLIYNPDY 77

                         90       100
                 ....*....|....*....|....*....
gi 256796963  81 QALETAGGIRKALDFFENEpfIVVNGDVW 109
Cdd:COG4750   78 AEYNNISSLYLVRDKLGNT--YICSSDNY 104
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 1-213 1.41e-20

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: 86.47  E-value: 1.41e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963   1 MKAMILAAGRGERMRPLTDERPKPLLKVNGKALIEWHIEALKEAGISDIIINTSwlGELIPEY---LGDGAYWGVNLSFs 77
Cdd:cd02538    1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIIST--PEDLPLFkelLGDGSDLGIRITY- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963  78 pEEQalETAGGIRKAL----DFFENEPFIVVNGD-VWTDIDYTGI---AKAPESSAHIVL--VPNPEHhpegdFCVTE-- 145
Cdd:cd02538   78 -AVQ--PKPGGLAQAFiigeEFIGDDPVCLILGDnIFYGQGLSPIlqrAAAQKEGATVFGyeVNDPER-----YGVVEfd 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963 146 -GGKVKSEGE----PKLTFS--GIGVYQPKVFadlpeDEAIPLGP----------ILRQLMEQDDVTYELYqGR---WHD 205
Cdd:cd02538  150 eNGRVLSIEEkpkkPKSNYAvtGLYFYDNDVF-----EIAKQLKPsargeleitdVNNEYLEKGKLSVELL-GRgfaWLD 223


                 ....*...
gi 256796963 206 IGTPERLQ 213
Cdd:cd02538  224 TGTHESLL 231
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 1-120 6.70e-19

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: 81.53  E-value: 6.70e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963   1 MKAMILAAGRGERMRPLTDERPKPLLKVNGKALIEWHIEALKEAGISDIIINTSWLGELIPEYLGDGAYWG------VNL 74
Cdd:cd02507    1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQAIIEHLLKSKWSSlsskmiVDV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 256796963  75 SFSPEEQALETAGGIRKALDfFENEPFIVVNGDVWTDIDYTGIAKA 120
Cdd:cd02507   81 ITSDLCESAGDALRLRDIRG-LIRSDFLLLSCDLVSNIPLSELLEE 125
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 1-108 5.06e-14

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: 70.44  E-value: 5.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963   1 MKAMILAAGRGERMRpltDERPKPLLKVNGKALIEWHIEALKEAGISDIIINTSWLGELIPEYLGDgaywgVNLSFSPEE 80
Cdd:COG1207    3 LAVVILAAGKGTRMK---SKLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVRAALAD-----LDVEFVLQE 74

                         90       100       110
                 ....*....|....*....|....*....|
gi 256796963  81 QALETAGGIRKALDFFE--NEPFIVVNGDV 108
Cdd:COG1207   75 EQLGTGHAVQQALPALPgdDGTVLVLYGDV 104
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 3-108 7.68e-14

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: 67.93  E-value: 7.68e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963   3 AMILAAGRGERMRpltDERPKPLLKVNGKALIEWHIEALKEAGISDIIINTSWLGELIPEYLGDGaywgvNLSFSPEEQA 82
Cdd:cd02540    1 AVILAAGKGTRMK---SDLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVKKALANP-----NVEFVLQEEQ 72

                         90       100
                 ....*....|....*....|....*...
gi 256796963  83 LETAGGIRKALDFFE--NEPFIVVNGDV 108
Cdd:cd02540   73 LGTGHAVKQALPALKdfEGDVLVLYGDV 100
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 1-113 1.23e-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: 67.30  E-value: 1.23e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963   1 MKAMILAAGRGERMRPLTDERPKPLLKVNGKALIEWHIEALKEAGISDIIINTS---------WLGELIPEYLGDGAYwg 71
Cdd:cd04198    1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPeeeqaeistYLRSFPLNLKQKLDE-- 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 256796963  72 vnlSFSPEEQALETAGGIRKALDfFENEPFIVVNGDVWTDID 113
Cdd:cd04198   79 ---VTIVLDEDMGTADSLRHIRK-KIKKDFLVLSCDLITDLP 116
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 3-108 7.27e-12

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: 61.44  E-value: 7.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963    3 AMILAAGRGERMRpltdeRPKPLLKVNGKALIEWHIEALKEAGiSDIIINTSWlGELIPEYLGDGAYWGVNlsfspEEQA 82
Cdd:pfam12804   1 AVILAGGRSSRMG-----GDKALLPLGGKPLLERVLERLRPAG-DEVVVVAND-EEVLAALAGLGVPVVPD-----PDPG 68

                          90       100
                  ....*....|....*....|....*..
gi 256796963   83 LETAGGIRKALDFFE-NEPFIVVNGDV 108
Cdd:pfam12804  69 QGPLAGLLAALRAAPgADAVLVLACDM 95
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 3-130 8.63e-12

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: 62.66  E-value: 8.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963   3 AMILAAG--RGERMRPLTDERPKPLLKVNGKALIEWHIEALKE-AGISDIIINTSWLGELIPEYLGDGA-YWGVNLSFSP 78
Cdd:cd06428    1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKvPDLKEVLLIGFYPESVFSDFISDAQqEFNVPIRYLQ 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 256796963  79 EEQALETAGGI---RKALDFFENEPFIVVNGDVWTDIDYTGIAKAPESSAHIVLV 130
Cdd:cd06428   81 EYKPLGTAGGLyhfRDQILAGNPSAFFVLNADVCCDFPLQELLEFHKKHGASGTI 135
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 1-210 9.42e-12

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: 62.94  E-value: 9.42e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963   1 MKAMILAAGRGERMRPLTDERPKPLLKVNGKALIEWHIEALKEAGISDIIINTSWLGELIPEYLgDGAY----------- 69
Cdd:cd02541    1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRGKRAIEDHF-DRSYeleetlekkgk 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963  70 -----------WGVNLSFSPEEQALETAGGIRKALDFFENEPFIVVNGDVWTDiDYTGIAK----APESSAHIVL----- 129
Cdd:cd02541   80 tdlleevriisDLANIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLID-SKEPCLKqlieAYEKTGASVIaveev 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963 130 ---------VPNPEHHPEGDFCVT---EggKVKSEGEPKlTFSGIG--VYQPKVFADLPEDEA-----IPLGPILRQLME 190
Cdd:cd02541  159 ppedvskygIVKGEKIDGDVFKVKglvE--KPKPEEAPS-NLAIVGryVLTPDIFDILENTKPgkggeIQLTDAIAKLLE 235

                        250       260
                 ....*....|....*....|
gi 256796963 191 QDDVTYELYQGRWHDIGTPE 210
Cdd:cd02541  236 EEPVYAYVFEGKRYDCGNKL 255
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
 3-221 1.85e-11

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: 61.82  E-value: 1.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963   3 AMILAAGRGERMRPLTDERPKPLLKVNGKALIeWHIEALKEA-GISDIIINTSWLGELIPEYLGDGAYWGVNLSFSPEEQ 81
Cdd:cd02524    1 VVILAGGLGTRLSEETELKPKPMVEIGGRPIL-WHIMKIYSHyGHNDFILCLGYKGHVIKEYFLNYFLHNSDVTIDLGTN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963  82 ALE---------------------TAGGIRKALDFFEN-EPFIVVNGDVWTDIDYTGIAKAPESSAHIVLVPNPehHPEG 139
Cdd:cd02524   80 RIElhnsdiedwkvtlvdtglntmTGGRLKRVRRYLGDdETFMLTYGDGVSDVNINALIEFHRSHGKLATVTAV--HPPG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963 140 DF-CVT--EGGKV-----KSEGEPKLTFSGIGVYQPKVFADLPEDEAI-PLGPiLRQLMEQDD-VTYElYQGRWHDIGTP 209
Cdd:cd02524  158 RFgELDldDDGQVtsfteKPQGDGGWINGGFFVLEPEVFDYIDGDDTVfEREP-LERLAKDGElMAYK-HTGFWQCMDTL 235

                        250
                 ....*....|..
gi 256796963 210 ERLQSLNESFQR 221
Cdd:cd02524  236 RDKQTLEELWNS 247
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 6-108 4.81e-11

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: 59.52  E-value: 4.81e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963   6 LAAGRGERMrpltDERPKPLLKVNGKALIEWHIEALKEAGISDIIINTSWLGELIPEYLGDgayWGVNLsfspeeqaLET 85
Cdd:COG2266    1 MAGGKGTRL----GGGEKPLLEICGKPMIDRVIDALEESCIDKIYVAVSPNTPKTREYLKE---RGVEV--------IET 65

                         90       100
                 ....*....|....*....|....*...
gi 256796963  86 AGG-----IRKALDFFEnEPFIVVNGDV 108
Cdd:COG2266   66 PGEgyvedLNEALESIS-GPVLVVPADL 92
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 3-120 5.23e-11

The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; N-terminal domain of epsilon 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 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: 133040 [Multi-domain]  Cd Length: 217  Bit Score: 59.93  E-value: 5.23e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963   3 AMILAAGRGERMRPLTDERPKPLLKVNGKALIEWHIEALKEAGISDIIINTSWLGELIPEYLGDGAYWG-------VNLS 75
Cdd:cd04197    3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQIKEYIEKSKWSKpksslmiVIII 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 256796963  76 FSPEEQA-------LETAGGIRkaldffenEPFIVVNGDVWTDIDYTGIAKA 120
Cdd:cd04197   83 MSEDCRSlgdalrdLDAKGLIR--------GDFILVSGDVVSNIDLKEILEE 126
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
 2-213 7.39e-11

glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase homotetramer This model describes a tightly conserved but broadly distributed subfamily (here designated as short form) of known and putative bacterial glucose-1-phosphate thymidylyltransferases. It is well characterized in several species as the first of four enzymes involved in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 130274 [Multi-domain]  Cd Length: 286  Bit Score: 60.48  E-value: 7.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963    2 KAMILAAGRGERMRPLTDERPKPLLKVNGKALIEWHIEALKEAGISDI-IINTSWLGELIPEYLGDGAYWGVNLSFS--P 78
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDIlIISTPEDTPRFQRLLGDGSQWGINLSYAvqP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963   79 EEQALETAGGIRKalDFFENEPFIVVNGD-VWTDIDYTGI---AKAPESSAHIV--LVPNPEHHPEGDFcvTEGGKVKSE 152
Cdd:TIGR01207  81 SPDGLAQAFIIGE--DFIGGDPSALVLGDnIFYGHDLSDLlrrAAARTEGATVFayQVSDPERYGVVEF--DSNGRAISI 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 256796963  153 GE----PKLTFSGIGVYqpkvFADLPEDE-AIPLGPILRQLMEQDDVTYE-LYQGR-----------WHDIGTPERLQ 213
Cdd:TIGR01207 157 EEkpaqPKSNYAVTGLY----FYDNRVVEiARQLKPSARGELEITDLNRVyLEEGRlsvellgrgyaWLDTGTHDSLL 230
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 3-210 9.95e-11

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 60.47  E-value: 9.95e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963   3 AMILAAGRGERMRPLTDERPKPLLKVNGKA-LIEWHIEALKEAGISDIIINTSWLG-ELIpEYLGDGAYWGVNLS----- 75
Cdd:COG0448    4 AIILAGGRGSRLGPLTKDRAKPAVPFGGKYrIIDFPLSNCVNSGIRRVGVLTQYKShSLN-DHIGSGKPWDLDRKrggvf 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963  76 -FSPEEQALE------TAGGIRKALDFFENEPF---IVVNGDVWTDIDYTG-IAKAPESSAHIVL----VPNPEHHPEGD 140
Cdd:COG0448   83 iLPPYQQREGedwyqgTADAVYQNLDFIERSDPdyvLILSGDHIYKMDYRQmLDFHIESGADITVacieVPREEASRFGV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963 141 FCVTEGGKVKS----EGEPKLTFSGIGVYqpkVF----------ADLPEDEAIPLGPILRQLMEQDDV-TYElYQGRWHD 205
Cdd:COG0448  163 MEVDEDGRITEfeekPKDPKSALASMGIY---VFnkdvlielleEDAPNSSHDFGKDIIPRLLDRGKVyAYE-FDGYWRD 238


                 ....*
gi 256796963 206 IGTPE 210
Cdd:COG0448  239 VGTID 243
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
3-51 1.14e-10

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 58.63  E-value: 1.14e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 256796963   3 AMILAAGRGERMrpltdERPKPLLKVNGKALIEWHIEALKEAGISDIII 51
Cdd:COG2068    6 AIILAAGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPVVV 49
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
 3-130 5.40e-10

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: 56.78  E-value: 5.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963   3 AMILAAGRGERMRPLTDERPKPLLKVNGKA-LIEWHIEALKEAGISDIIINTSWLGELIPEYLGDGAYWGVN-----LSF 76
Cdd:cd02508    1 AIILAGGEGTRLSPLTKKRAKPAVPFGGRYrLIDFPLSNMVNSGIRNVGVLTQYKSRSLNDHLGSGKEWDLDrknggLFI 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 256796963  77 SPEEQALE------TAGGIRKALDFFE---NEPFIVVNGDVWTDIDYTG-IAKAPESSAHIVLV 130
Cdd:cd02508   81 LPPQQRKGgdwyrgTADAIYQNLDYIErsdPEYVLILSGDHIYNMDYREmLDFHIESGADITVV 144
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 3-73 6.28e-10

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: 56.41  E-value: 6.28e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 256796963   3 AMILAAGRGERMRpltdeRPKPLLKVNGKALIEWHIEALKEAGISDIIINTSWLGELIPEYL-GDGAYWGVN 73
Cdd:cd04182    3 AIILAAGRSSRMG-----GNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALaGLPVVVVIN 69
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-107 7.61e-10

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 57.92  E-value: 7.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963   3 AMILAAGRGERMRpltDERPKPLLKVNGKALIEWHIEALKEAGISDIIINTSWLGELIPEYLGDGAywgvnlSFSPEEQA 82
Cdd:PRK14354   5 AIILAAGKGTRMK---SKLPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVGHGAEEVKEVLGDRS------EFALQEEQ 75

                         90       100
                 ....*....|....*....|....*..
gi 256796963  83 LETAGGIRKALDFFENEP--FIVVNGD 107
Cdd:PRK14354  76 LGTGHAVMQAEEFLADKEgtTLVICGD 102
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 2-212 1.38e-08

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 53.91  E-value: 1.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963   2 KAMILAAGRGERMRPLTDERPKPLLKVNGKALIEWHIEALKEAGISDI-IINTSWLGELIPEYLGDGAYWGVNLSFSPEE 80
Cdd:PRK15480   5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDIlIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963  81 QALETAGGIRKALDFFENEPFIVVNGD-VWTDIDYTGIAKAP---ESSAHIVL--VPNPEHHPEGDFcVTEGGKVKSEG- 153
Cdd:PRK15480  85 SPDGLAQAFIIGEEFIGGDDCALVLGDnIFYGHDLPKLMEAAvnkESGATVFAyhVNDPERYGVVEF-DQNGTAISLEEk 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 256796963 154 --EPKLTFSGIGVYqpkVFADLPEDEAIPLGPILRQLMEQDDVT-YELYQGR-----------WHDIGTPERL 212
Cdd:PRK15480 164 plQPKSNYAVTGLY---FYDNDVVEMAKNLKPSARGELEITDINrIYMEQGRlsvammgrgyaWLDTGTHQSL 233
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 1-107 1.40e-08

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: 52.89  E-value: 1.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963   1 MKAMILAAGRGERMRpltdeRPKPLLKVNGKALIEWHIEALKEAgISDIIINTSWlgelipeylgDGAYWGVNLSFSPEE 80
Cdd:COG0746    5 ITGVILAGGRSRRMG-----QDKALLPLGGRPLLERVLERLRPQ-VDEVVIVANR----------PERYAALGVPVVPDD 68

                         90       100       110
                 ....*....|....*....|....*....|
gi 256796963  81 qaLETAG---GIRKALDFFENEPFIVVNGD 107
Cdd:COG0746   69 --PPGAGplaGILAALEAAPAEWVLVLACD 96
ispD TIGR00453
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ...
 3-104 2.02e-08

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: 52.68  E-value: 2.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963    3 AMILAAGRGERMRPltdERPKPLLKVNGKALIEWHIEALKEA-GISDIIINTSWLG-ELIPEYLGDGAYWGVnlsfspee 80
Cdd:TIGR00453   2 AVIPAAGRGTRFGS---GVPKQYLELGGRPLLEHALDAFLAHpAIDEVVVVVSPDDtEFFQKYLVARAVPKI-------- 70

                          90       100       110
                  ....*....|....*....|....*....|
gi 256796963   81 qaleTAGG------IRKALDFFENEPFIVV 104
Cdd:TIGR00453  71 ----VAGGdtrqdsVRNGLKALKDAEFVLV 96
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 1-53 8.33e-08

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: 50.65  E-value: 8.33e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 256796963   1 MKAMILAAGRGERMrpltdERPKPLLKVNGKALIEWHIEALKEAgISDIIINT 53
Cdd:cd02503    1 ITGVILAGGKSRRM-----GGDKALLELGGKPLLEHVLERLKPL-VDEVVISA 47
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 5-51 1.06e-07

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: 50.90  E-value: 1.06e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 256796963   5 ILAAGRGERMRpltDERPKPLLKVNGKALIEWHIEALKEAG-ISDIII 51
Cdd:COG1211    2 IPAAGSGSRMG---AGIPKQFLPLGGKPVLEHTLEAFLAHPrIDEIVV 46
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
 5-114 1.18e-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: 50.72  E-value: 1.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963   5 ILAAGRGERMRPLTDERPKPLLKVNGKALIEWHIEALKEAGISDII-------INTSWLGELIPEYLGDGaywGVNLSFS 77
Cdd:cd04183    3 IPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEWVIESLAKIFDSRFIficrdehNTKFHLDESLKLLAPNA---TVVELDG 79

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 256796963  78 PEEQALETAGGIRKALDffENEPFIVVNGDVWTDIDY 114
Cdd:cd04183   80 ETLGAACTVLLAADLID--NDDPLLIFNCDQIVESDL 114
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
3-51 1.36e-07

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 50.52  E-value: 1.36e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 256796963   3 AMILAAGRGERMRPltdERPKPLLKVNGKALIEWHIEALKEAG-ISDIII 51
Cdd:PRK00155   6 AIIPAAGKGSRMGA---DRPKQYLPLGGKPILEHTLEAFLAHPrIDEIIV 52
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 3-51 3.30e-07

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: 49.06  E-value: 3.30e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 256796963   3 AMILAAGRGERMRPltdERPKPLLKVNGKALIEWHIEALKEAG-ISDIII 51
Cdd:cd02516    3 AIILAAGSGSRMGA---DIPKQFLELGGKPVLEHTLEAFLAHPaIDEIVV 49
mobA PRK00317
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
 1-53 4.68e-07

molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed


Pssm-ID: 234725 [Multi-domain]  Cd Length: 193  Bit Score: 48.64  E-value: 4.68e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 256796963   1 MKAMILAAGRGERMrpltDERPKPLLKVNGKALIEWHIEALKeAGISDIIINT 53
Cdd:PRK00317   4 ITGVILAGGRSRRM----GGVDKGLQELNGKPLIQHVIERLA-PQVDEIVINA 51
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-108 8.10e-07

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 48.99  E-value: 8.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963   1 MKAMILAAGRGERMRpltDERPKPLLKVNGKALIEWHIEALKEAGiSDIIINTSWLGELIPEYLGDgaywgvNLSFSPEE 80
Cdd:PRK14357   1 MRALVLAAGKGTRMK---SKIPKVLHKISGKPMINWVIDTAKKVA-QKVGVVLGHEAELVKKLLPE------WVKIFLQE 70

                         90       100
                 ....*....|....*....|....*....
gi 256796963  81 QALETAGGIRKALDFFE-NEPFIVVNGDV 108
Cdd:PRK14357  71 EQLGTAHAVMCARDFIEpGDDLLILYGDV 99
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
2-210 1.44e-06

UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 47.72  E-value: 1.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963   2 KAMILAAGRGERMRPLTDERPKPLLKVNGKALIEWHIEALKEAGISDIIINTSWLGELIPEYlgdgaywgvnlsF--SPE 79
Cdd:COG1210    5 KAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVTGRGKRAIEDH------------FdrSYE 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963  80 -EQALETAG--------------------------G----IRKALDFFENEPFIVVNGDVWTDiDYTG-----IAKAPES 123
Cdd:COG1210   73 lEATLEAKGkeelleevrsisplanihyvrqkeplGlghaVLCARPFVGDEPFAVLLGDDLID-SEKPclkqmIEVYEET 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963 124 SAHIVLV-PNPEHH--------PEGDfcvtEGGKVK--------SEGEPKLTFSGIGVY--QPKVFADLpedEAIPLG-- 182
Cdd:COG1210  152 GGSVIAVqEVPPEEvskygivdGEEI----EGGVYRvtglvekpAPEEAPSNLAIVGRYilTPEIFDIL---EKTKPGag 224

                        250       260       270
                 ....*....|....*....|....*....|....
gi 256796963 183 ------PILRQLMEQDDVTYELYQGRWHDIGTPE 210
Cdd:COG1210  225 geiqltDAIAALAKEEPVYAYEFEGKRYDCGDKL 258
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-94 6.35e-06

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 46.28  E-value: 6.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963   3 AMILAAGRGERMRpltDERPKPLLKVNGKALIEWHIEALKEAGISDIIINTSWLGELIPEYLGDGAywgvNLSFSPEEQA 82
Cdd:PRK14355   6 AIILAAGKGTRMK---SDLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHFAGDG----DVSFALQEEQ 78

                         90
                 ....*....|..
gi 256796963  83 LETAGGIRKALD 94
Cdd:PRK14355  79 LGTGHAVACAAP 90
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
 3-34 9.12e-06

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 45.60  E-value: 9.12e-06
                         10        20        30
                 ....*....|....*....|....*....|..
gi 256796963   3 AMILAAGRGERMRPLTDERPKPLLKVNGKALI 34
Cdd:PRK00725  18 ALILAGGRGSRLKELTDKRAKPAVYFGGKFRI 49
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-51 1.52e-05

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 45.24  E-value: 1.52e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 256796963   3 AMILAAGRGERMRpltDERPKPLLKVNGKALIEWHIEALKEAGISDIII 51
Cdd:PRK14353   8 AIILAAGEGTRMK---SSLPKVLHPVAGRPMLAHVLAAAASLGPSRVAV 53
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 1-85 2.94e-05

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 44.20  E-value: 2.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963   1 MKAMILAAGRGERMRpltDERPKPLLKVNGKALIEWHIEALKEAGISDIIINTSWLGELIpeylgDGAYWGVNLSFSPEE 80
Cdd:PRK14358   8 LDVVILAAGQGTRMK---SALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGAEQV-----EAALQGSGVAFARQE 79


                 ....*
gi 256796963  81 QALET 85
Cdd:PRK14358  80 QQLGT 84
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-108 8.61e-05

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 42.71  E-value: 8.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963   1 MKAMILAAGRGERMrplTDERPKPLLKVNGKALIEWHIEALKEAGISDIIINTSWLGELIPEYLGDGAywgVNLSFSPEE 80
Cdd:PRK09451   6 MSVVILAAGKGTRM---YSDLPKVLHTLAGKPMVQHVIDAANELGAQHVHLVYGHGGDLLKQTLADEP---LNWVLQAEQ 79

                         90       100
                 ....*....|....*....|....*....
gi 256796963  81 qaLETAGGIRKALDFF-ENEPFIVVNGDV 108
Cdd:PRK09451  80 --LGTGHAMQQAAPFFaDDEDILMLYGDV 106
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
 1-104 9.39e-05

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: 42.56  E-value: 9.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963   1 MKAMILAAGRGERMRPL-TDERPKPLLKVNG-KALIEWHIE-ALKEAGISDIIINTSW-LGELIPEYLGDGAYwGVNLSF 76
Cdd:cd02509    1 IYPVILAGGSGTRLWPLsRESYPKQFLKLFGdKSLLQQTLDrLKGLVPPDRILVVTNEeYRFLVREQLPEGLP-EENIIL 79

                         90       100       110
                 ....*....|....*....|....*....|..
gi 256796963  77 SPEeqALETAGGI----RKALDFFENEPFIVV 104
Cdd:cd02509   80 EPE--GRNTAPAIalaaLYLAKRDPDAVLLVL 109
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 5-108 2.41e-04

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 41.45  E-value: 2.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963   5 ILAAGRGERMRpltDERPKPLLKVNGKALIEWHIEALKEAGISDIIINTSWLGELIPEYLGDGAywgvNLSFSPEEQALE 84
Cdd:PRK14360   6 ILAAGKGTRMK---SSLPKVLHPLGGKSLVERVLDSCEELKPDRRLVIVGHQAEEVEQSLAHLP----GLEFVEQQPQLG 78

                         90       100
                 ....*....|....*....|....*.
gi 256796963  85 TAGGIRKALDFFEN--EPFIVVNGDV 108
Cdd:PRK14360  79 TGHAVQQLLPVLKGfeGDLLVLNGDV 104
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
2-53 6.89e-04

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 39.89  E-value: 6.89e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 256796963   2 KAMILAAGRGERMRPLTDERPKPLLKVNGKALIEWHIEALKEAGISDIIINT 53
Cdd:PRK13389  10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVT 61
IspD pfam01128
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ...
 3-51 8.06e-04

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes which catalyze the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from cytidine triphosphate and 2-C-methyl-D-erythritol 4-phosphate (MEP).


Pssm-ID: 460075  Cd Length: 219  Bit Score: 39.36  E-value: 8.06e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 256796963    3 AMILAAGRGERMRpltDERPKPLLKVNGKALIEWHIEALKEAGISDIII 51
Cdd:pfam01128   1 AVIPAAGSGKRMG---AGVPKQFLQLLGQPLLEHTVDAFLASPVVDRIV 46
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
1-53 8.75e-04

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 39.49  E-value: 8.75e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 256796963   1 MKAMILAAGRGERMRPLTDERPKPLLKVNGKALIEWHIEALKEAGISDIIINT 53
Cdd:PRK10122   4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVT 56
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-107 8.77e-04

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 39.71  E-value: 8.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963   3 AMILAAGRGERMRpltDERPKPLLKVNGKALIEWHIEALKEAGISDIIINTSWLGELIPEylgdgAYWGVNLSFSPEEQA 82
Cdd:PRK14356   8 ALILAAGKGTRMH---SDKPKVLQTLLGEPMLRFVYRALRPLFGDNVWTVVGHRADMVRA-----AFPDEDARFVLQEQQ 79

                         90       100
                 ....*....|....*....|....*...
gi 256796963  83 LETAGGIRKALDFFEN---EPFIVVNGD 107
Cdd:PRK14356  80 LGTGHALQCAWPSLTAaglDRVLVVNGD 107
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 3-24 1.26e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 39.42  E-value: 1.26e-03
                         10        20
                 ....*....|....*....|..
gi 256796963   3 AMILAAGRGERMRPLTDERPKP 24
Cdd:PRK00844   8 AIVLAGGEGKRLMPLTADRAKP 29
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 5-107 2.82e-03

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 38.05  E-value: 2.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256796963   5 ILAAGRGERMRpltDERPKPLLKVNGKALIeWHIeaLKEA-GIS-DIIINTSWLGELIPEYLgdgaywgvnLSFSPE--- 79
Cdd:PRK14359   7 ILAAGKGTRMK---SSLPKVLHTICGKPML-FYI--LKEAfAISdDVHVVLHHQKERIKEAV---------LEYFPGvif 71

                         90       100       110
                 ....*....|....*....|....*....|...
gi 256796963  80 -EQALE----TAGGIRKALdfFENEPFIVVNGD 107
Cdd:PRK14359  72 hTQDLEnypgTGGALMGIE--PKHERVLILNGD 102
GT2_SpsF cd02518
SpsF is a glycosyltrnasferase implicated in the synthesis of the spore coat; Spore coat ...
 23-54 2.96e-03

SpsF is a glycosyltrnasferase implicated in the synthesis of the spore coat; Spore coat polysaccharide biosynthesis protein F (spsF) is a glycosyltransferase implicated in the synthesis of the spore coat in a variety of bacteria challenged by stress as starvation. The spsF gene is expressed in the late stage of coat development responsible for a terminal step in coat formation that involves the glycosylation of the coat. SpsF gene mutation resulted in spores that appeared normal. But, the spores tended to aggregate and had abnormal adsorption properties, indicating a surface alteration.


Pssm-ID: 133011  Cd Length: 233  Bit Score: 37.55  E-value: 2.96e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 256796963  23 KPLLKVNGKALIEWHIEALKEA-GISDIIINTS 54
Cdd:cd02518   16 KVLKPLGGKPLLEHLLDRLKRSkLIDEIVIATS 48
ispDF PRK09382
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ...
 3-51 3.69e-03

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: 37.90  E-value: 3.69e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 256796963   3 AMILAAGRGERMRPltdERPKPLLKVNGKALIEWHIEALKEAG-ISDIII 51
Cdd:PRK09382   8 LVIVAAGRSTRFSA---EVKKQWLRIGGKPLWLHVLENLSSAPaFKEIVV 54
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH