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Conserved domains on  [gi|1253325054|gb|ATI80069|]
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nucleotidyltransferase family protein [Sphingobium yanoikuyae]

Protein Classification

nucleotidyltransferase family protein( domain architecture ID 10157586)

nucleotidyltransferase family protein similar to Pseudomonas putida N-acetylmuramic acid alpha-1-phosphate (MurNAc-alpha1-P) uridylyltransferase MurU, which catalyzes the synthesis of uridine diphosphate (UDP)-MurNAc, a crucial precursor of the bacterial peptidoglycan cell wall

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 4-225 6.74e-105

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: 302.18  E-value: 6.74e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253325054   4 TAMLMAAGLGKRMRPLTATRPKPLVKVAGKALMDHALDRLAAGGIKTVVVNVHYLADTVEAHLR-TRKDMDFRISDERAK 82
Cdd:cd06422     1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHLGdSRFGLRITISDEPDE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253325054  83 LLETGGGLIHARPLLGDKPFICANSDNLWIDGPAETLGMMQrlwdpERMDALLLLVPLARANCHSGPGDFHMDANGRLAR 162
Cdd:cd06422    81 LLETGGGIKKALPLLGDEPFLVVNGDILWDGDLAPLLLLHA-----WRMDALLLLLPLVRNPGHNGVGDFSLDADGRLRR 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1253325054 163 RKTAHVAPFVFTGVQILSPRLLVDPPADVFSTNIFWNRAIAAGRLYGAVHQGLWFDVGTPQAI 225
Cdd:cd06422   156 GGGGAVAPFTFTGIQILSPELFAGIPPGKFSLNPLWDRAIAAGRLFGLVYDGLWFDVGTPERL 218
 
Name Accession Description Interval E-value
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 4-225 6.74e-105

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: 302.18  E-value: 6.74e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253325054   4 TAMLMAAGLGKRMRPLTATRPKPLVKVAGKALMDHALDRLAAGGIKTVVVNVHYLADTVEAHLR-TRKDMDFRISDERAK 82
Cdd:cd06422     1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHLGdSRFGLRITISDEPDE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253325054  83 LLETGGGLIHARPLLGDKPFICANSDNLWIDGPAETLGMMQrlwdpERMDALLLLVPLARANCHSGPGDFHMDANGRLAR 162
Cdd:cd06422    81 LLETGGGIKKALPLLGDEPFLVVNGDILWDGDLAPLLLLHA-----WRMDALLLLLPLVRNPGHNGVGDFSLDADGRLRR 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1253325054 163 RKTAHVAPFVFTGVQILSPRLLVDPPADVFSTNIFWNRAIAAGRLYGAVHQGLWFDVGTPQAI 225
Cdd:cd06422   156 GGGGAVAPFTFTGIQILSPELFAGIPPGKFSLNPLWDRAIAAGRLFGLVYDGLWFDVGTPERL 218
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 4-235 4.49e-77

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: 232.35  E-value: 4.49e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253325054   4 TAMLMAAGLGKRMRPLTATRPKPLVKVAGKALMDHALDRLAAGGIKTVVVNVHYLADTVEAHLRTRKDMDFRI--SDERa 81
Cdd:COG1208     1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRFGVRItyVDEG- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253325054  82 KLLETGGGLIHARPLLGDKPFICANSDNLW-IDgpaetLGMMQRLWDPERMDALLLLVPLARancHSGPGDFHMDANGRL 160
Cdd:COG1208    80 EPLGTGGALKRALPLLGDEPFLVLNGDILTdLD-----LAALLAFHREKGADATLALVPVPD---PSRYGVVELDGDGRV 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1253325054 161 AR---RKTAHVAPFVFTGVQILSPRLLVD-PPADVFSTNIFWNRAIAAGRLYGAVHQGLWFDVGTPQAIPVVESMIAHG 235
Cdd:COG1208   152 TRfveKPEEPPSNLINAGIYVLEPEIFDYiPEGEPFDLEDLLPRLIAEGRVYGYVHDGYWLDIGTPEDLLEANALLLSG 230
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 5-110 1.10e-19

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: 86.49  E-value: 1.10e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253325054   5 AMLMAAGLGKRMRPLTATRPKPLVKVAGKALMDHALDRLAAGGIKTVVVNVHYLADTVEAHLRTRKDMDFRIS-DERAKL 83
Cdd:TIGR03992   3 AVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEKVREYFGDGSRGGVPIEyVVQEEQ 82

                          90       100
                  ....*....|....*....|....*..
gi 1253325054  84 LETGGGLIHARPLLgDKPFICANSDNL 110
Cdd:TIGR03992  83 LGTADALGSAKEYV-DDEFLVLNGDVL 108
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 5-225 4.57e-14

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: 69.20  E-value: 4.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253325054   5 AMLMAAGLGKRMRPLTATRPKPLVKVAGKA-LMDHALDRLAAGGI-KTVVVNVHYLADTVEAHLRTRKDMDFRISDerak 82
Cdd:pfam00483   2 AIILAGGSGTRLWPLTRTLAKPLVPVGGKYpLIDYPLSRLANAGIrEIIVILTQEHRFMLNELLGDGSKFGVQITY---- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253325054  83 LLE-----TGGGLIHARPLLGDKPFICA--NSDNLWIDGPAETLGMMQRLwdPERMDALLLLVPLARAnchSGPGDFHMD 155
Cdd:pfam00483  78 ALQpegkgTAPAVALAADFLGDEKSDVLvlGGDHIYRMDLEQAVKFHIEK--AADATVTFGIVPVEPP---TGYGVVEFD 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253325054 156 ANGRLAR----RKTAHVAPFVFTGVQILSPRLLVDPPADV--------FSTNIFwNRAIAAGRLYGAVhQGL---WFDVG 220
Cdd:pfam00483 153 DNGRVIRfvekPKLPKASNYASMGIYIFNSGVLDFLAKYLeelkrgedEITDIL-PKALEDGKLAYAF-IFKgyaWLDVG 230


                  ....*
gi 1253325054 221 TPQAI 225
Cdd:pfam00483 231 TWDSL 235
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-100 5.19e-11

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 61.77  E-value: 5.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253325054   1 MINTAMLMAAGLGKRMRpltATRPKPLVKVAGKALMDHALDRLAAGGIKTVVVNVHYLADTVEAHLRTRKDMDFrisdeR 80
Cdd:PRK14354    1 MNRYAIILAAGKGTRMK---SKLPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVGHGAEEVKEVLGDRSEFAL-----Q 72

                          90       100
                  ....*....|....*....|
gi 1253325054  81 AKLLETGGGLIHARPLLGDK 100
Cdd:PRK14354   73 EEQLGTGHAVMQAEEFLADK 92
 
Name Accession Description Interval E-value
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 4-225 6.74e-105

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: 302.18  E-value: 6.74e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253325054   4 TAMLMAAGLGKRMRPLTATRPKPLVKVAGKALMDHALDRLAAGGIKTVVVNVHYLADTVEAHLR-TRKDMDFRISDERAK 82
Cdd:cd06422     1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHLGdSRFGLRITISDEPDE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253325054  83 LLETGGGLIHARPLLGDKPFICANSDNLWIDGPAETLGMMQrlwdpERMDALLLLVPLARANCHSGPGDFHMDANGRLAR 162
Cdd:cd06422    81 LLETGGGIKKALPLLGDEPFLVVNGDILWDGDLAPLLLLHA-----WRMDALLLLLPLVRNPGHNGVGDFSLDADGRLRR 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1253325054 163 RKTAHVAPFVFTGVQILSPRLLVDPPADVFSTNIFWNRAIAAGRLYGAVHQGLWFDVGTPQAI 225
Cdd:cd06422   156 GGGGAVAPFTFTGIQILSPELFAGIPPGKFSLNPLWDRAIAAGRLFGLVYDGLWFDVGTPERL 218
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 4-235 4.49e-77

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: 232.35  E-value: 4.49e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253325054   4 TAMLMAAGLGKRMRPLTATRPKPLVKVAGKALMDHALDRLAAGGIKTVVVNVHYLADTVEAHLRTRKDMDFRI--SDERa 81
Cdd:COG1208     1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRFGVRItyVDEG- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253325054  82 KLLETGGGLIHARPLLGDKPFICANSDNLW-IDgpaetLGMMQRLWDPERMDALLLLVPLARancHSGPGDFHMDANGRL 160
Cdd:COG1208    80 EPLGTGGALKRALPLLGDEPFLVLNGDILTdLD-----LAALLAFHREKGADATLALVPVPD---PSRYGVVELDGDGRV 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1253325054 161 AR---RKTAHVAPFVFTGVQILSPRLLVD-PPADVFSTNIFWNRAIAAGRLYGAVHQGLWFDVGTPQAIPVVESMIAHG 235
Cdd:COG1208   152 TRfveKPEEPPSNLINAGIYVLEPEIFDYiPEGEPFDLEDLLPRLIAEGRVYGYVHDGYWLDIGTPEDLLEANALLLSG 230
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 5-220 1.06e-42

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: 143.88  E-value: 1.06e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253325054   5 AMLMAAGLGKRMRPLTATRPKPLVKVAGKALMDHALDRLAAGGIKTVVVNVHYLADTVEAHL--RTRKDMDFRISDERaK 82
Cdd:cd04181     1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFgdGSKFGVNIEYVVQE-E 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253325054  83 LLETGGGLIHARPLLGDKPFICANSDNLWIDGPAETLGMMQRlwdpERMDALLLLVPlarancHSGPGDF---HMDANGR 159
Cdd:cd04181    80 PLGTAGAVRNAEDFLGDDDFLVVNGDVLTDLDLSELLRFHRE----KGADATIAVKE------VEDPSRYgvvELDDDGR 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1253325054 160 LAR---RKTAHVAPFVFTGVQILSPRLL-----VDPPADVFSTNIFwNRAIAAGRLYGAVHQGLWFDVG 220
Cdd:cd04181   150 VTRfveKPTLPESNLANAGIYIFEPEILdyipeILPRGEDELTDAI-PLLIEEGKVYGYPVDGYWLDIG 217
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 5-223 2.70e-27

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: 104.17  E-value: 2.70e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253325054   5 AMLMAAGLGKRMRPLTATRPKPLVKVAGKALMDHALDRLAAGGIKTVVVNVHYLADTVEAHL--RTRKDMDFRISDERaK 82
Cdd:cd06915     1 AVILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYLAEQIEEYFgdGYRGGIRIYYVIEP-E 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253325054  83 LLETGGGLIHARPLLGDKPFICANSDNLW-IDgpaetLGMMQRLWDPERMDALLLLVPLARAnchSGPGDFHMDANGRLA 161
Cdd:cd06915    80 PLGTGGAIKNALPKLPEDQFLVLNGDTYFdVD-----LLALLAALRASGADATMALRRVPDA---SRYGNVTVDGDGRVI 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1253325054 162 R--RKTAHVAP-FVFTGVQILSPRLLVDPPADVFS--TNIFwNRAIAAGRLYGAVHQGLWFDVGTPQ 223
Cdd:cd06915   152 AfvEKGPGAAPgLINGGVYLLRKEILAEIPADAFSleADVL-PALVKRGRLYGFEVDGYFIDIGIPE 217
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 5-108 1.03e-23

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: 94.50  E-value: 1.03e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253325054   5 AMLMAAGLGKRMRPLTATRPKPLVKVAGKALMDHALDRLAAGGIKTVVVNVHYLADTVEAHLRTRKDMDFRIS----DER 80
Cdd:cd06426     1 VVIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNYLAEMIEDYFGDGSKFGVNISyvreDKP 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1253325054  81 aklLETGGGLIharpLLGDK---PFICANSD 108
Cdd:cd06426    81 ---LGTAGALS----LLPEKptdPFLVMNGD 104
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
5-233 2.87e-23

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 93.77  E-value: 2.87e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253325054   5 AMLMAAGLGKRMRPLTATRPKPLVKVAGKALMDHALDRLAAGGIKTVVVNVHYLADTVEAHLRtRKDMDFR-ISDERAKL 83
Cdd:COG1213     2 AVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEALA-RPGPDVTfVYNPDYDE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253325054  84 LETGGGLIHARPLLGDkPFICANSDNLW--------IDGPAETLGMMQRLWDPERMDALLLLVplaranchsgpgdfhmD 155
Cdd:COG1213    81 TNNIYSLWLAREALDE-DFLLLNGDVVFdpailkrlLASDGDIVLLVDRKWEKPLDEEVKVRV----------------D 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253325054 156 ANGRLAR-RKTAHVAPF--VFTGVQILSPRLL------VDPPADVFSTNIFWNRAI-AAGRLYGAVH-----QGLWFDVG 220
Cdd:COG1213   144 EDGRIVEiGKKLPPEEAdgEYIGIFKFSAEGAaalreaLEALIDEGGPNLYYEDALqELIDEGGPVKavdigGLPWVEID 223

                         250
                  ....*....|...
gi 1253325054 221 TPQAIPVVESMIA 233
Cdd:COG1213   224 TPEDLERAEELFA 236
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 5-222 4.04e-23

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: 93.40  E-value: 4.04e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253325054   5 AMLMAAGLGKRMRPLTATRPKPLVKVAGKALMDHALDRLAAGGIKTVVVNVHYLADTVEAHLRTRKDMDFRIS----DER 80
Cdd:cd04189     3 GLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEALGDGSRFGVRITyilqEEP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253325054  81 AklletggGLIHA----RPLLGDKPFICANSDNLWIDGpaetLGMMQRLWDPERMDALLLLVPlarancHSGPGDFhmda 156
Cdd:cd04189    83 L-------GLAHAvlaaRDFLGDEPFVVYLGDNLIQEG----ISPLVRDFLEEDADASILLAE------VEDPRRF---- 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253325054 157 ngrlarrktahvapfvftGVQILSPRLLV-------DPPAD-------VFSTNIF---------W----------NRAIA 203
Cdd:cd04189   142 ------------------GVAVVDDGRIVrlvekpkEPPSNlalvgvyAFTPAIFdaisrlkpsWrgeleitdaiQWLID 203

                         250       260
                  ....*....|....*....|
gi 1253325054 204 AGR-LYGAVHQGLWFDVGTP 222
Cdd:cd04189   204 RGRrVGYSIVTGWWKDTGTP 223
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 5-111 8.52e-21

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: 86.90  E-value: 8.52e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253325054   5 AMLMAAGLGKRMRPLTATRPKPLVKVAGKALMDHALDRLAAGGIKTVVVNVHYLADTVEAHLRTRKDMDFRISDERAkll 84
Cdd:cd02523     1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKKYPNIKFVYNPDYA--- 77

                          90       100
                  ....*....|....*....|....*....
gi 1253325054  85 ETG--GGLIHARPLLgDKPFICANSDNLW 111
Cdd:cd02523    78 ETNniYSLYLARDFL-DEDFLLLEGDVVF 105
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 5-110 1.10e-19

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: 86.49  E-value: 1.10e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253325054   5 AMLMAAGLGKRMRPLTATRPKPLVKVAGKALMDHALDRLAAGGIKTVVVNVHYLADTVEAHLRTRKDMDFRIS-DERAKL 83
Cdd:TIGR03992   3 AVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEKVREYFGDGSRGGVPIEyVVQEEQ 82

                          90       100
                  ....*....|....*....|....*..
gi 1253325054  84 LETGGGLIHARPLLgDKPFICANSDNL 110
Cdd:TIGR03992  83 LGTADALGSAKEYV-DDEFLVLNGDVL 108
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 5-223 7.58e-18

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: 79.18  E-value: 7.58e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253325054   5 AMLMAAGLGKRMRPLTATRPKPLVKVAGKALMDHALDRLAAGGIKTVVVNVHYLADTVEAHLRTRKD-----MDFRISDE 79
Cdd:cd06425     3 ALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYRPEDMVPFLKEYEKklgikITFSIETE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253325054  80 RaklLETGGGLIHARPLLG--DKPFICANSDNLwIDGP------------AETLGMMQRLWDPERMDALLllvplaranc 145
Cdd:cd06425    83 P---LGTAGPLALARDLLGddDEPFFVLNSDVI-CDFPlaelldfhkkhgAEGTILVTKVEDPSKYGVVV---------- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253325054 146 hsgpgdfHMDANGRLAR---RKTAHVAPFVFTGVQILSPRLL---VDPPA----DVFStnifwnRAIAAGRLYGAVHQGL 215
Cdd:cd06425   149 -------HDENTGRIERfveKPKVFVGNKINAGIYILNPSVLdriPLRPTsiekEIFP------KMASEGQLYAYELPGF 215


                  ....*...
gi 1253325054 216 WFDVGTPQ 223
Cdd:cd06425   216 WMDIGQPK 223
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 5-225 4.57e-14

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: 69.20  E-value: 4.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253325054   5 AMLMAAGLGKRMRPLTATRPKPLVKVAGKA-LMDHALDRLAAGGI-KTVVVNVHYLADTVEAHLRTRKDMDFRISDerak 82
Cdd:pfam00483   2 AIILAGGSGTRLWPLTRTLAKPLVPVGGKYpLIDYPLSRLANAGIrEIIVILTQEHRFMLNELLGDGSKFGVQITY---- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253325054  83 LLE-----TGGGLIHARPLLGDKPFICA--NSDNLWIDGPAETLGMMQRLwdPERMDALLLLVPLARAnchSGPGDFHMD 155
Cdd:pfam00483  78 ALQpegkgTAPAVALAADFLGDEKSDVLvlGGDHIYRMDLEQAVKFHIEK--AADATVTFGIVPVEPP---TGYGVVEFD 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253325054 156 ANGRLAR----RKTAHVAPFVFTGVQILSPRLLVDPPADV--------FSTNIFwNRAIAAGRLYGAVhQGL---WFDVG 220
Cdd:pfam00483 153 DNGRVIRfvekPKLPKASNYASMGIYIFNSGVLDFLAKYLeelkrgedEITDIL-PKALEDGKLAYAF-IFKgyaWLDVG 230


                  ....*
gi 1253325054 221 TPQAI 225
Cdd:pfam00483 231 TWDSL 235
LicC COG4750
CTP:phosphocholine cytidylyltransferase LicC [Cell wall/membrane/envelope biogenesis, Lipid ...
 5-109 2.54e-11

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


Pssm-ID: 443784 [Multi-domain]  Cd Length: 228  Bit Score: 61.00  E-value: 2.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253325054   5 AMLMAAGLGKRMRPLTATRPKPLVKVAGKALMDHALDRLAAGGIKTVVVNVHYLADTVEaHLRTRKDMDFRISDERAKlL 84
Cdd:COG4750     3 AIILAAGLGSRFAPITYETPKGLLKVNGEPLIERQIRQLHEAGITDITVVVGYLKEQFE-YLEDKYGVKLIYNPDYAE-Y 80

                          90       100
                  ....*....|....*....|....*
gi 1253325054  85 ETGGGLIHARPLLGDKpFICaNSDN 109
Cdd:COG4750    81 NNISSLYLVRDKLGNT-YIC-SSDN 103
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
9-110 2.68e-11

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 61.64  E-value: 2.68e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253325054   9 AAGLGKRMRPLTATRPKPLVKVAGKALMDHALDRLAAGGIK--TVVVNVHYLADtVEAHLRTRKDMDFRIS----DERAk 82
Cdd:COG1209     7 AGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIReiLIISTPEDGPQ-FERLLGDGSQLGIKISyavqPEPL- 84

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1253325054  83 lletggGLIHA----RPLLGDKPFICANSDNL 110
Cdd:COG1209    85 ------GLAHAfiiaEDFIGGDPVALVLGDNI 110
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 8-107 3.61e-11

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: 60.61  E-value: 3.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253325054   8 MAAGLGKRMRpltATRPKPLVKVAGKALMDHALDRLAAGGIKTVVVNVHYLADTVEAHLrTRKDMDFRISDERaklLETG 87
Cdd:cd02540     4 LAAGKGTRMK---SDLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVKKAL-ANPNVEFVLQEEQ---LGTG 76

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1253325054  88 GGLIHARPLL-----------GDKPFICANS 107
Cdd:cd02540    77 HAVKQALPALkdfegdvlvlyGDVPLITPET 107
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-100 5.19e-11

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 61.77  E-value: 5.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253325054   1 MINTAMLMAAGLGKRMRpltATRPKPLVKVAGKALMDHALDRLAAGGIKTVVVNVHYLADTVEAHLRTRKDMDFrisdeR 80
Cdd:PRK14354    1 MNRYAIILAAGKGTRMK---SKLPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVGHGAEEVKEVLGDRSEFAL-----Q 72

                          90       100
                  ....*....|....*....|
gi 1253325054  81 AKLLETGGGLIHARPLLGDK 100
Cdd:PRK14354   73 EEQLGTGHAVMQAEEFLADK 92
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 8-66 2.00e-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: 59.65  E-value: 2.00e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1253325054   8 MAAGLGKRMRpltATRPKPLVKVAGKALMDHALDRLAAGGIKTVVVNVHYLADTVEAHL 66
Cdd:COG1207     8 LAAGKGTRMK---SKLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVRAAL 63
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-123 3.71e-10

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 59.11  E-value: 3.71e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253325054   4 TAMLMAAGLGKRMRpltATRPKPLVKVAGKALMDHALDRLAAGGIKTVVVNVHYLADTVEAHLRT-RKDMDFRISDERak 82
Cdd:PRK14353    7 LAIILAAGEGTRMK---SSLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGPGAEAVAAAAAKiAPDAEIFVQKER-- 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1253325054  83 lLETGGGLIHARPLL-----------GDKPFIcansdnlwidgPAETLGMMQ 123
Cdd:PRK14353   82 -LGTAHAVLAAREALaggygdvlvlyGDTPLI-----------TAETLARLR 121
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 5-70 3.87e-10

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: 57.65  E-value: 3.87e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1253325054   5 AMLMAAGLGKRMRPLTATRPKPLVKVAGKALMDHALDRLAAGGIKT--VVVNVHylADTVEAHLRTRK 70
Cdd:cd02507     3 AVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEvfVVCCEH--SQAIIEHLLKSK 68
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
1-119 1.21e-09

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 57.21  E-value: 1.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253325054   1 MIN-TAMLMAAGLGKRMRPLTATRPKPLVKVAGKALMDHALDRLAAGGIKTVVVNVHYLADTVEAHLRTRKDMD----FR 75
Cdd:PRK10122    1 MTNlKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAVENHFDTSYELEslleQR 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1253325054  76 ISDE-------------------RAKLLETGGGLIHARPLLGDKPFICANSDNLWIDGPAETL 119
Cdd:PRK10122   81 VKRQllaevqsicppgvtimnvrQGQPLGLGHSILCARPAIGDNPFVVVLPDVVIDDASADPL 143
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 8-181 1.95e-08

GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP:adenosylcobinamide-phosphate guanylyltransferase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441867 [Multi-domain]  Cd Length: 185  Bit Score: 52.58  E-value: 1.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253325054   8 MAAGLGKRMRPltatRPKPLVKVAGKALMDHALDRLAAGGIKTVVVNVhyladtVEAHLRTRKdmdfRISDERAKLLETG 87
Cdd:COG2266     1 MAGGKGTRLGG----GEKPLLEICGKPMIDRVIDALEESCIDKIYVAV------SPNTPKTRE----YLKERGVEVIETP 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253325054  88 GG-----LIHA-----RPLL---GDKPFIcansdnlwidgPAETLGMMQRLWDPERMDALLLLVPLARANCHSGPGDFHM 154
Cdd:COG2266    67 GEgyvedLNEAlesisGPVLvvpADLPLL-----------TPEIIDDIIDAYLESGKPSLTVVVPAALKRELGVSPDTTF 135

                         170       180
                  ....*....|....*....|....*..
gi 1253325054 155 DANGRLarrktahvapfVFTGVQILSP 181
Cdd:COG2266   136 EIDGEL-----------VPTGINIVDG 151
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
 5-73 2.59e-08

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: 52.16  E-value: 2.59e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253325054   5 AMLMAAGLGKRMRPLTATRPKPLVKVAGKA-LMDHALDRLAAGGIKTVVVNVHYLADTVEAHLRTRKDMD 73
Cdd:cd02508     1 AIILAGGEGTRLSPLTKKRAKPAVPFGGRYrLIDFPLSNMVNSGIRNVGVLTQYKSRSLNDHLGSGKEWD 70
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 5-70 8.80e-08

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: 51.07  E-value: 8.80e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1253325054   5 AMLMAAGLGKRMRPLTATRPKPLVKVAGKALMDHALDRLAAGGIKTVVVNVHYLADTVEAHLRTRK 70
Cdd:cd04197     3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQIKEYIEKSK 68
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
4-67 2.75e-07

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 49.39  E-value: 2.75e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1253325054   4 TAMLMAAGLGKRMRpltatRPKPLVKVAGKALMDHALDRLAAGGIKTVVVNVHYLADTVEAHLR 67
Cdd:COG2068     5 AAIILAAGASSRMG-----RPKLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADAEEVAAALA 63
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 5-68 3.71e-07

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 50.21  E-value: 3.71e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1253325054   5 AMLMAAGLGKRMRPLTATRPKPLVKVAGK-ALMDHALDRLAAGGIKTVVVNVHYLADTVEAHLRT 68
Cdd:PRK00844    8 AIVLAGGEGKRLMPLTADRAKPAVPFGGSyRLIDFVLSNLVNSGYLRIYVLTQYKSHSLDRHISQ 72
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 5-79 1.22e-06

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: 47.65  E-value: 1.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253325054   5 AMLMAAGLGKRMRPLTATRPKPLVKVAGKALMDHALDRLAAGGIKTVVVNV---------HYLADTVEAHLRtRKDMDFR 75
Cdd:cd04198     3 AVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVpeeeqaeisTYLRSFPLNLKQ-KLDEVTI 81


                  ....
gi 1253325054  76 ISDE 79
Cdd:cd04198    82 VLDE 85
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 5-75 1.26e-06

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 48.53  E-value: 1.26e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1253325054   5 AMLMAAGLGKRMRPLTATRPKPLVKVAGKA-LMDHALDRLAAGGIKTVVVNVHYLADTVEAHLRTRKDMDFR 75
Cdd:COG0448     4 AIILAGGRGSRLGPLTKDRAKPAVPFGGKYrIIDFPLSNCVNSGIRRVGVLTQYKSHSLNDHIGSGKPWDLD 75
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 4-102 2.85e-06

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: 47.14  E-value: 2.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253325054   4 TAMLMAAGLGKRMRPLTATRPKPLVKVAGKALMDHALDRLAAGGIKTVVVNVHYLADTVEAH----------LRTRKDMD 73
Cdd:cd02541     2 KAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRGKRAIEDHfdrsyeleetLEKKGKTD 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1253325054  74 F----RISDERAKL--------LETGGGLIHARPLLGDKPF 102
Cdd:cd02541    82 LleevRIISDLANIhyvrqkepLGLGHAVLCAKPFIGDEPF 122
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 3-56 3.54e-06

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


Pssm-ID: 133009 [Multi-domain]  Cd Length: 218  Bit Score: 46.36  E-value: 3.54e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1253325054   3 NTAMLMAAGLGKRMRpltATRPKPLVKVAGKALMDHALDRLAA-GGIKTVVVNVH 56
Cdd:cd02516     1 VAAIILAAGSGSRMG---ADIPKQFLELGGKPVLEHTLEAFLAhPAIDEIVVVVP 52
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 7-97 3.57e-06

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: 46.28  E-value: 3.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253325054   7 LMAAGLGKRMRpltATRPKPLVKVAGKALMDHALDRLAA-GGIKTVVVNVH-----YLADTVEAHLRTRkdmdfRIS--- 77
Cdd:COG1211     2 IPAAGSGSRMG---AGIPKQFLPLGGKPVLEHTLEAFLAhPRIDEIVVVVPpddieYFEELLAKYGIDK-----PVRvva 73

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1253325054  78 --DERA-------KLLETGGG--LIH--ARPLL 97
Cdd:COG1211    74 ggATRQdsvrnglEALPDDDDwvLVHdaARPLV 106
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 13-108 8.14e-06

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: 45.71  E-value: 8.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253325054  13 GKRMRPLTATRPKPLVKVAGKALMDHALDRLAA-GGIKTVVVNVHY----LADTVEAhlrTRKDMDFRISDERA-KLLET 86
Cdd:cd06428    11 GTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKvPDLKEVLLIGFYpesvFSDFISD---AQQEFNVPIRYLQEyKPLGT 87

                          90       100
                  ....*....|....*....|....*.
gi 1253325054  87 GGGLIHARP-LLGDKP---FICaNSD 108
Cdd:cd06428    88 AGGLYHFRDqILAGNPsafFVL-NAD 112
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
2-101 3.58e-05

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 43.74  E-value: 3.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253325054   2 INTAMLMAAGLGKRMRPLTATRPKPLVKVAGKALMDHALDRLAAGGIKTVVVNVHYLADTVEAHLRTRKDMDfRISDERA 81
Cdd:PRK13389    8 VKKAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFDTSFELE-AMLEKRV 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1253325054  82 K--LLET------------------GGGLIH----ARPLLGDKP 101
Cdd:PRK13389   87 KrqLLDEvqsicpphvtimqvrqglAKGLGHavlcAHPVVGDEP 130
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 5-67 5.33e-05

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 43.77  E-value: 5.33e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1253325054   5 AMLMAAGLGKRMRpltATRPKPLVKVAGKALMDHALDRLAAGGIKTVVVNVHYLADTVEAHLR 67
Cdd:PRK14352    7 VIVLAAGAGTRMR---SDTPKVLHTLAGRSMLGHVLHAAAGLAPQHLVVVVGHDRERVAPAVA 66
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 4-67 1.06e-04

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


Pssm-ID: 133025 [Multi-domain]  Cd Length: 186  Bit Score: 41.78  E-value: 1.06e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1253325054   4 TAMLMAAGLGKRMRpltatRPKPLVKVAGKALMDHALDRLAAGGIKTVVVNVHYLADTVEAHLR 67
Cdd:cd04182     2 AAIILAAGRSSRMG-----GNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALA 60
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
 5-53 2.47e-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: 41.02  E-value: 2.47e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1253325054   5 AMLMAAGLGKRMRPLTATRPKPLVKVAGKALMDHALDRLAAGGIKTVVV 53
Cdd:cd02524     1 VVILAGGLGTRLSEETELKPKPMVEIGGRPILWHIMKIYSHYGHNDFIL 49
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
5-97 3.54e-04

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 40.50  E-value: 3.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253325054   5 AMLMAAGLGKRMRpltATRPKPLVKVAGKALMDHALDR-LAAGGIKT--VVVNVHYLADTVEAHLRTRKDMDFRIS-DER 80
Cdd:PRK00155    6 AIIPAAGKGSRMG---ADRPKQYLPLGGKPILEHTLEAfLAHPRIDEiiVVVPPDDRPDFAELLLAKDPKVTVVAGgAER 82

                          90       100
                  ....*....|....*....|....*..
gi 1253325054  81 AK-----LLETGGG---LIH--ARPLL 97
Cdd:PRK00155   83 QDsvlngLQALPDDdwvLVHdaARPFL 109
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 5-55 5.75e-04

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: 39.10  E-value: 5.75e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1253325054   5 AMLMAAGLGKRMRpltatRPKPLVKVAGKALMDHALDRLAAGGiKTVVVNV 55
Cdd:pfam12804   1 AVILAGGRSSRMG-----GDKALLPLGGKPLLERVLERLRPAG-DEVVVVA 45
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
 1-67 8.57e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 39.82  E-value: 8.57e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1253325054   1 MINT-AMLMAAGLGKRMRPLTATRPKPLVKVAGKA-LMDHALDRLAAGGIKTVVVNVHYLADTVEAHLR 67
Cdd:PRK00725   13 TRDTlALILAGGRGSRLKELTDKRAKPAVYFGGKFrIIDFALSNCINSGIRRIGVLTQYKAHSLIRHIQ 81
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 7-107 1.42e-03

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 39.20  E-value: 1.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253325054   7 LMAAGLGKRMRpltATRPKPLVKVAGKALMDHALDrlAAGGIKT-VVVNVHYLADTVEAHLRTR-KDMDFRISDeRAKLL 84
Cdd:PRK14359    7 ILAAGKGTRMK---SSLPKVLHTICGKPMLFYILK--EAFAISDdVHVVLHHQKERIKEAVLEYfPGVIFHTQD-LENYP 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1253325054  85 ETGGGLIHARP-------LLGDKPFICANS 107
Cdd:PRK14359   81 GTGGALMGIEPkhervliLNGDMPLVEKDE 110
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 5-53 1.53e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 39.08  E-value: 1.53e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1253325054   5 AMLMAAGLGKRMRPLTATRPKPLVKVAGK-ALMDHALDRLAAGGIKTVVV 53
Cdd:PRK05293    6 AMILAGGQGTRLGKLTKNIAKPAVPFGGKyRIIDFTLSNCANSGIDTVGV 55
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 5-107 1.68e-03

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 38.98  E-value: 1.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253325054   5 AMLMAAGLGKRMRpltATRPKPLVKVAGKALMDHALDRLAAGGIKTVVVnVHYLADTVEAHLrtRKDMDFRISDERaklL 84
Cdd:PRK14357    3 ALVLAAGKGTRMK---SKIPKVLHKISGKPMINWVIDTAKKVAQKVGVV-LGHEAELVKKLL--PEWVKIFLQEEQ---L 73

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1253325054  85 ETGGGLIHARP----------LLGDKPFICANS 107
Cdd:PRK14357   74 GTAHAVMCARDfiepgddlliLYGDVPLISENT 106
IspD pfam01128
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ...
 5-56 3.77e-03

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


Pssm-ID: 460075  Cd Length: 219  Bit Score: 37.43  E-value: 3.77e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1253325054   5 AMLMAAGLGKRMRpltATRPKPLVKVAGKALMDHALDRLAA-GGIKTVVVNVH 56
Cdd:pfam01128   1 AVIPAAGSGKRMG---AGVPKQFLQLLGQPLLEHTVDAFLAsPVVDRIVVAVS 50
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
 6-45 5.41e-03

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: 36.85  E-value: 5.41e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1253325054   6 MLMAaGLGKRMRPLTATRPKPLVKVAGKALMDHALDRLAA 45
Cdd:cd04183     3 IPMA-GLGSRFKKAGYTYPKPLIEVDGKPMIEWVIESLAK 41
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-138 6.13e-03

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 37.31  E-value: 6.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253325054   1 MINTAM---LMAAGLGKRMRpltATRPKPLVKVAGKALMDHALDRLAAGGIKtvvvNVHYL----ADTVEAHLrtrkdmd 73
Cdd:PRK09451    1 MLNSAMsvvILAAGKGTRMY---SDLPKVLHTLAGKPMVQHVIDAANELGAQ----HVHLVyghgGDLLKQTL------- 66

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1253325054  74 friSDE------RAKLLETGGGLIHARPLLGDKPFICAnsdnLWIDGP---AETLgmmQRLWD--PERMDALLLLV 138
Cdd:PRK09451   67 ---ADEplnwvlQAEQLGTGHAMQQAAPFFADDEDILM----LYGDVPlisVETL---QRLRDakPQGGIGLLTVK 132
 
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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