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Conserved domains on  [gi|512689147|ref|WP_016475171|]
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sugar phosphate nucleotidyltransferase [Sutterella wadsworthensis]

Protein Classification

nucleotidyltransferase family protein( domain architecture ID 11440233)

nucleotidyltransferase family protein such as Pseudomonas aeruginosa N-acetylmuramate alpha-1-phosphate uridylyltransferase MurU that catalyzes the formation of UDP-N-acetylmuramate (UDP-MurNAc), a crucial precursor of the bacterial peptidoglycan cell wall, from UTP and MurNAc-alpha-1P

EC:  2.7.7.-
Gene Ontology:  GO:0016779|GO:0009252
PubMed:  9445404
SCOP:  3000077

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 ...
2-239 3.31e-63

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: 197.30  E-value: 3.31e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689147   2 RAMLLCAGEGRRLRPLTQLYPKPLTTIGGVPLAVRQILALKRAGITEIVVNAAYGARILQAELGDGSRWGVHLVWSVEGh 81
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRFGVRITYVDEG- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689147  82 taaEALETRGGIVRALPLLmagsEDGAFIVAAGDIATDYDYAALAEQAQslsASGDWAHLVMVANPTFHPQGDFRL-VNG 160
Cdd:COG1208   80 ---EPLGTGGALKRALPLL----GDEPFLVLNGDILTDLDLAALLAFHR---EKGADATLALVPVPDPSRYGVVELdGDG 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689147 161 RIARRDAVGGEI---LTYASLAAFHPQLFAGLHADRAPLF-PWMFEALDAGRVSGERLVGRWANVGTLEELARAEDLFAA 236
Cdd:COG1208  150 RVTRFVEKPEEPpsnLINAGIYVLEPEIFDYIPEGEPFDLeDLLPRLIAEGRVYGYVHDGYWLDIGTPEDLLEANALLLS 229

                 ...
gi 512689147 237 AGA 239
Cdd:COG1208  230 GKA 232
 
Name Accession Description Interval E-value
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
2-239 3.31e-63

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: 197.30  E-value: 3.31e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689147   2 RAMLLCAGEGRRLRPLTQLYPKPLTTIGGVPLAVRQILALKRAGITEIVVNAAYGARILQAELGDGSRWGVHLVWSVEGh 81
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRFGVRITYVDEG- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689147  82 taaEALETRGGIVRALPLLmagsEDGAFIVAAGDIATDYDYAALAEQAQslsASGDWAHLVMVANPTFHPQGDFRL-VNG 160
Cdd:COG1208   80 ---EPLGTGGALKRALPLL----GDEPFLVLNGDILTDLDLAALLAFHR---EKGADATLALVPVPDPSRYGVVELdGDG 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689147 161 RIARRDAVGGEI---LTYASLAAFHPQLFAGLHADRAPLF-PWMFEALDAGRVSGERLVGRWANVGTLEELARAEDLFAA 236
Cdd:COG1208  150 RVTRFVEKPEEPpsnLINAGIYVLEPEIFDYIPEGEPFDLeDLLPRLIAEGRVYGYVHDGYWLDIGTPEDLLEANALLLS 229

                 ...
gi 512689147 237 AGA 239
Cdd:COG1208  230 GKA 232
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
2-230 9.10e-57

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: 180.07  E-value: 9.10e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689147   2 RAMLLCAGEGRRLRPLTQLYPKPLTTIGGVPLAVRQILALKRAGITEIVVNAAYGARILQAELGDgSRWGVHLVWSVEGh 81
Cdd:cd06422    1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHLGD-SRFGLRITISDEP- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689147  82 taAEALETRGGIVRALPLLMagseDGAFIVAAGDIATDYDYAALAEqAQSLSASGDWAHLVMVANPTFHPQGDFRL-VNG 160
Cdd:cd06422   79 --DELLETGGGIKKALPLLG----DEPFLVVNGDILWDGDLAPLLL-LHAWRMDALLLLLPLVRNPGHNGVGDFSLdADG 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689147 161 RIARRDAVGGEILTYASLAAFHPQLFAGLHADRAPLFPWMFEALDAGRVSGERLVGRWANVGTLEELARA 230
Cdd:cd06422  152 RLRRGGGGAVAPFTFTGIQILSPELFAGIPPGKFSLNPLWDRAIAAGRLFGLVYDGLWFDVGTPERLLAA 221
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
1-236 2.12e-20

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: 88.81  E-value: 2.12e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689147    1 MRAMLLCAGEGRRLRPLTQLYPKPLTTIGGVPLAVRQILALKRAGITEIVVNAAYGARILQAELGDGSRWGVHLVWSVEG 80
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEKVREYFGDGSRGGVPIEYVVQE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689147   81 htaaEALETRGGIVRALPLLmagseDGAFIVAAGDIATDYDyaaLAEQAqsLSASGDwahlVMVANPTFHPQ--GDFRLV 158
Cdd:TIGR03992  81 ----EQLGTADALGSAKEYV-----DDEFLVLNGDVLLDSD---LLERL--IRAEAP----AIAVVEVDDPSdyGVVETD 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689147  159 NGRIAR-----RDAVGGeiLTYASLAAFHPQLFAGLhaDRAPLFP-WMFEALDA-------GRVSGERLVGRWANVGtle 225
Cdd:TIGR03992 143 GGRVTGivekpENPPSN--LINAGIYLFSPEIFELL--EKTKLSPrGEYELTDAlqllideGKVKAVELDGFWLDVG--- 215
                         250
                  ....*....|.
gi 512689147  226 elaRAEDLFAA 236
Cdd:TIGR03992 216 ---RPWDLLDA 223
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
2-134 5.51e-16

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: 74.60  E-value: 5.51e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689147    2 RAMLLCAGEGRRLRPLTQLYPKPLTTIGG-VPLAVRQILALKRAGITE-IVVNAAYGARILQAELGDGSRWGVHLVWSVE 79
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGkYPLIDYPLSRLANAGIREiIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 512689147   80 GhtaaEALETRGGIvrALPLLMAGSEDGAFIVAAGDIATDYDYAALAEQAQSLSA 134
Cdd:pfam00483  81 P----EGKGTAPAV--ALAADFLGDEKSDVLVLGGDHIYRMDLEQAVKFHIEKAA 129
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
2-79 1.69e-05

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 45.05  E-value: 1.69e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 512689147   2 RAMLLCAGEGRRLRPLTQLYPKPLTTIGGVPLAVRQILALKRAGITEI-VVNAAYGARILQAELGDGSRWGVHLVWSVE 79
Cdd:PRK15480   5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDIlIISTPQDTPRFQQLLGDGSQWGLNLQYKVQ 83
 
Name Accession Description Interval E-value
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
2-239 3.31e-63

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: 197.30  E-value: 3.31e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689147   2 RAMLLCAGEGRRLRPLTQLYPKPLTTIGGVPLAVRQILALKRAGITEIVVNAAYGARILQAELGDGSRWGVHLVWSVEGh 81
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRFGVRITYVDEG- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689147  82 taaEALETRGGIVRALPLLmagsEDGAFIVAAGDIATDYDYAALAEQAQslsASGDWAHLVMVANPTFHPQGDFRL-VNG 160
Cdd:COG1208   80 ---EPLGTGGALKRALPLL----GDEPFLVLNGDILTDLDLAALLAFHR---EKGADATLALVPVPDPSRYGVVELdGDG 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689147 161 RIARRDAVGGEI---LTYASLAAFHPQLFAGLHADRAPLF-PWMFEALDAGRVSGERLVGRWANVGTLEELARAEDLFAA 236
Cdd:COG1208  150 RVTRFVEKPEEPpsnLINAGIYVLEPEIFDYIPEGEPFDLeDLLPRLIAEGRVYGYVHDGYWLDIGTPEDLLEANALLLS 229

                 ...
gi 512689147 237 AGA 239
Cdd:COG1208  230 GKA 232
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
2-230 9.10e-57

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: 180.07  E-value: 9.10e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689147   2 RAMLLCAGEGRRLRPLTQLYPKPLTTIGGVPLAVRQILALKRAGITEIVVNAAYGARILQAELGDgSRWGVHLVWSVEGh 81
Cdd:cd06422    1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHLGD-SRFGLRITISDEP- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689147  82 taAEALETRGGIVRALPLLMagseDGAFIVAAGDIATDYDYAALAEqAQSLSASGDWAHLVMVANPTFHPQGDFRL-VNG 160
Cdd:cd06422   79 --DELLETGGGIKKALPLLG----DEPFLVVNGDILWDGDLAPLLL-LHAWRMDALLLLLPLVRNPGHNGVGDFSLdADG 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689147 161 RIARRDAVGGEILTYASLAAFHPQLFAGLHADRAPLFPWMFEALDAGRVSGERLVGRWANVGTLEELARA 230
Cdd:cd06422  152 RLRRGGGGAVAPFTFTGIQILSPELFAGIPPGKFSLNPLWDRAIAAGRLFGLVYDGLWFDVGTPERLLAA 221
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
3-222 2.60e-33

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: 119.61  E-value: 2.60e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689147   3 AMLLCAGEGRRLRPLTQLYPKPLTTIGGVPLAVRQILALKRAGITEIVVNAAYGARILQAELGDGSRWGVHLVWSVEGht 82
Cdd:cd04181    1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGSKFGVNIEYVVQE-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689147  83 aaEALETRGGIVRALPLLmagsEDGAFIVAAGDIATDYDYAALAEQAQSLSasgdwAHLVMVANPTFHPQgDFRLV---- 158
Cdd:cd04181   79 --EPLGTAGAVRNAEDFL----GDDDFLVVNGDVLTDLDLSELLRFHREKG-----ADATIAVKEVEDPS-RYGVVeldd 146
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 512689147 159 NGRIAR-----RDAVGGEILT--YaslaAFHPQLFAGLHADRAP-------LFPWMfeaLDAGRVSGERLVGRWANVG 222
Cdd:cd04181  147 DGRVTRfvekpTLPESNLANAgiY----IFEPEILDYIPEILPRgedeltdAIPLL---IEEGKVYGYPVDGYWLDIG 217
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
1-236 2.12e-20

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: 88.81  E-value: 2.12e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689147    1 MRAMLLCAGEGRRLRPLTQLYPKPLTTIGGVPLAVRQILALKRAGITEIVVNAAYGARILQAELGDGSRWGVHLVWSVEG 80
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEKVREYFGDGSRGGVPIEYVVQE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689147   81 htaaEALETRGGIVRALPLLmagseDGAFIVAAGDIATDYDyaaLAEQAqsLSASGDwahlVMVANPTFHPQ--GDFRLV 158
Cdd:TIGR03992  81 ----EQLGTADALGSAKEYV-----DDEFLVLNGDVLLDSD---LLERL--IRAEAP----AIAVVEVDDPSdyGVVETD 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689147  159 NGRIAR-----RDAVGGeiLTYASLAAFHPQLFAGLhaDRAPLFP-WMFEALDA-------GRVSGERLVGRWANVGtle 225
Cdd:TIGR03992 143 GGRVTGivekpENPPSN--LINAGIYLFSPEIFELL--EKTKLSPrGEYELTDAlqllideGKVKAVELDGFWLDVG--- 215
                         250
                  ....*....|.
gi 512689147  226 elaRAEDLFAA 236
Cdd:TIGR03992 216 ---RPWDLLDA 223
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
3-231 8.53e-20

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: 84.53  E-value: 8.53e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689147   3 AMLLCAGEGRRLRPLTQLYPKPLTTIGGVPLAVRQILALKRAGITEIVVNAAYGARILQAELGDGSRWGVHLVWSVEght 82
Cdd:cd06915    1 AVILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYLAEQIEEYFGDGYRGGIRIYYVIE--- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689147  83 aAEALETRGGIVRALPLLmagsEDGAFIVAAGDIATDYDYAALAEQAQSLSASGdwahlVMVANPTFHPQ--------GD 154
Cdd:cd06915   78 -PEPLGTGGAIKNALPKL----PEDQFLVLNGDTYFDVDLLALLAALRASGADA-----TMALRRVPDASrygnvtvdGD 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 512689147 155 FRLVNGRIARRDAVGGEIltYASLAAFHPQLFAGLHADRAPLFPWMFEAL-DAGRVSGERLVGRWANVGTLEELARAE 231
Cdd:cd06915  148 GRVIAFVEKGPGAAPGLI--NGGVYLLRKEILAEIPADAFSLEADVLPALvKRGRLYGFEVDGYFIDIGIPEDYARAQ 223
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
3-125 5.77e-18

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: 79.48  E-value: 5.77e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689147   3 AMLLCAGEGRRLRPLTQLYPKPLTTIGGVPLAVRQILALKRAGITEIVVNAAYGARILQAELGDGSRWGVHLVWSVEGht 82
Cdd:cd06426    1 VVIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNYLAEMIEDYFGDGSKFGVNISYVRED-- 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 512689147  83 aaEALETRGGIVralplLMAGSEDGAFIVAAGDIATDYDYAAL 125
Cdd:cd06426   79 --KPLGTAGALS-----LLPEKPTDPFLVMNGDILTNLNYEHL 114
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
1-127 9.87e-17

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: 76.48  E-value: 9.87e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689147   1 MRAMLLCAGEGRRLRPLTQLYPKPLTTIGGVPLAVRQILALKRAGITEIVVNAAYGARILQAELGDGS-RWGVHLVWSVE 79
Cdd:cd06425    1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYRPEDMVPFLKEYEkKLGIKITFSIE 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 512689147  80 ghtaAEALETRGGIVRALPLLMAGSEDgaFIVAAGDIATDYDYAALAE 127
Cdd:cd06425   81 ----TEPLGTAGPLALARDLLGDDDEP--FFVLNSDVICDFPLAELLD 122
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
1-75 3.43e-16

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: 74.91  E-value: 3.43e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 512689147   1 MRAMLLCAGEGRRLRPLTQLYPKPLTTIGGVPLAVRQILALKRAGITEIVVNAAYGARILQAELGDGSRWGVHLV 75
Cdd:cd04189    1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEALGDGSRFGVRIT 75
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
2-51 3.78e-16

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 74.89  E-value: 3.78e-16
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 512689147   2 RAMLLCAGEGRRLRPLTQLYPKPLTTIGGVPLAVRQILALKRAGITEIVV 51
Cdd:COG1213    1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVV 50
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
2-134 5.51e-16

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: 74.60  E-value: 5.51e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689147    2 RAMLLCAGEGRRLRPLTQLYPKPLTTIGG-VPLAVRQILALKRAGITE-IVVNAAYGARILQAELGDGSRWGVHLVWSVE 79
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGkYPLIDYPLSRLANAGIREiIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 512689147   80 GhtaaEALETRGGIvrALPLLMAGSEDGAFIVAAGDIATDYDYAALAEQAQSLSA 134
Cdd:pfam00483  81 P----EGKGTAPAV--ALAADFLGDEKSDVLVLGGDHIYRMDLEQAVKFHIEKAA 129
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
3-51 1.26e-14

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: 70.34  E-value: 1.26e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 512689147   3 AMLLCAGEGRRLRPLTQLYPKPLTTIGGVPLAVRQILALKRAGITEIVV 51
Cdd:cd02523    1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVI 49
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-74 5.08e-13

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 67.04  E-value: 5.08e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 512689147   1 MRAMLLCAGEGRRLRPLTQLYPKPLTTIGGVPLAVRQILALKRAGITEI--VVNAAYGARIlQAELGDGSRWGVHL 74
Cdd:COG1209    1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREIliISTPEDGPQF-ERLLGDGSQLGIKI 75
LicC COG4750
CTP:phosphocholine cytidylyltransferase LicC [Cell wall/membrane/envelope biogenesis, Lipid ...
1-55 9.70e-13

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


Pssm-ID: 443784 [Multi-domain]  Cd Length: 228  Bit Score: 65.24  E-value: 9.70e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 512689147   1 MRAMLLCAGEGRRLRPLTQLYPKPLTTIGGVPLAVRQILALKRAGITEIVVNAAY 55
Cdd:COG4750    1 MNAIILAAGLGSRFAPITYETPKGLLKVNGEPLIERQIRQLHEAGITDITVVVGY 55
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
2-230 1.36e-12

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: 66.27  E-value: 1.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689147    2 RAMLLCAGEGRRLRPLTQLYPKPLTTIGGVPLAVRQILALKRAGITE--IVVNAAYGARIlQAELGDGSRWGVHLVWSVE 79
Cdd:TIGR01208   1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDigIVVGPVTGEEI-KEIVGEGERFGAKITYIVQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689147   80 GhtaaEALETRGGIVRALPLLmaGSEDgaFIVAAGD-IATDydyaALAEQAQSLSASGDWAH--LVMVANPTFHPQGDFR 156
Cdd:TIGR01208  80 G----EPLGLAHAVYTARDFL--GDDD--FVVYLGDnLIQD----GISRFVKSFEEKDYDALilLTKVRDPTAFGVAVLE 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689147  157 lVNGRIAR-----RDAVGGeiLTYASLAAFHPQLFAGLhADRAPLFPWMFEALDA--------GRVSGERLVGRWANVGT 223
Cdd:TIGR01208 148 -DGKRILKlvekpKEPPSN--LAVVGLYMFRPLIFEAI-KNIKPSWRGELEITDAiqwliekgYKVGGSKVTGWWKDTGK 223

                  ....*..
gi 512689147  224 LEELARA 230
Cdd:TIGR01208 224 PEDLLDA 230
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
1-147 9.25e-08

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: 51.42  E-value: 9.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689147   1 MRAMLLCAGEGRRLRPLTQLYPKPLTTIGGVPLAVRQILALKRAGITEI--VVNAAYGARILQAeLGDGSRWGVHLVWSV 78
Cdd:cd02538    1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREIliISTPEDLPLFKEL-LGDGSDLGIRITYAV 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 512689147  79 EghtaaealETRGGIVRALPLlmaGSE---DGAFIVAAGD-IATDYDYAALAEQAQSLSAsGDWAHLVMVANP 147
Cdd:cd02538   80 Q--------PKPGGLAQAFII---GEEfigDDPVCLILGDnIFYGQGLSPILQRAAAQKE-GATVFGYEVNDP 140
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
1-51 9.26e-08

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: 51.12  E-value: 9.26e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 512689147   1 MRAMLLCAGEGRRLRPLTQLYPKPLTTIGGVPLAVRQILALKRAGITEIVV 51
Cdd:cd04198    1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIV 51
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
3-128 2.27e-07

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: 49.94  E-value: 2.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689147   3 AMLLCAGEGRRLRPLTQLYPKPLTTIGGVPLAVRQILALKRAGITEI--VVNAAYGARILQAELGDGSRWG----VHLVW 76
Cdd:cd02507    3 AVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVfvVCCEHSQAIIEHLLKSKWSSLSskmiVDVIT 82
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 512689147  77 SVEGHTA--AEALETRGGIVRalpllmagsedGAFIVAAGDIATDYDYAALAEQ 128
Cdd:cd02507   83 SDLCESAgdALRLRDIRGLIR-----------SDFLLLSCDLVSNIPLSELLEE 125
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
2-79 1.69e-05

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 45.05  E-value: 1.69e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 512689147   2 RAMLLCAGEGRRLRPLTQLYPKPLTTIGGVPLAVRQILALKRAGITEI-VVNAAYGARILQAELGDGSRWGVHLVWSVE 79
Cdd:PRK15480   5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDIlIISTPQDTPRFQQLLGDGSQWGLNLQYKVQ 83
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
2-79 1.21e-04

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: 42.38  E-value: 1.21e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 512689147    2 RAMLLCAGEGRRLRPLTQLYPKPLTTIGGVPLAVRQILALKRAGITEI-VVNAAYGARILQAELGDGSRWGVHLVWSVE 79
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDIlIISTPEDTPRFQRLLGDGSQWGINLSYAVQ 79
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
3-76 2.34e-04

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 40.91  E-value: 2.34e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 512689147   3 AMLLCAGEGRRLRPltqlyPKPLTTIGGVPLAVRQILALKRAGITEIVVNAAYGARILQAELgdgSRWGVHLVW 76
Cdd:COG2068    6 AIILAAGASSRMGR-----PKLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADAEEVAAAL---AGLGVRVVV 71
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
3-73 2.56e-04

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: 40.60  E-value: 2.56e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 512689147   3 AMLLCAGEGRRLRPLTQLYPKPLTTIGGvplAVRQI-LALK---RAGITEIVVNAAYGARILQAELGDGSRWGVH 73
Cdd:cd02508    1 AIILAGGEGTRLSPLTKKRAKPAVPFGG---RYRLIdFPLSnmvNSGIRNVGVLTQYKSRSLNDHLGSGKEWDLD 72
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
3-148 6.06e-04

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: 39.93  E-value: 6.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689147   3 AMLLCAGE--GRRLRPLTQLYPKPLTTIGGVPLAVRQILALKR-AGITEIVVNAAYGARILQAELGDGSRwgvHLVWSVE 79
Cdd:cd06428    1 AVILVGGPqkGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKvPDLKEVLLIGFYPESVFSDFISDAQQ---EFNVPIR 77
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 512689147  80 GHTAAEALETRGGIVRALPLLMAGSEDgAFIVAAGDIATDYDYAALAEQAQSLSASgdwaHLVMVANPT 148
Cdd:cd06428   78 YLQEYKPLGTAGGLYHFRDQILAGNPS-AFFVLNADVCCDFPLQELLEFHKKHGAS----GTILGTEAS 141
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
3-33 6.32e-04

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: 39.86  E-value: 6.32e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 512689147   3 AMLLCAGEGRRLRPLTQLYPKPLTTIGGVPL 33
Cdd:cd02524    1 VVILAGGLGTRLSEETELKPKPMVEIGGRPI 31
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
6-94 1.37e-03

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: 38.65  E-value: 1.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689147   6 LCAGEGRRLRplTQLyPKPLTTIGGVPLAVRQILALKRAGITEIVVNAAYGARILQAELGDGsrwGVHLVWSVE----GH 81
Cdd:cd02540    4 LAAGKGTRMK--SDL-PKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVKKALANP---NVEFVLQEEqlgtGH 77
                         90
                 ....*....|....*.
gi 512689147  82 ---TAAEALETRGGIV 94
Cdd:cd02540   78 avkQALPALKDFEGDV 93
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
3-115 2.22e-03

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 38.66  E-value: 2.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689147   3 AMLLCAGEGRRLRpltQLYPKPLTTIGGVPLAVRQILALKRAGITEIVVNAAYGARILQAELGDGSRWGVHlvwsveght 82
Cdd:PRK14354   5 AIILAAGKGTRMK---SKLPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVGHGAEEVKEVLGDRSEFALQ--------- 72
                         90       100       110
                 ....*....|....*....|....*....|...
gi 512689147  83 aAEALETRGGIVRALPLLmaGSEDGAFIVAAGD 115
Cdd:PRK14354  73 -EEQLGTGHAVMQAEEFL--ADKEGTTLVICGD 102
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
3-77 4.83e-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: 36.77  E-value: 4.83e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 512689147   3 AMLLCAGEGRRLRPltqlyPKPLTTIGGVPLAVRQILALKRAGITE-IVVNAAYGARILQAELGDGSRWGVHLVWS 77
Cdd:cd04182    3 AIILAAGRSSRMGG-----NKLLLPLDGKPLLRHALDAALAAGLSRvIVVLGAEADAVRAALAGLPVVVVINPDWE 73
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
3-128 8.42e-03

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: 36.43  E-value: 8.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512689147   3 AMLLCAGEGRRLRPLTQLYPKPLTTIGGVPLAVRQILALKRAGITEIVVNA-AYGARI---LQAELGDGSRWG---VHLV 75
Cdd:cd04197    3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCcSHSDQIkeyIEKSKWSKPKSSlmiVIII 82
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 512689147  76 WSVEGHTAAEAL---ETRgGIVRalpllmagsedGAFIVAAGDIATDYDYAALAEQ 128
Cdd:cd04197   83 MSEDCRSLGDALrdlDAK-GLIR-----------GDFILVSGDVVSNIDLKEILEE 126
 
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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