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Conserved domains on  [gi|517482396|ref|WP_018652974|]
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UTP--glucose-1-phosphate uridylyltransferase GalU [Actinobacillus capsulatus]

Protein Classification

UTP--glucose-1-phosphate uridylyltransferase( domain architecture ID 10003115)

UTP--glucose-1-phosphate uridylyltransferase catalyzes the formation of UDP-glucose from glucose-1-phosphate and UTP, which is an intermediate step in the biosynthesis of diglucosyl-diacylglycerol (Glc2-DAG)

CATH:  3.90.550.10
EC:  2.7.7.9
Gene Ontology:  GO:0009225|GO:0003983
PubMed:  15020755

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
2-294 5.97e-175

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


:

Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 484.54  E-value: 5.97e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396   2 KVIIPVAGLGTRMLPATKAIPKEMLTIADKPLIQYIVNECVAAGIKEIVLVTHSSKNAIENHFDTSFELETMLEKRVKRQ 81
Cdd:COG1210    5 KAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVTGRGKRAIEDHFDRSYELEATLEAKGKEE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396  82 LLDEVRSIVPkDVTLMHVRQGQAKGLGHAVLCGRAVVGNEPFAVVLPDVILADfaanqKTENLAAMIKRFNETKHSQIMV 161
Cdd:COG1210   85 LLEEVRSISP-LANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDS-----EKPCLKQMIEVYEETGGSVIAV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396 162 APVPKEDVSSYGVADCAGVDipaGETAKIVKMVEKPSVEEAPSNLAVVGRYVFSENIWDLLEKTPVGVGDEIQLTDAIDM 241
Cdd:COG1210  159 QEVPPEEVSKYGIVDGEEIE---GGVYRVTGLVEKPAPEEAPSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDAIAA 235

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 517482396 242 LIEQETVEAFHMTGRTFDCGDKLGYMQAFTEYSLRHDKFGNEFKDFIKQLAKT 294
Cdd:COG1210  236 LAKEEPVYAYEFEGKRYDCGDKLGYLKATVEFALKRPDLGEEFREYLKELLKE 288
 
Name Accession Description Interval E-value
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
2-294 5.97e-175

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


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 484.54  E-value: 5.97e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396   2 KVIIPVAGLGTRMLPATKAIPKEMLTIADKPLIQYIVNECVAAGIKEIVLVTHSSKNAIENHFDTSFELETMLEKRVKRQ 81
Cdd:COG1210    5 KAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVTGRGKRAIEDHFDRSYELEATLEAKGKEE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396  82 LLDEVRSIVPkDVTLMHVRQGQAKGLGHAVLCGRAVVGNEPFAVVLPDVILADfaanqKTENLAAMIKRFNETKHSQIMV 161
Cdd:COG1210   85 LLEEVRSISP-LANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDS-----EKPCLKQMIEVYEETGGSVIAV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396 162 APVPKEDVSSYGVADCAGVDipaGETAKIVKMVEKPSVEEAPSNLAVVGRYVFSENIWDLLEKTPVGVGDEIQLTDAIDM 241
Cdd:COG1210  159 QEVPPEEVSKYGIVDGEEIE---GGVYRVTGLVEKPAPEEAPSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDAIAA 235

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 517482396 242 LIEQETVEAFHMTGRTFDCGDKLGYMQAFTEYSLRHDKFGNEFKDFIKQLAKT 294
Cdd:COG1210  236 LAKEEPVYAYEFEGKRYDCGDKLGYLKATVEFALKRPDLGEEFREYLKELLKE 288
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
2-291 7.72e-166

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 462.07  E-value: 7.72e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396   2 KVIIPVAGLGTRMLPATKAIPKEMLTIADKPLIQYIVNECVAAGIKEIVLVTHSSKNAIENHFDTSFELETMLEKRVKRQ 81
Cdd:PRK13389  10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFDTSFELEAMLEKRVKRQ 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396  82 LLDEVRSIVPKDVTLMHVRQGQAKGLGHAVLCGRAVVGNEPFAVVLPDVILADFAANQKTENLAAMIKRFNETKHSQIMV 161
Cdd:PRK13389  90 LLDEVQSICPPHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILDEYESDLSQDNLAEMIRRFDETGHSQIMV 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396 162 APVpkEDVSSYGVADCAGVDIPAGETAKIVKMVEKPSVEEAPSNLAVVGRYVFSENIWDLLEKTPVGVGDEIQLTDAIDM 241
Cdd:PRK13389 170 EPV--ADVTAYGVVDCKGVELAPGESVPMVGVVEKPKADVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTDAIDM 247

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 517482396 242 LIEQETVEAFHMTGRTFDCGDKLGYMQAFTEYSLRHDKFGNEFKDFIKQL 291
Cdd:PRK13389 248 LIEKETVEAYHMKGKSHDCGNKLGYMQAFVEYGIRHNTLGTEFKAWLEEE 297
galU TIGR01099
UTP--glucose-1-phosphate uridylyltransferase; Built to distinquish between the highly similar ...
 1-269 3.50e-157

UTP--glucose-1-phosphate uridylyltransferase; Built to distinquish between the highly similar genes galU and galF [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 273443 [Multi-domain]  Cd Length: 260  Bit Score: 438.71  E-value: 3.50e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396    1 MKVIIPVAGLGTRMLPATKAIPKEMLTIADKPLIQYIVNECVAAGIKEIVLVTHSSKNAIENHFDTSFELETMLEKRVKR 80
Cdd:TIGR01099   1 RKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYIVEEAVEAGIEEIVFVTGRGKRAIEDHFDYSYELEHQLEKRGKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396   81 QLLDEVRSIVPKdVTLMHVRQGQAKGLGHAVLCGRAVVGNEPFAVVLPDVILAdfaanQKTENLAAMIKRFNETKHSQIM 160
Cdd:TIGR01099  81 ELLEEVRKISNL-ATIFYVRQKEQKGLGHAVLCARPFVGDEPFAVILGDDIVV-----NEEPALKQMIKAYEKTGCSIIA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396  161 VAPVPKEDVSSYGVADCAGVDipaGETAKIVKMVEKPSVEEAPSNLAVVGRYVFSENIWDLLEKTPVGVGDEIQLTDAID 240
Cdd:TIGR01099 155 VQEVPKEEVSKYGVIDGEGIE---KDLYKVKNMVEKPKPEEAPSNLAIVGRYILTPDIFDLLEETPPGKGGEIQLTDAIN 231

                         250       260
                  ....*....|....*....|....*....
gi 517482396  241 MLIEQETVEAFHMTGRTFDCGDKLGYMQA 269
Cdd:TIGR01099 232 KLLENETVLAYKFNGKRYDCGSKLGYLEA 260
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 1-276 9.11e-152

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: 425.02  E-value: 9.11e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396   1 MKVIIPVAGLGTRMLPATKAIPKEMLTIADKPLIQYIVNECVAAGIKEIVLVTHSSKNAIENHFDTSFELETMLEKRVKR 80
Cdd:cd02541    1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRGKRAIEDHFDRSYELEETLEKKGKT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396  81 QLLDEVRsIVPKDVTLMHVRQGQAKGLGHAVLCGRAVVGNEPFAVVLPDVILadfaaNQKTENLAAMIKRFNETKHSQIM 160
Cdd:cd02541   81 DLLEEVR-IISDLANIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLI-----DSKEPCLKQLIEAYEKTGASVIA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396 161 VAPVPKEDVSSYGVADCAGVDipaGETAKIVKMVEKPSVEEAPSNLAVVGRYVFSENIWDLLEKTPVGVGDEIQLTDAID 240
Cdd:cd02541  155 VEEVPPEDVSKYGIVKGEKID---GDVFKVKGLVEKPKPEEAPSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTDAIA 231

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 517482396 241 MLIEQETVEAFHMTGRTFDCGDKLGYMQAFTEYSLR 276
Cdd:cd02541  232 KLLEEEPVYAYVFEGKRYDCGNKLGYLKATVEFALK 267
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-224 7.63e-23

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: 94.24  E-value: 7.63e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396    2 KVIIPVAGLGTRMLPATKAIPKEMLTIADK-PLIQYIVNECVAAGIKEIVLVThssknaieNHFDtSFELEtmlekrvkR 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVIL--------TQEH-RFMLN--------E 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396   81 QLLDEvrSIVPKDVTLMHvrQGQAKGLGHAVLCGRAVVGNEPF-AVVLPDVILADFAanqktenLAAMIKRFNETKhSQI 159
Cdd:pfam00483  64 LLGDG--SKFGVQITYAL--QPEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMD-------LEQAVKFHIEKA-ADA 131

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517482396  160 MVA--PVPKEDVSSYGVadcagvdIPAGETAKIVKMVEKPSVEEApSNLAVVGRYVFSENIWDLLEK 224
Cdd:pfam00483 132 TVTfgIVPVEPPTGYGV-------VEFDDNGRVIRFVEKPKLPKA-SNYASMGIYIFNSGVLDFLAK 190
 
Name Accession Description Interval E-value
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
2-294 5.97e-175

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


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 484.54  E-value: 5.97e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396   2 KVIIPVAGLGTRMLPATKAIPKEMLTIADKPLIQYIVNECVAAGIKEIVLVTHSSKNAIENHFDTSFELETMLEKRVKRQ 81
Cdd:COG1210    5 KAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVTGRGKRAIEDHFDRSYELEATLEAKGKEE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396  82 LLDEVRSIVPkDVTLMHVRQGQAKGLGHAVLCGRAVVGNEPFAVVLPDVILADfaanqKTENLAAMIKRFNETKHSQIMV 161
Cdd:COG1210   85 LLEEVRSISP-LANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDS-----EKPCLKQMIEVYEETGGSVIAV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396 162 APVPKEDVSSYGVADCAGVDipaGETAKIVKMVEKPSVEEAPSNLAVVGRYVFSENIWDLLEKTPVGVGDEIQLTDAIDM 241
Cdd:COG1210  159 QEVPPEEVSKYGIVDGEEIE---GGVYRVTGLVEKPAPEEAPSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDAIAA 235

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 517482396 242 LIEQETVEAFHMTGRTFDCGDKLGYMQAFTEYSLRHDKFGNEFKDFIKQLAKT 294
Cdd:COG1210  236 LAKEEPVYAYEFEGKRYDCGDKLGYLKATVEFALKRPDLGEEFREYLKELLKE 288
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
2-291 7.72e-166

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 462.07  E-value: 7.72e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396   2 KVIIPVAGLGTRMLPATKAIPKEMLTIADKPLIQYIVNECVAAGIKEIVLVTHSSKNAIENHFDTSFELETMLEKRVKRQ 81
Cdd:PRK13389  10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFDTSFELEAMLEKRVKRQ 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396  82 LLDEVRSIVPKDVTLMHVRQGQAKGLGHAVLCGRAVVGNEPFAVVLPDVILADFAANQKTENLAAMIKRFNETKHSQIMV 161
Cdd:PRK13389  90 LLDEVQSICPPHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILDEYESDLSQDNLAEMIRRFDETGHSQIMV 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396 162 APVpkEDVSSYGVADCAGVDIPAGETAKIVKMVEKPSVEEAPSNLAVVGRYVFSENIWDLLEKTPVGVGDEIQLTDAIDM 241
Cdd:PRK13389 170 EPV--ADVTAYGVVDCKGVELAPGESVPMVGVVEKPKADVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTDAIDM 247

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 517482396 242 LIEQETVEAFHMTGRTFDCGDKLGYMQAFTEYSLRHDKFGNEFKDFIKQL 291
Cdd:PRK13389 248 LIEKETVEAYHMKGKSHDCGNKLGYMQAFVEYGIRHNTLGTEFKAWLEEE 297
galU TIGR01099
UTP--glucose-1-phosphate uridylyltransferase; Built to distinquish between the highly similar ...
 1-269 3.50e-157

UTP--glucose-1-phosphate uridylyltransferase; Built to distinquish between the highly similar genes galU and galF [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 273443 [Multi-domain]  Cd Length: 260  Bit Score: 438.71  E-value: 3.50e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396    1 MKVIIPVAGLGTRMLPATKAIPKEMLTIADKPLIQYIVNECVAAGIKEIVLVTHSSKNAIENHFDTSFELETMLEKRVKR 80
Cdd:TIGR01099   1 RKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYIVEEAVEAGIEEIVFVTGRGKRAIEDHFDYSYELEHQLEKRGKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396   81 QLLDEVRSIVPKdVTLMHVRQGQAKGLGHAVLCGRAVVGNEPFAVVLPDVILAdfaanQKTENLAAMIKRFNETKHSQIM 160
Cdd:TIGR01099  81 ELLEEVRKISNL-ATIFYVRQKEQKGLGHAVLCARPFVGDEPFAVILGDDIVV-----NEEPALKQMIKAYEKTGCSIIA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396  161 VAPVPKEDVSSYGVADCAGVDipaGETAKIVKMVEKPSVEEAPSNLAVVGRYVFSENIWDLLEKTPVGVGDEIQLTDAID 240
Cdd:TIGR01099 155 VQEVPKEEVSKYGVIDGEGIE---KDLYKVKNMVEKPKPEEAPSNLAIVGRYILTPDIFDLLEETPPGKGGEIQLTDAIN 231

                         250       260
                  ....*....|....*....|....*....
gi 517482396  241 MLIEQETVEAFHMTGRTFDCGDKLGYMQA 269
Cdd:TIGR01099 232 KLLENETVLAYKFNGKRYDCGSKLGYLEA 260
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 1-276 9.11e-152

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: 425.02  E-value: 9.11e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396   1 MKVIIPVAGLGTRMLPATKAIPKEMLTIADKPLIQYIVNECVAAGIKEIVLVTHSSKNAIENHFDTSFELETMLEKRVKR 80
Cdd:cd02541    1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRGKRAIEDHFDRSYELEETLEKKGKT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396  81 QLLDEVRsIVPKDVTLMHVRQGQAKGLGHAVLCGRAVVGNEPFAVVLPDVILadfaaNQKTENLAAMIKRFNETKHSQIM 160
Cdd:cd02541   81 DLLEEVR-IISDLANIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLI-----DSKEPCLKQLIEAYEKTGASVIA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396 161 VAPVPKEDVSSYGVADCAGVDipaGETAKIVKMVEKPSVEEAPSNLAVVGRYVFSENIWDLLEKTPVGVGDEIQLTDAID 240
Cdd:cd02541  155 VEEVPPEDVSKYGIVKGEKID---GDVFKVKGLVEKPKPEEAPSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTDAIA 231

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 517482396 241 MLIEQETVEAFHMTGRTFDCGDKLGYMQAFTEYSLR 276
Cdd:cd02541  232 KLLEEEPVYAYVFEGKRYDCGNKLGYLKATVEFALK 267
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
1-291 1.91e-129

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 369.99  E-value: 1.91e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396   1 MKVIIPVAGLGTRMLPATKAIPKEMLTIADKPLIQYIVNECVAAGIKEIVLVTHSSKNAIENHFDTSFELETMLEKRVKR 80
Cdd:PRK10122   4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAVENHFDTSYELESLLEQRVKR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396  81 QLLDEVRSIVPKDVTLMHVRQGQAKGLGHAVLCGRAVVGNEPFAVVLPDVILADFAANQKTENLAAMIKRFNETKHSQIM 160
Cdd:PRK10122  84 QLLAEVQSICPPGVTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPDVVIDDASADPLRYNLAAMIARFNETGRSQVL 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396 161 VAPVPkEDVSSYGVADCAGVDIPAGETAKIVKMVEKPSVEEA-PSNLAVVGRYVFSENIWDLLEKTPVGVGDEIQLTDAI 239
Cdd:PRK10122 164 AKRMP-GDLSEYSVIQTKEPLDREGKVSRIVEFIEKPDQPQTlDSDLMAVGRYVLSADIWPELERTEPGAWGRIQLTDAI 242

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 517482396 240 DMLIEQETVEAFHMTGRTFDCGDKLGYMQAFTEYSLRHDKFGNEFKDFIKQL 291
Cdd:PRK10122 243 AELAKKQSVDAMLMTGDSYDCGKKMGYMQAFVKYGLRNLKEGAKFRKGIEKL 294
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 3-261 9.91e-55

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: 176.62  E-value: 9.91e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396   3 VIIPVAGLGTRMLPATKAIPKEMLTIADKPLIQYIVNECVAAGIKEIVLVTHSSKNAIENHFDTSFELetmlekrvkrql 82
Cdd:cd04181    1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGSKF------------ 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396  83 ldevrsivPKDVTLmhVRQGQAKGLGHAVLCGRAVVGNEPFAVVLPDVILadfaanqkTENLAAMIKRFNETK-HSQIMV 161
Cdd:cd04181   69 --------GVNIEY--VVQEEPLGTAGAVRNAEDFLGDDDFLVVNGDVLT--------DLDLSELLRFHREKGaDATIAV 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396 162 APVpkEDVSSYGVADCAGVDipagetaKIVKMVEKPSVEEapSNLAVVGRYVFSENIWDLLEKTPVGVGDEiqLTDAIDM 241
Cdd:cd04181  131 KEV--EDPSRYGVVELDDDG-------RVTRFVEKPTLPE--SNLANAGIYIFEPEILDYIPEILPRGEDE--LTDAIPL 197

                        250       260
                 ....*....|....*....|
gi 517482396 242 LIEQETVEAFHMTGRTFDCG 261
Cdd:cd04181  198 LIEEGKVYGYPVDGYWLDIG 217
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 1-269 9.97e-51

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: 166.98  E-value: 9.97e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396   1 MKVIIPVAGLGTRMLPATKAIPKEMLTIADKPLIQYIVNECVAAGIKEIVLVTHSSKNAIENHfdtsfeletmlekrvkr 80
Cdd:cd04189    1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEA----------------- 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396  81 qlldeVRSIVPKDVTLMHVRQGQAKGLGHAVLCGRAVVGNEPFAVVLPDVILAdfaanqktENLAAMIKRFNETKHS-QI 159
Cdd:cd04189   64 -----LGDGSRFGVRITYILQEEPLGLAHAVLAARDFLGDEPFVVYLGDNLIQ--------EGISPLVRDFLEEDADaSI 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396 160 MVAPVPkeDVSSYGVADCagvdipagETAKIVKMVEKPsvEEAPSNLAVVGRYVFSENIWDLLEKTPVGVGDEIQLTDAI 239
Cdd:cd04189  131 LLAEVE--DPRRFGVAVV--------DDGRIVRLVEKP--KEPPSNLALVGVYAFTPAIFDAISRLKPSWRGELEITDAI 198

                        250       260       270
                 ....*....|....*....|....*....|.
gi 517482396 240 DMLIEQ-ETVEAFHMTGRTFDCGDKLGYMQA 269
Cdd:cd04189  199 QWLIDRgRRVGYSIVTGWWKDTGTPEDLLEA 229
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-269 7.01e-47

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 159.10  E-value: 7.01e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396   1 MKVIIPVAGLGTRMLPATKAIPKEMLTIADKPLIQYIVNECVAAGIKEIVLVThssknaienhfdTSFELEtmlekRVKR 80
Cdd:COG1209    1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIIS------------TPEDGP-----QFER 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396  81 QLLDEVRsivpKDVTLMHVRQGQAKGLGHAVLCGRAVVGNEPFAVVLPDVILadfaanqKTENLAAMIKRFNETKH-SQI 159
Cdd:COG1209   64 LLGDGSQ----LGIKISYAVQPEPLGLAHAFIIAEDFIGGDPVALVLGDNIF-------YGDGLSELLREAAARESgATI 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396 160 MVAPVpkEDVSSYGVADcagVDipagETAKIVKMVEKPsvEEAPSNLAVVGRYVFSENIWDLLEKTPVGVGDEIQLTDAI 239
Cdd:COG1209  133 FGYKV--EDPERYGVVE---FD----EDGRVVSLEEKP--KEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDAN 201

                        250       260       270
                 ....*....|....*....|....*....|...
gi 517482396 240 DMLIEQETVEAFHMtGRTF---DCGDKLGYMQA 269
Cdd:COG1209  202 QAYLERGKLVVELL-GRGFawlDTGTHESLLEA 233
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 2-261 7.60e-44

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: 149.53  E-value: 7.60e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396   2 KVIIPVAGLGTRMLPATKAIPKEMLTIADKPLIQYIVNECVAAGIKEIVLVTHSSKNAIENHFDTSFELetmlekrvkrq 81
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRF----------- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396  82 lldevrsivpkDVTLMHVRQGQAKGLGHAVLCGRAVVGNEPFAVVLPDvILADFaanqkteNLAAMIKRFNETKhSQIMV 161
Cdd:COG1208   70 -----------GVRITYVDEGEPLGTGGALKRALPLLGDEPFLVLNGD-ILTDL-------DLAALLAFHREKG-ADATL 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396 162 APVPKEDVSSYGVADCAGVDipagetaKIVKMVEKPsvEEAPSNLAVVGRYVFSENIWDLLEKtpvgvGDEIQLTDAIDM 241
Cdd:COG1208  130 ALVPVPDPSRYGVVELDGDG-------RVTRFVEKP--EEPPSNLINAGIYVLEPEIFDYIPE-----GEPFDLEDLLPR 195

                        250       260
                 ....*....|....*....|
gi 517482396 242 LIEQETVEAFHMTGRTFDCG 261
Cdd:COG1208  196 LIAEGRVYGYVHDGYWLDIG 215
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-224 7.63e-23

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: 94.24  E-value: 7.63e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396    2 KVIIPVAGLGTRMLPATKAIPKEMLTIADK-PLIQYIVNECVAAGIKEIVLVThssknaieNHFDtSFELEtmlekrvkR 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVIL--------TQEH-RFMLN--------E 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396   81 QLLDEvrSIVPKDVTLMHvrQGQAKGLGHAVLCGRAVVGNEPF-AVVLPDVILADFAanqktenLAAMIKRFNETKhSQI 159
Cdd:pfam00483  64 LLGDG--SKFGVQITYAL--QPEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMD-------LEQAVKFHIEKA-ADA 131

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517482396  160 MVA--PVPKEDVSSYGVadcagvdIPAGETAKIVKMVEKPSVEEApSNLAVVGRYVFSENIWDLLEK 224
Cdd:pfam00483 132 TVTfgIVPVEPPTGYGV-------VEFDDNGRVIRFVEKPKLPKA-SNYASMGIYIFNSGVLDFLAK 190
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 1-269 1.18e-22

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: 93.79  E-value: 1.18e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396   1 MKVIIPVAGLGTRMLPATKAIPKEMLTIADKPLIQYIVNECVAAGIKEIVLVthSSKNAIENHfdtsfeletmlekrvkR 80
Cdd:cd02538    1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILII--STPEDLPLF----------------K 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396  81 QLLDEVRSIvpkDVTLMHVRQGQAKGLGHAVLCGRAVVGNEPFAVVLPDVILADfaanqktENLAAMIKRFNETKH-SQI 159
Cdd:cd02538   63 ELLGDGSDL---GIRITYAVQPKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYG-------QGLSPILQRAAAQKEgATV 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396 160 MVAPVPkeDVSSYGVADcagVDipagETAKIVKMVEKPsvEEAPSNLAVVGRYVFSENIWDLLEK-TPVGVGdEIQLTDA 238
Cdd:cd02538  133 FGYEVN--DPERYGVVE---FD----ENGRVLSIEEKP--KKPKSNYAVTGLYFYDNDVFEIAKQlKPSARG-ELEITDV 200

                        250       260       270
                 ....*....|....*....|....*....|....
gi 517482396 239 IDMLIEQETVEAFHMtGRTF---DCGDKLGYMQA 269
Cdd:cd02538  201 NNEYLEKGKLSVELL-GRGFawlDTGTHESLLEA 233
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 3-261 6.59e-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: 74.86  E-value: 6.59e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396   3 VIIPVAGLGTRMLPATKAIPKEMLTIADKPLIQYIVNECVAAGIKEIVLVTHSSKNAIENHF-DTSfeletmlEKRVKRQ 81
Cdd:cd06426    1 VVIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNYLAEMIEDYFgDGS-------KFGVNIS 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396  82 LLDEvrsivPKdvtlmhvRQGQAKGLGhaVLCGRAvvgNEPFAVVLPDVILadfaanqkTENLAAMIKRFNETKHSQIMV 161
Cdd:cd06426   74 YVRE-----DK-------PLGTAGALS--LLPEKP---TDPFLVMNGDILT--------NLNYEHLLDFHKENNADATVC 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396 162 A-----PVPkedvssYGVADCAGVdipagetaKIVKMVEKPSVeeapSNLAVVGRYVFSENIWDLLEKtpvgvGDEIQLT 236
Cdd:cd06426  129 VreyevQVP------YGVVETEGG--------RITSIEEKPTH----SFLVNAGIYVLEPEVLDLIPK-----NEFFDMP 185

                        250       260
                 ....*....|....*....|....*.
gi 517482396 237 DAIDMLI-EQETVEAFHMTGRTFDCG 261
Cdd:cd06426  186 DLIEKLIkEGKKVGVFPIHEYWLDIG 211
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 1-233 2.31e-14

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: 70.70  E-value: 2.31e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396   1 MKVIIPVAGLGTRMLPATKAIPKEMLTIADKPLIQYIVNECVAAGIKEIVL-VTHSSKNaienhfdtsfeLETMLEKRVK 79
Cdd:cd06425    1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILaVNYRPED-----------MVPFLKEYEK 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396  80 RQLLDEVRSIvpKDVTLmhvrqGQAKGLGHA--VLCGravvGNEPFAVVLPDVIlADFAanqktenLAAMIKrFNeTKHS 157
Cdd:cd06425   70 KLGIKITFSI--ETEPL-----GTAGPLALArdLLGD----DDEPFFVLNSDVI-CDFP-------LAELLD-FH-KKHG 128

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517482396 158 Q---IMVAPVpkEDVSSYGVADCagvdipAGETAKIVKMVEKPSveEAPSNLAVVGRYVFSENIWDLLEKTPVGVGDEI 233
Cdd:cd06425  129 AegtILVTKV--EDPSKYGVVVH------DENTGRIERFVEKPK--VFVGNKINAGIYILNPSVLDRIPLRPTSIEKEI 197
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 2-269 2.33e-14

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: 70.68  E-value: 2.33e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396   2 KVIIPVAGLGTRMLPATKAIPKEMLTIADKPLIQYIVNECVAAGIKEIVLVTHSSKNAIENHFDTSFeletmleKRVKRQ 81
Cdd:cd06422    1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHLGDSR-------FGLRIT 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396  82 LLDEVRSIvpkdvtlmhvrQGQAKGLGHAvlcgRAVVGNEPFAVVLPDVILadfaanqkTENLAAMIKRFNETKHSQIMV 161
Cdd:cd06422   74 ISDEPDEL-----------LETGGGIKKA----LPLLGDEPFLVVNGDILW--------DGDLAPLLLLHAWRMDALLLL 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396 162 AP-VPKEDVSSYGvadcagvDIPAGETAKIvkmveKPSVEEAPSNLAVVGRYVFSENIWDLLEKTPVGvgdeiqLTDAID 240
Cdd:cd06422  131 LPlVRNPGHNGVG-------DFSLDADGRL-----RRGGGGAVAPFTFTGIQILSPELFAGIPPGKFS------LNPLWD 192

                        250       260
                 ....*....|....*....|....*....
gi 517482396 241 MLIEQETVEAFHMTGRTFDCGDKLGYMQA 269
Cdd:cd06422  193 RAIAAGRLFGLVYDGLWFDVGTPERLLAA 221
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
2-65 2.19e-13

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 67.96  E-value: 2.19e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517482396   2 KVIIPVAGLGTRMLPATKAIPKEMLTIADKPLIQYIVNECVAAGIKEIVLVTHSSKNAIENHFD 65
Cdd:COG1213    1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEALA 64
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 2-274 9.07e-12

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 64.31  E-value: 9.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396   2 KVIIPVAGLGTRMLPATKAIPKEMLTIADKPLIQYIVNECVAAGIKEIVLVTHSSknaienhfDTSfeletmlekRVKRQ 81
Cdd:PRK15480   5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQ--------DTP---------RFQQL 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396  82 LLDEVRSivpkDVTLMHVRQGQAKGLGHAVLCGRAVVGNEPFAVVLPDVIladFAANQKTENLAAMIkrfneTKHSQIMV 161
Cdd:PRK15480  68 LGDGSQW----GLNLQYKVQPSPDGLAQAFIIGEEFIGGDDCALVLGDNI---FYGHDLPKLMEAAV-----NKESGATV 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396 162 APVPKEDVSSYGVadcagVDIPAGETAkiVKMVEKPSveEAPSNLAVVGRYVFSENIWDLLEKTPVGVGDEIQLTDAIDM 241
Cdd:PRK15480 136 FAYHVNDPERYGV-----VEFDQNGTA--ISLEEKPL--QPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRI 206

                        250       260       270
                 ....*....|....*....|....*....|...
gi 517482396 242 LIEQETVeAFHMTGRTFDCGDKlGYMQAFTEYS 274
Cdd:PRK15480 207 YMEQGRL-SVAMMGRGYAWLDT-GTHQSLIEAS 237
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 3-72 1.04e-11

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: 63.41  E-value: 1.04e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396   3 VIIPVAGLGTRMLPATKAIPKEMLTIADKPLIQYIVNECVAAGIKEIVLVTHSSKNAIENHFDTSFELET 72
Cdd:cd02523    1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKKYPNIKF 70
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 1-69 3.30e-11

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


Pssm-ID: 133041 [Multi-domain]  Cd Length: 214  Bit Score: 61.52  E-value: 3.30e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396   1 MKVIIPVAGLGTRMLPATKAIPKEMLTIADKPLIQYIVNECVAAGIKEI-VLVTHSSKNAIENHFDTSFE 69
Cdd:cd04198    1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDViVVVPEEEQAEISTYLRSFPL 70
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 3-65 5.56e-11

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: 61.03  E-value: 5.56e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517482396   3 VIIPVAGLGTRMLPATKAIPKEMLTIADKPLIQYIVNECVAAGIKEIVLVTHSSKNAIENHFD 65
Cdd:cd06915    1 AVILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYLAEQIEEYFG 63
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 3-253 9.40e-11

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


Pssm-ID: 133020 [Multi-domain]  Cd Length: 229  Bit Score: 60.61  E-value: 9.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396   3 VIIPVAGLGTRMlpatK-AIPKEMLTIADKPLIQYIVNECVAAGIKEIVLVTHSSKnaienhfdtsfeletmlekrvkrq 81
Cdd:cd02540    1 AVILAAGKGTRM----KsDLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGA------------------------ 52

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396  82 llDEVRSIVPK-DVTLmhVRQGQAKGLGHAVLCGRAVVG--NEPFAVVLPDVILADfaanqkTENLAAMIKRFNETKHSQ 158
Cdd:cd02540   53 --EQVKKALANpNVEF--VLQEEQLGTGHAVKQALPALKdfEGDVLVLYGDVPLIT------PETLQRLLEAHREAGADV 122

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396 159 IMVAPVPkEDVSSYG--VADcagvdipagETAKIVKMVEkpSVEEAPSNLAVV----GRYVF-SENIWDLLEKtpvgVGD 231
Cdd:cd02540  123 TVLTAEL-EDPTGYGriIRD---------GNGKVLRIVE--EKDATEEEKAIRevnaGIYAFdAEFLFEALPK----LTN 186

                        250       260
                 ....*....|....*....|....*...
gi 517482396 232 -----EIQLTDAIDMLIEQ-ETVEAFHM 253
Cdd:cd02540  187 nnaqgEYYLTDIIALAVADgLKVAAVLA 214
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 1-68 6.64e-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: 6.64e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517482396   1 MKVIIPVAGLGTRMLPATKAIPKEMLTIADKPLIQYIVNECVAAGIKEIVLVTHSSKNAIENHFDTSF 68
Cdd:cd02507    1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQAIIEHLLKSK 68
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-248 4.15e-09

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 57.08  E-value: 4.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396   1 MKVIIPVAGLGTRMlpaTKAIPKEMLTIADKPLIQYIVNECVAAGIKEIVLVTHSSknaienhfdtsfeletmlekrvkr 80
Cdd:PRK14357   1 MRALVLAAGKGTRM---KSKIPKVLHKISGKPMINWVIDTAKKVAQKVGVVLGHEA------------------------ 53

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396  81 qllDEVRSIVPKDVTLMHvrQGQAKGLGHAVLCGRAVVG-NEPFAVVLPDVILADFaanqktENLAAMIKRFNEtKHSQI 159
Cdd:PRK14357  54 ---ELVKKLLPEWVKIFL--QEEQLGTAHAVMCARDFIEpGDDLLILYGDVPLISE------NTLKRLIEEHNR-KGADV 121

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396 160 MVAPVPKEDVSSYGVAdcagvdIPAGETAKIVKMVEKPSVEEAPSNLAvVGRYVFSENIwdLLEKTPVGVGDEIQ----L 235
Cdd:PRK14357 122 TILVADLEDPTGYGRI------IRDGGKYRIVEDKDAPEEEKKIKEIN-TGIYVFSGDF--LLEVLPKIKNENAKgeyyL 192

                        250
                 ....*....|...
gi 517482396 236 TDAIDMLIEQETV 248
Cdd:PRK14357 193 TDAVNFAEKVRVV 205
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 1-157 5.36e-09

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: 56.57  E-value: 5.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396   1 MKVIIPVAGLGTRMlpatK-AIPKEMLTIADKPLIQYIVNECVAAGIKEIVLVTHSSKNAIENHFdtsfeletmlekrvk 79
Cdd:COG1207    3 LAVVILAAGKGTRM----KsKLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVRAAL--------------- 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396  80 rqlldevrsivpKDVTLMHVRQGQAKGLGHAVLCGRAVVGNEPFAV-VLP-DVILADfaanqkTENLAAMIKRFNETKHS 157
Cdd:COG1207   64 ------------ADLDVEFVLQEEQLGTGHAVQQALPALPGDDGTVlVLYgDVPLIR------AETLKALLAAHRAAGAA 125
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-253 8.10e-07

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 49.83  E-value: 8.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396   3 VIIPVAGLGTRMlpaTKAIPKEMLTIADKPLIQYIVNECVAAGIKEIVLVT-HSSknaienhfdtsfeletmleKRVKRQ 81
Cdd:PRK14354   5 AIILAAGKGTRM---KSKLPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVgHGA-------------------EEVKEV 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396  82 LLDEVRsivpkdvtlmHVRQGQAKGLGHAVLCGRAVVGNEP--FAVVLPDVILAdfaanqKTENLAAMIKRFNETK-HSQ 158
Cdd:PRK14354  63 LGDRSE----------FALQEEQLGTGHAVMQAEEFLADKEgtTLVICGDTPLI------TAETLKNLIDFHEEHKaAAT 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396 159 IMVAPVpkEDVSSYG--VADcagvdiPAGETAKIVKmvEK-PSVEEAPSNLAVVGRYVF-SENIWDLLEK-TPVGVGDEI 233
Cdd:PRK14354 127 ILTAIA--ENPTGYGriIRN------ENGEVEKIVE--QKdATEEEKQIKEINTGTYCFdNKALFEALKKiSNDNAQGEY 196

                        250       260
                 ....*....|....*....|.
gi 517482396 234 QLTDAIDMLIEQ-ETVEAFHM 253
Cdd:PRK14354 197 YLTDVIEILKNEgEKVGAYQT 217
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 3-164 3.90e-06

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: 46.40  E-value: 3.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396   3 VIIPVAGLGTRMLPatkaiPKEMLTIADKPLIQYIVNECVAAGIKEIVLVTHSSKNAIENHFDtsfeletmlekrvkrql 82
Cdd:cd04182    3 AIILAAGRSSRMGG-----NKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALA----------------- 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396  83 LDEVRSIVPKDvtlmhvrqgQAKGLGHAVLCGRAVVGNEPFAVVlpdVILADfaanQ---KTENLAAMIKRFNETKHSqi 159
Cdd:cd04182   61 GLPVVVVINPD---------WEEGMSSSLAAGLEALPADADAVL---ILLAD----QplvTAETLRALIDAFREDGAG-- 122


                 ....*
gi 517482396 160 MVAPV 164
Cdd:cd04182  123 IVAPV 127
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 1-254 4.33e-06

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 47.67  E-value: 4.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396   1 MKVIIPVAGLGTRMlpaTKAIPKEMLTIADKPLIQYIVNECVAAGIKEIVLVTHSSKNAIENHFDTSfeletmlekrvkr 80
Cdd:PRK14358   8 LDVVILAAGQGTRM---KSALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGAEQVEAALQGS------------- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396  81 qlldevrsivpkdvTLMHVRQGQAKGLGHAVLCGRAVV--GNEPFAVVLPDVILAdfaanqKTENLAAMIKRFNETKHS- 157
Cdd:PRK14358  72 --------------GVAFARQEQQLGTGDAFLSGASALteGDADILVLYGDTPLL------RPDTLRALVADHRAQGSAm 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396 158 QIMVAPVPkeDVSSYGvadcagvDIPAGETAKIVKMVEKPSVEEAPSNLAVV--GRYVFSENIWDLLEK----TPVGvgd 231
Cdd:PRK14358 132 TILTGELP--DATGYG-------RIVRGADGAVERIVEQKDATDAEKAIGEFnsGVYVFDARAPELARRigndNKAG--- 199

                        250       260
                 ....*....|....*....|....
gi 517482396 232 EIQLTDAIDML-IEQETVEAFHMT 254
Cdd:PRK14358 200 EYYLTDLLGLYrAGGAQVRAFKLS 223
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 3-225 5.03e-06

N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose pyrophosphorylase; N-terminal domain of the M1P-guanylyltransferase A-isoform like proteins: The proteins of this family are likely to be a isoform of GDP-mannose pyrophosphorylase. Their sequences are highly conserved with mannose-1-phosphate guanyltransferase, but generally about 40-60 bases longer. GDP-mannose pyrophosphorylase (GTP: alpha-d-mannose-1-phosphate guanyltransferase) catalyzes the formation of GDP-d-mannose from GTP and alpha-d-mannose-1-Phosphate. It contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain. GDP-d-mannose is the activated form of mannose for formation of cell wall lipoarabinomannan and various mannose-containing glycolipids and polysaccharides. The function of GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability. Repression of GDP-mannose pyrophosphorylase in yeast leads to phenotypes including cell lysis, defective cell wall, and failure of polarized growth and cell separation.


Pssm-ID: 133050 [Multi-domain]  Cd Length: 257  Bit Score: 46.86  E-value: 5.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396   3 VIIPVAG--LGTRMLPATKAIPKEMLTIADKPLIQYIVNECVA-AGIKEIVLVThssknaienhFDTSFELETMLEkRVK 79
Cdd:cd06428    1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKvPDLKEVLLIG----------FYPESVFSDFIS-DAQ 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396  80 RQLLDEVRSIvpKDVTLMhvrqGQAKGLGH---AVLCGravvGNEPFAVVLPDVIlADFAanqktenLAAMIkRFNETK- 155
Cdd:cd06428   70 QEFNVPIRYL--QEYKPL----GTAGGLYHfrdQILAG----NPSAFFVLNADVC-CDFP-------LQELL-EFHKKHg 130

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517482396 156 -HSQIMVAPVPKEDVSSYG--VADcagvdipaGETAKIVKMVEKPsvEEAPSNLAVVGRYVFSENIWDLLEKT 225
Cdd:cd06428  131 aSGTILGTEASREQASNYGciVED--------PSTGEVLHYVEKP--ETFVSDLINCGVYLFSPEIFDTIKKA 193
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 3-54 5.45e-06

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


Pssm-ID: 133009 [Multi-domain]  Cd Length: 218  Bit Score: 46.36  E-value: 5.45e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 517482396   3 VIIPVAGLGTRMlpaTKAIPKEMLTIADKPLIQYIVNECVAAG-IKEIVLVTH 54
Cdd:cd02516    3 AIILAAGSGSRM---GADIPKQFLELGGKPVLEHTLEAFLAHPaIDEIVVVVP 52
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
3-164 3.40e-05

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 43.61  E-value: 3.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396   3 VIIPVAGLGTRMlpatkAIPKEMLTIADKPLIQYIVNECVAAGIKEIVLVTHSSKNAIENHFDtsfeletmlekrvkrql 82
Cdd:COG2068    6 AIILAAGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADAEEVAAALA----------------- 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396  83 ldevrsivPKDVTLMHVRQgQAKGLGHAVLCG-RAVVGNEPFAVVLPdviladfaANQ---KTENLAAMIKRFNETKHSq 158
Cdd:COG2068   64 --------GLGVRVVVNPD-WEEGMSSSLRAGlAALPADADAVLVLL--------GDQplvTAETLRRLLAAFRESPAS- 125


                 ....*.
gi 517482396 159 iMVAPV 164
Cdd:COG2068  126 -IVAPT 130
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-196 3.45e-05

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 45.12  E-value: 3.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396   4 IIPVAGLGTRMlpaTKAIPKEMLTIADKPLIQYIVNECVAAGIKEIVLVTHSSKNAIENHF----DTSFELetmlekrvk 79
Cdd:PRK14355   7 IILAAGKGTRM---KSDLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHFagdgDVSFAL--------- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396  80 rqlldevrsivpkdvtlmhvrQGQAKGLGHAVLCGRAVVgnEPFAVVLpdVILADFAANQKTENLAAMIKrFNETKHSQI 159
Cdd:PRK14355  75 ---------------------QEEQLGTGHAVACAAPAL--DGFSGTV--LILCGDVPLLRAETLQGMLA-AHRATGAAV 128

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 517482396 160 MVAPVPKEDVSSYGvadcagvDIPAGETAKIVKMVEK 196
Cdd:PRK14355 129 TVLTARLENPFGYG-------RIVRDADGRVLRIVEE 158
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 11-127 4.41e-05

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: 43.75  E-value: 4.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396  11 GTRMLPATKAIPKEMLTIADKPLIQYIVNECVAAGIKEIVLVTHSSKNAIENHFDTSfeletmlEKRVKRQLLDEVRSIV 90
Cdd:cd04197   11 NRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQIKEYIEKS-------KWSKPKSSLMIVIIIM 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 517482396  91 PK------DVtlmhVRQGQAKGL--GHAVLCGRAVVGNEPFAVVL 127
Cdd:cd04197   84 SEdcrslgDA----LRDLDAKGLirGDFILVSGDVVSNIDLKEIL 124
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-116 5.45e-05

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 44.47  E-value: 5.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517482396   4 IIPVAGLGTRMlpaTKAIPKEMLTIADKPLIQYIVNECVAAGIKEIVLVTHSSKNAIEnhfdtsfeletmlekrvkrqll 83
Cdd:PRK14353   9 IILAAGEGTRM---KSSLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGPGAEAVA---------------------- 63

                         90       100       110
                 ....*....|....*....|....*....|...
gi 517482396  84 DEVRSIVPKDVTlmhVRQGQAKGLGHAVLCGRA 116
Cdd:PRK14353  64 AAAAKIAPDAEI---FVQKERLGTAHAVLAARE 93
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 4-54 7.70e-05

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: 42.81  E-value: 7.70e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 517482396   4 IIPVAGLGTRMlpaTKAIPKEMLTIADKPLIQYIVNECVAAG-IKEIVLVTH 54
Cdd:COG1211    1 IIPAAGSGSRM---GAGIPKQFLPLGGKPVLEHTLEAFLAHPrIDEIVVVVP 49
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
 3-67 2.21e-04

GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; GT2_BcbE_like: The bcbE gene is one of the genes in the capsule biosynthetic locus of Pasteurella multocida. Its deducted product is likely involved in the biosynthesis of the polysaccharide capsule, which is found on surface of a wide range of bacteria. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.


Pssm-ID: 133026 [Multi-domain]  Cd Length: 231  Bit Score: 41.86  E-value: 2.21e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517482396   3 VIIPVAGLGTRMLPATKAIPKEMLTIADKPLIQYIVNECVAAGIKEIVLVThsSKNAIENHFDTS 67
Cdd:cd04183    1 IIIPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEWVIESLAKIFDSRFIFIC--RDEHNTKFHLDE 63
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-52 3.43e-04

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 41.94  E-value: 3.43e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 517482396   1 MKVIIPVAGLGTRMLpatKAIPKEMLTIADKPLIQYIVNECVAAGIKEIVLV 52
Cdd:PRK09451   6 MSVVILAAGKGTRMY---SDLPKVLHTLAGKPMVQHVIDAANELGAQHVHLV 54
ispDF PRK09382
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ...
 3-55 3.58e-04

bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase protein; Provisional


Pssm-ID: 236492 [Multi-domain]  Cd Length: 378  Bit Score: 41.76  E-value: 3.58e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 517482396   3 VIIPVAGLGTRmlpATKAIPKEMLTIADKPLIQYIVNECVAAG-IKEIVLVTHS 55
Cdd:PRK09382   8 LVIVAAGRSTR---FSAEVKKQWLRIGGKPLWLHVLENLSSAPaFKEIVVVIHP 58
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
 3-51 3.91e-04

G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; Alpha-D-Glucose-1-phosphate Cytidylyltransferase catalyzes the production of CDP-D-Glucose from alpha-D-Glucose-1-phosphate and MgCTP as substrate. CDP-D-Glucose is the precursor for synthesizing four of the five naturally occurring 3,6-dideoxy sugars-abequose (3,6-dideoxy-D-Xylo-hexose), ascarylose (3,6-dideoxy-L-arabino-hexose), paratose (3,6-dideoxy-D-ribohexose), and tyvelose (3,6-dideoxy-D-arabino-hexose. Deoxysugars are ubiquitous in nature where they function in a variety of biological processes, including cell adhesion, immune response, determination of ABO blood groups, fertilization, antibiotic function, and microbial pathogenicity.


Pssm-ID: 133015 [Multi-domain]  Cd Length: 253  Bit Score: 41.02  E-value: 3.91e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 517482396   3 VIIPVAGLGTRMLPATKAIPKEMLTIADKPLIQYIVNECVAAGIKEIVL 51
Cdd:cd02524    1 VVILAGGLGTRLSEETELKPKPMVEIGGRPILWHIMKIYSHYGHNDFIL 49
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
3-54 4.81e-04

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 40.50  E-value: 4.81e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 517482396   3 VIIPVAGLGTRMlpatKA-IPKEMLTIADKPLIQYIVnECVAA--GIKEIVLVTH 54
Cdd:PRK00155   6 AIIPAAGKGSRM----GAdRPKQYLPLGGKPILEHTL-EAFLAhpRIDEIIVVVP 55
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-65 8.42e-03

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 37.28  E-value: 8.42e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517482396   3 VIIPVAGLGTRMLPATkaiPKEMLTIADKPLIQYIVNECVAAGIKEIVLVTHSS---KNAIENHFD 65
Cdd:PRK14359   5 IIILAAGKGTRMKSSL---PKVLHTICGKPMLFYILKEAFAISDDVHVVLHHQKeriKEAVLEYFP 67
 
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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