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Conserved domains on  [gi|33568709|emb|CAE34467|]
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putative nucleotidyl transferase [Bordetella bronchiseptica RB50]

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 1.42e-86

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: 256.23  E-value: 1.42e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33568709   2 RAMILAAGRGERMRPLTDTTPKPLLAVGGKPLIVWHIERLVAAGLRDIVINHAWLGQRIVDHLGDGGAYGARLRYSAEAA 81
Cdd:COG1208   1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRFGVRITYVDEGE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33568709  82 ALETAGGIAQALPLLGDAPFLVINGDIWCDWDPaqaRRQAAALDAAGAQAWLLLVDNPPQHPQGDFRLEDDGRV------ 155
Cdd:COG1208  81 PLGTGGALKRALPLLGDEPFLVLNGDILTDLDL---AALLAFHREKGADATLALVPVPDPSRYGVVELDGDGRVtrfvek 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 33568709 156 ADDGAPKLTFAGIGLYRPALFDPVARGSAAPLAPLLRQAMARRAVIGARHAGRWTDVGTPQRLAALDGQLR 226
Cdd:COG1208 158 PEEPPSNLINAGIYVLEPEIFDYIPEGEPFDLEDLLPRLIAEGRVYGYVHDGYWLDIGTPEDLLEANALLL 228
 
Name Accession Description Interval E-value
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 2-226 1.42e-86

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: 256.23  E-value: 1.42e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33568709   2 RAMILAAGRGERMRPLTDTTPKPLLAVGGKPLIVWHIERLVAAGLRDIVINHAWLGQRIVDHLGDGGAYGARLRYSAEAA 81
Cdd:COG1208   1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRFGVRITYVDEGE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33568709  82 ALETAGGIAQALPLLGDAPFLVINGDIWCDWDPaqaRRQAAALDAAGAQAWLLLVDNPPQHPQGDFRLEDDGRV------ 155
Cdd:COG1208  81 PLGTGGALKRALPLLGDEPFLVLNGDILTDLDL---AALLAFHREKGADATLALVPVPDPSRYGVVELDGDGRVtrfvek 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 33568709 156 ADDGAPKLTFAGIGLYRPALFDPVARGSAAPLAPLLRQAMARRAVIGARHAGRWTDVGTPQRLAALDGQLR 226
Cdd:COG1208 158 PEEPPSNLINAGIYVLEPEIFDYIPEGEPFDLEDLLPRLIAEGRVYGYVHDGYWLDIGTPEDLLEANALLL 228
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 2-221 5.01e-81

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: 241.32  E-value: 5.01e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33568709   2 RAMILAAGRGERMRPLTDTTPKPLLAVGGKPLIVWHIERLVAAGLRDIVINHAWLGQRIVDHLGDgGAYGARLRYSAE-A 80
Cdd:cd06422   1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHLGD-SRFGLRITISDEpD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33568709  81 AALETAGGIAQALPLLGDAPFLVINGDIWCDWDPAQARRQAAALDAAGAQAwLLLVDNPPQHPQGDFRLEDDGRV---AD 157
Cdd:cd06422  80 ELLETGGGIKKALPLLGDEPFLVVNGDILWDGDLAPLLLLHAWRMDALLLL-LPLVRNPGHNGVGDFSLDADGRLrrgGG 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 33568709 158 DGAPKLTFAGIGLYRPALFDPVARGsAAPLAPLLRQAMARRAVIGARHAGRWTDVGTPQRLAAL 221
Cdd:cd06422 159 GAVAPFTFTGIQILSPELFAGIPPG-KFSLNPLWDRAIAAGRLFGLVYDGLWFDVGTPERLLAA 221
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 1-215 1.09e-33

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: 124.63  E-value: 1.09e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33568709     1 MRAMILAAGRGERMRPLTDTTPKPLLAVGGKPLIVWHIERLVAAGLRDIVINHAWLGQRIVDHLGDGGAYGARLRYSAEA 80
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEKVREYFGDGSRGGVPIEYVVQE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33568709    81 AALETAGGIAQALPLLGDaPFLVINGDIWCDWDPAQARRQAAALDAAGAQawlllVDNPPQHpqGDFRLeDDGRV----- 155
Cdd:TIGR03992  81 EQLGTADALGSAKEYVDD-EFLVLNGDVLLDSDLLERLIRAEAPAIAVVE-----VDDPSDY--GVVET-DGGRVtgive 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 33568709   156 -ADDGAPKLTFAGIGLYRPALFDPVARGSAAP-----LAPLLrQAMARRAVIGA-RHAGRWTDVGTP 215
Cdd:TIGR03992 152 kPENPPSNLINAGIYLFSPEIFELLEKTKLSPrgeyeLTDAL-QLLIDEGKVKAvELDGFWLDVGRP 217
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-218 1.06e-21

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: 89.62  E-value: 1.06e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33568709     2 RAMILAAGRGERMRPLTDTTPKPLLAVGGKPLIVWH-IERLVAAGLRD-IVINHAWLGQRIVDHLGDGGAYGARLRYSAE 79
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKYPLIDYpLSRLANAGIREiIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33568709    80 AAALETAGGIAQALPLLGD--APFLVINGDIWCDWDPAQARRQAAALDAAGaqawLLLVDNPPQHPQGDF---RLEDDGR 154
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDekSDVLVLGGDHIYRMDLEQAVKFHIEKAADA----TVTFGIVPVEPPTGYgvvEFDDNGR 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33568709   155 VAD-----DGAPKLTFAGIGLYrpaLFDPV----ARGSAAPLAP-------LLRQAMARRAVIGA--RHAGRWTDVGTPQ 216
Cdd:pfam00483 157 VIRfvekpKLPKASNYASMGIY---IFNSGvldfLAKYLEELKRgedeitdILPKALEDGKLAYAfiFKGYAWLDVGTWD 233


                  ..
gi 33568709   217 RL 218
Cdd:pfam00483 234 SL 235
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 2-93 8.15e-09

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 54.68  E-value: 8.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33568709    2 RAMILAAGRGERMRPLTDTTPKPLLAVGGKPLIVWHIERLVAAGLRDI-VINHAWLGQRIVDHLGDGGAYGARLRYSAEA 80
Cdd:PRK15480   5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDIlIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84

                         90
                 ....*....|...
gi 33568709   81 aaleTAGGIAQAL 93
Cdd:PRK15480  85 ----SPDGLAQAF 93
 
Name Accession Description Interval E-value
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 2-226 1.42e-86

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: 256.23  E-value: 1.42e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33568709   2 RAMILAAGRGERMRPLTDTTPKPLLAVGGKPLIVWHIERLVAAGLRDIVINHAWLGQRIVDHLGDGGAYGARLRYSAEAA 81
Cdd:COG1208   1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRFGVRITYVDEGE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33568709  82 ALETAGGIAQALPLLGDAPFLVINGDIWCDWDPaqaRRQAAALDAAGAQAWLLLVDNPPQHPQGDFRLEDDGRV------ 155
Cdd:COG1208  81 PLGTGGALKRALPLLGDEPFLVLNGDILTDLDL---AALLAFHREKGADATLALVPVPDPSRYGVVELDGDGRVtrfvek 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 33568709 156 ADDGAPKLTFAGIGLYRPALFDPVARGSAAPLAPLLRQAMARRAVIGARHAGRWTDVGTPQRLAALDGQLR 226
Cdd:COG1208 158 PEEPPSNLINAGIYVLEPEIFDYIPEGEPFDLEDLLPRLIAEGRVYGYVHDGYWLDIGTPEDLLEANALLL 228
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 2-221 5.01e-81

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: 241.32  E-value: 5.01e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33568709   2 RAMILAAGRGERMRPLTDTTPKPLLAVGGKPLIVWHIERLVAAGLRDIVINHAWLGQRIVDHLGDgGAYGARLRYSAE-A 80
Cdd:cd06422   1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHLGD-SRFGLRITISDEpD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33568709  81 AALETAGGIAQALPLLGDAPFLVINGDIWCDWDPAQARRQAAALDAAGAQAwLLLVDNPPQHPQGDFRLEDDGRV---AD 157
Cdd:cd06422  80 ELLETGGGIKKALPLLGDEPFLVVNGDILWDGDLAPLLLLHAWRMDALLLL-LPLVRNPGHNGVGDFSLDADGRLrrgGG 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 33568709 158 DGAPKLTFAGIGLYRPALFDPVARGsAAPLAPLLRQAMARRAVIGARHAGRWTDVGTPQRLAAL 221
Cdd:cd06422 159 GAVAPFTFTGIQILSPELFAGIPPG-KFSLNPLWDRAIAAGRLFGLVYDGLWFDVGTPERLLAA 221
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 3-213 2.45e-48

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: 158.13  E-value: 2.45e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33568709   3 AMILAAGRGERMRPLTDTTPKPLLAVGGKPLIVWHIERLVAAGLRDIVINHAWLGQRIVDHLGDGGAYGARLRYSAEAAA 82
Cdd:cd04181   1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGSKFGVNIEYVVQEEP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33568709  83 LETAGGIAQALPLLGDAPFLVINGDIWCDWDpaqARRQAAALDAAGAQAWLLLVDNPPQHPQGDFRLEDDGRVAD----- 157
Cdd:cd04181  81 LGTAGAVRNAEDFLGDDDFLVVNGDVLTDLD---LSELLRFHREKGADATIAVKEVEDPSRYGVVELDDDGRVTRfvekp 157

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 33568709 158 -DGAPKLTFAGIGLYRPALFDPVARGSAAP---LAPLLRQAMARRAVIGARHAGRWTDVG 213
Cdd:cd04181 158 tLPESNLANAGIYIFEPEILDYIPEILPRGedeLTDAIPLLIEEGKVYGYPVDGYWLDIG 217
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 3-222 4.27e-35

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: 124.20  E-value: 4.27e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33568709   3 AMILAAGRGERMRPLTDTTPKPLLAVGGKPLIVWHIERLVAAGLRDIVINHAWLGQRIVDHLGDGGAYGARLRYSAEAAA 82
Cdd:cd06915   1 AVILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYLAEQIEEYFGDGYRGGIRIYYVIEPEP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33568709  83 LETAGGIAQALPLLGDAPFLVINGDIWCDWDPAQARRQAAALDAAGAqawLLLVDNPPQHPQGDFRLEDDGRVAD----- 157
Cdd:cd06915  81 LGTGGAIKNALPKLPEDQFLVLNGDTYFDVDLLALLAALRASGADAT---MALRRVPDASRYGNVTVDGDGRVIAfvekg 157

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 33568709 158 -DGAPKLTFAGIGLYRPALFDPVARGSAAPLAPLLRQAMARRAVIGARHAGRWTDVGTPQRLAALD 222
Cdd:cd06915 158 pGAAPGLINGGVYLLRKEILAEIPADAFSLEADVLPALVKRGRLYGFEVDGYFIDIGIPEDYARAQ 223
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 1-215 1.09e-33

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: 124.63  E-value: 1.09e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33568709     1 MRAMILAAGRGERMRPLTDTTPKPLLAVGGKPLIVWHIERLVAAGLRDIVINHAWLGQRIVDHLGDGGAYGARLRYSAEA 80
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEKVREYFGDGSRGGVPIEYVVQE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33568709    81 AALETAGGIAQALPLLGDaPFLVINGDIWCDWDPAQARRQAAALDAAGAQawlllVDNPPQHpqGDFRLeDDGRV----- 155
Cdd:TIGR03992  81 EQLGTADALGSAKEYVDD-EFLVLNGDVLLDSDLLERLIRAEAPAIAVVE-----VDDPSDY--GVVET-DGGRVtgive 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 33568709   156 -ADDGAPKLTFAGIGLYRPALFDPVARGSAAP-----LAPLLrQAMARRAVIGA-RHAGRWTDVGTP 215
Cdd:TIGR03992 152 kPENPPSNLINAGIYLFSPEIFELLEKTKLSPrgeyeLTDAL-QLLIDEGKVKAvELDGFWLDVGRP 217
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 3-108 2.37e-31

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: 114.53  E-value: 2.37e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33568709   3 AMILAAGRGERMRPLTDTTPKPLLAVGGKPLIVWHIERLVAAGLRDIVINHAWLGQRIVDHLGDGGAYGARLRYSAEAAA 82
Cdd:cd06426   1 VVIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNYLAEMIEDYFGDGSKFGVNISYVREDKP 80

                        90       100
                ....*....|....*....|....*....
gi 33568709  83 LETAGgiaqALPLLG---DAPFLVINGDI 108
Cdd:cd06426  81 LGTAG----ALSLLPekpTDPFLVMNGDI 105
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 1-218 4.21e-31

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: 114.20  E-value: 4.21e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33568709   1 MRAMILAAGRGERMRPLTDTTPKPLLAVGGKPLIVWHIERLVAAGLRDIVINHAWLGQRIVDHLGDGGAYGARLRYSAEA 80
Cdd:cd04189   1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEALGDGSRFGVRITYILQE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33568709  81 AALETAGGIAQALPLLGDAPFLVINGD--IWCDWDPAQARRQAAALDAAgaqawLLL--VDNPPQHPQGDFrleDDGRVA 156
Cdd:cd04189  81 EPLGLAHAVLAARDFLGDEPFVVYLGDnlIQEGISPLVRDFLEEDADAS-----ILLaeVEDPRRFGVAVV---DDGRIV 152

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 33568709 157 D----DGAPKLTFAGIGLY--RPALFDPVARgsaapLAPLLR---------QAM--ARRAVIGARHAGRWTDVGTPQRL 218
Cdd:cd04189 153 RlvekPKEPPSNLALVGVYafTPAIFDAISR-----LKPSWRgeleitdaiQWLidRGRRVGYSIVTGWWKDTGTPEDL 226
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-107 3.78e-26

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 102.48  E-value: 3.78e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33568709   1 MRAMILAAGRGERMRPLTDTTPKPLLAVGGKPLIVWHIERLVAAGLRDIVI---NHawLGQRIVDHLGDGGAYGARLRYs 77
Cdd:COG1209   1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIistPE--DGPQFERLLGDGSQLGIKISY- 77

                        90       100       110
                ....*....|....*....|....*....|....
gi 33568709  78 aeaAALETAGGIAQAL----PLLGDAPFLVINGD 107
Cdd:COG1209  78 ---AVQPEPLGLAHAFiiaeDFIGGDPVALVLGD 108
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
2-108 5.73e-24

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 95.31  E-value: 5.73e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33568709   2 RAMILAAGRGERMRPLTDTTPKPLLAVGGKPLIVWHIERLVAAGLRDIVINHAWLGQRIVDHLGDGGaYGARLRYSAEAA 81
Cdd:COG1213   1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEALARPG-PDVTFVYNPDYD 79

                        90       100
                ....*....|....*....|....*..
gi 33568709  82 ALETAGGIAQALPLLGDaPFLVINGDI 108
Cdd:COG1213  80 ETNNIYSLWLAREALDE-DFLLLNGDV 105
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 1-111 1.00e-22

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: 92.27  E-value: 1.00e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33568709   1 MRAMILAAGRGERMRPLTDTTPKPLLAVGGKPLIVWHIERLVAAGLRDIVINHAWLGQRIVDHLGD-GGAYGARLRYSAE 79
Cdd:cd06425   1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYRPEDMVPFLKEyEKKLGIKITFSIE 80

                        90       100       110
                ....*....|....*....|....*....|....
gi 33568709  80 AAALETAGGIAQALPLLG--DAPFLVINGDIWCD 111
Cdd:cd06425  81 TEPLGTAGPLALARDLLGddDEPFFVLNSDVICD 114
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 3-109 1.06e-22

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: 91.91  E-value: 1.06e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33568709   3 AMILAAGRGERMRPLTDTTPKPLLAVGGKPLIVWHIERLVAAGLRDIVINHAWLGQRIVDHLGDGgaYGARLRYSAEAAA 82
Cdd:cd02523   1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKKY--PNIKFVYNPDYAE 78

                        90       100
                ....*....|....*....|....*..
gi 33568709  83 LETAGGIAQALPLLGDaPFLVINGDIW 109
Cdd:cd02523  79 TNNIYSLYLARDFLDE-DFLLLEGDVV 104
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-218 1.06e-21

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: 89.62  E-value: 1.06e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33568709     2 RAMILAAGRGERMRPLTDTTPKPLLAVGGKPLIVWH-IERLVAAGLRD-IVINHAWLGQRIVDHLGDGGAYGARLRYSAE 79
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKYPLIDYpLSRLANAGIREiIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33568709    80 AAALETAGGIAQALPLLGD--APFLVINGDIWCDWDPAQARRQAAALDAAGaqawLLLVDNPPQHPQGDF---RLEDDGR 154
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDekSDVLVLGGDHIYRMDLEQAVKFHIEKAADA----TVTFGIVPVEPPTGYgvvEFDDNGR 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33568709   155 VAD-----DGAPKLTFAGIGLYrpaLFDPV----ARGSAAPLAP-------LLRQAMARRAVIGA--RHAGRWTDVGTPQ 216
Cdd:pfam00483 157 VIRfvekpKLPKASNYASMGIY---IFNSGvldfLAKYLEELKRgedeitdILPKALEDGKLAYAfiFKGYAWLDVGTWD 233


                  ..
gi 33568709   217 RL 218
Cdd:pfam00483 234 SL 235
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 1-107 1.33e-19

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: 83.78  E-value: 1.33e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33568709   1 MRAMILAAGRGERMRPLTDTTPKPLLAVGGKPLIVWHIERLVAAGLRDIVI----NHAWLGQRIvdhLGDGGAYGARLRY 76
Cdd:cd02538   1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIistpEDLPLFKEL---LGDGSDLGIRITY 77

                        90       100       110
                ....*....|....*....|....*....|....*
gi 33568709  77 saeaAALETAGGIAQALPL----LGDAPFLVINGD 107
Cdd:cd02538  78 ----AVQPKPGGLAQAFIIgeefIGDDPVCLILGD 108
LicC COG4750
CTP:phosphocholine cytidylyltransferase LicC [Cell wall/membrane/envelope biogenesis, Lipid ...
 1-51 5.95e-15

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


Pssm-ID: 443784 [Multi-domain]  Cd Length: 228  Bit Score: 71.01  E-value: 5.95e-15
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 33568709   1 MRAMILAAGRGERMRPLTDTTPKPLLAVGGKPLIVWHIERLVAAGLRDIVI 51
Cdd:COG4750   1 MNAIILAAGLGSRFAPITYETPKGLLKVNGEPLIERQIRQLHEAGITDITV 51
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 3-111 1.20e-11

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: 62.27  E-value: 1.20e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33568709   3 AMILAAG--RGERMRPLTDTTPKPLLAVGGKPLIVWHIERLVA-AGLRDIVINHAWLGQRIVDHLGDGGA-YGARLRYSA 78
Cdd:cd06428   1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKvPDLKEVLLIGFYPESVFSDFISDAQQeFNVPIRYLQ 80

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 33568709  79 EAAALETAGGIA----QalpLLGDAP--FLVINGDIWCD 111
Cdd:cd06428  81 EYKPLGTAGGLYhfrdQ---ILAGNPsaFFVLNADVCCD 116
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 1-51 2.69e-11

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: 60.75  E-value: 2.69e-11
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 33568709   1 MRAMILAAGRGERMRPLTDTTPKPLLAVGGKPLIVWHIERLVAAGLRDIVI 51
Cdd:cd04198   1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIV 51
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 3-64 5.62e-11

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: 59.96  E-value: 5.62e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 33568709   3 AMILAAGRGERMRPLTDTTPKPLLAVGGKPLIVWHIERLVAAGLRDIVI---NHAwlgQRIVDHL 64
Cdd:cd02507   3 AVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVvccEHS---QAIIEHL 64
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 1-111 7.86e-11

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: 60.24  E-value: 7.86e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33568709   1 MRAMILAAGRGERMRPLTDTTPKPLLAVGGKPLIVWHIERLVAAGLRDIVI----------NH--------AWLGQR--- 59
Cdd:cd02541   1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIvtgrgkraieDHfdrsyeleETLEKKgkt 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 33568709  60 ----IVDHLGDGGAygARLRYSAEAAALETAggIAQALPLLGDAPFLVINGDIWCD 111
Cdd:cd02541  81 dlleEVRIISDLAN--IHYVRQKEPLGLGHA--VLCAKPFIGDEPFAVLLGDDLID 132
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 3-107 1.46e-10

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: 60.04  E-value: 1.46e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33568709   3 AMILAAGRGERMRpltDTTPKPLLAVGGKPLIVWHIERLVAAGLRDI--VINHAwlGQRIVDHLGDggaygARLRYSAEA 80
Cdd:COG1207   5 VVILAAGKGTRMK---SKLPKVLHPLAGKPMLEHVLDAARALGPDRIvvVVGHG--AEQVRAALAD-----LDVEFVLQE 74

                        90       100
                ....*....|....*....|....*....
gi 33568709  81 AALETAGGIAQALPLLG--DAPFLVINGD 107
Cdd:COG1207  75 EQLGTGHAVQQALPALPgdDGTVLVLYGD 103
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 3-108 3.55e-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: 57.91  E-value: 3.55e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33568709   3 AMILAAGRGERMRpltDTTPKPLLAVGGKPLIVWHIERLVAAGLRDI--VINHAwlGQRIVDHLGDGGaygarLRYSAEA 80
Cdd:cd02540   1 AVILAAGKGTRMK---SDLPKVLHPLAGKPMLEHVLDAARALGPDRIvvVVGHG--AEQVKKALANPN-----VEFVLQE 70

                        90       100       110
                ....*....|....*....|....*....|
gi 33568709  81 AALETAGGIAQALPLLGD--APFLVINGDI 108
Cdd:cd02540  71 EQLGTGHAVKQALPALKDfeGDVLVLYGDV 100
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
 3-51 1.44e-09

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: 56.43  E-value: 1.44e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 33568709   3 AMILAAGRGERMRPLTDTTPKPLLAVGGKPlIVWHIERLVAA-GLRDIVI 51
Cdd:cd02524   1 VVILAGGLGTRLSEETELKPKPMVEIGGRP-ILWHIMKIYSHyGHNDFIL 49
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 2-93 8.15e-09

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 54.68  E-value: 8.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33568709    2 RAMILAAGRGERMRPLTDTTPKPLLAVGGKPLIVWHIERLVAAGLRDI-VINHAWLGQRIVDHLGDGGAYGARLRYSAEA 80
Cdd:PRK15480   5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDIlIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84

                         90
                 ....*....|...
gi 33568709   81 aaleTAGGIAQAL 93
Cdd:PRK15480  85 ----SPDGLAQAF 93
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
3-107 3.90e-08

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


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 52.34  E-value: 3.90e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33568709   3 AMILAAGRGERMRPLTDTTPKPLLAVGGKPLIVWHIERLVAAGLRDIVI-NHAwlGQR-IVDH----------LGDGG-- 68
Cdd:COG1210   6 AVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFvTGR--GKRaIEDHfdrsyeleatLEAKGke 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 33568709  69 AYGARLRYSAEAAAL------ETAG-G--IAQALPLLGDAPFLVINGD 107
Cdd:COG1210  84 ELLEEVRSISPLANIhyvrqkEPLGlGhaVLCARPFVGDEPFAVLLGD 131
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
1-111 3.92e-08

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 52.58  E-value: 3.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33568709    1 MRAMILAAGRGERMRPLTDTTPKPLLAVGGKPLIVWHIERLVAAGLRDIVI----------NH--------AWLGQRI-- 60
Cdd:PRK10122   4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLvthasknaveNHfdtsyeleSLLEQRVkr 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 33568709   61 -----VDHLGDGGAYGARLRysaEAAALETAGGIAQALPLLGDAPFLVINGDIWCD 111
Cdd:PRK10122  84 qllaeVQSICPPGVTIMNVR---QGQPLGLGHSILCARPAIGDNPFVVVLPDVVID 136
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 3-71 3.09e-07

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 50.07  E-value: 3.09e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 33568709   3 AMILAAGRGERMRPLTDTTPKPLLAVGGK------PLivwhiERLVAAGLRDIVInhawLGQR----IVDHLGDGGAYG 71
Cdd:COG0448   4 AIILAGGRGSRLGPLTKDRAKPAVPFGGKyriidfPL-----SNCVNSGIRRVGV----LTQYkshsLNDHIGSGKPWD 73
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
3-51 3.58e-07

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 49.00  E-value: 3.58e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 33568709   3 AMILAAGRGERMRpltdtTPKPLLAVGGKPLIVWHIERLVAAGLRDIVI 51
Cdd:COG2068   6 AIILAAGASSRMG-----RPKLLLPLGGKPLLERAVEAALAAGLDPVVV 49
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 3-102 5.43e-07

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: 48.33  E-value: 5.43e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33568709   3 AMILAAGRGERMRpltdtTPKPLLAVGGKPLIVWHIERLVAAGLRDIVINHAWLGQRIVDHLGDGGAYGARLRYSAE--- 79
Cdd:cd04182   3 AIILAAGRSSRMG-----GNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALAGLPVVVVINPDWEEgms 77

                        90       100
                ....*....|....*....|....*..
gi 33568709  80 ---AAALETAGGIAQA-LPLLGDAPFL 102
Cdd:cd04182  78 sslAAGLEALPADADAvLILLADQPLV 104
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 6-108 7.15e-07

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: 47.96  E-value: 7.15e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33568709   6 LAAGRGERMrpltDTTPKPLLAVGGKPLIVWHIERLVAAGLRDIVI----NH----AWLGQRIVDHL-GDGGAYGARLRY 76
Cdd:COG2266   1 MAGGKGTRL----GGGEKPLLEICGKPMIDRVIDALEESCIDKIYVavspNTpktrEYLKERGVEVIeTPGEGYVEDLNE 76

                        90       100       110
                ....*....|....*....|....*....|..
gi 33568709  77 saeaaALETAGGiaqalpllgdaPFLVINGDI 108
Cdd:COG2266  77 -----ALESISG-----------PVLVVPADL 92
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 3-102 8.17e-07

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: 47.19  E-value: 8.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33568709     3 AMILAAGRGERMRpltdtTPKPLLAVGGKPLIVWHIERLVAAGlRDIVINHAWlgQRIVDHLGDGGAYGARLRYSAE--- 79
Cdd:pfam12804   1 AVILAGGRSSRMG-----GDKALLPLGGKPLLERVLERLRPAG-DEVVVVAND--EEVLAALAGLGVPVVPDPDPGQgpl 72

                          90       100
                  ....*....|....*....|....*.
gi 33568709    80 ---AAALETAGGIAQALPLLGDAPFL 102
Cdd:pfam12804  73 aglLAALRAAPGADAVLVLACDMPFL 98
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
 5-113 9.27e-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: 9.27e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33568709   5 ILAAGRGERMRPLTDTTPKPLLAVGGKPLIVWHIERLVAAG-------LRDIVINHAWLGQRIVDhlgdgGAYGAR-LRY 76
Cdd:cd04183   3 IPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEWVIESLAKIFdsrfifiCRDEHNTKFHLDESLKL-----LAPNATvVEL 77

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 33568709  77 SAE-AAALETAGGIAQALPllGDAPFLVINGDIWCDWD 113
Cdd:cd04183  78 DGEtLGAACTVLLAADLID--NDDPLLIFNCDQIVESD 113
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-107 1.59e-06

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 48.29  E-value: 1.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33568709    3 AMILAAGRGERMRpltDTTPKPLLAVGGKPLIVWHIERLVAAGLRDI--VINHAwlGQRIVDHLGDggaygaRLRYSAEA 80
Cdd:PRK14354   5 AIILAAGKGTRMK---SKLPKVLHKVCGKPMVEHVVDSVKKAGIDKIvtVVGHG--AEEVKEVLGD------RSEFALQE 73

                         90       100
                 ....*....|....*....|....*....
gi 33568709   81 AALETAGGIAQALPLLGDAP--FLVINGD 107
Cdd:PRK14354  74 EQLGTGHAVMQAEEFLADKEgtTLVICGD 102
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 3-56 4.55e-06

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: 45.98  E-value: 4.55e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 33568709   3 AMILAAGRGERMRPltdTTPKPLLAVGGKPLIVWHIERLVAAGLRD---IVINHAWL 56
Cdd:cd02516   3 AIILAAGSGSRMGA---DIPKQFLELGGKPVLEHTLEAFLAHPAIDeivVVVPPDDI 56
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
 3-71 9.78e-06

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: 44.84  E-value: 9.78e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 33568709   3 AMILAAGRGERMRPLTDTTPKPLLAVGGK-PLIVWHIERLVAAGLRDIVInhawLGQR----IVDHLGDGGAYG 71
Cdd:cd02508   1 AIILAGGEGTRLSPLTKKRAKPAVPFGGRyRLIDFPLSNMVNSGIRNVGV----LTQYksrsLNDHLGSGKEWD 70
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 5-56 1.12e-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: 44.74  E-value: 1.12e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 33568709   5 ILAAGRGERMRpltDTTPKPLLAVGGKPLIVWHIERLVAAGLRD---IVINHAWL 56
Cdd:COG1211   2 IPAAGSGSRMG---AGIPKQFLPLGGKPVLEHTLEAFLAHPRIDeivVVVPPDDI 53
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
 3-31 1.36e-05

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 45.22  E-value: 1.36e-05
                         10        20
                 ....*....|....*....|....*....
gi 33568709    3 AMILAAGRGERMRPLTDTTPKPLLAVGGK 31
Cdd:PRK00725  18 ALILAGGRGSRLKELTDKRAKPAVYFGGK 46
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
2-111 1.44e-05

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 44.90  E-value: 1.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33568709    2 RAMILAAGRGERMRPLTDTTPKPLLAVGGKPLIVWHIERLVAAGLRDIVINHAWLGQRIVDHLGDGGAYGARLRYSAEAA 81
Cdd:PRK13389  10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFDTSFELEAMLEKRVKRQ 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 33568709   82 ALET------------------AGGIAQAL----PLLGDAPFLVINGDIWCD 111
Cdd:PRK13389  90 LLDEvqsicpphvtimqvrqglAKGLGHAVlcahPVVGDEPVAVILPDVILD 141
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
3-51 2.11e-05

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 43.97  E-value: 2.11e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 33568709    3 AMILAAGRGERMRPltdTTPKPLLAVGGKPLIVWHIERLVAAGLRDIVI 51
Cdd:PRK00155   6 AIIPAAGKGSRMGA---DRPKQYLPLGGKPILEHTLEAFLAHPRIDEII 51
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 1-102 1.06e-04

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 42.66  E-value: 1.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33568709    1 MRAMILAAGRGERMRpltDTTPKPLLAVGGKPLIVWHIERLVAAGLRDIVINHAWLGQRIVDHLGDGGAYGARLR----- 75
Cdd:PRK14358   8 LDVVILAAGQGTRMK---SALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGAEQVEAALQGSGVAFARQEqqlgt 84

                         90       100       110
                 ....*....|....*....|....*....|
gi 33568709   76 ---YSAEAAALETAGgiAQALPLLGDAPFL 102
Cdd:PRK14358  85 gdaFLSGASALTEGD--ADILVLYGDTPLL 112
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 1-102 1.78e-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: 41.02  E-value: 1.78e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33568709   1 MRAMILAAGRGERMrpltdTTPKPLLAVGGKPLIVWHIERLVAAGLrDIVIN-------HAWLGQR-IVDHLGD----GG 68
Cdd:cd02503   1 ITGVILAGGKSRRM-----GGDKALLELGGKPLLEHVLERLKPLVD-EVVISanrdqerYALLGVPvIPDEPPGkgplAG 74

                        90       100       110
                ....*....|....*....|....*....|....
gi 33568709  69 AYGArLRYSAEAAALETAggiaqalpllGDAPFL 102
Cdd:cd02503  75 ILAA-LRAAPADWVLVLA----------CDMPFL 97
ispD TIGR00453
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ...
 3-51 2.06e-04

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: 41.12  E-value: 2.06e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 33568709     3 AMILAAGRGERMRPltdTTPKPLLAVGGKPLIVWHIERLVAAGLRDIVI 51
Cdd:TIGR00453   2 AVIPAAGRGTRFGS---GVPKQYLELGGRPLLEHALDAFLAHPAIDEVV 47
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 3-64 2.88e-04

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: 40.67  E-value: 2.88e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 33568709   3 AMILAAGRGERMRPLTDTTPKPLLAVGGKPLIVWHIERLVAAGLRDIVINHAWLGQRIVDHL 64
Cdd:cd04197   3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQIKEYI 64
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
 1-103 3.03e-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: 41.02  E-value: 3.03e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33568709   1 MRAMILAAGRGERMRPL-TDTTPKPLLAV-GGKPLIVWHIERLVAAGLRD---IVINHAwLGQRIVDHLGDGGAYGarlR 75
Cdd:cd02509   1 IYPVILAGGSGTRLWPLsRESYPKQFLKLfGDKSLLQQTLDRLKGLVPPDrilVVTNEE-YRFLVREQLPEGLPEE---N 76

                        90       100       110
                ....*....|....*....|....*....|..
gi 33568709  76 YSAEAAALETAGGIAQALPLL----GDAPFLV 103
Cdd:cd02509  77 IILEPEGRNTAPAIALAALYLakrdPDAVLLV 108
mobA PRK00317
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
 1-52 4.77e-04

molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed


Pssm-ID: 234725 [Multi-domain]  Cd Length: 193  Bit Score: 39.78  E-value: 4.77e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 33568709    1 MRAMILAAGRGERMrpltDTTPKPLLAVGGKPLIVWHIERLvAAGLRDIVIN 52
Cdd:PRK00317   4 ITGVILAGGRSRRM----GGVDKGLQELNGKPLIQHVIERL-APQVDEIVIN 50
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-39 6.29e-04

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 40.13  E-value: 6.29e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 33568709    1 MRAMILAAGRGERMRpltDTTPKPLLAVGGKPLIVWHIE 39
Cdd:PRK14357   1 MRALVLAAGKGTRMK---SKIPKVLHKISGKPMINWVID 36
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-102 6.43e-04

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 40.11  E-value: 6.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33568709    3 AMILAAGRGERMRpltDTTPKPLLAVGGKPLIVWHIERLVAAGLRDIVINHAWLGQRIVDHLGDGGAygarLRYSAEAAA 82
Cdd:PRK14355   6 AIILAAGKGTRMK---SDLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHFAGDGD----VSFALQEEQ 78

                         90       100       110
                 ....*....|....*....|....*....|.
gi 33568709   83 LETAGGIAQALP-----------LLGDAPFL 102
Cdd:PRK14355  79 LGTGHAVACAAPaldgfsgtvliLCGDVPLL 109
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 1-31 9.33e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 39.47  E-value: 9.33e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 33568709    1 MRAMILAAGRGERMRPLTDTTPKPLLAVGGK 31
Cdd:PRK05293   4 MLAMILAGGQGTRLGKLTKNIAKPAVPFGGK 34
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-107 1.18e-03

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 39.32  E-value: 1.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33568709    3 AMILAAGRGERMRpltDTTPKPLLAVGGKPLIvWHIER----LVAAGLRDIVINHAWLGQRIVDHLGDggaygarlRYSA 78
Cdd:PRK14356   8 ALILAAGKGTRMH---SDKPKVLQTLLGEPML-RFVYRalrpLFGDNVWTVVGHRADMVRAAFPDEDA--------RFVL 75

                         90       100       110
                 ....*....|....*....|....*....|..
gi 33568709   79 EAAALETAGGIAQALPLLGDAPF---LVINGD 107
Cdd:PRK14356  76 QEQQLGTGHALQCAWPSLTAAGLdrvLVVNGD 107
ispDF PRK09382
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ...
 3-64 1.23e-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: 39.45  E-value: 1.23e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 33568709    3 AMILAAGRGERMRPltdTTPKPLLAVGGKPLIVWHIERLVAAGLRD---IVINHAWLG--QRIVDHL 64
Cdd:PRK09382   8 LVIVAAGRSTRFSA---EVKKQWLRIGGKPLWLHVLENLSSAPAFKeivVVIHPDDIAymKKALPEI 71
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-102 1.53e-03

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 39.07  E-value: 1.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33568709    3 AMILAAGRGERMRpltDTTPKPLLAVGGKPLIVWHIERLVAAGLRDIVI----NHAWLGQRIVDHLGDGGAYGARLR--- 75
Cdd:PRK14353   8 AIILAAGEGTRMK---SSLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVvvgpGAEAVAAAAAKIAPDAEIFVQKERlgt 84

                         90       100
                 ....*....|....*....|....*...
gi 33568709   76 -YSAEAAALETAGGIAQALPLLGDAPFL 102
Cdd:PRK14353  85 aHAVLAAREALAGGYGDVLVLYGDTPLI 112
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 3-52 1.64e-03

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: 38.25  E-value: 1.64e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 33568709   3 AMILAAGRGERMRpltdtTPKPLLAVGGKPLIVWHIERLvAAGLRDIVIN 52
Cdd:COG0746   7 GVILAGGRSRRMG-----QDKALLPLGGRPLLERVLERL-RPQVDEVVIV 50
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 5-108 2.35e-03

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 38.37  E-value: 2.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33568709    5 ILAAGRGERMRpltDTTPKPLLAVGGKPLIVWHIE--RLVAAGLRDIVINHAwlGQRIVDHLGDGGaygaRLRYSAEAAA 82
Cdd:PRK14360   6 ILAAGKGTRMK---SSLPKVLHPLGGKSLVERVLDscEELKPDRRLVIVGHQ--AEEVEQSLAHLP----GLEFVEQQPQ 76

                         90       100       110
                 ....*....|....*....|....*....|
gi 33568709   83 LETAGGIAQALPLL----GDapFLVINGDI 108
Cdd:PRK14360  77 LGTGHAVQQLLPVLkgfeGD--LLVLNGDV 104
PRK05450 PRK05450
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
 23-51 7.35e-03

3-deoxy-manno-octulosonate cytidylyltransferase; Provisional


Pssm-ID: 235473  Cd Length: 245  Bit Score: 36.63  E-value: 7.35e-03
                         10        20
                 ....*....|....*....|....*....
gi 33568709   23 KPLLAVGGKPLIVWHIERLVAAGLRDIVI 51
Cdd:PRK05450  19 KPLADIGGKPMIVRVYERASKAGADRVVV 47
 
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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