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Conserved domains on  [gi|647818525|gb|AIC10640|]
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mannose-1-phosphate guanylyltransferase [Xylella fastidiosa subsp. sandyi Ann-1]

Protein Classification

NDP-sugar synthase( domain architecture ID 11440233)

NDP-sugar synthase such as mannose-1-phosphate guanyltransferase and UTP--glucose-1-phosphate uridylyltransferase, which catalyzes the formation of UDP-glucose from UTP and glucose 1-phosphate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 2-235 4.57e-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: 4.57e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647818525   2 KALIFAAGIGQRMRPLTNYTPKPLLCAGGEPLIVWNLRKLAALGISEVVINTAWLGEQFPEILGDGQRFGLRLFYSNEGS 81
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRFGVRITYVDEGE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647818525  82 lPLETGGGMLHALPLLGNAPFLAINGDIWTDADLTRL---PTEPVGDAHLMLVNNPEYHPQGDFVLQADSSVLD----RT 154
Cdd:COG1208   81 -PLGTGGALKRALPLLGDEPFLVLNGDILTDLDLAALlafHREKGADATLALVPVPDPSRYGVVELDGDGRVTRfvekPE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647818525 155 PGIPTLTFAGLGIYRSQLLADWRniigdtpdthaQPPRFKLAPLLRAAMRSGRIHGTHHRGQWTDVGTPQRLHALDTWLR 234
Cdd:COG1208  160 EPPSNLINAGIYVLEPEIFDYIP-----------EGEPFDLEDLLPRLIAEGRVYGYVHDGYWLDIGTPEDLLEANALLL 228


                 .
gi 647818525 235 S 235
Cdd:COG1208  229 S 229
 
Name Accession Description Interval E-value
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 2-235 4.57e-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: 4.57e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647818525   2 KALIFAAGIGQRMRPLTNYTPKPLLCAGGEPLIVWNLRKLAALGISEVVINTAWLGEQFPEILGDGQRFGLRLFYSNEGS 81
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRFGVRITYVDEGE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647818525  82 lPLETGGGMLHALPLLGNAPFLAINGDIWTDADLTRL---PTEPVGDAHLMLVNNPEYHPQGDFVLQADSSVLD----RT 154
Cdd:COG1208   81 -PLGTGGALKRALPLLGDEPFLVLNGDILTDLDLAALlafHREKGADATLALVPVPDPSRYGVVELDGDGRVTRfvekPE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647818525 155 PGIPTLTFAGLGIYRSQLLADWRniigdtpdthaQPPRFKLAPLLRAAMRSGRIHGTHHRGQWTDVGTPQRLHALDTWLR 234
Cdd:COG1208  160 EPPSNLINAGIYVLEPEIFDYIP-----------EGEPFDLEDLLPRLIAEGRVYGYVHDGYWLDIGTPEDLLEANALLL 228


                 .
gi 647818525 235 S 235
Cdd:COG1208  229 S 229
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 2-229 8.73e-76

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: 228.61  E-value: 8.73e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647818525   2 KALIFAAGIGQRMRPLTNYTPKPLLCAGGEPLIVWNLRKLAALGISEVVINTAWLGEQFPEILGDgQRFGLRLFYSNEGS 81
Cdd:cd06422    1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHLGD-SRFGLRITISDEPD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647818525  82 LPLETGGGMLHALPLLGNAPFLAINGDIWTDADLTRLPTE-----PVGDAHLMLVNNPEYHPQGDFVLQADSSVLDRTPG 156
Cdd:cd06422   80 ELLETGGGIKKALPLLGDEPFLVVNGDILWDGDLAPLLLLhawrmDALLLLLPLVRNPGHNGVGDFSLDADGRLRRGGGG 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 647818525 157 IPT-LTFAGLGIYRSQLLADwrniigdtpdthAQPPRFKLAPLLRAAMRSGRIHGTHHRGQWTDVGTPQRLHAL 229
Cdd:cd06422  160 AVApFTFTGIQILSPELFAG------------IPPGKFSLNPLWDRAIAAGRLFGLVYDGLWFDVGTPERLLAA 221
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 1-223 1.77e-25

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: 102.67  E-value: 1.77e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647818525    1 MKALIFAAGIGQRMRPLTNYTPKPLLCAGGEPLIVWNLRKLAALGISEVVINTAWLGEQFPEILGDGQRFGLRLFYSNEG 80
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEKVREYFGDGSRGGVPIEYVVQE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647818525   81 SlPLETGGGMLHALPLLgNAPFLAINGDIWTD-ADLTRLPTEPvgdAHLML---VNNPEyhpqgDF-VLQAD----SSVL 151
Cdd:TIGR03992  81 E-QLGTADALGSAKEYV-DDEFLVLNGDVLLDsDLLERLIRAE---APAIAvveVDDPS-----DYgVVETDggrvTGIV 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 647818525  152 DRtPGIPTLTFAGLGIYRsqLLADWRNIIGDTPDThaqpPR--FKLAPLLRAAMRSGRIHGTHHRGQWTDVGTP 223
Cdd:TIGR03992 151 EK-PENPPSNLINAGIYL--FSPEIFELLEKTKLS----PRgeYELTDALQLLIDEGKVKAVELDGFWLDVGRP 217
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-118 1.30e-12

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: 64.97  E-value: 1.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647818525    2 KALIFAAGIGQRMRPLTNYTPKPL-LCAGGEPLIVWNLRKLAALGISE-VVINTAWLGEQFPEILGDGQRFGLRLFYSNE 79
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLvPVGGKYPLIDYPLSRLANAGIREiIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 647818525   80 GSlPLETGGGMLHALPLLGN--APFLAINGDIWTDADLTRL 118
Cdd:pfam00483  81 PE-GKGTAPAVALAADFLGDekSDVLVLGGDHIYRMDLEQA 120
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 2-226 1.47e-09

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 56.99  E-value: 1.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647818525   2 KALIFAAGIGQRMRPLTNYTPKPLLCAGGEPLIVWNLRKLAALGISEV-VINTAWLGEQFPEILGDGQRFGLRLFYSNEG 80
Cdd:PRK15480   5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDIlIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647818525  81 SlPLETGGGMLHALPLLGNAPFLAINGD-IWTDADLTRLPTEPV-----GDAHLMLVNNPEYHPQGDFVLQADSSVLDRT 154
Cdd:PRK15480  85 S-PDGLAQAFIIGEEFIGGDDCALVLGDnIFYGHDLPKLMEAAVnkesgATVFAYHVNDPERYGVVEFDQNGTAISLEEK 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 647818525 155 PGIPTLTFA--GLGIYRSQLLADWRNIigdTPDTHAQpprFKLAPLLRAAMRSGRIH-GTHHRG-QWTDVGTPQRL 226
Cdd:PRK15480 164 PLQPKSNYAvtGLYFYDNDVVEMAKNL---KPSARGE---LEITDINRIYMEQGRLSvAMMGRGyAWLDTGTHQSL 233
 
Name Accession Description Interval E-value
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 2-235 4.57e-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: 4.57e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647818525   2 KALIFAAGIGQRMRPLTNYTPKPLLCAGGEPLIVWNLRKLAALGISEVVINTAWLGEQFPEILGDGQRFGLRLFYSNEGS 81
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRFGVRITYVDEGE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647818525  82 lPLETGGGMLHALPLLGNAPFLAINGDIWTDADLTRL---PTEPVGDAHLMLVNNPEYHPQGDFVLQADSSVLD----RT 154
Cdd:COG1208   81 -PLGTGGALKRALPLLGDEPFLVLNGDILTDLDLAALlafHREKGADATLALVPVPDPSRYGVVELDGDGRVTRfvekPE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647818525 155 PGIPTLTFAGLGIYRSQLLADWRniigdtpdthaQPPRFKLAPLLRAAMRSGRIHGTHHRGQWTDVGTPQRLHALDTWLR 234
Cdd:COG1208  160 EPPSNLINAGIYVLEPEIFDYIP-----------EGEPFDLEDLLPRLIAEGRVYGYVHDGYWLDIGTPEDLLEANALLL 228


                 .
gi 647818525 235 S 235
Cdd:COG1208  229 S 229
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 2-229 8.73e-76

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: 228.61  E-value: 8.73e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647818525   2 KALIFAAGIGQRMRPLTNYTPKPLLCAGGEPLIVWNLRKLAALGISEVVINTAWLGEQFPEILGDgQRFGLRLFYSNEGS 81
Cdd:cd06422    1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHLGD-SRFGLRITISDEPD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647818525  82 LPLETGGGMLHALPLLGNAPFLAINGDIWTDADLTRLPTE-----PVGDAHLMLVNNPEYHPQGDFVLQADSSVLDRTPG 156
Cdd:cd06422   80 ELLETGGGIKKALPLLGDEPFLVVNGDILWDGDLAPLLLLhawrmDALLLLLPLVRNPGHNGVGDFSLDADGRLRRGGGG 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 647818525 157 IPT-LTFAGLGIYRSQLLADwrniigdtpdthAQPPRFKLAPLLRAAMRSGRIHGTHHRGQWTDVGTPQRLHAL 229
Cdd:cd06422  160 AVApFTFTGIQILSPELFAG------------IPPGKFSLNPLWDRAIAAGRLFGLVYDGLWFDVGTPERLLAA 221
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 3-221 1.51e-39

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: 135.79  E-value: 1.51e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647818525   3 ALIFAAGIGQRMRPLTNYTPKPLLCAGGEPLIVWNLRKLAALGISEVVINTAWLGEQFPEILGDGQRFGLRLFYSNEGSl 82
Cdd:cd04181    1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGSKFGVNIEYVVQEE- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647818525  83 PLETGGGMLHALPLLGNAPFLAINGDIWTDADLTRLPTEPV-GDAHLMLVNNPEYHPQ--GDFVLQADSSVLD--RTPGI 157
Cdd:cd04181   80 PLGTAGAVRNAEDFLGDDDFLVVNGDVLTDLDLSELLRFHReKGADATIAVKEVEDPSryGVVELDDDGRVTRfvEKPTL 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 647818525 158 PTLTFAGLGIYrsqlLADwRNIIGDTPDTHAQPPRFkLAPLLRAAMRSGRIHGTHHRGQWTDVG 221
Cdd:cd04181  160 PESNLANAGIY----IFE-PEILDYIPEILPRGEDE-LTDAIPLLIEEGKVYGYPVDGYWLDIG 217
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 3-224 6.95e-32

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: 116.11  E-value: 6.95e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647818525   3 ALIFAAGIGQRMRPLTNYTPKPLLCAGGEPLIVWNLRKLAALGISEVVINTAWLGEQFPEILGDGQRFGLRLFYSNEGSl 82
Cdd:cd06915    1 AVILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYLAEQIEEYFGDGYRGGIRIYYVIEPE- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647818525  83 PLETGGGMLHALPLLGNAPFLAINGDIWTDADLTRLPT---EPVGDAHLMLVNNPEYHPQGDFVLQADSSVL-----DRT 154
Cdd:cd06915   80 PLGTGGAIKNALPKLPEDQFLVLNGDTYFDVDLLALLAalrASGADATMALRRVPDASRYGNVTVDGDGRVIafvekGPG 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647818525 155 PGiPTLTFAGLGIYRSQLLADWrniigdtpdthAQPPRFKLAPLLRAAMRSGRIHGTHHRGQWTDVGTPQ 224
Cdd:cd06915  160 AA-PGLINGGVYLLRKEILAEI-----------PADAFSLEADVLPALVKRGRLYGFEVDGYFIDIGIPE 217
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 1-226 2.49e-29

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: 109.97  E-value: 2.49e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647818525   1 MKALIFAAGIGQRMRPLTNYTPKPLLCAGGEPLIVWNLRKLAALGISEVVINTAWLGEQFPEILGDGQRFGLRLFYSNEG 80
Cdd:cd04189    1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEALGDGSRFGVRITYILQE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647818525  81 SlPLETGGGMLHALPLLGNAPFLAINGDIWTDADLTRLPTEPV---GDAHLML--VNNPEYHpqGDFVLQADSSV-LDRT 154
Cdd:cd04189   81 E-PLGLAHAVLAARDFLGDEPFVVYLGDNLIQEGISPLVRDFLeedADASILLaeVEDPRRF--GVAVVDDGRIVrLVEK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647818525 155 PGIPTLTFAGLGIYR---------SQLLADWRniiGDTPDTHAqpprfklapLLRAAMRSGRIHGTHHRGQWTDVGTPQR 225
Cdd:cd04189  158 PKEPPSNLALVGVYAftpaifdaiSRLKPSWR---GELEITDA---------IQWLIDRGRRVGYSIVTGWWKDTGTPED 225


                 .
gi 647818525 226 L 226
Cdd:cd04189  226 L 226
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 1-223 1.77e-25

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: 102.67  E-value: 1.77e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647818525    1 MKALIFAAGIGQRMRPLTNYTPKPLLCAGGEPLIVWNLRKLAALGISEVVINTAWLGEQFPEILGDGQRFGLRLFYSNEG 80
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEKVREYFGDGSRGGVPIEYVVQE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647818525   81 SlPLETGGGMLHALPLLgNAPFLAINGDIWTD-ADLTRLPTEPvgdAHLML---VNNPEyhpqgDF-VLQAD----SSVL 151
Cdd:TIGR03992  81 E-QLGTADALGSAKEYV-DDEFLVLNGDVLLDsDLLERLIRAE---APAIAvveVDDPS-----DYgVVETDggrvTGIV 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 647818525  152 DRtPGIPTLTFAGLGIYRsqLLADWRNIIGDTPDThaqpPR--FKLAPLLRAAMRSGRIHGTHHRGQWTDVGTP 223
Cdd:TIGR03992 151 EK-PENPPSNLINAGIYL--FSPEIFELLEKTKLS----PRgeYELTDALQLLIDEGKVKAVELDGFWLDVGRP 217
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 3-223 7.22e-25

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: 97.58  E-value: 7.22e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647818525   3 ALIFAAGIGQRMRPLTNYTPKPLLCAGGEPLIVWNLRKLAALGISEVVINTAWLGEQFPEILGDGQRFGLRLFYSNEGSl 82
Cdd:cd06426    1 VVIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNYLAEMIEDYFGDGSKFGVNISYVREDK- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647818525  83 PLETGGGmLHALPLLGNAPFLAINGDIwtdadLTRLPTEPVGDAHL-------MLVNNPEYH-PQGdfVLQADSSVLDrt 154
Cdd:cd06426   80 PLGTAGA-LSLLPEKPTDPFLVMNGDI-----LTNLNYEHLLDFHKennadatVCVREYEVQvPYG--VVETEGGRIT-- 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 647818525 155 pGI---PTLTF-AGLGIYrsqLLAdwRNIIGDTPDTHaqppRFKLAPLLRAAMRSGRIHGTH-HRGQWTDVGTP 223
Cdd:cd06426  150 -SIeekPTHSFlVNAGIY---VLE--PEVLDLIPKNE----FFDMPDLIEKLIKEGKKVGVFpIHEYWLDIGRP 213
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 3-122 4.53e-19

Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family contains proteins similar to prokaryotic phosphocholine (P-cho) cytidylyltransferases. Phosphocholine (PC) cytidylyltransferases catalyze the transfer of a cytidine monophosphate from CTP to phosphocholine to form CDP-choline. PC is the most abundant phospholipid in eukaryotic membranes and it is also important in prokaryotic membranes. For pathogenic prokaryotes, the cell surface PC facilitates the interaction with host surface and induces attachment and invasion. In addition cell wall PC serves as scaffold for a group of choline-binding proteins that are secreted from the cells. Phosphocholine (PC) cytidylyltransferase is a key enzyme in the prokaryotic choline metabolism pathway. It has been hypothesized to consist of a choline transport system, a choline kinase, CTP:phosphocholine cytidylyltransferase, and a choline phosphotransferase that transfers P-Cho from CDP-Cho to either lipoteichoic acid or lipopolysaccharide.


Pssm-ID: 133014 [Multi-domain]  Cd Length: 229  Bit Score: 82.67  E-value: 4.53e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647818525   3 ALIFAAGIGQRMRPLTNYTPKPLLCAGGEPLIVWNLRKLAALGISEVVINTAWLGEQFPEILGDgqRFGLRLFYSnegSL 82
Cdd:cd02523    1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKK--YPNIKFVYN---PD 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 647818525  83 PLETG--GGMLHALPLLGNaPFLAINGDIWTDAD-LTRLPTEP 122
Cdd:cd02523   76 YAETNniYSLYLARDFLDE-DFLLLEGDVVFDPSiLERLLSSP 117
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-135 3.07e-18

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 81.29  E-value: 3.07e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647818525   1 MKALIFAAGIGQRMRPLTNYTPKPLLCAGGEPLIVWNLRKLAALGISEV-VINTAWLGEQFPEILGDGQRFGLRLFYSNE 79
Cdd:COG1209    1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREIlIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 647818525  80 GSlPLetggGMLHAL----PLLGNAPFLAINGD-IWTDADLTRLPTEPV---GDAHLML--VNNPE 135
Cdd:COG1209   81 PE-PL----GLAHAFiiaeDFIGGDPVALVLGDnIFYGDGLSELLREAAareSGATIFGykVEDPE 141
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
2-109 5.95e-18

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 79.51  E-value: 5.95e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647818525   2 KALIFAAGIGQRMRPLTNYTPKPLLCAGGEPLIVWNLRKLAALGISEVVINTAWLGEQFPEILGDGqRFGLRLFYsNEgs 81
Cdd:COG1213    1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEALARP-GPDVTFVY-NP-- 76

                         90       100       110
                 ....*....|....*....|....*....|
gi 647818525  82 LPLETGGG--MLHALPLLgNAPFLAINGDI 109
Cdd:COG1213   77 DYDETNNIysLWLAREAL-DEDFLLLNGDV 105
LicC COG4750
CTP:phosphocholine cytidylyltransferase LicC [Cell wall/membrane/envelope biogenesis, Lipid ...
 1-110 2.07e-15

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


Pssm-ID: 443784 [Multi-domain]  Cd Length: 228  Bit Score: 72.55  E-value: 2.07e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647818525   1 MKALIFAAGIGQRMRPLTNYTPKPLLCAGGEPLIVWNLRKLAALGISEVVINTAWLGEQFpEILGDgqRFGLRLFYSNE- 79
Cdd:COG4750    1 MNAIILAAGLGSRFAPITYETPKGLLKVNGEPLIERQIRQLHEAGITDITVVVGYLKEQF-EYLED--KYGVKLIYNPDy 77

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 647818525  80 ------GSLpletgggmLHALPLLGNApfLAINGDIW 110
Cdd:COG4750   78 aeynniSSL--------YLVRDKLGNT--YICSSDNY 104
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 1-112 4.71e-13

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: 66.08  E-value: 4.71e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647818525   1 MKALIFAAGIGQRMRPLTNYTPKPLLCAGGEPLIVWNLRKLAALGISEVVINTAWLGEQFPEILGD-GQRFGLRLFYSNE 79
Cdd:cd06425    1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYRPEDMVPFLKEyEKKLGIKITFSIE 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 647818525  80 gSLPLETGGGMLHALPLLG--NAPFLAINGDIWTD 112
Cdd:cd06425   81 -TEPLGTAGPLALARDLLGddDEPFFVLNSDVICD 114
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-118 1.30e-12

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: 64.97  E-value: 1.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647818525    2 KALIFAAGIGQRMRPLTNYTPKPL-LCAGGEPLIVWNLRKLAALGISE-VVINTAWLGEQFPEILGDGQRFGLRLFYSNE 79
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLvPVGGKYPLIDYPLSRLANAGIREiIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 647818525   80 GSlPLETGGGMLHALPLLGN--APFLAINGDIWTDADLTRL 118
Cdd:pfam00483  81 PE-GKGTAPAVALAADFLGDekSDVLVLGGDHIYRMDLEQA 120
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 1-135 2.02e-11

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: 61.82  E-value: 2.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647818525   1 MKALIFAAGIGQRMRPLTNYTPKPLLCAGGEPLIVWNLRKLAALGISEV-VINTAWLGEQFPEILGDGQRFGLRLFYSNE 79
Cdd:cd02538    1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREIlIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 647818525  80 gslplETGGGMLHALPL----LGNAPFLAINGD-IWTDADLT----RLPTEPVGdAHLML--VNNPE 135
Cdd:cd02538   81 -----PKPGGLAQAFIIgeefIGDDPVCLILGDnIFYGQGLSpilqRAAAQKEG-ATVFGyeVNDPE 141
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 2-226 1.47e-09

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 56.99  E-value: 1.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647818525   2 KALIFAAGIGQRMRPLTNYTPKPLLCAGGEPLIVWNLRKLAALGISEV-VINTAWLGEQFPEILGDGQRFGLRLFYSNEG 80
Cdd:PRK15480   5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDIlIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647818525  81 SlPLETGGGMLHALPLLGNAPFLAINGD-IWTDADLTRLPTEPV-----GDAHLMLVNNPEYHPQGDFVLQADSSVLDRT 154
Cdd:PRK15480  85 S-PDGLAQAFIIGEEFIGGDDCALVLGDnIFYGHDLPKLMEAAVnkesgATVFAYHVNDPERYGVVEFDQNGTAISLEEK 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 647818525 155 PGIPTLTFA--GLGIYRSQLLADWRNIigdTPDTHAQpprFKLAPLLRAAMRSGRIH-GTHHRG-QWTDVGTPQRL 226
Cdd:PRK15480 164 PLQPKSNYAvtGLYFYDNDVVEMAKNL---KPSARGE---LEITDINRIYMEQGRLSvAMMGRGyAWLDTGTHQSL 233
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 11-134 3.55e-09

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: 55.34  E-value: 3.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647818525  11 GQRMRPLTNYTPKPLLCAGGEPLIVWNLRKLAAL-GISEVVINTAWLGEQFPEILGDGQR-FGLRLFYSNEGSlPLETGG 88
Cdd:cd06428   11 GTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKVpDLKEVLLIGFYPESVFSDFISDAQQeFNVPIRYLQEYK-PLGTAG 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 647818525  89 GMLH--ALPLLGNaP--FLAINGDIWTDADLTRLPT--EPVGDAHLMLVNNP 134
Cdd:cd06428   90 GLYHfrDQILAGN-PsaFFVLNADVCCDFPLQELLEfhKKHGASGTILGTEA 140
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 1-51 7.28e-09

The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; N-terminal domain of eEIF-2B epsilon and gamma, subunits of eukaryotic translation initiators, is a subfamily of glycosyltranferase 2 and is predicted to have glycosyltranferase activity. eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit epsilon shares sequence similarity with gamma subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.


Pssm-ID: 133001 [Multi-domain]  Cd Length: 216  Bit Score: 54.18  E-value: 7.28e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 647818525   1 MKALIFAAGIGQRMRPLTNYTPKPLLCAGGEPLIVWNLRKLAALGISEVVI 51
Cdd:cd02507    1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFV 51
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 1-78 1.63e-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: 53.05  E-value: 1.63e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 647818525   1 MKALIFAAGIGQRMRPLTNYTPKPLLCAGGEPLIVWNLRKLAALGISEVVINTawlgeqfPEILGDGQRFGLRLFYSN 78
Cdd:cd04198    1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVV-------PEEEQAEISTYLRSFPLN 71
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 3-109 2.72e-06

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: 46.74  E-value: 2.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647818525   3 ALIFAAGIGQRMRplTNYtPKPLLCAGGEPLIVWNLRKLAALGISEVVINTAWLGEQFPEILGDgqrFGLRLFYSNEgsl 82
Cdd:cd02540    1 AVILAAGKGTRMK--SDL-PKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVKKALAN---PNVEFVLQEE--- 71

                         90       100
                 ....*....|....*....|....*....
gi 647818525  83 PLETGGGMLHALPLLG--NAPFLAINGDI 109
Cdd:cd02540   72 QLGTGHAVKQALPALKdfEGDVLVLYGDV 100
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 1-53 6.47e-05

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: 42.90  E-value: 6.47e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 647818525   1 MKALIFAAGIGQRMRPLTNYTPKPLLCAGGEPLIVWNLRKLAALGISEVVINT 53
Cdd:cd02541    1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVT 53
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
1-113 7.29e-05

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 42.95  E-value: 7.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647818525   1 MKALIFAAGIGQRMRPLTNYTPKPLLCAGGEPLIVWNLRKLAALGISEVVI-------------NTAWLGEQFPE----- 62
Cdd:PRK10122   4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLvthasknavenhfDTSYELESLLEqrvkr 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 647818525  63 -ILGDGQRF---GLRLFYSNEGSlPLETGGGMLHALPLLGNAPFLAINGDIWTDA 113
Cdd:PRK10122  84 qLLAEVQSIcppGVTIMNVRQGQ-PLGLGHSILCARPAIGDNPFVVVLPDVVIDD 137
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
3-51 8.03e-05

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 42.43  E-value: 8.03e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 647818525   3 ALIFAAGIGQRMRPLtnyTPKPLLCAGGEPLIVWNLRKLAALG-ISEVVI 51
Cdd:PRK00155   6 AIIPAAGKGSRMGAD---RPKQYLPLGGKPILEHTLEAFLAHPrIDEIIV 52
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 3-51 8.04e-05

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: 42.51  E-value: 8.04e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 647818525   3 ALIFAAGIGQRMRPLtnyTPKPLLCAGGEPLIVWNLRKLAALG-ISEVVI 51
Cdd:cd02516    3 AIILAAGSGSRMGAD---IPKQFLELGGKPVLEHTLEAFLAHPaIDEIVV 49
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
2-53 1.10e-04

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 42.59  E-value: 1.10e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 647818525   2 KALIFAAGIGQRMRPLTNYTPKPLLCAGGEPLIVWNLRKLAALGISEVVINT 53
Cdd:PRK13389  10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVT 61
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 4-66 1.27e-04

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440824  Cd Length: 224  Bit Score: 41.65  E-value: 1.27e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 647818525   4 LIFAAGIGQRMRpltNYTPKPLLCAGGEPLIVWNLRKLAALG-ISE--VVINTAWLgEQFPEILGD 66
Cdd:COG1211    1 IIPAAGSGSRMG---AGIPKQFLPLGGKPVLEHTLEAFLAHPrIDEivVVVPPDDI-EYFEELLAK 62
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 1-108 1.44e-04

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: 42.32  E-value: 1.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647818525   1 MKALIFAAGIGQRMRplTNyTPKPLLCAGGEPLIVWNLRKLAALGISEVVINTAWLGEQFPEILGDgqrFGLRLFYSNEg 80
Cdd:COG1207    3 LAVVILAAGKGTRMK--SK-LPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVRAALAD---LDVEFVLQEE- 75

                         90       100       110
                 ....*....|....*....|....*....|
gi 647818525  81 slPLETGGGMLHALPLLG--NAPFLAINGD 108
Cdd:COG1207   76 --QLGTGHAVQQALPALPgdDGTVLVLYGD 103
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 3-94 2.43e-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: 40.26  E-value: 2.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647818525    3 ALIFAAGIGQRMRpltnyTPKPLLCAGGEPLIVWNLRKLAALGiSEVVINTAWlgeqfPEILGDGQRFGLRLFYSnegsl 82
Cdd:pfam12804   1 AVILAGGRSSRMG-----GDKALLPLGGKPLLERVLERLRPAG-DEVVVVAND-----EEVLAALAGLGVPVVPD----- 64

                          90
                  ....*....|..
gi 647818525   83 pLETGGGMLHAL 94
Cdd:pfam12804  65 -PDPGQGPLAGL 75
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
3-74 4.73e-04

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 39.76  E-value: 4.73e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 647818525   3 ALIFAAGIGQRMRpltnyTPKPLLCAGGEPLIVWNLRKLAALGISEVVINtawLGEQFPEILGDGQRFGLRL 74
Cdd:COG2068    6 AIILAAGASSRMG-----RPKLLLPLGGKPLLERAVEAALAAGLDPVVVV---LGADAEEVAAALAGLGVRV 69
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
 3-51 6.21e-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: 6.21e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 647818525   3 ALIFAAGIGQRMRPLTNYTPKPLLCAGGEPlIVWNLRKL-AALGISEVVI 51
Cdd:cd02524    1 VVILAGGLGTRLSEETELKPKPMVEIGGRP-ILWHIMKIySHYGHNDFIL 49
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 1-108 1.69e-03

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 39.19  E-value: 1.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647818525   1 MKALIFAAGIGQRMRpltNYTPKPLLCAGGEPLIVWNLRKLAALGISEVVINTAWLGEQFPEIL-GDGQRFGLRlfysne 79
Cdd:PRK14358   8 LDVVILAAGQGTRMK---SALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGAEQVEAALqGSGVAFARQ------ 78

                         90       100       110
                 ....*....|....*....|....*....|.
gi 647818525  80 gSLPLETGGGMLHALPLL--GNAPFLAINGD 108
Cdd:PRK14358  79 -EQQLGTGDAFLSGASALteGDADILVLYGD 108
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-51 2.15e-03

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 38.69  E-value: 2.15e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 647818525   3 ALIFAAGIGQRMRpltNYTPKPLLCAGGEPLIVWNLRKLAALGISEVVI 51
Cdd:PRK14353   8 AIILAAGEGTRMK---SSLPKVLHPVAGRPMLAHVLAAAASLGPSRVAV 53
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 7-109 3.28e-03

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: 37.18  E-value: 3.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647818525   7 AAGIGQRMrpltNYTPKPLLCAGGEPLIVWNLRKLAALGISEVVI----NTawlgeqfPEilgdgqrfgLRLFYSNEGSL 82
Cdd:COG2266    2 AGGKGTRL----GGGEKPLLEICGKPMIDRVIDALEESCIDKIYVavspNT-------PK---------TREYLKERGVE 61

                         90       100       110
                 ....*....|....*....|....*....|..
gi 647818525  83 PLETGGG-----MLHALPLLGnAPFLAINGDI 109
Cdd:COG2266   62 VIETPGEgyvedLNEALESIS-GPVLVVPADL 92
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 3-59 5.93e-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: 36.82  E-value: 5.93e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 647818525   3 ALIFAAGIGQRMRPLTNYTPKPLLCAGGEPLIVWNLRKLAALGISEVVINTAWLGEQ 59
Cdd:cd04197    3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQ 59
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 3-51 6.04e-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: 36.38  E-value: 6.04e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 647818525   3 ALIFAAGIGQRMRpltnyTPKPLLCAGGEPLIVWNLRKLAALGISEVVI 51
Cdd:cd04182    3 AIILAAGRSSRMG-----GNKLLLPLDGKPLLRHALDAALAAGLSRVIV 46
 
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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