|
Name |
Accession |
Description |
Interval |
E-value |
| GalU |
COG1210 |
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis]; |
2-289 |
0e+00 |
|
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440823 [Multi-domain] Cd Length: 288 Bit Score: 515.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 2 KKIRKAIIPAAGLGTRFLPETKAMPKEMLPVVDKPAIQLIVEEAIASGITDILIIIGKGKRAIEDHFDSNTELELNLESK 81
Cdd:COG1210 1 MKIRKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVTGRGKRAIEDHFDRSYELEATLEAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 82 GKDEMLKAVKKT-NGLNIYFKRQEHPNGLGDAVHTAKSFVGEDPFVIMLGDDLMTDETPLTKQLIDSYEETGSSTLAVMK 160
Cdd:COG1210 81 GKEELLEEVRSIsPLANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSEKPCLKQMIEVYEETGGSVIAVQE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 161 VPHEDTSKYGVINPaKEVSEGLYDVTNFVEKPNPEDAPSDLAIIGRYLLTADIFDILENTKPGKGNEIQLTDAIDTLNKK 240
Cdd:COG1210 161 VPPEEVSKYGIVDG-EEIEGGVYRVTGLVEKPAPEEAPSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDAIAALAKE 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 752296517 241 GKVYAHEFKGDRYDTGNKFGWLQTNIEFGLKHPEVSDELKQYIKDLAKK 289
Cdd:COG1210 240 EPVYAYEFEGKRYDCGDKLGYLKATVEFALKRPDLGEEFREYLKELLKE 288
|
|
| UGPase_prokaryotic |
cd02541 |
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ... |
5-271 |
1.98e-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: 426.56 E-value: 1.98e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 5 RKAIIPAAGLGTRFLPETKAMPKEMLPVVDKPAIQLIVEEAIASGITDILIIIGKGKRAIEDHFDSNTELELNLESKGKD 84
Cdd:cd02541 1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRGKRAIEDHFDRSYELEETLEKKGKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 85 EMLKAVKKTNGL-NIYFKRQEHPNGLGDAVHTAKSFVGEDPFVIMLGDDLMTDETPLTKQLIDSYEETGSSTLAVMKVPH 163
Cdd:cd02541 81 DLLEEVRIISDLaNIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLIDSKEPCLKQLIEAYEKTGASVIAVEEVPP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 164 EDTSKYGVINPaKEVSEGLYDVTNFVEKPNPEDAPSDLAIIGRYLLTADIFDILENTKPGKGNEIQLTDAIDTLNKKGKV 243
Cdd:cd02541 161 EDVSKYGIVKG-EKIDGDVFKVKGLVEKPKPEEAPSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTDAIAKLLEEEPV 239
|
250 260
....*....|....*....|....*...
gi 752296517 244 YAHEFKGDRYDTGNKFGWLQTNIEFGLK 271
Cdd:cd02541 240 YAYVFEGKRYDCGNKLGYLKATVEFALK 267
|
|
| galU |
TIGR01099 |
UTP--glucose-1-phosphate uridylyltransferase; Built to distinquish between the highly similar ... |
5-264 |
2.94e-136 |
|
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: 385.55 E-value: 2.94e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 5 RKAIIPAAGLGTRFLPETKAMPKEMLPVVDKPAIQLIVEEAIASGITDILIIIGKGKRAIEDHFDSNTELELNLESKGKD 84
Cdd:TIGR01099 1 RKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYIVEEAVEAGIEEIVFVTGRGKRAIEDHFDYSYELEHQLEKRGKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 85 EMLKAVKK-TNGLNIYFKRQEHPNGLGDAVHTAKSFVGEDPFVIMLGDDLMTDETPLTKQLIDSYEETGSSTLAVMKVPH 163
Cdd:TIGR01099 81 ELLEEVRKiSNLATIFYVRQKEQKGLGHAVLCARPFVGDEPFAVILGDDIVVNEEPALKQMIKAYEKTGCSIIAVQEVPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 164 EDTSKYGVINPaKEVSEGLYDVTNFVEKPNPEDAPSDLAIIGRYLLTADIFDILENTKPGKGNEIQLTDAIDTLNKKGKV 243
Cdd:TIGR01099 161 EEVSKYGVIDG-EGIEKDLYKVKNMVEKPKPEEAPSNLAIVGRYILTPDIFDLLEETPPGKGGEIQLTDAINKLLENETV 239
|
250 260
....*....|....*....|.
gi 752296517 244 YAHEFKGDRYDTGNKFGWLQT 264
Cdd:TIGR01099 240 LAYKFNGKRYDCGSKLGYLEA 260
|
|
| PRK13389 |
PRK13389 |
UTP--glucose-1-phosphate uridylyltransferase GalU; |
2-286 |
7.56e-82 |
|
UTP--glucose-1-phosphate uridylyltransferase GalU;
Pssm-ID: 184021 [Multi-domain] Cd Length: 302 Bit Score: 249.05 E-value: 7.56e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 2 KKIRKAIIPAAGLGTRFLPETKAMPKEMLPVVDKPAIQLIVEEAIASGITDILIIIGKGKRAIEDHFDSNTELELNLESK 81
Cdd:PRK13389 6 TKVKKAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFDTSFELEAMLEKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 82 GKDEMLKAVKKT--NGLNIYFKRQEHPNGLGDAVHTAKSFVGEDPFVIMLGDDLMTD-ETPLTK----QLIDSYEETGSS 154
Cdd:PRK13389 86 VKRQLLDEVQSIcpPHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILDEyESDLSQdnlaEMIRRFDETGHS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 155 TlaVMKVPHEDTSKYGVIN-PAKEVSEG-LYDVTNFVEKPNPEDAPSDLAIIGRYLLTADIFDILENTKPGKGNEIQLTD 232
Cdd:PRK13389 166 Q--IMVEPVADVTAYGVVDcKGVELAPGeSVPMVGVVEKPKADVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTD 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 752296517 233 AIDTLNKKGKVYAHEFKGDRYDTGNKFGWLQTNIEFGLKHPEVSDELKQYIKDL 286
Cdd:PRK13389 244 AIDMLIEKETVEAYHMKGKSHDCGNKLGYMQAFVEYGIRHNTLGTEFKAWLEEE 297
|
|
| PRK10122 |
PRK10122 |
UTP--glucose-1-phosphate uridylyltransferase GalF; |
6-289 |
3.83e-75 |
|
UTP--glucose-1-phosphate uridylyltransferase GalF;
Pssm-ID: 182252 [Multi-domain] Cd Length: 297 Bit Score: 231.70 E-value: 3.83e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 6 KAIIPAAGLGTRFLPETKAMPKEMLPVVDKPAIQLIVEEAIASGITDILIIIGKGKRAIEDHFDSNTELELNLESKGKDE 85
Cdd:PRK10122 5 KAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAVENHFDTSYELESLLEQRVKRQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 86 MLKAVKKT--NGLNIYFKRQEHPNGLGDAVHTAKSFVGEDPFVIMLGDDLMTDET--PLTKQL---IDSYEETGSSTLAV 158
Cdd:PRK10122 85 LLAEVQSIcpPGVTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPDVVIDDASadPLRYNLaamIARFNETGRSQVLA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 159 MKVPhEDTSKYGVINPAKEV-SEG-LYDVTNFVEKP-NPEDAPSDLAIIGRYLLTADIFDILENTKPGKGNEIQLTDAID 235
Cdd:PRK10122 165 KRMP-GDLSEYSVIQTKEPLdREGkVSRIVEFIEKPdQPQTLDSDLMAVGRYVLSADIWPELERTEPGAWGRIQLTDAIA 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 752296517 236 TLNKKGKVYAHEFKGDRYDTGNKFGWLQTNIEFGLKHPEVSDELKQYIKDLAKK 289
Cdd:PRK10122 244 ELAKKQSVDAMLMTGDSYDCGKKMGYMQAFVKYGLRNLKEGAKFRKGIEKLLSE 297
|
|
| NTP_transferase |
cd04181 |
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ... |
7-256 |
9.71e-58 |
|
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: 184.32 E-value: 9.71e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 7 AIIPAAGLGTRFLPETKAMPKEMLPVVDKPAIQLIVEEAIASGITDILIIIGKGKRAIEDHFDSNTELelnleskgkdem 86
Cdd:cd04181 1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGSKF------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 87 lkavkktnGLNIYFKRQEHPNGLGDAVHTAKSFVGEDPFVIMLGDDLmTDEtPLTKQLIDSYEETGSSTLAVMKVphEDT 166
Cdd:cd04181 69 --------GVNIEYVVQEEPLGTAGAVRNAEDFLGDDDFLVVNGDVL-TDL-DLSELLRFHREKGADATIAVKEV--EDP 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 167 SKYGVInpakeVSEGLYDVTNFVEKpnPEDAPSDLAIIGRYLLTADIFDILENTKPgkGNEIQLTDAIDTLNKKGKVYAH 246
Cdd:cd04181 137 SRYGVV-----ELDDDGRVTRFVEK--PTLPESNLANAGIYIFEPEILDYIPEILP--RGEDELTDAIPLLIEEGKVYGY 207
|
250
....*....|
gi 752296517 247 EFKGDRYDTG 256
Cdd:cd04181 208 PVDGYWLDIG 217
|
|
| G1P_TT_long |
cd04189 |
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ... |
6-265 |
6.68e-57 |
|
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: 182.77 E-value: 6.68e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 6 KAIIPAAGLGTRFLPETKAMPKEMLPVVDKPAIQLIVEEAIASGITDILIIIGKGKRAIEDHFDSNTELelnleskgkde 85
Cdd:cd04189 2 KGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEALGDGSRF----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 86 mlkavkktnGLNIYFKRQEHPNGLGDAVHTAKSFVGEDPFVIMLGDDLMTDEtplTKQLIDSYEETGSSTLAVMKvPHED 165
Cdd:cd04189 71 ---------GVRITYILQEEPLGLAHAVLAARDFLGDEPFVVYLGDNLIQEG---ISPLVRDFLEEDADASILLA-EVED 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 166 TSKYGVInpakEVSEGlyDVTNFVEKPNPEdaPSDLAIIGRYLLTADIFDILENTKPGKGNEIQLTDAIDTL-NKKGKVY 244
Cdd:cd04189 138 PRRFGVA----VVDDG--RIVRLVEKPKEP--PSNLALVGVYAFTPAIFDAISRLKPSWRGELEITDAIQWLiDRGRRVG 209
|
250 260
....*....|....*....|.
gi 752296517 245 AHEFKGDRYDTGNKFGWLQTN 265
Cdd:cd04189 210 YSIVTGWWKDTGTPEDLLEAN 230
|
|
| RmlA1 |
COG1209 |
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis]; |
5-265 |
5.98e-51 |
|
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440822 [Multi-domain] Cd Length: 294 Bit Score: 169.50 E-value: 5.98e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 5 RKAIIPAAGLGTRFLPETKAMPKEMLPVVDKPAIQLIVEEAIASGITDILIIIGK-GKRAIEDHFDSNTELelnleskgk 83
Cdd:COG1209 1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPeDGPQFERLLGDGSQL--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 84 demlkavkktnGLNIYFKRQEHPNGLGDAVHTAKSFVGEDPFVIMLGDDLmTDETPLTKQLIDSYEETGSSTLAVMKVph 163
Cdd:COG1209 72 -----------GIKISYAVQPEPLGLAHAFIIAEDFIGGDPVALVLGDNI-FYGDGLSELLREAAARESGATIFGYKV-- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 164 EDTSKYGVInpakEVSEGlYDVTNFVEKpnPEDAPSDLAIIGRYLLTADIFDILENTKPGKGNEIQLTDAIDTLNKKGK- 242
Cdd:COG1209 138 EDPERYGVV----EFDED-GRVVSLEEK--PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKl 210
|
250 260
....*....|....*....|....
gi 752296517 243 VYAHEFKGDR-YDTGNKFGWLQTN 265
Cdd:COG1209 211 VVELLGRGFAwLDTGTHESLLEAN 234
|
|
| GCD1 |
COG1208 |
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ... |
6-257 |
2.50e-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: 150.69 E-value: 2.50e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 6 KAIIPAAGLGTRFLPETKAMPKEMLPVVDKPAIQLIVEEAIASGITDILIIIGKGKRAIEDHFDSNTELelnleskgkde 85
Cdd:COG1208 1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRF----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 86 mlkavkktnGLNIYFKRQEHPNGLGDAVHTAKSFVGEDPFVIMLGDDLmTDEtPLTKqLIDSYEETGSS-TLAVmkVPHE 164
Cdd:COG1208 70 ---------GVRITYVDEGEPLGTGGALKRALPLLGDEPFLVLNGDIL-TDL-DLAA-LLAFHREKGADaTLAL--VPVP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 165 DTSKYGVInpakeVSEGLYDVTNFVEKpnPEDAPSDLAIIGRYLLTADIFDILEntkpgKGNEIQLTDAIDTLNKKGKVY 244
Cdd:COG1208 136 DPSRYGVV-----ELDGDGRVTRFVEK--PEEPPSNLINAGIYVLEPEIFDYIP-----EGEPFDLEDLLPRLIAEGRVY 203
|
250
....*....|...
gi 752296517 245 AHEFKGDRYDTGN 257
Cdd:COG1208 204 GYVHDGYWLDIGT 216
|
|
| NTP_transferase |
pfam00483 |
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ... |
6-257 |
7.59e-29 |
|
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: 110.42 E-value: 7.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 6 KAIIPAAGLGTRFLPETKAMPKEMLPVVDK-PAIQLIVEEAIASGITDILIIIGKGKRA-IEDHFDSNTELelnleskgk 83
Cdd:pfam00483 1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFmLNELLGDGSKF--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 84 demlkavkktnGLNIYFKRQEHPNGLGDAVHTAKSFVGEDPFVIM-LGDDLMTDETPltKQLIDSYEETGSS-TLAVMKV 161
Cdd:pfam00483 72 -----------GVQITYALQPEGKGTAPAVALAADFLGDEKSDVLvLGGDHIYRMDL--EQAVKFHIEKAADaTVTFGIV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 162 PHEDTSKYGVInpakeVSEGLYDVTNFVEKPNpEDAPSDLAIIGRYLLTADIFD-ILENTKPGKGNEIQLTDAIDTLNKK 240
Cdd:pfam00483 139 PVEPPTGYGVV-----EFDDNGRVIRFVEKPK-LPKASNYASMGIYIFNSGVLDfLAKYLEELKRGEDEITDILPKALED 212
|
250
....*....|....*....
gi 752296517 241 GKV-YAHEFKGDR-YDTGN 257
Cdd:pfam00483 213 GKLaYAFIFKGYAwLDVGT 231
|
|
| G1P_TT_short |
cd02538 |
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ... |
5-232 |
8.79e-27 |
|
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: 104.58 E-value: 8.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 5 RKAIIPAAGLGTRFLPETKAMPKEMLPVVDKPAIQLIVEEAIASGITDILIIIGKGkraiedhfdsNTELELNLESKGKD 84
Cdd:cd02538 1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPE----------DLPLFKELLGDGSD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 85 EmlkavkktnGLNIYFKRQEHPNGLGDAVHTAKSFVGEDPFVIMLGDDLMTDETpLTKQLIDSYEETGSSTLAVMKVPhe 164
Cdd:cd02538 71 L---------GIRITYAVQPKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQG-LSPILQRAAAQKEGATVFGYEVN-- 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 752296517 165 DTSKYGVInpakEVSEGlYDVTNFVEKpnPEDAPSDLAIIGRYLLTADIFDILENTKPGKGNEIQLTD 232
Cdd:cd02538 139 DPERYGVV----EFDEN-GRVLSIEEK--PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITD 199
|
|
| NTP_transferase_WcbM_like |
cd06915 |
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ... |
7-256 |
1.67e-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: 90.30 E-value: 1.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 7 AIIPAAGLGTRFLPETKAMPKEMLPVVDKPAIQLIVEEAIASGITDILIIIGKGKRAIEDHFDSNTELelnleskgkdem 86
Cdd:cd06915 1 AVILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYLAEQIEEYFGDGYRG------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 87 lkavkktnGLNIYFKRQEHPNGLGDAVHTAKSFVGEDPFVIMLGDD-LMTDetplTKQLIDSYEETGS-STLAVMKVPhe 164
Cdd:cd06915 69 --------GIRIYYVIEPEPLGTGGAIKNALPKLPEDQFLVLNGDTyFDVD----LLALLAALRASGAdATMALRRVP-- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 165 DTSKYGVInpakEVSEGLYdVTNFVEKpNPEDAPsdlAII--GRYLLTADIFDILENTKPGkgneiQLTDAIDTLNKKGK 242
Cdd:cd06915 135 DASRYGNV----TVDGDGR-VIAFVEK-GPGAAP---GLIngGVYLLRKEILAEIPADAFS-----LEADVLPALVKRGR 200
|
250
....*....|....
gi 752296517 243 VYAHEFKGDRYDTG 256
Cdd:cd06915 201 LYGFEVDGYFIDIG 214
|
|
| NTP_transferase_like_2 |
cd06426 |
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ... |
7-242 |
4.63e-19 |
|
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: 83.33 E-value: 4.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 7 AIIPAAGLGTRFLPETKAMPKEMLPVVDKPAIQLIVEEAIASGITDILIIIGKGKRAIEDHFdsntelelnleSKGKDEm 86
Cdd:cd06426 1 VVIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNYLAEMIEDYF-----------GDGSKF- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 87 lkavkktnGLNIYFKRQEHPNGLGDAVHTAKSFVgEDPFVIMLGdDLMTDETPLtkQLIDSYEETGSS-TLAV----MKV 161
Cdd:cd06426 69 --------GVNISYVREDKPLGTAGALSLLPEKP-TDPFLVMNG-DILTNLNYE--HLLDFHKENNADaTVCVreyeVQV 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 162 PhedtskYGVInpakEVSEGLydVTNFVEKPNpedaPSDLAIIGRYLLTADIFDILEntkpgKGNEIQLTDAIDTLNKKG 241
Cdd:cd06426 137 P------YGVV----ETEGGR--ITSIEEKPT----HSFLVNAGIYVLEPEVLDLIP-----KNEFFDMPDLIEKLIKEG 195
|
.
gi 752296517 242 K 242
Cdd:cd06426 196 K 196
|
|
| PRK15480 |
PRK15480 |
glucose-1-phosphate thymidylyltransferase RfbA; Provisional |
3-264 |
8.23e-19 |
|
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
Pssm-ID: 185377 [Multi-domain] Cd Length: 292 Bit Score: 84.34 E-value: 8.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 3 KIRKAIIPAAGLGTRFLPETKAMPKEMLPVVDKPAIQLIVEEAIASGITDILIIIGKgkraiedhfdsntelelnlESKG 82
Cdd:PRK15480 2 KTRKGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTP-------------------QDTP 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 83 KDEMLKAVKKTNGLNIYFKRQEHPNGLGDAVHTAKSFVGEDPFVIMLGDDLMT--DETPLTKQLIDsyEETGSSTLAVMK 160
Cdd:PRK15480 63 RFQQLLGDGSQWGLNLQYKVQPSPDGLAQAFIIGEEFIGGDDCALVLGDNIFYghDLPKLMEAAVN--KESGATVFAYHV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 161 vphEDTSKYGVInpakevsEGLYDVTNFVEKPNPEDAPSDLAIIGRYLLTADIFDILENTKPGKGNEIQLTDAidtlnkk 240
Cdd:PRK15480 141 ---NDPERYGVV-------EFDQNGTAISLEEKPLQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDI------- 203
|
250 260
....*....|....*....|....
gi 752296517 241 GKVYAHEFKGDRYDTGNKFGWLQT 264
Cdd:PRK15480 204 NRIYMEQGRLSVAMMGRGYAWLDT 227
|
|
| M1P_guanylylT_B_like_N |
cd06425 |
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ... |
6-250 |
4.55e-15 |
|
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: 72.63 E-value: 4.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 6 KAIIPAAGLGTRFLPETKAMPKEMLPVVDKPAIQLIVEEAIASGITDILiiigkgkraiedhfdsnteLELNLESKGKDE 85
Cdd:cd06425 2 KALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEII-------------------LAVNYRPEDMVP 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 86 MLKAVKKTNGLNIYFKRQEHPNGLGDAVHTAKSFVGED--PFvIMLGDDLMTDeTPLtKQLIDSYEETGS-STLAVMKVp 162
Cdd:cd06425 63 FLKEYEKKLGIKITFSIETEPLGTAGPLALARDLLGDDdePF-FVLNSDVICD-FPL-AELLDFHKKHGAeGTILVTKV- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 163 hEDTSKYGVInpakEVSEGLYDVTNFVEKpnPEDAPSDLAIIGRYLLTADIFDILENTKPGKGNEIqltdaIDTLNKKGK 242
Cdd:cd06425 139 -EDPSKYGVV----VHDENTGRIERFVEK--PKVFVGNKINAGIYILNPSVLDRIPLRPTSIEKEI-----FPKMASEGQ 206
|
....*...
gi 752296517 243 VYAHEFKG 250
Cdd:cd06425 207 LYAYELPG 214
|
|
| COG1213 |
COG1213 |
Choline kinase [Lipid transport and metabolism]; |
6-250 |
7.08e-13 |
|
Choline kinase [Lipid transport and metabolism];
Pssm-ID: 440826 [Multi-domain] Cd Length: 236 Bit Score: 66.80 E-value: 7.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 6 KAIIPAAGLGTRFLPETKAMPKEMLPVVDKPAIQLIVEEAIASGITDILIIIGKGKRAIEDHFDSntelelnleskgKDE 85
Cdd:COG1213 1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEALAR------------PGP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 86 MLKAV-----KKTNglNIYfkrqehpnglgdAVHTAKSFVGEDpFVIMLGDDLMTDEtpLTKQLIDSyeeTGSSTLAV-- 158
Cdd:COG1213 69 DVTFVynpdyDETN--NIY------------SLWLAREALDED-FLLLNGDVVFDPA--ILKRLLAS---DGDIVLLVdr 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 159 -MKVPHEDTSKYgvinpakEVSEGLYdVTNFVEKPNPEDApsdLAI-IGRYLLTAD----IFDILENTKPGKGNEIQLTD 232
Cdd:COG1213 129 kWEKPLDEEVKV-------RVDEDGR-IVEIGKKLPPEEA---DGEyIGIFKFSAEgaaaLREALEALIDEGGPNLYYED 197
|
250
....*....|....*....
gi 752296517 233 AIDTL-NKKGKVYAHEFKG 250
Cdd:COG1213 198 ALQELiDEGGPVKAVDIGG 216
|
|
| NTP_transferase_like_1 |
cd06422 |
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ... |
6-264 |
2.51e-12 |
|
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: 64.90 E-value: 2.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 6 KAIIPAAGLGTRFLPETKAMPKEMLPVVDKPAIQLIVEEAIASGITDILIIIGKGKRAIEDHFDSNTElelnleskgkde 85
Cdd:cd06422 1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHLGDSRF------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 86 mlkavkktnGLNIYFkRQEHPNGL--GDAVHTAKSFVGEDPFVIMLGDDLMTDETPLtkqLIDSYEETGSSTLAVMKVPH 163
Cdd:cd06422 69 ---------GLRITI-SDEPDELLetGGGIKKALPLLGDEPFLVVNGDILWDGDLAP---LLLLHAWRMDALLLLLPLVR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 164 edtskygviNPAKEvSEGLYDVTNFVE-KPNPEDAPSDLAIIGRYLLTADIFDileNTKPGKGNeiqLTDAIDTLNKKGK 242
Cdd:cd06422 136 ---------NPGHN-GVGDFSLDADGRlRRGGGGAVAPFTFTGIQILSPELFA---GIPPGKFS---LNPLWDRAIAAGR 199
|
250 260
....*....|....*....|..
gi 752296517 243 VYAHEFKGDRYDTGNKFGWLQT 264
Cdd:cd06422 200 LFGLVYDGLWFDVGTPERLLAA 221
|
|
| M1P_guanylylT_A_like_N |
cd06428 |
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ... |
15-250 |
3.37e-11 |
|
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: 62.27 E-value: 3.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 15 GTRFLPETKAMPKEMLPVVDKPAIQLIVeEAIA--SGITDILiIIGkgkraiedhFDSNTELELnleskgkdeMLKAVKK 92
Cdd:cd06428 11 GTRFRPLSLDVPKPLFPVAGKPMIHHHI-EACAkvPDLKEVL-LIG---------FYPESVFSD---------FISDAQQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 93 TNGLNIYFKRQEHPNGLGDA-VHTAKSFVGEDP--FVIMLGDdlMTDETPLtKQLIDSYEE-TGSSTLAVMKVPHEDTSK 168
Cdd:cd06428 71 EFNVPIRYLQEYKPLGTAGGlYHFRDQILAGNPsaFFVLNAD--VCCDFPL-QELLEFHKKhGASGTILGTEASREQASN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 169 YGVINPAKEVSEglydVTNFVEKpnPEDAPSDLAIIGRYLLTADIFDILENTKPGKGNEIQL----------------TD 232
Cdd:cd06428 148 YGCIVEDPSTGE----VLHYVEK--PETFVSDLINCGVYLFSPEIFDTIKKAFQSRQQEAQLgddnnregraevirleQD 221
|
250
....*....|....*...
gi 752296517 233 AIDTLNKKGKVYAHEFKG 250
Cdd:cd06428 222 VLTPLAGSGKLYVYKTDD 239
|
|
| GT2_GlmU_N_bac |
cd02540 |
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ... |
7-243 |
5.22e-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: 60.99 E-value: 5.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 7 AIIPAAGLGTRflpetkaM----PKEMLPVVDKPAIQLIVEEAIASGITDILIIIGkgkraiedhfdsntelelnlesKG 82
Cdd:cd02540 1 AVILAAGKGTR-------MksdlPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVG----------------------HG 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 83 KDEMLKAVKktnGLNIYFKRQEHPNGLGDAVHTAKSFVG--EDPFVIMLGD-DLMTDETplTKQLIDSYEETGsSTLAVM 159
Cdd:cd02540 52 AEQVKKALA---NPNVEFVLQEEQLGTGHAVKQALPALKdfEGDVLVLYGDvPLITPET--LQRLLEAHREAG-ADVTVL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 160 KVPHEDTSKYGVInpakeVSEGLYDVTNFVEKpnpEDA-PSDLAI----IGRYLL-TADIFDILE--NTKPGKGnEIQLT 231
Cdd:cd02540 126 TAELEDPTGYGRI-----IRDGNGKVLRIVEE---KDAtEEEKAIrevnAGIYAFdAEFLFEALPklTNNNAQG-EYYLT 196
|
250
....*....|..
gi 752296517 232 DAIDTLNKKGKV 243
Cdd:cd02540 197 DIIALAVADGLK 208
|
|
| PC_cytidylyltransferase |
cd02523 |
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ... |
7-246 |
6.31e-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: 61.09 E-value: 6.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 7 AIIPAAGLGTRFLPETKAMPKEMLPVVDKPAIQLIVEEAIASGITDILIIIGKGKRAIEDHFDSNTELELnleskgkdem 86
Cdd:cd02523 1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKKYPNIKF---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 87 lkaV-----KKTNglNIY--FKrqehpnglgdavhtAKSFVGEDpFVIMLGDDLmtdetpLTKQLIDSYEET-GSSTLAV 158
Cdd:cd02523 71 ---VynpdyAETN--NIYslYL--------------ARDFLDED-FLLLEGDVV------FDPSILERLLSSpADNAILV 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 159 MKVPHEDTSKYGVINPAKEVSEGLYDVTNFVEKPNPEDapsdlaiIGRYLLTADIFD----ILENTKPGKGNEIQLTDAI 234
Cdd:cd02523 125 DKKTKEWEDEYVKDLDDAGVLLGIISKAKNLEEIQGEY-------VGISKFSPEDADrlaeALEELIEAGRVNLYYEDAL 197
|
250
....*....|..
gi 752296517 235 DTLNKKGKVYAH 246
Cdd:cd02523 198 QRLISEEGVKVK 209
|
|
| GlmU |
COG1207 |
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ... |
5-172 |
1.67e-10 |
|
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440820 [Multi-domain] Cd Length: 457 Bit Score: 61.20 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 5 RKAIIPAAGLGTRFlpetK-AMPKEMLPVVDKPAIQLIVEEAIASGITDILIIIGKGKRAIEDHFDsntelelnleskgk 83
Cdd:COG1207 3 LAVVILAAGKGTRM----KsKLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVRAALA-------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 84 demlkavkktnGLNIYFKRQEHPNGLGDAVHTAKSFVG--EDPFVIMLGDdlmtdeTPLT-----KQLIDSYEETGSStL 156
Cdd:COG1207 65 -----------DLDVEFVLQEEQLGTGHAVQQALPALPgdDGTVLVLYGD------VPLIraetlKALLAAHRAAGAA-A 126
|
170
....*....|....*.
gi 752296517 157 AVMKVPHEDTSKYGVI 172
Cdd:COG1207 127 TVLTAELDDPTGYGRI 142
|
|
| GlgC |
COG0448 |
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ... |
142-250 |
1.28e-09 |
|
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate transport and metabolism];
Pssm-ID: 440217 [Multi-domain] Cd Length: 377 Bit Score: 58.16 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 142 KQLIDSYEETGSS-TLAVMKVPHEDTSKYGVINpakeVSEGLYdVTNFVEKPnpEDAPSDLAIIGRYLLTADIF-DILEN 219
Cdd:COG0448 132 RQMLDFHIESGADiTVACIEVPREEASRFGVME----VDEDGR-ITEFEEKP--KDPKSALASMGIYVFNKDVLiELLEE 204
|
90 100 110
....*....|....*....|....*....|.
gi 752296517 220 TKPgKGNEIQLTDAIDTLNKKGKVYAHEFKG 250
Cdd:COG0448 205 DAP-NSSHDFGKDIIPRLLDRGKVYAYEFDG 234
|
|
| LicC |
COG4750 |
CTP:phosphocholine cytidylyltransferase LicC [Cell wall/membrane/envelope biogenesis, Lipid ... |
5-58 |
2.05e-08 |
|
CTP:phosphocholine cytidylyltransferase LicC [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism];
Pssm-ID: 443784 [Multi-domain] Cd Length: 228 Bit Score: 53.68 E-value: 2.05e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 752296517 5 RKAIIPAAGLGTRFLPETKAMPKEMLPVVDKPAIQLIVEEAIASGITDILIIIG 58
Cdd:COG4750 1 MNAIILAAGLGSRFAPITYETPKGLLKVNGEPLIERQIRQLHEAGITDITVVVG 54
|
|
| glmU |
PRK14354 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
5-243 |
2.34e-08 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184643 [Multi-domain] Cd Length: 458 Bit Score: 54.45 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 5 RKAIIPAAGLGTRFlpeTKAMPKEMLPVVDKPAIQLIVEEAIASGITDILIIIGKGKRAIEDHFDSNTElelnleskgkd 84
Cdd:PRK14354 3 RYAIILAAGKGTRM---KSKLPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVGHGAEEVKEVLGDRSE----------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 85 emlkavkktnglniyFKRQEHPNGLGDAVHTAKSFVGEDPFVIML--GDD-LMTDETplTKQLIDSYEETGSS-TLAVMK 160
Cdd:PRK14354 69 ---------------FALQEEQLGTGHAVMQAEEFLADKEGTTLVicGDTpLITAET--LKNLIDFHEEHKAAaTILTAI 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 161 VphEDTSKYGVInpakeVSEGLYDVTNFVEKpnpEDA-PSDLAII----GRYLL-TADIFDILENTKPGKG-NEIQLTDA 233
Cdd:PRK14354 132 A--ENPTGYGRI-----IRNENGEVEKIVEQ---KDAtEEEKQIKeintGTYCFdNKALFEALKKISNDNAqGEYYLTDV 201
|
250
....*....|
gi 752296517 234 IDTLNKKGKV 243
Cdd:PRK14354 202 IEILKNEGEK 211
|
|
| glmU |
PRK14355 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
7-241 |
6.66e-08 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237685 [Multi-domain] Cd Length: 459 Bit Score: 53.21 E-value: 6.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 7 AIIPAAGLGTRFlpeTKAMPKEMLPVVDKPAIQLIVEEAIASGITDILIIIGKGKRAIEDHFDSNTElelnleskgkdem 86
Cdd:PRK14355 6 AIILAAGKGTRM---KSDLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHFAGDGD------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 87 lkavkktnglnIYFKRQEHPNGLGDAVHTAKSFVgeDPF----VIMLGD-DLMTDETplTKQLIDSYEETGSStLAVMKV 161
Cdd:PRK14355 70 -----------VSFALQEEQLGTGHAVACAAPAL--DGFsgtvLILCGDvPLLRAET--LQGMLAAHRATGAA-VTVLTA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 162 PHEDTSKYGVInpakeVSEGLYDVTNFVEKpnpEDAPSDLAII-----GRYLLTAD-IFDILENTKPGKG-NEIQLTDAI 234
Cdd:PRK14355 134 RLENPFGYGRI-----VRDADGRVLRIVEE---KDATPEERSIrevnsGIYCVEAAfLFDAIGRLGNDNAqGEYYLTDIV 205
|
....*..
gi 752296517 235 DTLNKKG 241
Cdd:PRK14355 206 AMAAAEG 212
|
|
| eIF-2B_gamma_N |
cd04198 |
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ... |
6-178 |
1.07e-07 |
|
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; N-terminal domain of gamma subunit of the eukaryotic translation initiation factor 2B (eIF-2B): eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit gamma shares sequence similarity with epsilon subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.
Pssm-ID: 133041 [Multi-domain] Cd Length: 214 Bit Score: 51.51 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 6 KAIIPAAGLGTRFLPETKAMPKEMLPVVDKPAIQLIVEEAIASGITDILIIIGKG-KRAIEDHFDSNTelelnLESKGKD 84
Cdd:cd04198 2 QAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEeQAEISTYLRSFP-----LNLKQKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 85 EmlkavkktnglnIYFKRQEHPNGLGDAVHTAKSFVGEDpfVIMLGDDLMTDETPLtkQLIDSYEETGSSTLAVMKVPHE 164
Cdd:cd04198 77 D------------EVTIVLDEDMGTADSLRHIRKKIKKD--FLVLSCDLITDLPLI--ELVDLHRSHDASLTVLLYPPPV 140
|
170
....*....|....
gi 752296517 165 DTSKYGVINPAKEV 178
Cdd:cd04198 141 SSEQKGGKGKSKKA 154
|
|
| MocA |
COG2068 |
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism]; |
1-70 |
3.43e-07 |
|
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
Pssm-ID: 441671 [Multi-domain] Cd Length: 195 Bit Score: 49.77 E-value: 3.43e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 1 MKKIRkAIIPAAGLGTRFlpetkAMPKEMLPVVDKPAIQLIVEEAIASGITDILIIIGKGKRAIEDHFDS 70
Cdd:COG2068 1 MSKVA-AIILAAGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADAEEVAAALAG 64
|
|
| GDP-M1P_Guanylyltransferase |
cd02509 |
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ... |
6-214 |
3.81e-07 |
|
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: 50.27 E-value: 3.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 6 KAIIPAAGLGTRFLPE-TKAMPKEMLPVV-DKPAIQLIVEEAI-ASGITDILIIIGK--GKRAIEDHFDSNTELELNLES 80
Cdd:cd02509 2 YPVILAGGSGTRLWPLsRESYPKQFLKLFgDKSLLQQTLDRLKgLVPPDRILVVTNEeyRFLVREQLPEGLPEENIILEP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 81 KGKDeMLKAvkktnglnIYFkrqehpnglgdAVHTAKSFVGEDPFVIMLGDDLMTDEtpltkqliDSYEET---GSS--- 154
Cdd:cd02509 82 EGRN-TAPA--------IAL-----------AALYLAKRDPDAVLLVLPSDHLIEDV--------EAFLKAvkkAVEaae 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 752296517 155 -----TLAVmkVPHEDTSKYGVINPAKEVSEGLYDVTNFVEKPNPEDAPSDLAiIGRYLLTADIF 214
Cdd:cd02509 134 egylvTFGI--KPTRPETGYGYIEAGEKLGGGVYRVKRFVEKPDLETAKEYLE-SGNYLWNSGIF 195
|
|
| glmU |
PRK14358 |
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ... |
8-172 |
5.21e-07 |
|
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase; Provisional
Pssm-ID: 237688 [Multi-domain] Cd Length: 481 Bit Score: 50.75 E-value: 5.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 8 IIPAAGLGTRFlpeTKAMPKEMLPVVDKPAIQLIVEEAIASGITDILIIIGKGKRaiedhfdsntELELNLESKGkdeml 87
Cdd:PRK14358 11 VILAAGQGTRM---KSALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGAE----------QVEAALQGSG----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 88 kavkktnglnIYFKRQEHPNGLGDAVHTAKSFVGE-DPFVIMLGDDLMTDETPLTKQLIDSYEETGSStLAVMKVPHEDT 166
Cdd:PRK14358 73 ----------VAFARQEQQLGTGDAFLSGASALTEgDADILVLYGDTPLLRPDTLRALVADHRAQGSA-MTILTGELPDA 141
|
....*.
gi 752296517 167 SKYGVI 172
Cdd:PRK14358 142 TGYGRI 147
|
|
| eIF-2B_gamma_N_like |
cd02507 |
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ... |
6-67 |
1.26e-06 |
|
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: 48.40 E-value: 1.26e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 752296517 6 KAIIPAAGLGTRFLPETKAMPKEMLPVVDKPAIQLIVEEAIASGITDILIIIGKGKRAIEDH 67
Cdd:cd02507 2 QAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQAIIEH 63
|
|
| GT_2_like_f |
cd04182 |
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ... |
7-157 |
1.69e-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: 47.55 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 7 AIIPAAGLGTRFlpetkAMPKEMLPVVDKPAIQLIVEEAIASGITDILIIIGKGKRAIEDHFDsntelelnleskgkdem 86
Cdd:cd04182 3 AIILAAGRSSRM-----GGNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALA----------------- 60
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 752296517 87 lkavkktnGLNIYFKRQEHP-NGLGDAVHTAKSFVGEDP--FVIMLGDdlMTDETPLT-KQLIDSYEETGSSTLA 157
Cdd:cd04182 61 --------GLPVVVVINPDWeEGMSSSLAAGLEALPADAdaVLILLAD--QPLVTAETlRALIDAFREDGAGIVA 125
|
|
| glgC |
PRK00725 |
glucose-1-phosphate adenylyltransferase; Provisional |
155-248 |
6.96e-06 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 234824 [Multi-domain] Cd Length: 425 Bit Score: 47.14 E-value: 6.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 155 TLAVMKVPHEDTSKYGVInpakEVSEGlYDVTNFVEKP-NPEDAPSD----LAIIGRYLLTAD-IFDILE--NTKP---- 222
Cdd:PRK00725 160 TVACLEVPREEASAFGVM----AVDEN-DRITAFVEKPaNPPAMPGDpdksLASMGIYVFNADyLYELLEedAEDPnssh 234
|
90 100
....*....|....*....|....*...
gi 752296517 223 --GKgneiqltDAIDTLNKKGKVYAHEF 248
Cdd:PRK00725 235 dfGK-------DIIPKIVEEGKVYAHPF 255
|
|
| glmU |
PRK14357 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
6-240 |
2.52e-05 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237687 [Multi-domain] Cd Length: 448 Bit Score: 45.14 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 6 KAIIPAAGLGTRFlpeTKAMPKEMLPVVDKPAIQLIVEEAIASGiTDILIIIGKGKRAIEDHFDSNTELELnleskgkde 85
Cdd:PRK14357 2 RALVLAAGKGTRM---KSKIPKVLHKISGKPMINWVIDTAKKVA-QKVGVVLGHEAELVKKLLPEWVKIFL--------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 86 mlkavkktnglniyfkrQEHPNGLGDAVHTAKSFVGEDPFVIMLGDD--LMTDETplTKQLIDSYEETGSSTlAVMKVPH 163
Cdd:PRK14357 69 -----------------QEEQLGTAHAVMCARDFIEPGDDLLILYGDvpLISENT--LKRLIEEHNRKGADV-TILVADL 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 164 EDTSKYGVI-------------------NPAKEVSEGLYDVT-NFVEKPNPEDAPSDLAiiGRYLLTaDIFDILENTK-- 221
Cdd:PRK14357 129 EDPTGYGRIirdggkyrivedkdapeeeKKIKEINTGIYVFSgDFLLEVLPKIKNENAK--GEYYLT-DAVNFAEKVRvv 205
|
250 260
....*....|....*....|....*..
gi 752296517 222 --------PGKGNEIQLTDAIDTLNKK 240
Cdd:PRK14357 206 ktedlleiTGVNTRIQLAWLEKQLRMR 232
|
|
| glgC |
PRK00844 |
glucose-1-phosphate adenylyltransferase; Provisional |
142-252 |
4.86e-05 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 234846 [Multi-domain] Cd Length: 407 Bit Score: 44.43 E-value: 4.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 142 KQLIDSYEETGSS-TLAVMKVPHEDTSKYGVInpakEV-SEGlyDVTNFVEKP-NPEDAPSD----LAIIGRYLLTADI- 213
Cdd:PRK00844 134 RQMVDFHIESGAGvTVAAIRVPREEASAFGVI----EVdPDG--RIRGFLEKPaDPPGLPDDpdeaLASMGNYVFTTDAl 207
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 752296517 214 FDIL------ENTKPGKGNEIqltdaIDTLNKKGKVYAHEFKGDR 252
Cdd:PRK00844 208 VDALrrdaadEDSSHDMGGDI-----IPRLVERGRAYVYDFSTNE 247
|
|
| glgC |
PRK05293 |
glucose-1-phosphate adenylyltransferase; Provisional |
143-274 |
4.01e-04 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 179997 [Multi-domain] Cd Length: 380 Bit Score: 41.39 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 143 QLIDSYEETGSS-TLAVMKVPHEDTSKYGVINPAKEvseglYDVTNFVEKP-NPEdapSDLAIIGRYlltadIFD----- 215
Cdd:PRK05293 135 KMLDYHKEKEADvTIAVIEVPWEEASRFGIMNTDEN-----MRIVEFEEKPkNPK---SNLASMGIY-----IFNwkrlk 201
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 752296517 216 ---ILENTKP------GKgNEIQLtdaidTLNKKGKVYAHEFKGDRYDTGNKFGWLQTNIEFGLKHPE 274
Cdd:PRK05293 202 eylIEDEKNPnsshdfGK-NVIPL-----YLEEGEKLYAYPFKGYWKDVGTIESLWEANMELLRPENP 263
|
|
| eIF-2B_epsilon_N |
cd04197 |
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ... |
7-131 |
8.38e-04 |
|
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: 39.90 E-value: 8.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 7 AIIPAAGLGTRFLPETKAMPKEMLPVVDKPAIQLIVEEAIASGITDILIIIGKGKRAIEDHFDSntelelnleSKGKDem 86
Cdd:cd04197 3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQIKEYIEK---------SKWSK-- 71
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 752296517 87 lkavKKTNGLNIYFKRQEHPNGLGDAVHT--AKSFVgEDPFVIMLGD 131
Cdd:cd04197 72 ----PKSSLMIVIIIMSEDCRSLGDALRDldAKGLI-RGDFILVSGD 113
|
|
| glmU |
PRK14353 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
7-138 |
1.81e-03 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184642 [Multi-domain] Cd Length: 446 Bit Score: 39.46 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 7 AIIPAAGLGTRFlpeTKAMPKEMLPVVDKPAIQLIVEEAIASGITDILIIIGKGKRAIEdhfdsntelelnleskgkdem 86
Cdd:PRK14353 8 AIILAAGEGTRM---KSSLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGPGAEAVA--------------------- 63
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 752296517 87 lKAVKKTNGLNIYFkRQEHPNGLGDAVHTAKSFV--GEDPFVIMLGDD-LMTDET 138
Cdd:PRK14353 64 -AAAAKIAPDAEIF-VQKERLGTAHAVLAAREALagGYGDVLVLYGDTpLITAET 116
|
|
| G1P_cytidylyltransferase |
cd02524 |
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ... |
7-68 |
5.68e-03 |
|
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: 37.55 E-value: 5.68e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 752296517 7 AIIPAAGLGTRFLPETKAMPKEMLPVVDKPAIQLIVEEAIASGITDILIIIGKGKRAIEDHF 68
Cdd:cd02524 1 VVILAGGLGTRLSEETELKPKPMVEIGGRPILWHIMKIYSHYGHNDFILCLGYKGHVIKEYF 62
|
|
| CDP-ME_synthetase |
cd02516 |
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ... |
7-60 |
6.93e-03 |
|
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: 37.12 E-value: 6.93e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 752296517 7 AIIPAAGLGTRFlpeTKAMPKEMLPVVDKPAIQLIVEEAIASG-ITDILIIIGKG 60
Cdd:cd02516 3 AIILAAGSGSRM---GADIPKQFLELGGKPVLEHTLEAFLAHPaIDEIVVVVPPD 54
|
|
| glmU |
PRK09451 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
7-172 |
7.90e-03 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 181867 [Multi-domain] Cd Length: 456 Bit Score: 37.70 E-value: 7.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 7 AIIPAAGLGTRFLPEtkaMPKEMLPVVDKPAIQLIVEEAIASGITDILIIIGKGkraiedhfdsntelelnleskgkDEM 86
Cdd:PRK09451 8 VVILAAGKGTRMYSD---LPKVLHTLAGKPMVQHVIDAANELGAQHVHLVYGHG-----------------------GDL 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752296517 87 LKAVKKTNGLNIYFkrQEHPNGLGDAVHTAKSFVGEDPFVIML-GD-DLMTDETpLTKqLIDSYEETGsstLAVMKVPHE 164
Cdd:PRK09451 62 LKQTLADEPLNWVL--QAEQLGTGHAMQQAAPFFADDEDILMLyGDvPLISVET-LQR-LRDAKPQGG---IGLLTVKLD 134
|
....*...
gi 752296517 165 DTSKYGVI 172
Cdd:PRK09451 135 NPTGYGRI 142
|
|
| |
