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Conserved domains on  [gi|315411137|gb|ADU09254|]
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Nucleotidyl transferase [Micromonospora sp. L5]

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 ...
 17-223 6.34e-45

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: 152.23  E-value: 6.34e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315411137  17 AVVLAAGEGTRLRPLTERVPKALCPVGNVPLLDRALARLAGLGLTgpeRVAVNACYLGDQVVTRVGDRAHLS-----VEP 91
Cdd:COG1208    2 AVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGIT---EIVINVGYLAEQIEEYFGDGSRFGvrityVDE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315411137  92 GAPLGTAGGVGRLRDWIDGRGVLVGNADAYLadpqappGPDIAALLDGWDGHG--VRLLGRPADDPHAPGTFD------- 162
Cdd:COG1208   79 GEPLGTGGALKRALPLLGDEPFLVLNGDILT-------DLDLAALLAFHREKGadATLALVPVPDPSRYGVVEldgdgrv 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 315411137 163 ------------GHEFVGFSLLPWRLVRDLPP-TFGDLVrAVWRPAEAAGALTVVPYRGTFYDTGTPADYLAAN 223
Cdd:COG1208  152 trfvekpeeppsNLINAGIYVLEPEIFDYIPEgEPFDLE-DLLPRLIAEGRVYGYVHDGYWLDIGTPEDLLEAN 224
 
Name Accession Description Interval E-value
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 17-223 6.34e-45

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: 152.23  E-value: 6.34e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315411137  17 AVVLAAGEGTRLRPLTERVPKALCPVGNVPLLDRALARLAGLGLTgpeRVAVNACYLGDQVVTRVGDRAHLS-----VEP 91
Cdd:COG1208    2 AVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGIT---EIVINVGYLAEQIEEYFGDGSRFGvrityVDE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315411137  92 GAPLGTAGGVGRLRDWIDGRGVLVGNADAYLadpqappGPDIAALLDGWDGHG--VRLLGRPADDPHAPGTFD------- 162
Cdd:COG1208   79 GEPLGTGGALKRALPLLGDEPFLVLNGDILT-------DLDLAALLAFHREKGadATLALVPVPDPSRYGVVEldgdgrv 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 315411137 163 ------------GHEFVGFSLLPWRLVRDLPP-TFGDLVrAVWRPAEAAGALTVVPYRGTFYDTGTPADYLAAN 223
Cdd:COG1208  152 trfvekpeeppsNLINAGIYVLEPEIFDYIPEgEPFDLE-DLLPRLIAEGRVYGYVHDGYWLDIGTPEDLLEAN 224
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 17-222 8.10e-41

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: 140.78  E-value: 8.10e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315411137  17 AVVLAAGEGTRLRPLTERVPKALCPVGNVPLLDRALARLAGLgltGPERVAVNACYLGDQVV-----TRVGDRAHLSVEP 91
Cdd:cd06422    2 AMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAA---GIRRIVVNTHHLADQIEahlgdSRFGLRITISDEP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315411137  92 GAPLGTAGGVGRLRDWIDGRGVLVGNADAYLADpqaPPGPDIAALLDGWDGHGVRLLGRPADDPHAPGTFDGHE------ 165
Cdd:cd06422   79 DELLETGGGIKKALPLLGDEPFLVVNGDILWDG---DLAPLLLLHAWRMDALLLLLPLVRNPGHNGVGDFSLDAdgrlrr 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 315411137 166 ----------FVGFSLLPWRLVRDLPPTFGDLvRAVWRPAEAAGALTVVPYRGTFYDTGTPADYLAA 222
Cdd:cd06422  156 ggggavapftFTGIQILSPELFAGIPPGKFSL-NPLWDRAIAAGRLFGLVYDGLWFDVGTPERLLAA 221
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
 17-276 5.80e-13

glucose-1-phosphate thymidylylransferase, long form; The family of known and putative glucose-1-phosphate thymidyltransferase (also called dTDP-glucose synthase) shows a deep split into a short form (see TIGR01207) and a long form described by this model. The homotetrameric short form is found in numerous bacterial species that incorporate dTDP-L-rhamnose, which it helps synthesize, into the cell wall. It is subject to feedback inhibition. This form, in contrast, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced. Alternate name: dTDP-D-glucose synthase


Pssm-ID: 273500 [Multi-domain]  Cd Length: 353  Bit Score: 68.20  E-value: 5.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315411137   17 AVVLAAGEGTRLRPLTERVPKALCPVGNVPLLDRALARLAGLGLTgpERVAVNACYLGDQVVTRVGDRAHLSVE-----P 91
Cdd:TIGR01208   2 ALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGIT--DIGIVVGPVTGEEIKEIVGEGERFGAKityivQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315411137   92 GAPLGTAGGVGRLRDWID--------GRGVLVGNADAYL-----ADPQA---------PPGPDIAALLDGwdGHGVRLLG 149
Cdd:TIGR01208  80 GEPLGLAHAVYTARDFLGdddfvvylGDNLIQDGISRFVksfeeKDYDAlilltkvrdPTAFGVAVLEDG--KRILKLVE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315411137  150 RPADDPhapgtfDGHEFVG---FSLLPWRLVRDLPPTfgdlvravWR-PAEAAGAL--------TVVPYR--GTFYDTGT 215
Cdd:TIGR01208 158 KPKEPP------SNLAVVGlymFRPLIFEAIKNIKPS--------WRgELEITDAIqwliekgyKVGGSKvtGWWKDTGK 223

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 315411137  216 PADYLAAN---LHAAGPDGL-VDPAATVDGRV--------TGSVIGGGARVHGDV--DRSVVWPGATVAAGERLR 276
Cdd:TIGR01208 224 PEDLLDANrliLDEVEREVQgVDDESKIRGRVvvgegakiVNSVIRGPAVIGEDCiiENSYIGPYTSIGEGVVIR 298
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 17-159 7.84e-11

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 62.19  E-value: 7.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315411137  17 AVVLAAGEGTRLRpltERVPKALCPVGNVPLLDRALARLAGLgltGPERVAVNACYLGDQVVTRVGDRA--HLSVEPGAP 94
Cdd:PRK14353   8 AIILAAGEGTRMK---SSLPKVLHPVAGRPMLAHVLAAAASL---GPSRVAVVVGPGAEAVAAAAAKIApdAEIFVQKER 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 315411137  95 LGTAGGVGRLRDWI-DGRG-VLVGNADAYLADPQappgpDIAALLDGW-DGHGVRLLGRPADDPHAPG 159
Cdd:PRK14353  82 LGTAHAVLAAREALaGGYGdVLVLYGDTPLITAE-----TLARLRERLaDGADVVVLGFRAADPTGYG 144
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 17-119 2.52e-09

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: 56.49  E-value: 2.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315411137   17 AVVLAAGEGTRLRPLTERVPKALCPVGN-VPLLDRALARLAGLGLTgpERVAVNACYLGDQVVTRVGDRAHLSVEPGA-- 93
Cdd:pfam00483   2 AIILAGGSGTRLWPLTRTLAKPLVPVGGkYPLIDYPLSRLANAGIR--EIIVILTQEHRFMLNELLGDGSKFGVQITYal 79

                          90       100       110
                  ....*....|....*....|....*....|.
gi 315411137   94 ---PLGTAGGVGRLRDWIDG--RGVLVGNAD 119
Cdd:pfam00483  80 qpeGKGTAPAVALAADFLGDekSDVLVLGGD 110
 
Name Accession Description Interval E-value
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 17-223 6.34e-45

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: 152.23  E-value: 6.34e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315411137  17 AVVLAAGEGTRLRPLTERVPKALCPVGNVPLLDRALARLAGLGLTgpeRVAVNACYLGDQVVTRVGDRAHLS-----VEP 91
Cdd:COG1208    2 AVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGIT---EIVINVGYLAEQIEEYFGDGSRFGvrityVDE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315411137  92 GAPLGTAGGVGRLRDWIDGRGVLVGNADAYLadpqappGPDIAALLDGWDGHG--VRLLGRPADDPHAPGTFD------- 162
Cdd:COG1208   79 GEPLGTGGALKRALPLLGDEPFLVLNGDILT-------DLDLAALLAFHREKGadATLALVPVPDPSRYGVVEldgdgrv 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 315411137 163 ------------GHEFVGFSLLPWRLVRDLPP-TFGDLVrAVWRPAEAAGALTVVPYRGTFYDTGTPADYLAAN 223
Cdd:COG1208  152 trfvekpeeppsNLINAGIYVLEPEIFDYIPEgEPFDLE-DLLPRLIAEGRVYGYVHDGYWLDIGTPEDLLEAN 224
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 17-222 8.10e-41

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: 140.78  E-value: 8.10e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315411137  17 AVVLAAGEGTRLRPLTERVPKALCPVGNVPLLDRALARLAGLgltGPERVAVNACYLGDQVV-----TRVGDRAHLSVEP 91
Cdd:cd06422    2 AMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAA---GIRRIVVNTHHLADQIEahlgdSRFGLRITISDEP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315411137  92 GAPLGTAGGVGRLRDWIDGRGVLVGNADAYLADpqaPPGPDIAALLDGWDGHGVRLLGRPADDPHAPGTFDGHE------ 165
Cdd:cd06422   79 DELLETGGGIKKALPLLGDEPFLVVNGDILWDG---DLAPLLLLHAWRMDALLLLLPLVRNPGHNGVGDFSLDAdgrlrr 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 315411137 166 ----------FVGFSLLPWRLVRDLPPTFGDLvRAVWRPAEAAGALTVVPYRGTFYDTGTPADYLAA 222
Cdd:cd06422  156 ggggavapftFTGIQILSPELFAGIPPGKFSL-NPLWDRAIAAGRLFGLVYDGLWFDVGTPERLLAA 221
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 17-122 2.76e-26

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: 102.66  E-value: 2.76e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315411137  17 AVVLAAGEGTRLRPLTERVPKALCPVGNVPLLDRALARLAGLgltGPERVAVNACYLGDQVVTRVGDRA------HLSVE 90
Cdd:cd04181    1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARA---GIDEIILVVGYLGEQIEEYFGDGSkfgvniEYVVQ 77

                         90       100       110
                 ....*....|....*....|....*....|..
gi 315411137  91 PgAPLGTAGGVGRLRDWIDGRGVLVGNADAYL 122
Cdd:cd04181   78 E-EPLGTAGAVRNAEDFLGDDDFLVVNGDVLT 108
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 17-219 2.15e-21

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: 89.92  E-value: 2.15e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315411137  17 AVVLAAGEGTRLRPLTERVPKALCPVGNVPLLDRALARLAGLGLTgpeRVAVNACYLGDQVVTRVGDRA------HLSVE 90
Cdd:cd06915    1 AVILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGIS---RIVLSVGYLAEQIEEYFGDGYrggiriYYVIE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315411137  91 PgAPLGTAGGVGRLRDWIDGRGVLVGNADAYLAdpqappgPDIAALLDGWDGHG--VRLLGRPADDPHAPG--TFDGHEF 166
Cdd:cd06915   78 P-EPLGTGGAIKNALPKLPEDQFLVLNGDTYFD-------VDLLALLAALRASGadATMALRRVPDASRYGnvTVDGDGR 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315411137 167 V-----------------GFSLLPWRLVRDLPPTFGDLVRAVWRPAEAAGALTVVPYRGTFYDTGTPADY 219
Cdd:cd06915  150 ViafvekgpgaapglingGVYLLRKEILAEIPADAFSLEADVLPALVKRGRLYGFEVDGYFIDIGIPEDY 219
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 17-119 4.39e-16

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: 75.24  E-value: 4.39e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315411137  17 AVVLAAGEGTRLRPLTERVPKALCPVGNVPLLDRALARLAGLGLtgpER--VAVNacYLGDQVVTRVGDRAHLSV----- 89
Cdd:cd06426    1 VVIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGF---RNfyISVN--YLAEMIEDYFGDGSKFGVnisyv 75

                         90       100       110
                 ....*....|....*....|....*....|
gi 315411137  90 EPGAPLGTAGGVGRLRDWIDgRGVLVGNAD 119
Cdd:cd06426   76 REDKPLGTAGALSLLPEKPT-DPFLVMNGD 104
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 17-77 3.99e-14

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


Pssm-ID: 133014 [Multi-domain]  Cd Length: 229  Bit Score: 69.95  E-value: 3.99e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 315411137  17 AVVLAAGEGTRLRPLTERVPKALCPVGNVPLLDRALARLAGLGLtgpERVAVNACYLGDQV 77
Cdd:cd02523    1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGI---DDIVIVTGYKKEQI 58
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 17-223 5.51e-14

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: 69.91  E-value: 5.51e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315411137  17 AVVLAAGEGTRLRPLTERVPKALCPVGNVPLLDRALARLAGLGLtgpERVAVNACYLGDQVVTRVGDRAHLSV-----EP 91
Cdd:cd04189    3 GLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGI---EDIGIVVGPTGEEIKEALGDGSRFGVrityiLQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315411137  92 GAPLGTAGGVGRLRDWIDGRGVLVgnadaYLADPQAPPGpdIAALLDGWDGHG--VRLLGRPADDPHAPGT--FDGHEFV 167
Cdd:cd04189   80 EEPLGLAHAVLAARDFLGDEPFVV-----YLGDNLIQEG--ISPLVRDFLEEDadASILLAEVEDPRRFGVavVDDGRIV 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 315411137 168 G-------------------FSLLPWRLVRDLPPTF-GDL--VRAVWRPAEAAGALTVVPYRGTFYDTGTPADYLAAN 223
Cdd:cd04189  153 RlvekpkeppsnlalvgvyaFTPAIFDAISRLKPSWrGELeiTDAIQWLIDRGRRVGYSIVTGWWKDTGTPEDLLEAN 230
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
17-84 3.50e-13

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 67.57  E-value: 3.50e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 315411137  17 AVVLAAGEGTRLRPLTERVPKALCPVGNVPLLDRALARLAGLGLTgpeRVAVNACYLGDQVVTRVGDR 84
Cdd:COG1213    2 AVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIK---DIVVVTGYKAELIEEALARP 66
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
 17-276 5.80e-13

glucose-1-phosphate thymidylylransferase, long form; The family of known and putative glucose-1-phosphate thymidyltransferase (also called dTDP-glucose synthase) shows a deep split into a short form (see TIGR01207) and a long form described by this model. The homotetrameric short form is found in numerous bacterial species that incorporate dTDP-L-rhamnose, which it helps synthesize, into the cell wall. It is subject to feedback inhibition. This form, in contrast, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced. Alternate name: dTDP-D-glucose synthase


Pssm-ID: 273500 [Multi-domain]  Cd Length: 353  Bit Score: 68.20  E-value: 5.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315411137   17 AVVLAAGEGTRLRPLTERVPKALCPVGNVPLLDRALARLAGLGLTgpERVAVNACYLGDQVVTRVGDRAHLSVE-----P 91
Cdd:TIGR01208   2 ALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGIT--DIGIVVGPVTGEEIKEIVGEGERFGAKityivQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315411137   92 GAPLGTAGGVGRLRDWID--------GRGVLVGNADAYL-----ADPQA---------PPGPDIAALLDGwdGHGVRLLG 149
Cdd:TIGR01208  80 GEPLGLAHAVYTARDFLGdddfvvylGDNLIQDGISRFVksfeeKDYDAlilltkvrdPTAFGVAVLEDG--KRILKLVE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315411137  150 RPADDPhapgtfDGHEFVG---FSLLPWRLVRDLPPTfgdlvravWR-PAEAAGAL--------TVVPYR--GTFYDTGT 215
Cdd:TIGR01208 158 KPKEPP------SNLAVVGlymFRPLIFEAIKNIKPS--------WRgELEITDAIqwliekgyKVGGSKvtGWWKDTGK 223

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 315411137  216 PADYLAAN---LHAAGPDGL-VDPAATVDGRV--------TGSVIGGGARVHGDV--DRSVVWPGATVAAGERLR 276
Cdd:TIGR01208 224 PEDLLDANrliLDEVEREVQgVDDESKIRGRVvvgegakiVNSVIRGPAVIGEDCiiENSYIGPYTSIGEGVVIR 298
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
17-124 5.92e-12

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 64.73  E-value: 5.92e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315411137  17 AVVLAAGEGTRLRPLTERVPKALCPVGNVPLLDRALARLAGLG------LTGPervavnacYLGDQVVTRVGDRAHLS-- 88
Cdd:COG1209    3 GIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGireiliISTP--------EDGPQFERLLGDGSQLGik 74

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 315411137  89 ---VEPGAPLGTAGGVGRLRDWIDGRGVLVgnadaYLAD 124
Cdd:COG1209   75 isyAVQPEPLGLAHAFIIAEDFIGGDPVAL-----VLGD 108
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 17-119 7.62e-11

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: 60.69  E-value: 7.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315411137  17 AVVLAAGEGTRLRPLTERVPKALCPVGNVPLLDRALARLAGLGLTgpERV-AVNacYLGDQVV-------TRVGDRAHLS 88
Cdd:cd06425    3 ALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVK--EIIlAVN--YRPEDMVpflkeyeKKLGIKITFS 78

                         90       100       110
                 ....*....|....*....|....*....|...
gi 315411137  89 VEPgAPLGTAGGVGRLRDWIDGRG--VLVGNAD 119
Cdd:cd06425   79 IET-EPLGTAGPLALARDLLGDDDepFFVLNSD 110
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 17-159 7.84e-11

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 62.19  E-value: 7.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315411137  17 AVVLAAGEGTRLRpltERVPKALCPVGNVPLLDRALARLAGLgltGPERVAVNACYLGDQVVTRVGDRA--HLSVEPGAP 94
Cdd:PRK14353   8 AIILAAGEGTRMK---SSLPKVLHPVAGRPMLAHVLAAAASL---GPSRVAVVVGPGAEAVAAAAAKIApdAEIFVQKER 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 315411137  95 LGTAGGVGRLRDWI-DGRG-VLVGNADAYLADPQappgpDIAALLDGW-DGHGVRLLGRPADDPHAPG 159
Cdd:PRK14353  82 LGTAHAVLAAREALaGGYGdVLVLYGDTPLITAE-----TLARLRERLaDGADVVVLGFRAADPTGYG 144
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 17-156 2.28e-10

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


Pssm-ID: 133020 [Multi-domain]  Cd Length: 229  Bit Score: 59.45  E-value: 2.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315411137  17 AVVLAAGEGTRLRpltERVPKALCPVGNVPLLDRALARLAGLgltGPERVAVNACYLGDQVVTRVGDRAHLSVEPGAPLG 96
Cdd:cd02540    1 AVILAAGKGTRMK---SDLPKVLHPLAGKPMLEHVLDAARAL---GPDRIVVVVGHGAEQVKKALANPNVEFVLQEEQLG 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 315411137  97 TAGGVGRLRDWIDGRG--VLVGNADAYLADPQappgpDIAALLDGWDGHG--VRLLGRPADDPH 156
Cdd:cd02540   75 TGHAVKQALPALKDFEgdVLVLYGDVPLITPE-----TLQRLLEAHREAGadVTVLTAELEDPT 133
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 17-49 5.30e-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: 58.03  E-value: 5.30e-10
                         10        20        30
                 ....*....|....*....|....*....|...
gi 315411137  17 AVVLAAGEGTRLRPLTERVPKALCPVGNVPLLD 49
Cdd:cd02507    3 AVVLADGFGSRFLPLTSDIPKALLPVANVPLID 35
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 17-48 1.38e-09

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: 56.90  E-value: 1.38e-09
                         10        20        30
                 ....*....|....*....|....*....|..
gi 315411137  17 AVVLAAGEGTRLRPLTERVPKALCPVGNVPLL 48
Cdd:cd04198    3 AVILAGGGGSRLYPLTDNIPKALLPVANKPMI 34
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 17-119 2.52e-09

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: 56.49  E-value: 2.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315411137   17 AVVLAAGEGTRLRPLTERVPKALCPVGN-VPLLDRALARLAGLGLTgpERVAVNACYLGDQVVTRVGDRAHLSVEPGA-- 93
Cdd:pfam00483   2 AIILAGGSGTRLWPLTRTLAKPLVPVGGkYPLIDYPLSRLANAGIR--EIIVILTQEHRFMLNELLGDGSKFGVQITYal 79

                          90       100       110
                  ....*....|....*....|....*....|.
gi 315411137   94 ---PLGTAGGVGRLRDWIDG--RGVLVGNAD 119
Cdd:pfam00483  80 qpeGKGTAPAVALAADFLGDekSDVLVLGGD 110
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 15-156 1.21e-08

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: 55.42  E-value: 1.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315411137  15 VCAVVLAAGEGTRLRpltERVPKALCPVGNVPLLDRALARLAGLgltGPERVAVNACYLGDQVVTRVGDRAHLSVEPGAP 94
Cdd:COG1207    3 LAVVILAAGKGTRMK---SKLPKVLHPLAGKPMLEHVLDAARAL---GPDRIVVVVGHGAEQVRAALADLDVEFVLQEEQ 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 315411137  95 LGTAGGVGRLRDWIDGRG--VLVGNADAYLADPQAppgpdIAALLDGW--DGHGVRLLGRPADDPH 156
Cdd:COG1207   77 LGTGHAVQQALPALPGDDgtVLVLYGDVPLIRAET-----LKALLAAHraAGAAATVLTAELDDPT 137
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 17-77 2.72e-07

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: 50.30  E-value: 2.72e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 315411137  17 AVVLAAGEGTRLRPLTERVPKALCPVGNVPLLDRALARLAglgLTGPERVAVNACYLGDQV 77
Cdd:cd04197    3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLA---LNGVEEVFVFCCSHSDQI 60
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 17-119 7.67e-07

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: 49.17  E-value: 7.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315411137  17 AVVLAAGE--GTRLRPLTERVPKALCPVGNVPLLDRALARLAGLG------LTGpervavnacYLGDQVVTRVGDRAH-- 86
Cdd:cd06428    1 AVILVGGPqkGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKVPdlkevlLIG---------FYPESVFSDFISDAQqe 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 315411137  87 --LSV----EPgAPLGTAGGVGRLRDWI---DGRGVLVGNAD 119
Cdd:cd06428   72 fnVPIrylqEY-KPLGTAGGLYHFRDQIlagNPSAFFVLNAD 112
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 19-167 7.13e-06

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 46.84  E-value: 7.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315411137  19 VLAAGEGTRLRpltERVPKALCPVGNVPLLDRALARLAGLgltGPERVAVNACYLGDQVVTRVGDRAHLS-VEPGAPLGT 97
Cdd:PRK14360   6 ILAAGKGTRMK---SSLPKVLHPLGGKSLVERVLDSCEEL---KPDRRLVIVGHQAEEVEQSLAHLPGLEfVEQQPQLGT 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 315411137  98 AGGVGRLRDWIDG-RG-VLVGNADAYLADPQAppgpdIAALLDGWDGHG--VRLLGRPADDPHAPG-TF-DGHEFV 167
Cdd:PRK14360  80 GHAVQQLLPVLKGfEGdLLVLNGDVPLLRPET-----LEALLNTHRSSNadVTLLTARLPNPKGYGrVFcDGNNLV 150
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 17-144 4.50e-05

MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine dinucleotide biosynthesis protein A). The family also includes a wide range of other NTP transferase domain.


Pssm-ID: 463715 [Multi-domain]  Cd Length: 159  Bit Score: 42.95  E-value: 4.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315411137   17 AVVLAAGEGTRLRplterVPKALCPVGNVPLLDRALARLAGLGltgpERVAVNACYlgDQVVTRVGD-RAHLSVEPGAPL 95
Cdd:pfam12804   1 AVILAGGRSSRMG-----GDKALLPLGGKPLLERVLERLRPAG----DEVVVVAND--EEVLAALAGlGVPVVPDPDPGQ 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 315411137   96 GTAGGVGRLRDWIDG-RGVLVGNADAYLADPQAppgpdIAALLDGWDGHG 144
Cdd:pfam12804  70 GPLAGLLAALRAAPGaDAVLVLACDMPFLTPEL-----LRRLLAAAEESG 114
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 17-163 6.64e-05

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: 43.33  E-value: 6.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315411137  17 AVVLAAGEGTRLRPLTERVPKALCPVGNVPLLDRALA--RLAG----LGLTGPERVAVNACYLGDQVvtRVGDRAHLSVE 90
Cdd:cd02538    3 GIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLStlMLAGireiLIISTPEDLPLFKELLGDGS--DLGIRITYAVQ 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 315411137  91 PgAPLGTAGGVGRLRDWIDGRGVLVGNADAYLAdpqappGPDIAALLDGW--DGHGVRLLGRPADDPHAPG--TFDG 163
Cdd:cd02538   81 P-KPGGLAQAFIIGEEFIGDDPVCLILGDNIFY------GQGLSPILQRAaaQKEGATVFGYEVNDPERYGvvEFDE 150
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
15-222 8.17e-05

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 42.46  E-value: 8.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315411137  15 VCAVVLAAGEGTRLRplterVPKALCPVGNVPLLDRALARLAGLGL------TGPERVAVNACYLGDQVVTRVGDRAHLs 88
Cdd:COG2068    4 VAAIILAAGASSRMG-----RPKLLLPLGGKPLLERAVEAALAAGLdpvvvvLGADAEEVAAALAGLGVRVVVNPDWEE- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315411137  89 vepgaPLGT--AGGVGRLRDWIDgrGVLVGNADAYLADPQappgpDIAALLDGWDGHGVRLL-----GRPaddphapgtf 161
Cdd:COG2068   78 -----GMSSslRAGLAALPADAD--AVLVLLGDQPLVTAE-----TLRRLLAAFRESPASIVaptydGRR---------- 135

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 315411137 162 dGHEfVGFSLLPWRLVRDLPPTFGdlVRAVWRPAEAAGALTVVPYRGTFYDTGTPADYLAA 222
Cdd:COG2068  136 -GHP-VLFSRRLFPELLALTGDQG--ARALLRRHPDRVRLVPVDDPGVLLDIDTPEDLARL 192
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
 17-48 1.35e-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: 42.56  E-value: 1.35e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 315411137  17 AVVLAAGEGTRLRPLTERVPKALCPVGNVPLL 48
Cdd:cd02524    1 VVILAGGLGTRLSEETELKPKPMVEIGGRPIL 32
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 14-70 1.64e-04

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


Pssm-ID: 440509 [Multi-domain]  Cd Length: 188  Bit Score: 41.72  E-value: 1.64e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 315411137  14 EVCAVVLAAGEGTRLRplterVPKALCPVGNVPLLDRALARLAGLGltgpERVAVNA 70
Cdd:COG0746    4 PITGVILAGGRSRRMG-----QDKALLPLGGRPLLERVLERLRPQV----DEVVIVA 51
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 15-85 1.80e-04

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


Pssm-ID: 133025 [Multi-domain]  Cd Length: 186  Bit Score: 41.39  E-value: 1.80e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 315411137  15 VCAVVLAAGEGTRLRPltervPKALCPVGNVPLLDRALARLAGLGL------TGPERVAVNACYLGDQVVTRVGDRA 85
Cdd:cd04182    1 IAAIILAAGRSSRMGG-----NKLLLPLDGKPLLRHALDAALAAGLsrvivvLGAEADAVRAALAGLPVVVVINPDW 72
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 17-159 2.71e-04

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 42.23  E-value: 2.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315411137  17 AVVLAAGEGTRLRpltERVPKALCPVGNVPLLDRALARLAGLgltGPERVAVNACYLGDQV---VTRVGDRAHLSVE--- 90
Cdd:PRK14352   7 VIVLAAGAGTRMR---SDTPKVLHTLAGRSMLGHVLHAAAGL---APQHLVVVVGHDRERVapaVAELAPEVDIAVQdeq 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 315411137  91 PGAPLGTAGGVGRLRDWIDGRgVLVGNADAYLADPQAppgpdIAALLD--GWDGHGVRLLGRPADDPHAPG 159
Cdd:PRK14352  81 PGTGHAVQCALEALPADFDGT-VVVTAGDVPLLDGET-----LADLVAthTAEGNAVTVLTTTLDDPTGYG 145
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 14-43 2.94e-04

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 41.98  E-value: 2.94e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 315411137  14 EVCAVVLAAGEGTRLRPLTERVPKALCPVG 43
Cdd:COG0448    1 KVLAIILAGGRGSRLGPLTKDRAKPAVPFG 30
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 17-48 4.55e-04

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: 40.98  E-value: 4.55e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 315411137  17 AVVLAAGEGTRLRPLTERVPKALCPVGNVPLL 48
Cdd:cd02541    3 AVIPAAGLGTRFLPATKAIPKEMLPIVDKPVI 34
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
 17-43 6.78e-04

ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ADP-glucose pyrophosphorylase (glucose-1-phosphate adenylyltransferase) catalyzes a very important step in the biosynthesis of alpha 1,4-glucans (glycogen or starch) in bacteria and plants: synthesis of the activated glucosyl donor, ADP-glucose, from glucose-1-phosphate and ATP. ADP-glucose pyrophosphorylase is a tetrameric allosterically regulated enzyme. While a homotetramer in bacteria, in plant chloroplasts and amyloplasts, it is a heterotetramer of two different, yet evolutionary related, subunits. There are a number of conserved regions in the sequence of bacterial and plant ADP-glucose pyrophosphorylase subunits. It is a subfamily of a very diverse glycosy transferase family 2.


Pssm-ID: 133002 [Multi-domain]  Cd Length: 200  Bit Score: 39.83  E-value: 6.78e-04
                         10        20
                 ....*....|....*....|....*..
gi 315411137  17 AVVLAAGEGTRLRPLTERVPKALCPVG 43
Cdd:cd02508    1 AIILAGGEGTRLSPLTKKRAKPAVPFG 27
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 15-56 9.11e-04

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


Pssm-ID: 133009 [Multi-domain]  Cd Length: 218  Bit Score: 39.81  E-value: 9.11e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 315411137  15 VCAVVLAAGEGTRLRPLterVPKALCPVGNVPLLDRALARLA 56
Cdd:cd02516    1 VAAIILAAGSGSRMGAD---IPKQFLELGGKPVLEHTLEAFL 39
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
15-55 5.33e-03

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 37.42  E-value: 5.33e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 315411137  15 VCAVVLAAGEGTRLRpltERVPKALCPVGNVPLLDRALARL 55
Cdd:PRK00155   4 VYAIIPAAGKGSRMG---ADRPKQYLPLGGKPILEHTLEAF 41
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
 17-68 5.44e-03

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


Pssm-ID: 133003 [Multi-domain]  Cd Length: 274  Bit Score: 37.56  E-value: 5.44e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 315411137  17 AVVLAAGEGTRLRPL-TERVPKALCPV-GNVPLLDRALARLAglGLTGPERVAV 68
Cdd:cd02509    3 PVILAGGSGTRLWPLsRESYPKQFLKLfGDKSLLQQTLDRLK--GLVPPDRILV 54
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 18-56 5.61e-03

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: 37.42  E-value: 5.61e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 315411137  18 VVLAAGEGTRLRpltERVPKALCPVGNVPLLDRALARLA 56
Cdd:COG1211    1 IIPAAGSGSRMG---AGIPKQFLPLGGKPVLEHTLEAFL 36
 
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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