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Conserved domains on  [gi|446598830|ref|WP_000676176|]
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MULTISPECIES: sugar phosphate nucleotidyltransferase [Bacillus]

Protein Classification

glycosyltransferase family protein( domain architecture ID 27718)

glycosyltransferase family protein may synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Glyco_tranf_GTA_type super family cl11394
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 1-236 7.74e-132

Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold; Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases 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. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.


The actual alignment was detected with superfamily member cd02538:

Pssm-ID: 472172 [Multi-domain]  Cd Length: 240  Bit Score: 371.52  E-value: 7.74e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830   1 MKGIILAGGTGSRLYPITKVTNKHLLPVGRYPMIYHAVYKLKQCEITDIMIITGKEHMGDVVSFLGSGQEFGVSFTYRVQ 80
Cdd:cd02538    1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830  81 DKAGGIAQALGLCEDFVGNDRMVVILGDNIFSD-DIRPYVEEFTNQKEGAKVLLQSVDDPERFGVANI-QNRKIIEIEEK 158
Cdd:cd02538   81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGqGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFdENGRVLSIEEK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830 159 PKEPKSSYAVTGIYLYDSKVFSYIKELKPSARGELEITDINNWYLKRGVLTYNEMS--GWWTDAGTHVSLQRANALARDI 236
Cdd:cd02538  161 PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGrgFAWLDTGTHESLLEASNFVQTI 240
 
Name Accession Description Interval E-value
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 1-236 7.74e-132

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: 371.52  E-value: 7.74e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830   1 MKGIILAGGTGSRLYPITKVTNKHLLPVGRYPMIYHAVYKLKQCEITDIMIITGKEHMGDVVSFLGSGQEFGVSFTYRVQ 80
Cdd:cd02538    1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830  81 DKAGGIAQALGLCEDFVGNDRMVVILGDNIFSD-DIRPYVEEFTNQKEGAKVLLQSVDDPERFGVANI-QNRKIIEIEEK 158
Cdd:cd02538   81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGqGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFdENGRVLSIEEK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830 159 PKEPKSSYAVTGIYLYDSKVFSYIKELKPSARGELEITDINNWYLKRGVLTYNEMS--GWWTDAGTHVSLQRANALARDI 236
Cdd:cd02538  161 PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGrgFAWLDTGTHESLLEASNFVQTI 240
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-236 1.77e-109

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 317.03  E-value: 1.77e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830   1 MKGIILAGGTGSRLYPITKVTNKHLLPVGRYPMIYHAVYKLKQCEITDIMIITGKEHMGDVVSFLGSGQEFGVSFTYRVQ 80
Cdd:COG1209    1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830  81 DKAGGIAQALGLCEDFVGNDRMVVILGDNIF-SDDIRPYVEEFTNQKEGAKVLLQSVDDPERFGVANI-QNRKIIEIEEK 158
Cdd:COG1209   81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFyGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFdEDGRVVSLEEK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830 159 PKEPKSSYAVTGIYLYDSKVFSYIKELKPSARGELEITDINNWYLKRGVLTYNEM--SGWWTDAGTHVSLQRANALARDI 236
Cdd:COG1209  161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLgrGFAWLDTGTHESLLEANRFVLTI 240
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
 2-236 1.61e-83

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


Pssm-ID: 130274 [Multi-domain]  Cd Length: 286  Bit Score: 250.77  E-value: 1.61e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830    2 KGIILAGGTGSRLYPITKVTNKHLLPVGRYPMIYHAVYKLKQCEITDIMIITGKEHMGDVVSFLGSGQEFGVSFTYRVQD 81
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830   82 KAGGIAQALGLCEDFVGNDRMVVILGDNIF-SDDIRPYVEEFTNQKEGAKVLLQSVDDPERFGVANI-QNRKIIEIEEKP 159
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFyGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFdSNGRAISIEEKP 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446598830  160 KEPKSSYAVTGIYLYDSKVFSYIKELKPSARGELEITDINNWYLKRGVLTYNEMS-GW-WTDAGTHVSLQRANALARDI 236
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGrGYaWLDTGTHDSLLEASNFIQTI 239
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 2-230 4.93e-66

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 206.45  E-value: 4.93e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830   2 KGIILAGGTGSRLYPITKVTNKHLLPVGRYPMIYHAVYKLKQCEITDIMIITGKEHMGDVVSFLGSGQEFGVSFTYRVQD 81
Cdd:PRK15480   5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830  82 KAGGIAQALGLCEDFVGNDRMVVILGDNIF-SDDIRPYVEEFTNQKEGAKVLLQSVDDPERFGVANI-QNRKIIEIEEKP 159
Cdd:PRK15480  85 SPDGLAQAFIIGEEFIGGDDCALVLGDNIFyGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFdQNGTAISLEEKP 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446598830 160 KEPKSSYAVTGIYLYDSKVFSYIKELKPSARGELEITDINNWYLKRGVLTYNEMS-GW-WTDAGTHVSLQRAN 230
Cdd:PRK15480 165 LQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGrGYaWLDTGTHQSLIEAS 237
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-231 7.78e-61

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: 191.31  E-value: 7.78e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830    2 KGIILAGGTGSRLYPITKVTNKHLLPVG-RYPMIYHAVYKLKQCEITDIMIITGKEHMGDVVSFLGSGQEFGVSFTYRVQ 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGgKYPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830   81 DKAGGIAQALGLCEDFVGND--RMVVILGDNIFSDDIRPYVEEF--TNQKEGAKVLLQSVDDPERFGVANI-QNRKIIEI 155
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEksDVLVLGGDHIYRMDLEQAVKFHieKAADATVTFGIVPVEPPTGYGVVEFdDNGRVIRF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830  156 EEKPKEPK-SSYAVTGIYLYDSKVFSYI-KELKPSARGELEITDINNWYLKRGVLTYN-EMSGW-WTDAGTHVSLQRANA 231
Cdd:pfam00483 161 VEKPKLPKaSNYASMGIYIFNSGVLDFLaKYLEELKRGEDEITDILPKALEDGKLAYAfIFKGYaWLDVGTWDSLWEANL 240
 
Name Accession Description Interval E-value
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 1-236 7.74e-132

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: 371.52  E-value: 7.74e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830   1 MKGIILAGGTGSRLYPITKVTNKHLLPVGRYPMIYHAVYKLKQCEITDIMIITGKEHMGDVVSFLGSGQEFGVSFTYRVQ 80
Cdd:cd02538    1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830  81 DKAGGIAQALGLCEDFVGNDRMVVILGDNIFSD-DIRPYVEEFTNQKEGAKVLLQSVDDPERFGVANI-QNRKIIEIEEK 158
Cdd:cd02538   81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGqGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFdENGRVLSIEEK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830 159 PKEPKSSYAVTGIYLYDSKVFSYIKELKPSARGELEITDINNWYLKRGVLTYNEMS--GWWTDAGTHVSLQRANALARDI 236
Cdd:cd02538  161 PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGrgFAWLDTGTHESLLEASNFVQTI 240
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-236 1.77e-109

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 317.03  E-value: 1.77e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830   1 MKGIILAGGTGSRLYPITKVTNKHLLPVGRYPMIYHAVYKLKQCEITDIMIITGKEHMGDVVSFLGSGQEFGVSFTYRVQ 80
Cdd:COG1209    1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830  81 DKAGGIAQALGLCEDFVGNDRMVVILGDNIF-SDDIRPYVEEFTNQKEGAKVLLQSVDDPERFGVANI-QNRKIIEIEEK 158
Cdd:COG1209   81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFyGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFdEDGRVVSLEEK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830 159 PKEPKSSYAVTGIYLYDSKVFSYIKELKPSARGELEITDINNWYLKRGVLTYNEM--SGWWTDAGTHVSLQRANALARDI 236
Cdd:COG1209  161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLgrGFAWLDTGTHESLLEANRFVLTI 240
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 1-232 3.54e-90

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: 265.97  E-value: 3.54e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830   1 MKGIILAGGTGSRLYPITKVTNKHLLPVGRYPMIYHAVYKLKQCEITDIMIITGkEHMGDVVSFLGSGQEFGVSFTYRVQ 80
Cdd:cd04189    1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVG-PTGEEIKEALGDGSRFGVRITYILQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830  81 DKAGGIAQALGLCEDFVGNDRMVVILGDNIFSDDIRPYVEEFTNQKEGAKVLLQSVDDPERFGVANIQNRKIIEIEEKPK 160
Cdd:cd04189   80 EEPLGLAHAVLAARDFLGDEPFVVYLGDNLIQEGISPLVRDFLEEDADASILLAEVEDPRRFGVAVVDDGRIVRLVEKPK 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446598830 161 EPKSSYAVTGIYLYDSKVFSYIKELKPSARGELEITDINNWYLKRG--VLtYNEMSGWWTDAGTHVSLQRANAL 232
Cdd:cd04189  160 EPPSNLALVGVYAFTPAIFDAISRLKPSWRGELEITDAIQWLIDRGrrVG-YSIVTGWWKDTGTPEDLLEANRL 232
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
 2-236 1.61e-83

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


Pssm-ID: 130274 [Multi-domain]  Cd Length: 286  Bit Score: 250.77  E-value: 1.61e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830    2 KGIILAGGTGSRLYPITKVTNKHLLPVGRYPMIYHAVYKLKQCEITDIMIITGKEHMGDVVSFLGSGQEFGVSFTYRVQD 81
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830   82 KAGGIAQALGLCEDFVGNDRMVVILGDNIF-SDDIRPYVEEFTNQKEGAKVLLQSVDDPERFGVANI-QNRKIIEIEEKP 159
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFyGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFdSNGRAISIEEKP 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446598830  160 KEPKSSYAVTGIYLYDSKVFSYIKELKPSARGELEITDINNWYLKRGVLTYNEMS-GW-WTDAGTHVSLQRANALARDI 236
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGrGYaWLDTGTHDSLLEASNFIQTI 239
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
 2-235 1.50e-70

glucose-1-phosphate thymidylylransferase, long form; The family of known and putative glucose-1-phosphate thymidyltransferase (also called dTDP-glucose synthase) shows a deep split into a short form (see TIGR01207) and a long form described by this model. The homotetrameric short form is found in numerous bacterial species that incorporate dTDP-L-rhamnose, which it helps synthesize, into the cell wall. It is subject to feedback inhibition. This form, in contrast, 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. Alternate name: dTDP-D-glucose synthase


Pssm-ID: 273500 [Multi-domain]  Cd Length: 353  Bit Score: 219.97  E-value: 1.50e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830    2 KGIILAGGTGSRLYPITKVTNKHLLPVGRYPMIYHAVYKLKQCEITDIMIITGKEHMGDVVSFLGSGQEFGVSFTYRVQD 81
Cdd:TIGR01208   1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIGIVVGPVTGEEIKEIVGEGERFGAKITYIVQG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830   82 KAGGIAQALGLCEDFVGNDRMVVILGDNIFSDDIRPYVEEFTNQKEGAKVLLQSVDDPERFGVANIQN-RKIIEIEEKPK 160
Cdd:TIGR01208  81 EPLGLAHAVYTARDFLGDDDFVVYLGDNLIQDGISRFVKSFEEKDYDALILLTKVRDPTAFGVAVLEDgKRILKLVEKPK 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446598830  161 EPKSSYAVTGIYLYDSKVFSYIKELKPSARGELEITDINNWYLKRGV-LTYNEMSGWWTDAGTHVSLQRANALARD 235
Cdd:TIGR01208 161 EPPSNLAVVGLYMFRPLIFEAIKNIKPSWRGELEITDAIQWLIEKGYkVGGSKVTGWWKDTGKPEDLLDANRLILD 236
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 2-230 4.93e-66

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 206.45  E-value: 4.93e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830   2 KGIILAGGTGSRLYPITKVTNKHLLPVGRYPMIYHAVYKLKQCEITDIMIITGKEHMGDVVSFLGSGQEFGVSFTYRVQD 81
Cdd:PRK15480   5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830  82 KAGGIAQALGLCEDFVGNDRMVVILGDNIF-SDDIRPYVEEFTNQKEGAKVLLQSVDDPERFGVANI-QNRKIIEIEEKP 159
Cdd:PRK15480  85 SPDGLAQAFIIGEEFIGGDDCALVLGDNIFyGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFdQNGTAISLEEKP 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446598830 160 KEPKSSYAVTGIYLYDSKVFSYIKELKPSARGELEITDINNWYLKRGVLTYNEMS-GW-WTDAGTHVSLQRAN 230
Cdd:PRK15480 165 LQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGrGYaWLDTGTHQSLIEAS 237
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 3-221 5.92e-65

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: 200.88  E-value: 5.92e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830   3 GIILAGGTGSRLYPITKVTNKHLLPVGRYPMIYHAVYKLKQCEITDIMIITGkeHMGDVV-SFLGSGQEFGVSFTYRVQD 81
Cdd:cd04181    1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVG--YLGEQIeEYFGDGSKFGVNIEYVVQE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830  82 KAGGIAQALGLCEDFVGNDRMVVILGDNIFSDDIRPYVEEFTNQKEGAKVLLQSVDDPERFGVANI-QNRKIIEIEEKPK 160
Cdd:cd04181   79 EPLGTAGAVRNAEDFLGDDDFLVVNGDVLTDLDLSELLRFHREKGADATIAVKEVEDPSRYGVVELdDDGRVTRFVEKPT 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446598830 161 EPKSSYAVTGIYLYDSKVFSYIKELKPsaRGELEITDINNWYLKRGVLTYNEMSGWWTDAG 221
Cdd:cd04181  159 LPESNLANAGIYIFEPEILDYIPEILP--RGEDELTDAIPLLIEEGKVYGYPVDGYWLDIG 217
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-231 7.78e-61

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: 191.31  E-value: 7.78e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830    2 KGIILAGGTGSRLYPITKVTNKHLLPVG-RYPMIYHAVYKLKQCEITDIMIITGKEHMGDVVSFLGSGQEFGVSFTYRVQ 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGgKYPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830   81 DKAGGIAQALGLCEDFVGND--RMVVILGDNIFSDDIRPYVEEF--TNQKEGAKVLLQSVDDPERFGVANI-QNRKIIEI 155
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEksDVLVLGGDHIYRMDLEQAVKFHieKAADATVTFGIVPVEPPTGYGVVEFdDNGRVIRF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830  156 EEKPKEPK-SSYAVTGIYLYDSKVFSYI-KELKPSARGELEITDINNWYLKRGVLTYN-EMSGW-WTDAGTHVSLQRANA 231
Cdd:pfam00483 161 VEKPKLPKaSNYASMGIYIFNSGVLDFLaKYLEELKRGEDEITDILPKALEDGKLAYAfIFKGYaWLDVGTWDSLWEANL 240
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 1-221 9.32e-56

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: 182.79  E-value: 9.32e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830    1 MKGIILAGGTGSRLYPITKVTNKHLLPVGRYPMIYHAVYKLKQCEITDIMIITG--KEHmgdVVSFLGSGQEFGVSFTYR 78
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGygKEK---VREYFGDGSRGGVPIEYV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830   79 VQDKAGGIAQALGLCEDFVgNDRMVVILGDNIF-SDDIRPYVEEftnqkEGAKVLLQSVDDPERFGVANIQNRKIIEIEE 157
Cdd:TIGR03992  78 VQEEQLGTADALGSAKEYV-DDEFLVLNGDVLLdSDLLERLIRA-----EAPAIAVVEVDDPSDYGVVETDGGRVTGIVE 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446598830  158 KPKEPKSSYAVTGIYLYDSKVFSYIKELKPSARGELEITDINNWYLKRGVLTYNEMSGWWTDAG 221
Cdd:TIGR03992 152 KPENPPSNLINAGIYLFSPEIFELLEKTKLSPRGEYELTDALQLLIDEGKVKAVELDGFWLDVG 215
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 2-235 1.41e-55

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: 177.65  E-value: 1.41e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830   2 KGIILAGGTGSRLYPITKVTNKHLLPVGRYPMIYHAVYKLKQCEITDIMIITGkeHMGDVV-SFLGSGQEFGVSFTYRVQ 80
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVG--YLAEQIeEYFGDGSRFGVRITYVDE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830  81 DKAGGIAQALGLCEDFVGNDRMVVILGDNIFSDDIRPYVEEFTNQKEGAKVLLQSVDDPERFGVANIQNR-KIIEIEEKP 159
Cdd:COG1208   79 GEPLGTGGALKRALPLLGDEPFLVLNGDILTDLDLAALLAFHREKGADATLALVPVPDPSRYGVVELDGDgRVTRFVEKP 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446598830 160 KEPKSSYAVTGIYLYDSKVFSYIKElkpsaRGELEITDINNWYLKRGVLTYNEMSGWWTDAGTHVSLQRANALARD 235
Cdd:COG1208  159 EEPPSNLINAGIYVLEPEIFDYIPE-----GEPFDLEDLLPRLIAEGRVYGYVHDGYWLDIGTPEDLLEANALLLS 229
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 1-241 7.00e-32

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: 117.63  E-value: 7.00e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830   1 MKGIILAGGTGSRLYPITKVTNKHLLPVGRYPMIYHAVYKLKQCEITDIMIIT------------------------GKE 56
Cdd:cd02541    1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTgrgkraiedhfdrsyeleetlekkGKT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830  57 HMGDVVSFLGSGqefgVSFTYRVQDKAGGIAQALGLCEDFVGNDRMVVILGDNIFSDD---IRPYVEEFtNQKEGAKVLL 133
Cdd:cd02541   81 DLLEEVRIISDL----ANIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLIDSKepcLKQLIEAY-EKTGASVIAV 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830 134 QSVDDPE--RFGVANI-----QNRKIIEIEEKPK--EPKSSYAVTGIYLYDSKVFSYIKELKPSARGELEITD-INNWYL 203
Cdd:cd02541  156 EEVPPEDvsKYGIVKGekidgDVFKVKGLVEKPKpeEAPSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTDaIAKLLE 235

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 446598830 204 KRGVLTYNeMSGWWTDAGTHVSLQRANalardINFGKQ 241
Cdd:cd02541  236 EEPVYAYV-FEGKRYDCGNKLGYLKAT-----VEFALK 267
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 4-230 5.18e-26

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: 101.05  E-value: 5.18e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830   4 IILAGGTGSRLYPITKVTNKHLLPVGRYPMIYHAVYKLKQCEITDIMIITGkeHMGDVV-SFLGSGQEFGVSFTYRVQDK 82
Cdd:cd06426    2 VIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVN--YLAEMIeDYFGDGSKFGVNISYVREDK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830  83 AGGIAQALGLCEDFVgNDRMVVILGDNIFSDDIRPYVEEFTNQKEGAK--VLLQSVDDPerFGVANIQNRKIIEIEEKPK 160
Cdd:cd06426   80 PLGTAGALSLLPEKP-TDPFLVMNGDILTNLNYEHLLDFHKENNADATvcVREYEVQVP--YGVVETEGGRITSIEEKPT 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446598830 161 EpkSSYAVTGIYLYDSKVFSYIKElkpsarGE-LEITDINNWYLKRG--VLTYNeMSGWWTDAGTHVSLQRAN 230
Cdd:cd06426  157 H--SFLVNAGIYVLEPEVLDLIPK------NEfFDMPDLIEKLIKEGkkVGVFP-IHEYWLDIGRPEDYEKAN 220
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 2-229 4.21e-24

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: 95.72  E-value: 4.21e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830   2 KGIILAGGTGSRLYPITKVTNKHLLPVGRYPMIYHAVYKLKQCEITDIMIITGkeHMGD-VVSFLGSgQEFGVSFTYR-- 78
Cdd:cd06422    1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTH--HLADqIEAHLGD-SRFGLRITISde 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830  79 ---VQDKAGGIAQALglceDFVGNDRMVVILGDNIFSDDIRPYVEEFTNQKEGAKVLLQSVDDPERFGVANIQNRKIIEI 155
Cdd:cd06422   78 pdeLLETGGGIKKAL----PLLGDEPFLVVNGDILWDGDLAPLLLLHAWRMDALLLLLPLVRNPGHNGVGDFSLDADGRL 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446598830 156 EEKPKEPKSSYAVTGIYLYDSKVFSYIKElkpsarGELEITDINNWYLKRGVLTYNEMSGWWTDAGTHVSLQRA 229
Cdd:cd06422  154 RRGGGGAVAPFTFTGIQILSPELFAGIPP------GKFSLNPLWDRAIAAGRLFGLVYDGLWFDVGTPERLLAA 221
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 4-229 1.45e-22

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: 91.85  E-value: 1.45e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830   4 IILAGGTGSRLYPITKVTNKHLLPVGRYPMIYHAVYKLKQCEITDIMIITGkeHMGD-VVSFLGSGQEFGVSFTYRVQDK 82
Cdd:cd06915    2 VILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVG--YLAEqIEEYFGDGYRGGIRIYYVIEPE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830  83 ----AGGIAQALGLCEDfvgnDRMVVILGDNIFSDDIRPYVEEFTNQKEGAKVLLQSVDDPERFGVANIQN-RKIIEIEE 157
Cdd:cd06915   80 plgtGGAIKNALPKLPE----DQFLVLNGDTYFDVDLLALLAALRASGADATMALRRVPDASRYGNVTVDGdGRVIAFVE 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446598830 158 KPKEPKSSYAVTGIYLYDSKVFSYIKELKPSargeLEiTDINNWYLKRGVLTYNEMSGWWTDAGTHVSLQRA 229
Cdd:cd06915  156 KGPGAAPGLINGGVYLLRKEILAEIPADAFS----LE-ADVLPALVKRGRLYGFEVDGYFIDIGIPEDYARA 222
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
2-242 7.39e-22

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


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 91.25  E-value: 7.39e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830   2 KGIILAGGTGSRLYPITKVTNKHLLPVGRYPMIYHAVYKLKQCEITDIMIIT------------------------GKEH 57
Cdd:COG1210    5 KAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVTgrgkraiedhfdrsyeleatleakGKEE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830  58 MGDVVSFLGSGqefgVSFTYRVQDKAGGiaqaLG---LC-EDFVGNDRMVVILGDNIFSDD---IRPYVEEFtnQKEGAK 130
Cdd:COG1210   85 LLEEVRSISPL----ANIHYVRQKEPLG----LGhavLCaRPFVGDEPFAVLLGDDLIDSEkpcLKQMIEVY--EETGGS 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830 131 VL-LQSVDDPE--RFGVANIQNR-----KIIEIEEKPK--EPKSSYAVTGIYLYDSKVFSYIKELKPSARGELEITD-IN 199
Cdd:COG1210  155 VIaVQEVPPEEvsKYGIVDGEEIeggvyRVTGLVEKPApeEAPSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDaIA 234

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 446598830 200 NWYLKRGVLTYnEMSGWWTDAGTHVSLQRAN---ALARDiNFGKQF 242
Cdd:COG1210  235 ALAKEEPVYAY-EFEGKRYDCGDKLGYLKATvefALKRP-DLGEEF 278
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 1-222 2.72e-21

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


Pssm-ID: 133047 [Multi-domain]  Cd Length: 233  Bit Score: 88.81  E-value: 2.72e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830   1 MKGIILAGGTGSRLYPITKVTNKHLLPVGRYPMIYHAVYKLKQCEITDIMIITGKEHmGDVVSFLGS-GQEFGVSFTYRV 79
Cdd:cd06425    1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYRP-EDMVPFLKEyEKKLGIKITFSI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830  80 QDKAGGIAQALGLCEDFVG--NDRMVVILGDNIFSDDIRPYVEEFTNQKEGAKVLLQSVDDPERFGV--ANIQNRKIIEI 155
Cdd:cd06425   80 ETEPLGTAGPLALARDLLGddDEPFFVLNSDVICDFPLAELLDFHKKHGAEGTILVTKVEDPSKYGVvvHDENTGRIERF 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446598830 156 EEKPKEPKSSYAVTGIYLYDSKVFSYIkELKPSargELEiTDINNWYLKRGVLTYNEMSGWWTDAGT 222
Cdd:cd06425  160 VEKPKVFVGNKINAGIYILNPSVLDRI-PLRPT---SIE-KEIFPKMASEGQLYAYELPGFWMDIGQ 221
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 4-198 6.45e-19

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: 82.28  E-value: 6.45e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830   4 IILAGGTGSRLYPITKVTNKHLLPVGRYPMIYHAVYKLKQCEITDIMIITGkeHMGDVVSFLGSgQEFGVSFTYRVQDKA 83
Cdd:cd02523    2 IILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTG--YKKEQIEELLK-KYPNIKFVYNPDYAE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830  84 GGIAQALGLCEDFVGNDrMVVILGDNIFSDDIrpyVEEFTNQKEGAKVLLQSVDDPE--RFGVANIQNRKIIEIEEKPKE 161
Cdd:cd02523   79 TNNIYSLYLARDFLDED-FLLLEGDVVFDPSI---LERLLSSPADNAILVDKKTKEWedEYVKDLDDAGVLLGIISKAKN 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 446598830 162 PKSSYAVT-GIYLYD----SKVFSYIKELKPSARGELEITDI 198
Cdd:cd02523  155 LEEIQGEYvGISKFSpedaDRLAEALEELIEAGRVNLYYEDA 196
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 4-198 9.97e-16

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: 73.70  E-value: 9.97e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830   4 IILAGGTGSRLY-PITKVtnkhLLPVGRYPMIYHAVYKLKQCEITDIMIITGkeHMGDVVsfLGSGQEFGVSFTYrvQDK 82
Cdd:cd02540    2 VILAAGKGTRMKsDLPKV----LHPLAGKPMLEHVLDAARALGPDRIVVVVG--HGAEQV--KKALANPNVEFVL--QEE 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830  83 ----AGGIAQALGLCEDFvgNDRMVVILGDN--IFSDDIRPYVEEFTNQKEGAKVLLQSVDDPERFG--VANiQNRKIIE 154
Cdd:cd02540   72 qlgtGHAVKQALPALKDF--EGDVLVLYGDVplITPETLQRLLEAHREAGADVTVLTAELEDPTGYGriIRD-GNGKVLR 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 446598830 155 I-EEK---PKEPKSSYAVTGIYLYDSKV-FSYIKELKPS-ARGELEITDI 198
Cdd:cd02540  149 IvEEKdatEEEKAIREVNAGIYAFDAEFlFEALPKLTNNnAQGEYYLTDI 198
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 3-222 1.04e-14

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 72.42  E-value: 1.04e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830   3 GIILAGGTGSRLYPITKVTNKHLLPV-GRYPMI-------YHAvyklkqcEITDIMIITGK------EHmgdvvsfLGSG 68
Cdd:COG0448    4 AIILAGGRGSRLGPLTKDRAKPAVPFgGKYRIIdfplsncVNS-------GIRRVGVLTQYkshslnDH-------IGSG 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830  69 QEFGVS--------FTYRVQDKAGG--------IAQALGLCEDFvgNDRMVVIL-GDNIFSDDIRPYVEEFtnQKEGAKV 131
Cdd:COG0448   70 KPWDLDrkrggvfiLPPYQQREGEDwyqgtadaVYQNLDFIERS--DPDYVLILsGDHIYKMDYRQMLDFH--IESGADI 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830 132 LL----QSVDDPERFGVANI-QNRKIIEIEEKPKEPKSSYAVTGIYLYDSKVFsyIKELKPSARGELE--ITDINNWYLK 204
Cdd:COG0448  146 TVacieVPREEASRFGVMEVdEDGRITEFEEKPKDPKSALASMGIYVFNKDVL--IELLEEDAPNSSHdfGKDIIPRLLD 223

                        250
                 ....*....|....*....
gi 446598830 205 RG-VLTYnEMSGWWTDAGT 222
Cdd:COG0448  224 RGkVYAY-EFDGYWRDVGT 241
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 1-58 1.41e-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: 61.91  E-value: 1.41e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446598830   1 MKGIILAGGTGSRLYPITKVTNKHLLPVGRYPMIYHAVYKLKQCEITDIMIITGKEHM 58
Cdd:cd04198    1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEEQ 58
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 3-200 2.89e-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: 61.50  E-value: 2.89e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830   3 GIILAGG--TGSRLYPITKVTNKHLLPVGRYPMIYHAVYKLKQC-EITDIMIITGKEHMgDVVSFLGSG-QEFGVSFTYR 78
Cdd:cd06428    1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKVpDLKEVLLIGFYPES-VFSDFISDAqQEFNVPIRYL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830  79 VQDKAGGIAQALGLCED--FVGNDRMVVILGDNIFSDdiRPYVEEFTNQKE-GAKVLLQSV----DDPERFG--VANIQN 149
Cdd:cd06428   80 QEYKPLGTAGGLYHFRDqiLAGNPSAFFVLNADVCCD--FPLQELLEFHKKhGASGTILGTeasrEQASNYGciVEDPST 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446598830 150 RKIIEIEEKPKEPKSSYAVTGIYLYDSKVFSYIKELKPSARGELEITDINN 200
Cdd:cd06428  158 GEVLHYVEKPETFVSDLINCGVYLFSPEIFDTIKKAFQSRQQEAQLGDDNN 208
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
2-234 1.67e-10

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 59.10  E-value: 1.67e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830   2 KGIILAGGTGSRLYPITKVTNKHLLPVGRYPMIYHAVYKLKQCEITDIMIITGkeHMGDVVSFLGSGQEFGVSFTY-RVQ 80
Cdd:COG1213    1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTG--YKAELIEEALARPGPDVTFVYnPDY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830  81 DKAGGIAqALGLCEDFVGNDrmVVIL-GDNIFSDDIrpyVEEFtNQKEGAKVLL------QSVDDPERFgVANIQNRkII 153
Cdd:COG1213   79 DETNNIY-SLWLAREALDED--FLLLnGDVVFDPAI---LKRL-LASDGDIVLLvdrkweKPLDEEVKV-RVDEDGR-IV 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830 154 EIEEKPKEPKSSYAVTGIYLY---DSKVF-SYIKELKPSARGELEITDINNWYLKRGV-LTYNEMSG-WWTDAGTHVSLQ 227
Cdd:COG1213  150 EIGKKLPPEEADGEYIGIFKFsaeGAAALrEALEALIDEGGPNLYYEDALQELIDEGGpVKAVDIGGlPWVEIDTPEDLE 229


                 ....*..
gi 446598830 228 RANALAR 234
Cdd:COG1213  230 RAEELFA 236
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
2-197 2.61e-10

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 59.15  E-value: 2.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830   2 KGIILAGGTGSRLYPITKVTNKHLLPVGRYPMIYHAVYKLKQCEITDIMIITgKEHMGDVVSFLGSGQEFGVSFTYRVQD 81
Cdd:PRK13389  10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVT-HSSKNSIENHFDTSFELEAMLEKRVKR 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830  82 K------------------AGGIAQALG---LC-EDFVGNDRMVVILGDNIF--------SDDIRPYVEEFtNQKEGAKV 131
Cdd:PRK13389  89 QlldevqsicpphvtimqvRQGLAKGLGhavLCaHPVVGDEPVAVILPDVILdeyesdlsQDNLAEMIRRF-DETGHSQI 167

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446598830 132 LLQSVDDPERFGVANIQNRKI--------IEIEEKPK--EPKSSYAVTGIYLYDSKVFSYIKELKPSARGELEITD 197
Cdd:PRK13389 168 MVEPVADVTAYGVVDCKGVELapgesvpmVGVVEKPKadVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTD 243
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 4-198 4.31e-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: 58.88  E-value: 4.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830   4 IILAGGTGSRLY---PitKVtnkhLLPVGRYPMIYHAVYKLKQCEITDIMIITGkeHMGDVV-SFLGsgqEFGVSFTyrV 79
Cdd:COG1207    6 VILAAGKGTRMKsklP--KV----LHPLAGKPMLEHVLDAARALGPDRIVVVVG--HGAEQVrAALA---DLDVEFV--L 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830  80 QDKAGG----IAQALGLCEDFVGNdrmVVIL-GDN--IFSDDIRPYVEEFTNQKEGAKVLLQSVDDPERFG--VANIQNR 150
Cdd:COG1207   73 QEEQLGtghaVQQALPALPGDDGT---VLVLyGDVplIRAETLKALLAAHRAAGAAATVLTAELDDPTGYGriVRDEDGR 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446598830 151 --KIIE-----IEEKpkepkssyAV----TGIYLYDSKV-FSYIKELKPS-ARGELEITDI 198
Cdd:COG1207  150 vlRIVEekdatEEQR--------AIreinTGIYAFDAAAlREALPKLSNDnAQGEYYLTDV 202
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 1-230 8.20e-09

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 55.26  E-value: 8.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830   1 MKGIILAGGTGSRLYPITKVTNKHLLPVG-RYPMIYHAvykLKQCE---ITDIMIITGKE------HMGDVVSFLGSGQE 70
Cdd:PRK05293   4 MLAMILAGGQGTRLGKLTKNIAKPAVPFGgKYRIIDFT---LSNCAnsgIDTVGVLTQYQplelnnHIGIGSPWDLDRIN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830  71 FGVSFTYRVQDKAGG---------IAQALGLCEDFvgNDRMVVIL-GDNIFSDDirpYVE--EFTNQKeGAKVLLQSVDD 138
Cdd:PRK05293  81 GGVTILPPYSESEGGkwykgtahaIYQNIDYIDQY--DPEYVLILsGDHIYKMD---YDKmlDYHKEK-EADVTIAVIEV 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830 139 P----ERFGVANI-QNRKIIEIEEKPKEPKSSYAVTGIYLYDskvFSYIKE-LKPSARGELEITD-----INNwYLKRG- 206
Cdd:PRK05293 155 PweeaSRFGIMNTdENMRIVEFEEKPKNPKSNLASMGIYIFN---WKRLKEyLIEDEKNPNSSHDfgknvIPL-YLEEGe 230

                        250       260
                 ....*....|....*....|....*
gi 446598830 207 -VLTYNeMSGWWTDAGTHVSLQRAN 230
Cdd:PRK05293 231 kLYAYP-FKGYWKDVGTIESLWEAN 254
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 1-58 1.10e-08

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: 1.10e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446598830   1 MKGIILAGGTGSRLYPITKVTNKHLLPVGRYPMIYHAVYKLKQCEITDIMIITGKEHM 58
Cdd:cd02507    1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQ 58
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-198 4.89e-08

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 52.91  E-value: 4.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830   4 IILAGGTG----SRLYpitKVtnkhLLPVGRYPMIYHAVYKLKQCEITDIMIITGKEHmGDVVSFLGSGQEFGvsftyrV 79
Cdd:PRK14354   6 IILAAGKGtrmkSKLP---KV----LHKVCGKPMVEHVVDSVKKAGIDKIVTVVGHGA-EEVKEVLGDRSEFA------L 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830  80 QDKAGGIAQALGLCEDFVGNDR--MVVILGDN--IFSDDIRPYVEEFTNQKEGAKVLLQSVDDPERFG--VANIQNR--K 151
Cdd:PRK14354  72 QEEQLGTGHAVMQAEEFLADKEgtTLVICGDTplITAETLKNLIDFHEEHKAAATILTAIAENPTGYGriIRNENGEveK 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446598830 152 IieIEEK---PKEPKSSYAVTGIYLYDSKV-FSYIKELKP-SARGELEITDI 198
Cdd:PRK14354 152 I--VEQKdatEEEKQIKEINTGTYCFDNKAlFEALKKISNdNAQGEYYLTDV 201
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 3-222 1.30e-07

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 51.75  E-value: 1.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830   3 GIILAGGTGSRLYPITKVTNKHLLPV-GRYPMIYHAVYKLKQCEITDIMIITG-K-----EHM----------GDVVS-- 63
Cdd:PRK00844   8 AIVLAGGEGKRLMPLTADRAKPAVPFgGSYRLIDFVLSNLVNSGYLRIYVLTQyKshsldRHIsqtwrlsgllGNYITpv 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830  64 ----------FLGSgqefgvsftyrvqdkAGGIAQALGLCEDFvgNDRMVVILG-DNIFSDDIRPYVEEftNQKEGAKV- 131
Cdd:PRK00844  88 paqqrlgkrwYLGS---------------ADAIYQSLNLIEDE--DPDYVVVFGaDHVYRMDPRQMVDF--HIESGAGVt 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830 132 ---LLQSVDDPERFGVanIQ---NRKIIEIEEKPKEPKS-------SYAVTGIYLYDSKVFsyIKELKPSARGELEITD- 197
Cdd:PRK00844 149 vaaIRVPREEASAFGV--IEvdpDGRIRGFLEKPADPPGlpddpdeALASMGNYVFTTDAL--VDALRRDAADEDSSHDm 224

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 446598830 198 ---INNWYLKRG-VLTY----NEMSG-------WWTDAGT 222
Cdd:PRK00844 225 ggdIIPRLVERGrAYVYdfstNEVPGaterdrgYWRDVGT 264
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-212 2.02e-06

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 48.22  E-value: 2.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830   1 MKGIILAGGTGSRL---YPitKVTNKHLlpvGRyPMIyhavyklkqceitDIMIITGKEHMGDVVSFLGSGQEFGVSFTY 77
Cdd:PRK14357   1 MRALVLAAGKGTRMkskIP--KVLHKIS---GK-PMI-------------NWVIDTAKKVAQKVGVVLGHEAELVKKLLP 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830  78 R-----VQDKAGGIAQALGLCEDFVG-NDRMVVILGDN--IFSDDIRPYVEEFTNQKEGAKVLLQSVDDPERFG--VANI 147
Cdd:PRK14357  62 EwvkifLQEEQLGTAHAVMCARDFIEpGDDLLILYGDVplISENTLKRLIEEHNRKGADVTILVADLEDPTGYGriIRDG 141

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446598830 148 QNRKIIEIEEKPKEPKSSYAV-TGIYLYDSK-VFSYIKELKP-SARGELEITDINNWYLKRGVLTYNE 212
Cdd:PRK14357 142 GKYRIVEDKDAPEEEKKIKEInTGIYVFSGDfLLEVLPKIKNeNAKGEYYLTDAVNFAEKVRVVKTED 209
CpsB COG0836
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
1-57 6.99e-06

Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440598 [Multi-domain]  Cd Length: 347  Bit Score: 46.21  E-value: 6.99e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830   1 MKGIILAGGTGSRLYPI-TKVTNKHLLP-VGRYPMIYHAVYKLKQ-CEITDIMIITGKEH 57
Cdd:COG0836    3 IYPVILAGGSGTRLWPLsRESYPKQFLPlLGEKSLLQQTVERLAGlVPPENILVVTNEEH 62
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
 1-116 1.26e-05

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


Pssm-ID: 133003 [Multi-domain]  Cd Length: 274  Bit Score: 45.26  E-value: 1.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830   1 MKGIILAGGTGSRLYPITKVTN-KHLLPV-GRYPMIYHAVYKLKQC-EITDIMIITGKEHMGDVVSFLGSGQEfgvsfTY 77
Cdd:cd02509    1 IYPVILAGGSGTRLWPLSRESYpKQFLKLfGDKSLLQQTLDRLKGLvPPDRILVVTNEEYRFLVREQLPEGLP-----EE 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446598830  78 RV------QDKAGGIAQALGLCEDFVGNDRMVV------ILGDNIFSDDIR 116
Cdd:cd02509   76 NIilepegRNTAPAIALAALYLAKRDPDAVLLVlpsdhlIEDVEAFLKAVK 126
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
 4-218 2.05e-05

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: 44.17  E-value: 2.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830   4 IILAGGTGSRL------YPitkvtnKHLLPVGRYPMIYHAVYKLKQCEITDIMIITGKEH-----MGDVVSFLGSGQEFg 72
Cdd:cd04183    2 IIPMAGLGSRFkkagytYP------KPLIEVDGKPMIEWVIESLAKIFDSRFIFICRDEHntkfhLDESLKLLAPNATV- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830  73 vsftYRVQDKAGGIAQALGLCEDFVGNDRMVVIL-GDNIFSDDIRPYVEEFTNQKEGAKVLLQSVDDPERFGVANIQNRK 151
Cdd:cd04183   75 ----VELDGETLGAACTVLLAADLIDNDDPLLIFnCDQIVESDLLAFLAAFRERDLDGGVLTFFSSHPRWSYVKLDENGR 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446598830 152 IIEIEEKpkEPKSSYAVTGIYLYDSK---VFSYIKELKPSAR--GELEITDINNWYLKRG--VLTY----NEMSGWWT 218
Cdd:cd04183  151 VIETAEK--EPISDLATAGLYYFKSGslfVEAAKKMIRKDDSvnGEFYISPLYNELILDGkkVGIYlidkDDYHSFGT 226
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-198 4.23e-05

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 43.96  E-value: 4.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830   4 IILAGGTGSRLYP-ITKVtnkhLLPVGRYPMIYHAVYKLKQCEITDIMIITGkeHMGDVVSFLGSGQEfGVSFTyrVQDK 82
Cdd:PRK14355   7 IILAAGKGTRMKSdLVKV----MHPLAGRPMVSWPVAAAREAGAGRIVLVVG--HQAEKVREHFAGDG-DVSFA--LQEE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830  83 AGGIAQALGLC-EDFVGNDRMVVIL-GDN--IFSDDIRPYVEEFTNQKEGAKVLLQSVDDPerFGVANI---QNRKIIEI 155
Cdd:PRK14355  78 QLGTGHAVACAaPALDGFSGTVLILcGDVplLRAETLQGMLAAHRATGAAVTVLTARLENP--FGYGRIvrdADGRVLRI 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 446598830 156 -EEK---PKEPKSSYAVTGIYLYDSK-VFSYIKELK-PSARGELEITDI 198
Cdd:PRK14355 156 vEEKdatPEERSIREVNSGIYCVEAAfLFDAIGRLGnDNAQGEYYLTDI 204
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 3-108 4.90e-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: 42.57  E-value: 4.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830    3 GIILAGGTGSRLYpitkvTNKHLLPVGRYPMIYHAVYKLKQCEiTDIMIITGKEHMGDVVsflgsgQEFGVSFTY-RVQD 81
Cdd:pfam12804   1 AVILAGGRSSRMG-----GDKALLPLGGKPLLERVLERLRPAG-DEVVVVANDEEVLAAL------AGLGVPVVPdPDPG 68

                          90       100
                  ....*....|....*....|....*....
gi 446598830   82 K--AGGIAQALGLCEDfvgNDRMVVILGD 108
Cdd:pfam12804  69 QgpLAGLLAALRAAPG---ADAVLVLACD 94
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
 3-53 6.50e-05

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: 42.53  E-value: 6.50e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446598830   3 GIILAGGTGSRLYPITKVTNKHLLPV-GRYPMIYHAVYKLKQCEITDIMIIT 53
Cdd:cd02508    1 AIILAGGEGTRLSPLTKKRAKPAVPFgGRYRLIDFPLSNMVNSGIRNVGVLT 52
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 1-53 8.65e-05

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: 42.10  E-value: 8.65e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446598830   1 MKGIILAGGTGSRLYpitkvTNKHLLPVGRYPMIYHAVYKLKQCeITDIMIIT 53
Cdd:COG0746    5 ITGVILAGGRSRRMG-----QDKALLPLGGRPLLERVLERLRPQ-VDEVVIVA 51
PLN02241 PLN02241
glucose-1-phosphate adenylyltransferase
 3-160 4.79e-04

glucose-1-phosphate adenylyltransferase


Pssm-ID: 215133 [Multi-domain]  Cd Length: 436  Bit Score: 40.61  E-value: 4.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830   3 GIILAGGTGSRLYPITKVTNKHLLPVGrypmiyhAVYKL-----KQC---EITDIMIITG------KEHMGDVVSFlGSG 68
Cdd:PLN02241   6 AIILGGGAGTRLFPLTKRRAKPAVPIG-------GNYRLidipmSNCinsGINKIYVLTQfnsaslNRHLSRAYNF-GNG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830  69 QEFGVSF------TYRVQDK------AGGIAQALGLCEDFVGNDRM-VVIL-GDNIFSDDIRPYVEefTNQKEGAKVLL- 133
Cdd:PLN02241  78 GNFGDGFvevlaaTQTPGEKgwfqgtADAVRQFLWLFEDAKNKNVEeVLILsGDHLYRMDYMDFVQ--KHRESGADITIa 155

                        170       180       190
                 ....*....|....*....|....*....|.
gi 446598830 134 -QSVDDPE--RFGVANIQNR-KIIEIEEKPK 160
Cdd:PLN02241 156 cLPVDESRasDFGLMKIDDTgRIIEFSEKPK 186
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 4-206 5.05e-04

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 40.73  E-value: 5.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830   4 IILAGGTGSRLypiTKVTNKHLLPVGRYPMIYHAVYKLKQCEITDIMIITGkeHMGDVVSflGSGQEFGVSFTYRVQDKA 83
Cdd:PRK14358  11 VILAAGQGTRM---KSALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTG--HGAEQVE--AALQGSGVAFARQEQQLG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830  84 GGIAQALGLCEDFVGNDRMVVILGDN--IFSDDIRPYVEEFTNQKEGAKVLLQSVDDPERFG-VANIQNRKIIEIEEKPK 160
Cdd:PRK14358  84 TGDAFLSGASALTEGDADILVLYGDTplLRPDTLRALVADHRAQGSAMTILTGELPDATGYGrIVRGADGAVERIVEQKD 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446598830 161 EPKSSYAV----TGIYLYDSKVFSYIKEL-KPSARGELEITDINNWYLKRG 206
Cdd:PRK14358 164 ATDAEKAIgefnSGVYVFDARAPELARRIgNDNKAGEYYLTDLLGLYRAGG 214
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
4-60 7.15e-04

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 39.73  E-value: 7.15e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446598830   4 IILAGGTGSRLypitKV-TNKHLLPVGRYPMIYHAVYKLKQC-EITDIMIITGKEHMGD 60
Cdd:PRK00155   7 IIPAAGKGSRM----GAdRPKQYLPLGGKPILEHTLEAFLAHpRIDEIIVVVPPDDRPD 61
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 4-58 7.39e-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: 39.73  E-value: 7.39e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446598830   4 IILAGGTGSRL-YPItkvtNKHLLPVGRYPMIYHAVYKLKQC-EITDIMIITGKEHM 58
Cdd:COG1211    1 IIPAAGSGSRMgAGI----PKQFLPLGGKPVLEHTLEAFLAHpRIDEIVVVVPPDDI 53
glgC PRK02862
glucose-1-phosphate adenylyltransferase; Provisional
 3-34 8.24e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179486 [Multi-domain]  Cd Length: 429  Bit Score: 40.25  E-value: 8.24e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 446598830   3 GIILAGGTGSRLYPITKVTNKHLLPV-GRYPMI 34
Cdd:PRK02862   6 AIILGGGAGTRLYPLTKLRAKPAVPLaGKYRLI 38
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
3-57 1.16e-03

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 38.99  E-value: 1.16e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446598830   3 GIILAGGTGSRLypitkVTNKHLLPV-GRyPMIYHAVYKLKQCEITDIMIITGKEH 57
Cdd:COG2068    6 AIILAAGASSRM-----GRPKLLLPLgGK-PLLERAVEAALAAGLDPVVVVLGADA 55
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 4-58 3.53e-03

CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; 4-diphosphocytidyl-2-methyl-D-erythritol synthase (CDP-ME), also called 2C-methyl-d-erythritol 4-phosphate cytidylyltransferase catalyzes the third step in the alternative (non-mevalonate) pathway of Isopentenyl diphosphate (IPP) biosynthesis: the formation of 4-diphosphocytidyl-2C-methyl-D-erythritol from CTP and 2C-methyl-D-erythritol 4-phosphate. This mevalonate independent pathway that utilizes pyruvate and glyceraldehydes 3-phosphate as starting materials for production of IPP occurs in a variety of bacteria, archaea and plant cells, but is absent in mammals. Thus, CDP-ME synthetase is an attractive targets for the structure-based design of selective antibacterial, herbicidal and antimalarial drugs.


Pssm-ID: 133009 [Multi-domain]  Cd Length: 218  Bit Score: 37.50  E-value: 3.53e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446598830   4 IILAGGTGSRLypiTKVTNKHLLPVGRYPMIYHAVYKLKQC-EITDIMIITGKEHM 58
Cdd:cd02516    4 IILAAGSGSRM---GADIPKQFLELGGKPVLEHTLEAFLAHpAIDEIVVVVPPDDI 56
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 3-54 3.99e-03

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: 37.15  E-value: 3.99e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446598830   3 GIILAGGTGSRLYpitkvTNKHLLPVGRYPMIYHAVYKLKQCEITDIMIITG 54
Cdd:cd04182    3 AIILAAGRSSRMG-----GNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLG 49
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-198 4.42e-03

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 37.92  E-value: 4.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830   4 IILAGGTGSRL-YPITKVtnkhLLPVGRYPMIYHAVYKLKQCEITDIMIITGKeHMGDVVSFLGSGQEFGVSFtyrVQDK 82
Cdd:PRK14353   9 IILAAGEGTRMkSSLPKV----LHPVAGRPMLAHVLAAAASLGPSRVAVVVGP-GAEAVAAAAAKIAPDAEIF---VQKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830  83 AGGIA----QALGLCEDFVGNdrMVVILGDN--IFSDDIRPYVEEFTnqkEGAK--VLLQSVDDPERFGVANIQNRKIIE 154
Cdd:PRK14353  81 RLGTAhavlAAREALAGGYGD--VLVLYGDTplITAETLARLRERLA---DGADvvVLGFRAADPTGYGRLIVKGGRLVA 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 446598830 155 I-EEK---PKEPKSSYAVTGIYLYDSKV-FSYIKELKPS-ARGELEITDI 198
Cdd:PRK14353 156 IvEEKdasDEERAITLCNSGVMAADGADaLALLDRVGNDnAKGEYYLTDI 205
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 1-90 4.67e-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: 36.78  E-value: 4.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446598830   1 MKGIILAGGTGSRLypitkVTNKHLLPVGRYPMIYHAVYKLK-QCEitDIMIITGKEhmgdvvsfLGSGQEFGVSFTY-R 78
Cdd:cd02503    1 ITGVILAGGKSRRM-----GGDKALLELGGKPLLEHVLERLKpLVD--EVVISANRD--------QERYALLGVPVIPdE 65

                         90
                 ....*....|....
gi 446598830  79 VQDKA--GGIAQAL 90
Cdd:cd02503   66 PPGKGplAGILAAL 79
 
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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