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Conserved domains on  [gi|489190177|ref|WP_003099549|]
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MULTISPECIES: N-acetylmuramate alpha-1-phosphate uridylyltransferase MurU [Pseudomonas]

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 ...
2-222 1.74e-98

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: 285.89  E-value: 1.74e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177   2 KAMILAAGRGERMRPTTLHTPKPLIEAAGVPLIERQLLALRQAGVDDWVINHAWLGEQIEAYLGDGSRLGGRIAYSPEGE 81
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRFGVRITYVDEGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177  82 PLETGGGIFRALPLLGEQPFLLLNGDVWSDFDYSRL---HLADGDLAHLVLVDNPAHHPAGDFHLDAGGRVGETRE---- 154
Cdd:COG1208   81 PLGTGGALKRALPLLGDEPFLVLNGDILTDLDLAALlafHREKGADATLALVPVPDPSRYGVVELDGDGRVTRFVEkpee 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489190177 155 AGGNLTYSGIAVLHPALFEGCQPG-AFKLAPLLRKAIAAGRVSGEHHRGQWVDVGTHERLAEVERLLAE 222
Cdd:COG1208  161 PPSNLINAGIYVLEPEIFDYIPEGePFDLEDLLPRLIAEGRVYGYVHDGYWLDIGTPEDLLEANALLLS 229
 
Name Accession Description Interval E-value
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
2-222 1.74e-98

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: 285.89  E-value: 1.74e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177   2 KAMILAAGRGERMRPTTLHTPKPLIEAAGVPLIERQLLALRQAGVDDWVINHAWLGEQIEAYLGDGSRLGGRIAYSPEGE 81
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRFGVRITYVDEGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177  82 PLETGGGIFRALPLLGEQPFLLLNGDVWSDFDYSRL---HLADGDLAHLVLVDNPAHHPAGDFHLDAGGRVGETRE---- 154
Cdd:COG1208   81 PLGTGGALKRALPLLGDEPFLVLNGDILTDLDLAALlafHREKGADATLALVPVPDPSRYGVVELDGDGRVTRFVEkpee 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489190177 155 AGGNLTYSGIAVLHPALFEGCQPG-AFKLAPLLRKAIAAGRVSGEHHRGQWVDVGTHERLAEVERLLAE 222
Cdd:COG1208  161 PPSNLINAGIYVLEPEIFDYIPEGePFDLEDLLPRLIAEGRVYGYVHDGYWLDIGTPEDLLEANALLLS 229
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
2-215 6.79e-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: 268.67  E-value: 6.79e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177   2 KAMILAAGRGERMRPTTLHTPKPLIEAAGVPLIERQLLALRQAGVDDWVINHAWLGEQIEAYLGDgSRLGGRIAYSPE-G 80
Cdd:cd06422    1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHLGD-SRFGLRITISDEpD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177  81 EPLETGGGIFRALPLLGEQPFLLLNGDVWSDFDYSRLHLA-----DGDLAHLVLVDNPAHHPAGDFHLDAGGRV-GETRE 154
Cdd:cd06422   80 ELLETGGGIKKALPLLGDEPFLVVNGDILWDGDLAPLLLLhawrmDALLLLLPLVRNPGHNGVGDFSLDADGRLrRGGGG 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489190177 155 AGGNLTYSGIAVLHPALFEGCQPGAFKLAPLLRKAIAAGRVSGEHHRGQWVDVGTHERLAE 215
Cdd:cd06422  160 AVAPFTFTGIQILSPELFAGIPPGKFSLNPLWDRAIAAGRLFGLVYDGLWFDVGTPERLLA 220
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
1-208 8.43e-39

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: 137.73  E-value: 8.43e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177    1 MKAMILAAGRGERMRPTTLHTPKPLIEAAGVPLIERQLLALRQAGVDDWVINHAWLGEQIEAYLGDGSRLGGRIAYSPEG 80
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEKVREYFGDGSRGGVPIEYVVQE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177   81 EPLETGGGIFRALPLLgEQPFLLLNGDVWSDFD-YSRLHLADGDLAHLVLVDNPAHHpaGDFHLDaGGRVGETRE----A 155
Cdd:TIGR03992  81 EQLGTADALGSAKEYV-DDEFLVLNGDVLLDSDlLERLIRAEAPAIAVVEVDDPSDY--GVVETD-GGRVTGIVEkpenP 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 489190177  156 GGNLTYSGIAVLHPALF---EGCQP---GAFKLAPLLRKAIAAGRVSGEHHRGQWVDVG 208
Cdd:TIGR03992 157 PSNLINAGIYLFSPEIFellEKTKLsprGEYELTDALQLLIDEGKVKAVELDGFWLDVG 215
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
2-221 1.10e-24

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: 97.32  E-value: 1.10e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177    2 KAMILAAGRGERMRPTTLHTPKPLIEAAG-VPLIERQLLALRQAGVDD-WVINHAWLGEQIEAYLGDGSRLGGRIAYSPE 79
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGkYPLIDYPLSRLANAGIREiIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177   80 GEPLETGGGIFRALPLLGEQ--PFLLLNGDVWSDFDYS---RLHLADGDLAhLVLVDNPAHHPAGDFHL---DAGGRVGE 151
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEksDVLVLGGDHIYRMDLEqavKFHIEKAADA-TVTFGIVPVEPPTGYGVvefDDNGRVIR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177  152 -----TREAGGNLTYSGIAVLHPALF-------EGCQPGAFKLAPLLRKAIAAGRVSGEHHR--GQWVDVGTHERLAEVE 217
Cdd:pfam00483 160 fvekpKLPKASNYASMGIYIFNSGVLdflakylEELKRGEDEITDILPKALEDGKLAYAFIFkgYAWLDVGTWDSLWEAN 239

                  ....
gi 489190177  218 RLLA 221
Cdd:pfam00483 240 LFLL 243
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
2-221 9.74e-07

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 48.52  E-value: 9.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177   2 KAMILAAGRGERMRPTTLHTPKPLIEAAGVPLIERQLLALRQAGVDD-WVINHAWLGEQIEAYLGDGSRLGGRIAYSPEG 80
Cdd:PRK15480   5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDiLIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177  81 EPletgGGIFRALpLLGEQPF------LLLNGDVWSDFDYSRLHLA-----DGDLAHLVLVDNPAHHPAGDFHLDAGGRV 149
Cdd:PRK15480  85 SP----DGLAQAF-IIGEEFIggddcaLVLGDNIFYGHDLPKLMEAavnkeSGATVFAYHVNDPERYGVVEFDQNGTAIS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177 150 GETR--EAGGNLTYSGIAVLHPALFE---GCQP---GAFKLAPLLRKAIAAGRVS-GEHHRG-QWVDVGTHERLAEVERL 219
Cdd:PRK15480 160 LEEKplQPKSNYAVTGLYFYDNDVVEmakNLKPsarGELEITDINRIYMEQGRLSvAMMGRGyAWLDTGTHQSLIEASNF 239

                 ..
gi 489190177 220 LA 221
Cdd:PRK15480 240 IA 241
 
Name Accession Description Interval E-value
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
2-222 1.74e-98

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: 285.89  E-value: 1.74e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177   2 KAMILAAGRGERMRPTTLHTPKPLIEAAGVPLIERQLLALRQAGVDDWVINHAWLGEQIEAYLGDGSRLGGRIAYSPEGE 81
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRFGVRITYVDEGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177  82 PLETGGGIFRALPLLGEQPFLLLNGDVWSDFDYSRL---HLADGDLAHLVLVDNPAHHPAGDFHLDAGGRVGETRE---- 154
Cdd:COG1208   81 PLGTGGALKRALPLLGDEPFLVLNGDILTDLDLAALlafHREKGADATLALVPVPDPSRYGVVELDGDGRVTRFVEkpee 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489190177 155 AGGNLTYSGIAVLHPALFEGCQPG-AFKLAPLLRKAIAAGRVSGEHHRGQWVDVGTHERLAEVERLLAE 222
Cdd:COG1208  161 PPSNLINAGIYVLEPEIFDYIPEGePFDLEDLLPRLIAEGRVYGYVHDGYWLDIGTPEDLLEANALLLS 229
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
2-215 6.79e-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: 268.67  E-value: 6.79e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177   2 KAMILAAGRGERMRPTTLHTPKPLIEAAGVPLIERQLLALRQAGVDDWVINHAWLGEQIEAYLGDgSRLGGRIAYSPE-G 80
Cdd:cd06422    1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHLGD-SRFGLRITISDEpD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177  81 EPLETGGGIFRALPLLGEQPFLLLNGDVWSDFDYSRLHLA-----DGDLAHLVLVDNPAHHPAGDFHLDAGGRV-GETRE 154
Cdd:cd06422   80 ELLETGGGIKKALPLLGDEPFLVVNGDILWDGDLAPLLLLhawrmDALLLLLPLVRNPGHNGVGDFSLDADGRLrRGGGG 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489190177 155 AGGNLTYSGIAVLHPALFEGCQPGAFKLAPLLRKAIAAGRVSGEHHRGQWVDVGTHERLAE 215
Cdd:cd06422  160 AVAPFTFTGIQILSPELFAGIPPGKFSLNPLWDRAIAAGRLFGLVYDGLWFDVGTPERLLA 220
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
3-208 3.72e-54

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


Pssm-ID: 133024 [Multi-domain]  Cd Length: 217  Bit Score: 172.76  E-value: 3.72e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177   3 AMILAAGRGERMRPTTLHTPKPLIEAAGVPLIERQLLALRQAGVDDWVINHAWLGEQIEAYLGDGSRLGGRIAYSPEGEP 82
Cdd:cd04181    1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGSKFGVNIEYVVQEEP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177  83 LETGGGIFRALPLLGEQPFLLLNGDVWSDFDYSRL---HLADGDLAHLVL--VDNPAHHpaGDFHLDAGGRVGETRE--- 154
Cdd:cd04181   81 LGTAGAVRNAEDFLGDDDFLVVNGDVLTDLDLSELlrfHREKGADATIAVkeVEDPSRY--GVVELDDDGRVTRFVEkpt 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489190177 155 -AGGNLTYSGIAVLHPALFEGCQPGAFK----LAPLLRKAIAAGRVSGEHHRGQWVDVG 208
Cdd:cd04181  159 lPESNLANAGIYIFEPEILDYIPEILPRgedeLTDAIPLLIEEGKVYGYPVDGYWLDIG 217
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
3-215 4.46e-43

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


Pssm-ID: 133065 [Multi-domain]  Cd Length: 223  Bit Score: 144.62  E-value: 4.46e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177   3 AMILAAGRGERMRPTTLHTPKPLIEAAGVPLIERQLLALRQAGVDDWVINHAWLGEQIEAYLGDGSRLGGRIAYSPEGEP 82
Cdd:cd06915    1 AVILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYLAEQIEEYFGDGYRGGIRIYYVIEPEP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177  83 LETGGGIFRALPLLGEQPFLLLNGDVWSDFDYSRL---HLADGDLAHLVLVDNPAHHPAGDFHLDAGGRVGETREAGGNL 159
Cdd:cd06915   81 LGTGGAIKNALPKLPEDQFLVLNGDTYFDVDLLALlaaLRASGADATMALRRVPDASRYGNVTVDGDGRVIAFVEKGPGA 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489190177 160 TY----SGIAVLHPALFEG-CQPGAFKLAPLLRKAIAAGRVSGEHHRGQWVDVGTHERLAE 215
Cdd:cd06915  161 APglinGGVYLLRKEILAEiPADAFSLEADVLPALVKRGRLYGFEVDGYFIDIGIPEDYAR 221
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
1-208 8.43e-39

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: 137.73  E-value: 8.43e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177    1 MKAMILAAGRGERMRPTTLHTPKPLIEAAGVPLIERQLLALRQAGVDDWVINHAWLGEQIEAYLGDGSRLGGRIAYSPEG 80
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEKVREYFGDGSRGGVPIEYVVQE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177   81 EPLETGGGIFRALPLLgEQPFLLLNGDVWSDFD-YSRLHLADGDLAHLVLVDNPAHHpaGDFHLDaGGRVGETRE----A 155
Cdd:TIGR03992  81 EQLGTADALGSAKEYV-DDEFLVLNGDVLLDSDlLERLIRAEAPAIAVVEVDDPSDY--GVVETD-GGRVTGIVEkpenP 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 489190177  156 GGNLTYSGIAVLHPALF---EGCQP---GAFKLAPLLRKAIAAGRVSGEHHRGQWVDVG 208
Cdd:TIGR03992 157 PSNLINAGIYLFSPEIFellEKTKLsprGEYELTDALQLLIDEGKVKAVELDGFWLDVG 215
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
1-223 1.98e-36

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: 127.68  E-value: 1.98e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177   1 MKAMILAAGRGERMRPTTLHTPKPLIEAAGVPLIERQLLALRQAGVDDWVINHAWLGEQIEAYLGDGSRLGGRIAYSPEG 80
Cdd:cd04189    1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEALGDGSRFGVRITYILQE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177  81 EPLETGGGIFRALPLLGEQPFLLLNGD-----VWSDFdYSRLHLADGDlAHLVL--VDNPAHHpaGDFHLDAG---GRVG 150
Cdd:cd04189   81 EPLGLAHAVLAARDFLGDEPFVVYLGDnliqeGISPL-VRDFLEEDAD-ASILLaeVEDPRRF--GVAVVDDGrivRLVE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177 151 ETREAGGNLTYSGIAVLHPALFE---GCQP---GAFKLAPLLRKAIAAGR-VSGEHHRGQWVDVGTHERLAEVERLLAEH 223
Cdd:cd04189  157 KPKEPPSNLALVGVYAFTPAIFDaisRLKPswrGELEITDAIQWLIDRGRrVGYSIVTGWWKDTGTPEDLLEANRLLLDK 236
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
3-211 6.09e-36

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: 126.09  E-value: 6.09e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177   3 AMILAAGRGERMRPTTLHTPKPLIEAAGVPLIERQLLALRQAGVDDWVINHAWLGEQIEAYLGDGSRLGGRIAYSPEGEP 82
Cdd:cd06426    1 VVIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNYLAEMIEDYFGDGSKFGVNISYVREDKP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177  83 LETGGgifrALPLLGEQ---PFLLLNGDVWSDFDYSRL---HLADGDLAHLVLVDNPAHHPAGDFHLDaGGRVGETREAg 156
Cdd:cd06426   81 LGTAG----ALSLLPEKptdPFLVMNGDILTNLNYEHLldfHKENNADATVCVREYEVQVPYGVVETE-GGRITSIEEK- 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177 157 GNLTY---SGIAVLHPALFEGCQPGAFKLAP-LLRKAIAAG-RVSGEHHRGQWVDVGTHE 211
Cdd:cd06426  155 PTHSFlvnAGIYVLEPEVLDLIPKNEFFDMPdLIEKLIKEGkKVGVFPIHEYWLDIGRPE 214
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
2-221 1.00e-29

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 110.33  E-value: 1.00e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177   2 KAMILAAGRGERMRPTTLHTPKPLIEAAGVPLIERQLLALRQAGVDDWVINHAWLGEQIEAYLgDGSRLGGRIAYSPEGE 81
Cdd:COG1213    1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEAL-ARPGPDVTFVYNPDYD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177  82 PLETGGGIFRALPLLGEqPFLLLNGD-VWSDFDYSRLHLADGDLAhlVLVDNPAHHPAGD---FHLDAGGRVGET----R 153
Cdd:COG1213   80 ETNNIYSLWLAREALDE-DFLLLNGDvVFDPAILKRLLASDGDIV--LLVDRKWEKPLDEevkVRVDEDGRIVEIgkklP 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177 154 EAGGNLTYSGIAVLHPALFEgcqpgafKLAPLLRKAIAAGRVSGEH-------------------HRGQWVDVGTHERLA 214
Cdd:COG1213  157 PEEADGEYIGIFKFSAEGAA-------ALREALEALIDEGGPNLYYedalqelideggpvkavdiGGLPWVEIDTPEDLE 229

                 ....*..
gi 489190177 215 EVERLLA 221
Cdd:COG1213  230 RAEELFA 236
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
1-170 4.09e-28

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: 106.14  E-value: 4.09e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177   1 MKAMILAAGRGERMRPTTLHTPKPLIEAAGVPLIERQLLALRQAGVDDWVINHAWLGEQIEAYLGDGS-RLGGRIAYSPE 79
Cdd:cd06425    1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYRPEDMVPFLKEYEkKLGIKITFSIE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177  80 GEPLETGGGIFRALPLLGE--QPFLLLNGDVWSDFDYSRL---HLADGDLAHLVL--VDNPAhhpagDF----HLDAGGR 148
Cdd:cd06425   81 TEPLGTAGPLALARDLLGDddEPFFVLNSDVICDFPLAELldfHKKHGAEGTILVtkVEDPS-----KYgvvvHDENTGR 155
                        170       180
                 ....*....|....*....|....*.
gi 489190177 149 VGETRE----AGGNLTYSGIAVLHPA 170
Cdd:cd06425  156 IERFVEkpkvFVGNKINAGIYILNPS 181
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
3-217 1.07e-26

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: 102.31  E-value: 1.07e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177   3 AMILAAGRGERMRPTTLHTPKPLIEAAGVPLIERQLLALRQAGVDDWVINHAWLGEQIEAYLGDGSRLggRIAYSPegEP 82
Cdd:cd02523    1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKKYPNI--KFVYNP--DY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177  83 LETGGGI--FRALPLLGEqPFLLLNGDVWsdFDYS---RLHLADGDLAhlVLVD---NPAHHPAGDFHLDAGGRVGETRE 154
Cdd:cd02523   77 AETNNIYslYLARDFLDE-DFLLLEGDVV--FDPSileRLLSSPADNA--ILVDkktKEWEDEYVKDLDDAGVLLGIISK 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177 155 AGGNLT----YSGIAVLHPALFEgcqpgafKLAPLLRKAIAAGRVSGEHHR------------------GQWVDVGTHER 212
Cdd:cd02523  152 AKNLEEiqgeYVGISKFSPEDAD-------RLAEALEELIEAGRVNLYYEDalqrliseegvkvkdisdGFWYEIDDLED 224

                 ....*
gi 489190177 213 LAEVE 217
Cdd:cd02523  225 LERAE 229
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
2-221 1.10e-24

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: 97.32  E-value: 1.10e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177    2 KAMILAAGRGERMRPTTLHTPKPLIEAAG-VPLIERQLLALRQAGVDD-WVINHAWLGEQIEAYLGDGSRLGGRIAYSPE 79
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGkYPLIDYPLSRLANAGIREiIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177   80 GEPLETGGGIFRALPLLGEQ--PFLLLNGDVWSDFDYS---RLHLADGDLAhLVLVDNPAHHPAGDFHL---DAGGRVGE 151
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEksDVLVLGGDHIYRMDLEqavKFHIEKAADA-TVTFGIVPVEPPTGYGVvefDDNGRVIR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177  152 -----TREAGGNLTYSGIAVLHPALF-------EGCQPGAFKLAPLLRKAIAAGRVSGEHHR--GQWVDVGTHERLAEVE 217
Cdd:pfam00483 160 fvekpKLPKASNYASMGIYIFNSGVLdflakylEELKRGEDEITDILPKALEDGKLAYAFIFkgYAWLDVGTWDSLWEAN 239

                  ....
gi 489190177  218 RLLA 221
Cdd:pfam00483 240 LFLL 243
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-107 1.76e-21

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 89.76  E-value: 1.76e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177   1 MKAMILAAGRGERMRPTTLHTPKPLIEAAGVPLIERQLLALRQAGVDDWVI---NHawLGEQIEAYLGDGSRLGGRIAYS 77
Cdd:COG1209    1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIistPE--DGPQFERLLGDGSQLGIKISYA 78
                         90       100       110
                 ....*....|....*....|....*....|
gi 489190177  78 PEGEPLETGGGIFRALPLLGEQPFLLLNGD 107
Cdd:COG1209   79 VQPEPLGLAHAFIIAEDFIGGDPVALVLGD 108
LicC COG4750
CTP:phosphocholine cytidylyltransferase LicC [Cell wall/membrane/envelope biogenesis, Lipid ...
1-66 7.94e-17

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


Pssm-ID: 443784 [Multi-domain]  Cd Length: 228  Bit Score: 76.02  E-value: 7.94e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489190177   1 MKAMILAAGRGERMRPTTLHTPKPLIEAAGVPLIERQLLALRQAGVDDWVINHAWLGEQIEaYLGD 66
Cdd:COG4750    1 MNAIILAAGLGSRFAPITYETPKGLLKVNGEPLIERQIRQLHEAGITDITVVVGYLKEQFE-YLED 65
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
3-117 4.20e-13

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


Pssm-ID: 133050 [Multi-domain]  Cd Length: 257  Bit Score: 66.51  E-value: 4.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177   3 AMILAAG--RGERMRPTTLHTPKPLIEAAGVPLIERQLLALRQ-AGVDDWVINHAWLGEQIEAYLGDGSR-LGGRIAYSP 78
Cdd:cd06428    1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKvPDLKEVLLIGFYPESVFSDFISDAQQeFNVPIRYLQ 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 489190177  79 EGEPLETGGGI--FRALPLLGE-QPFLLLNGDVWSDFDYSRL 117
Cdd:cd06428   81 EYKPLGTAGGLyhFRDQILAGNpSAFFVLNADVCCDFPLQEL 122
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
1-108 6.68e-11

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


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 60.81  E-value: 6.68e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177   1 MKAMILAAGRGERMRPTtlhTPKPLIEAAGVPLIERQLLALRQAGVDD--WVINHAwlGEQIEAYLGDgsrlgGRIAYSP 78
Cdd:COG1207    3 LAVVILAAGKGTRMKSK---LPKVLHPLAGKPMLEHVLDAARALGPDRivVVVGHG--AEQVRAALAD-----LDVEFVL 72
                         90       100       110
                 ....*....|....*....|....*....|..
gi 489190177  79 EGEPLETGGGIFRALPLLG--EQPFLLLNGDV 108
Cdd:COG1207   73 QEEQLGTGHAVQQALPALPgdDGTVLVLYGDV 104
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
3-108 2.66e-10

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


Pssm-ID: 133020 [Multi-domain]  Cd Length: 229  Bit Score: 58.30  E-value: 2.66e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177   3 AMILAAGRGERMRPttlHTPKPLIEAAGVPLIERQLLALRQAGVDDW--VINHAwlGEQIEAYLGDGSrlggrIAYSPEG 80
Cdd:cd02540    1 AVILAAGKGTRMKS---DLPKVLHPLAGKPMLEHVLDAARALGPDRIvvVVGHG--AEQVKKALANPN-----VEFVLQE 70
                         90       100       110
                 ....*....|....*....|....*....|
gi 489190177  81 EPLETGGGIFRALPLLGEQ--PFLLLNGDV 108
Cdd:cd02540   71 EQLGTGHAVKQALPALKDFegDVLVLYGDV 100
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
3-204 4.87e-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: 54.89  E-value: 4.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177   3 AMILAAGRGERMRPTTLHTPKPLIEAAGVPLIERQLLALRQAGVDDWVINHAWLGEQIEAYLGDG---------SRLGGR 73
Cdd:cd02524    1 VVILAGGLGTRLSEETELKPKPMVEIGGRPILWHIMKIYSHYGHNDFILCLGYKGHVIKEYFLNYflhnsdvtiDLGTNR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177  74 IAYSPE------------GEPLETGGGIFRALPLLG-EQPFLLLNGDVWSDFDYSRL---HLADGDLAHLVLVdnpahHP 137
Cdd:cd02524   81 IELHNSdiedwkvtlvdtGLNTMTGGRLKRVRRYLGdDETFMLTYGDGVSDVNINALiefHRSHGKLATVTAV-----HP 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489190177 138 AGDFH---LDAGGRVGETRE---AGGNLTYSGIAVLHPALFEGCQPGA--FKLAPlLRKAIAAGRVSGEHHRGQW 204
Cdd:cd02524  156 PGRFGeldLDDDGQVTSFTEkpqGDGGWINGGFFVLEPEVFDYIDGDDtvFEREP-LERLAKDGELMAYKHTGFW 229
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
1-107 5.82e-09

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: 54.50  E-value: 5.82e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177   1 MKAMILAAGRGERMRPTTLHTPKPLIEAAGVPLIERQLLALRQAGVDDWVINHAwlGEQIEAY---LGDGSRLGGRIAYS 77
Cdd:cd02538    1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIIST--PEDLPLFkelLGDGSDLGIRITYA 78
                         90       100       110
                 ....*....|....*....|....*....|....
gi 489190177  78 PEGEPletgGGIFRALPL----LGEQPFLLLNGD 107
Cdd:cd02538   79 VQPKP----GGLAQAFIIgeefIGDDPVCLILGD 108
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
1-117 8.08e-09

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: 53.80  E-value: 8.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177   1 MKAMILAAGRGERMRPTTLHTPKPLIEAAGVPLIERQLLALRQAGVDDWVI---NHAwlgEQIEAYLGDGSRLGGR---- 73
Cdd:cd02507    1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVvccEHS---QAIIEHLLKSKWSSLSskmi 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 489190177  74 --IAYSPEGEPLETGGGIFRALPLLgEQPFLLLNGDVWSDFDYSRL 117
Cdd:cd02507   78 vdVITSDLCESAGDALRLRDIRGLI-RSDFLLLSCDLVSNIPLSEL 122
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
1-120 1.57e-07

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: 49.96  E-value: 1.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177   1 MKAMILAAGRGERMRPTTLHTPKPLIEAAGVPLIERQLLALRQAGVDDWVI----NHAwlgEQIEAYL---GDGSRLGGR 73
Cdd:cd04198    1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVvvpeEEQ---AEISTYLrsfPLNLKQKLD 77
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489190177  74 IAYSPEGEPLETgGGIFRALPLLGEQPFLLLNGDVWSD------FDYSRLHLA 120
Cdd:cd04198   78 EVTIVLDEDMGT-ADSLRHIRKKIKKDFLVLSCDLITDlplielVDLHRSHDA 129
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
3-79 7.11e-07

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 47.85  E-value: 7.11e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489190177   3 AMILAAGRGERMrpttlHTPKPLIEAAGVPLIERQLLALRQAGVDDW--VINHAwlGEQIEAYLgdgSRLGGRIAYSPE 79
Cdd:COG2068    6 AIILAAGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPVvvVLGAD--AEEVAAAL---AGLGVRVVVNPD 74
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
2-221 9.74e-07

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 48.52  E-value: 9.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177   2 KAMILAAGRGERMRPTTLHTPKPLIEAAGVPLIERQLLALRQAGVDD-WVINHAWLGEQIEAYLGDGSRLGGRIAYSPEG 80
Cdd:PRK15480   5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDiLIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177  81 EPletgGGIFRALpLLGEQPF------LLLNGDVWSDFDYSRLHLA-----DGDLAHLVLVDNPAHHPAGDFHLDAGGRV 149
Cdd:PRK15480  85 SP----DGLAQAF-IIGEEFIggddcaLVLGDNIFYGHDLPKLMEAavnkeSGATVFAYHVNDPERYGVVEFDQNGTAIS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177 150 GETR--EAGGNLTYSGIAVLHPALFE---GCQP---GAFKLAPLLRKAIAAGRVS-GEHHRG-QWVDVGTHERLAEVERL 219
Cdd:PRK15480 160 LEEKplQPKSNYAVTGLYFYDNDVVEmakNLKPsarGELEITDINRIYMEQGRLSvAMMGRGyAWLDTGTHQSLIEASNF 239

                 ..
gi 489190177 220 LA 221
Cdd:PRK15480 240 IA 241
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
5-154 4.76e-06

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: 46.09  E-value: 4.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177   5 ILAAGRGERMRPTTLHTPKPLIEAAGVPLIERQLLALrqAGVDDWVINHAWLGEQIEAYlGDGSRLggrIAYSPEGE--- 81
Cdd:cd04183    3 IPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEWVIESL--AKIFDSRFIFICRDEHNTKF-HLDESL---KLLAPNATvve 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177  82 -PLETGGGIFRALPLL----GEQPFLLLNGDVWSDFDYSRLHLA----DGDLAHLVLvdnPAHHPAGDF-HLDAGGRVGE 151
Cdd:cd04183   77 lDGETLGAACTVLLAAdlidNDDPLLIFNCDQIVESDLLAFLAAfrerDLDGGVLTF---FSSHPRWSYvKLDENGRVIE 153

                 ...
gi 489190177 152 TRE 154
Cdd:cd04183  154 TAE 156
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
3-107 9.89e-06

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 45.59  E-value: 9.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177   3 AMILAAGRGERMRPTtlhTPKPLIEAAGVPLIERQLLALRQAGVDD--WVINHAwlGEQIEAylgdgsRLGGRIAYSPEG 80
Cdd:PRK14354   5 AIILAAGKGTRMKSK---LPKVLHKVCGKPMVEHVVDSVKKAGIDKivTVVGHG--AEEVKE------VLGDRSEFALQE 73
                         90       100
                 ....*....|....*....|....*....
gi 489190177  81 EPLETGGGIFRALPLLGEQP--FLLLNGD 107
Cdd:PRK14354  74 EQLGTGHAVMQAEEFLADKEgtTLVICGD 102
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
3-51 1.09e-05

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 44.74  E-value: 1.09e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 489190177   3 AMILAAGRGERMRPTTlhtPKPLIEAAGVPLIERQLLALRQAGVDDWVI 51
Cdd:PRK00155   6 AIIPAAGKGSRMGADR---PKQYLPLGGKPILEHTLEAFLAHPRIDEII 51
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
3-108 1.40e-05

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 45.12  E-value: 1.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177   3 AMILAAGRGERMRPttlHTPKPLIEAAGVPLIERQLLALRQAGVDDWVINHAWLGEQIEAYLGDgsrlGGRIAYSPEGEP 82
Cdd:PRK14355   6 AIILAAGKGTRMKS---DLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHFAG----DGDVSFALQEEQ 78
                         90       100       110
                 ....*....|....*....|....*....|
gi 489190177  83 LETGGGIFRALPLLgeQPF----LLLNGDV 108
Cdd:PRK14355  79 LGTGHAVACAAPAL--DGFsgtvLILCGDV 106
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
3-108 1.66e-05

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: 43.34  E-value: 1.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177    3 AMILAAGRGERMRpttlhTPKPLIEAAGVPLIERQLLALRQAGvDDWVINHAWlgEQIEAYLgdgSRLGGRIAYSPEGEP 82
Cdd:pfam12804   1 AVILAGGRSSRMG-----GDKALLPLGGKPLLERVLERLRPAG-DEVVVVAND--EEVLAAL---AGLGVPVVPDPDPGQ 69
                          90       100
                  ....*....|....*....|....*..
gi 489190177   83 lETGGGIFRALP-LLGEQPFLLLNGDV 108
Cdd:pfam12804  70 -GPLAGLLAALRaAPGADAVLVLACDM 95
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
6-48 9.03e-05

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: 41.80  E-value: 9.03e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 489190177   6 LAAGRGERMRPTTlhtpKPLIEAAGVPLIERQLLALRQAGVDD 48
Cdd:COG2266    1 MAGGKGTRLGGGE----KPLLEICGKPMIDRVIDALEESCIDK 39
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
3-48 1.12e-04

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


Pssm-ID: 133025 [Multi-domain]  Cd Length: 186  Bit Score: 41.39  E-value: 1.12e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 489190177   3 AMILAAGRGERMrpttlHTPKPLIEAAGVPLIERQLLALRQAGVDD 48
Cdd:cd04182    3 AIILAAGRSSRM-----GGNKLLLPLDGKPLLRHALDAALAAGLSR 43
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
3-64 1.69e-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: 41.44  E-value: 1.69e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489190177   3 AMILAAGRGERMRPTTLHTPKPLIEAAGVPLIERQLLALRQAGVDDWVINHAWLGEQIEAYL 64
Cdd:cd04197    3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQIKEYI 64
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
5-51 1.77e-04

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: 41.27  E-value: 1.77e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 489190177   5 ILAAGRGERMRpttLHTPKPLIEAAGVPLIERQLLALRQAGVDDWVI 51
Cdd:COG1211    2 IPAAGSGSRMG---AGIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIV 45
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
3-63 4.19e-04

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: 40.20  E-value: 4.19e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489190177   3 AMILAAGRGERMRPTtlhTPKPLIEAAGVPLIERQLLALRQAGVDDWVI-----NHAWLGEQIEAY 63
Cdd:cd02516    3 AIILAAGSGSRMGAD---IPKQFLELGGKPVLEHTLEAFLAHPAIDEIVvvvppDDIDLAKELAKY 65
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
1-52 5.10e-04

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


Pssm-ID: 440509 [Multi-domain]  Cd Length: 188  Bit Score: 39.41  E-value: 5.10e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489190177   1 MKAMILAAGRGERMrpttlHTPKPLIEAAGVPLIERQLLALRQAgVDDWVIN 52
Cdd:COG0746    5 ITGVILAGGRSRRM-----GQDKALLPLGGRPLLERVLERLRPQ-VDEVVIV 50
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
3-139 1.02e-03

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 39.46  E-value: 1.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177   3 AMILAAGRGERMRPTtlhTPKPLIEAAGVPLIERQLLALRQAGVDDWVI---NHAwlgEQIEAYLgdgSRLGGRIAYSPE 79
Cdd:PRK14353   8 AIILAAGEGTRMKSS---LPKVLHPVAGRPMLAHVLAAAASLGPSRVAVvvgPGA---EAVAAAA---AKIAPDAEIFVQ 78
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489190177  80 GEPLETGGGIFRALPLL--GEQPFLLLNGDV----WSDFDYSRLHLADGdlAHLVLVDNPAHHPAG 139
Cdd:PRK14353  79 KERLGTAHAVLAAREALagGYGDVLVLYGDTplitAETLARLRERLADG--ADVVVLGFRAADPTG 142
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
1-107 1.16e-03

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 39.58  E-value: 1.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177   1 MKAMILAAGRGERMRPTTlhtPKPLIEAAGVPLIERQLLALRQAGVDDWVINHAWLGEQIEAYLGdgsrlGGRIAYSPEG 80
Cdd:PRK14358   8 LDVVILAAGQGTRMKSAL---PKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGAEQVEAALQ-----GSGVAFARQE 79
                         90       100
                 ....*....|....*....|....*....
gi 489190177  81 EPLETGGGIFRALPLLGEQ--PFLLLNGD 107
Cdd:PRK14358  80 QQLGTGDAFLSGASALTEGdaDILVLYGD 108
ispD TIGR00453
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ...
3-51 1.73e-03

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: 38.42  E-value: 1.73e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 489190177    3 AMILAAGRGERMRPTtlhTPKPLIEAAGVPLIERQLLALRQAGVDDWVI 51
Cdd:TIGR00453   2 AVIPAAGRGTRFGSG---VPKQYLELGGRPLLEHALDAFLAHPAIDEVV 47
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
1-111 2.24e-03

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 38.33  E-value: 2.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177   1 MKAMILAAGRGERMRPTTLHTPKPLIEAAGVPLIERQLLALRQAGVDDWVI----------NHAWLGEQIEAYLGDGSRL 70
Cdd:PRK10122   4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLvthasknaveNHFDTSYELESLLEQRVKR 83
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489190177  71 ------------GGRIAYSPEGEPLETGGGIFRALPLLGEQPFLLLNGDVWSD 111
Cdd:PRK10122  84 qllaevqsicppGVTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPDVVID 136
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
1-51 3.02e-03

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: 37.17  E-value: 3.02e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489190177   1 MKAMILAAGRGERMrpttlHTPKPLIEAAGVPLIERQLLALRQAGVDDWVI 51
Cdd:cd02503    1 ITGVILAGGKSRRM-----GGDKALLELGGKPLLEHVLERLKPLVDEVVIS 46
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
5-108 4.81e-03

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 37.60  E-value: 4.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190177   5 ILAAGRGERMRpTTLhtPKPLIEAAGVPLIERQLLALRQAGVDDWVINHAWLGEQIEAYLGDGSRLggriAYSPEGEPLE 84
Cdd:PRK14360   6 ILAAGKGTRMK-SSL--PKVLHPLGGKSLVERVLDSCEELKPDRRLVIVGHQAEEVEQSLAHLPGL----EFVEQQPQLG 78
                         90       100
                 ....*....|....*....|....*.
gi 489190177  85 TGGGIFRALPLLG--EQPFLLLNGDV 108
Cdd:PRK14360  79 TGHAVQQLLPVLKgfEGDLLVLNGDV 104
mobA PRK00317
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
1-52 7.71e-03

molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed


Pssm-ID: 234725 [Multi-domain]  Cd Length: 193  Bit Score: 36.32  E-value: 7.71e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489190177   1 MKAMILAAGRGERMRpttlHTPKPLIEAAGVPLIERQLLALR-QagVDDWVIN 52
Cdd:PRK00317   4 ITGVILAGGRSRRMG----GVDKGLQELNGKPLIQHVIERLApQ--VDEIVIN 50
 
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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