|
Name |
Accession |
Description |
Interval |
E-value |
| GalU |
COG1210 |
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis]; |
1-288 |
0e+00 |
|
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440823 [Multi-domain] Cd Length: 288 Bit Score: 520.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 1 MKVRKAVIPAAGLGTRFLPATKAIAKEMLPIVDKPTIQFIVEEAMASGIEDILVVTGKAKRPIEDHFDANIELEQNLKST 80
Cdd:COG1210 1 MKIRKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVTGRGKRAIEDHFDRSYELEATLEAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 81 GKTDLLKLVEETTD-INLHFVRQKRPLGLGHAILQAKAFVGDEPFVVMLGDDITSNKIPLTKQLINDYEKTKASTLAVMP 159
Cdd:COG1210 81 GKEELLEEVRSISPlANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSEKPCLKQMIEVYEETGGSVIAVQE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 160 VPHEETSKYGIIEPnGEIAKGLYDVNSFVEKPKPEQAPSNLAIIGRYLLTPEIFSLLEKQKPGKGGEIQLTDSIDELNKT 239
Cdd:COG1210 161 VPPEEVSKYGIVDG-EEIEGGVYRVTGLVEKPAPEEAPSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDAIAALAKE 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1520517018 240 QRVFAQEFSGKRYDVGTKIGMLEANIEYGLQHPETKDALKAYLKSMSAK 288
Cdd:COG1210 240 EPVYAYEFEGKRYDCGDKLGYLKATVEFALKRPDLGEEFREYLKELLKE 288
|
|
| UGPase_prokaryotic |
cd02541 |
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ... |
4-270 |
9.42e-155 |
|
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: 432.34 E-value: 9.42e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 4 RKAVIPAAGLGTRFLPATKAIAKEMLPIVDKPTIQFIVEEAMASGIEDILVVTGKAKRPIEDHFDANIELEQNLKSTGKT 83
Cdd:cd02541 1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRGKRAIEDHFDRSYELEETLEKKGKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 84 DLLKLVEETTD-INLHFVRQKRPLGLGHAILQAKAFVGDEPFVVMLGDDITSNKIPLTKQLINDYEKTKASTLAVMPVPH 162
Cdd:cd02541 81 DLLEEVRIISDlANIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLIDSKEPCLKQLIEAYEKTGASVIAVEEVPP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 163 EETSKYGIIEPnGEIAKGLYDVNSFVEKPKPEQAPSNLAIIGRYLLTPEIFSLLEKQKPGKGGEIQLTDSIDELNKTQRV 242
Cdd:cd02541 161 EDVSKYGIVKG-EKIDGDVFKVKGLVEKPKPEEAPSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTDAIAKLLEEEPV 239
|
250 260
....*....|....*....|....*...
gi 1520517018 243 FAQEFSGKRYDVGTKIGMLEANIEYGLQ 270
Cdd:cd02541 240 YAYVFEGKRYDCGNKLGYLKATVEFALK 267
|
|
| galU |
TIGR01099 |
UTP--glucose-1-phosphate uridylyltransferase; Built to distinquish between the highly similar ... |
4-263 |
1.63e-139 |
|
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: 393.64 E-value: 1.63e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 4 RKAVIPAAGLGTRFLPATKAIAKEMLPIVDKPTIQFIVEEAMASGIEDILVVTGKAKRPIEDHFDANIELEQNLKSTGKT 83
Cdd:TIGR01099 1 RKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYIVEEAVEAGIEEIVFVTGRGKRAIEDHFDYSYELEHQLEKRGKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 84 DLLKLVEETTD-INLHFVRQKRPLGLGHAILQAKAFVGDEPFVVMLGDDITSNKIPLTKQLINDYEKTKASTLAVMPVPH 162
Cdd:TIGR01099 81 ELLEEVRKISNlATIFYVRQKEQKGLGHAVLCARPFVGDEPFAVILGDDIVVNEEPALKQMIKAYEKTGCSIIAVQEVPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 163 EETSKYGIIEPNGeIAKGLYDVNSFVEKPKPEQAPSNLAIIGRYLLTPEIFSLLEKQKPGKGGEIQLTDSIDELNKTQRV 242
Cdd:TIGR01099 161 EEVSKYGVIDGEG-IEKDLYKVKNMVEKPKPEEAPSNLAIVGRYILTPDIFDLLEETPPGKGGEIQLTDAINKLLENETV 239
|
250 260
....*....|....*....|.
gi 1520517018 243 FAQEFSGKRYDVGTKIGMLEA 263
Cdd:TIGR01099 240 LAYKFNGKRYDCGSKLGYLEA 260
|
|
| PRK13389 |
PRK13389 |
UTP--glucose-1-phosphate uridylyltransferase GalU; |
2-284 |
2.41e-78 |
|
UTP--glucose-1-phosphate uridylyltransferase GalU;
Pssm-ID: 184021 [Multi-domain] Cd Length: 302 Bit Score: 239.81 E-value: 2.41e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 2 KVRKAVIPAAGLGTRFLPATKAIAKEMLPIVDKPTIQFIVEEAMASGIEDILVVTGKAKRPIEDHFDANIELEQNLKSTG 81
Cdd:PRK13389 7 KVKKAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFDTSFELEAMLEKRV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 82 KTDLLKLVEETT--DINLHFVRQKRPLGLGHAILQAKAFVGDEPFVVMLGDDITSNKIPLTKQ-----LINDYEKTKAST 154
Cdd:PRK13389 87 KRQLLDEVQSICppHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILDEYESDLSQdnlaeMIRRFDETGHSQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 155 LAVMPVphEETSKYGIIEPNGEIAKGLYDVN--SFVEKPKPEQAPSNLAIIGRYLLTPEIFSLLEKQKPGKGGEIQLTDS 232
Cdd:PRK13389 167 IMVEPV--ADVTAYGVVDCKGVELAPGESVPmvGVVEKPKADVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTDA 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1520517018 233 IDELNKTQRVFAQEFSGKRYDVGTKIGMLEANIEYGLQHPETKDALKAYLKS 284
Cdd:PRK13389 245 IDMLIEKETVEAYHMKGKSHDCGNKLGYMQAFVEYGIRHNTLGTEFKAWLEE 296
|
|
| PRK10122 |
PRK10122 |
UTP--glucose-1-phosphate uridylyltransferase GalF; |
5-288 |
3.37e-71 |
|
UTP--glucose-1-phosphate uridylyltransferase GalF;
Pssm-ID: 182252 [Multi-domain] Cd Length: 297 Bit Score: 221.69 E-value: 3.37e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 5 KAVIPAAGLGTRFLPATKAIAKEMLPIVDKPTIQFIVEEAMASGIEDILVVTGKAKRPIEDHFDANIELEQNLKSTGKTD 84
Cdd:PRK10122 5 KAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAVENHFDTSYELESLLEQRVKRQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 85 LLKLVEETT--DINLHFVRQKRPLGLGHAILQAKAFVGDEPFVVMLGDDI--TSNKIPLTKQL---INDYEKTKASTLAV 157
Cdd:PRK10122 85 LLAEVQSICppGVTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPDVVidDASADPLRYNLaamIARFNETGRSQVLA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 158 MPVPhEETSKYGII---EP---NGEIAKglydVNSFVEKP-KPEQAPSNLAIIGRYLLTPEIFSLLEKQKPGKGGEIQLT 230
Cdd:PRK10122 165 KRMP-GDLSEYSVIqtkEPldrEGKVSR----IVEFIEKPdQPQTLDSDLMAVGRYVLSADIWPELERTEPGAWGRIQLT 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1520517018 231 DSIDELNKTQRVFAQEFSGKRYDVGTKIGMLEANIEYGLQHPETKDALKAYLKSMSAK 288
Cdd:PRK10122 240 DAIAELAKKQSVDAMLMTGDSYDCGKKMGYMQAFVKYGLRNLKEGAKFRKGIEKLLSE 297
|
|
| NTP_transferase |
cd04181 |
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ... |
6-255 |
8.19e-60 |
|
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: 189.71 E-value: 8.19e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 6 AVIPAAGLGTRFLPATKAIAKEMLPIVDKPTIQFIVEEAMASGIEDILVVTGKAKRPIEDHFDANIELeqnlkstgktdl 85
Cdd:cd04181 1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGSKF------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 86 lklveettDINLHFVRQKRPLGLGHAILQAKAFVGDEPFVVMLGDDITSnkIPLTKQLINDYEKTKASTLAVMPVPHeeT 165
Cdd:cd04181 69 --------GVNIEYVVQEEPLGTAGAVRNAEDFLGDDDFLVVNGDVLTD--LDLSELLRFHREKGADATIAVKEVED--P 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 166 SKYGIIE--PNGEIAKglydvnsFVEKPKPEqaPSNLAIIGRYLLTPEIFSLLEKQKPgkGGEIQLTDSIDELNKTQRVF 243
Cdd:cd04181 137 SRYGVVEldDDGRVTR-------FVEKPTLP--ESNLANAGIYIFEPEILDYIPEILP--RGEDELTDAIPLLIEEGKVY 205
|
250
....*....|..
gi 1520517018 244 AQEFSGKRYDVG 255
Cdd:cd04181 206 GYPVDGYWLDIG 217
|
|
| G1P_TT_long |
cd04189 |
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ... |
5-264 |
1.02e-59 |
|
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: 190.09 E-value: 1.02e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 5 KAVIPAAGLGTRFLPATKAIAKEMLPIVDKPTIQFIVEEAMASGIEDILVVTGKAKRPIEDHFDANieleqnlkstgktd 84
Cdd:cd04189 2 KGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEALGDG-------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 85 llklveETTDINLHFVRQKRPLGLGHAILQAKAFVGDEPFVVMLGDDITSNKIpltKQLINDYEKTKASTLAVMpVPHEE 164
Cdd:cd04189 68 ------SRFGVRITYILQEEPLGLAHAVLAARDFLGDEPFVVYLGDNLIQEGI---SPLVRDFLEEDADASILL-AEVED 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 165 TSKYGIIEPNGEIAKGLydvnsfVEKPKPEqaPSNLAIIGRYLLTPEIFSLLEKQKPGKGGEIQLTDSIDEL-NKTQRVF 243
Cdd:cd04189 138 PRRFGVAVVDDGRIVRL------VEKPKEP--PSNLALVGVYAFTPAIFDAISRLKPSWRGELEITDAIQWLiDRGRRVG 209
|
250 260
....*....|....*....|.
gi 1520517018 244 AQEFSGKRYDVGTKIGMLEAN 264
Cdd:cd04189 210 YSIVTGWWKDTGTPEDLLEAN 230
|
|
| RmlA1 |
COG1209 |
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis]; |
4-264 |
2.16e-51 |
|
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440822 [Multi-domain] Cd Length: 294 Bit Score: 170.27 E-value: 2.16e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 4 RKAVIPAAGLGTRFLPATKAIAKEMLPIVDKPTIQFIVEEAMASGIEDILVVTGkakrpieDHFDANIEleqnlkstgkt 83
Cdd:COG1209 1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIIST-------PEDGPQFE----------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 84 dllKLVEETTD--INLHFVRQKRPLGLGHAILQAKAFVGDEPFVVMLGDDITsNKIPLTKQLINDYEKTKASTLAVMPVP 161
Cdd:COG1209 63 ---RLLGDGSQlgIKISYAVQPEPLGLAHAFIIAEDFIGGDPVALVLGDNIF-YGDGLSELLREAAARESGATIFGYKVE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 162 HEEtsKYGIIE--PNGEIAkglydvnSFVEKPKpeQAPSNLAIIGRYLLTPEIFSLLEKQKPGKGGEIQLTDSIDE-LNK 238
Cdd:COG1209 139 DPE--RYGVVEfdEDGRVV-------SLEEKPK--EPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAyLER 207
|
250 260
....*....|....*....|....*..
gi 1520517018 239 TQRVFAQEFSGKR-YDVGTKIGMLEAN 264
Cdd:COG1209 208 GKLVVELLGRGFAwLDTGTHESLLEAN 234
|
|
| GCD1 |
COG1208 |
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ... |
5-264 |
2.50e-47 |
|
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: 158.01 E-value: 2.50e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 5 KAVIPAAGLGTRFLPATKAIAKEMLPIVDKPTIQFIVEEAMASGIEDILVVTGKAKRPIEDHFDANIELeqnlkstgktd 84
Cdd:COG1208 1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRF----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 85 llklveettDINLHFVRQKRPLGLGHAILQAKAFVGDEPFVVMLGDDITSnkIPLTKqLINDYEKTKAS-TLAVMPVPHe 163
Cdd:COG1208 70 ---------GVRITYVDEGEPLGTGGALKRALPLLGDEPFLVLNGDILTD--LDLAA-LLAFHREKGADaTLALVPVPD- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 164 eTSKYGIIEPNGEiakGLydVNSFVEkpKPEQAPSNLAIIGRYLLTPEIFSLLEkqkpgKGGEIQLTDSIDELNKTQRVF 243
Cdd:COG1208 137 -PSRYGVVELDGD---GR--VTRFVE--KPEEPPSNLINAGIYVLEPEIFDYIP-----EGEPFDLEDLLPRLIAEGRVY 203
|
250 260
....*....|....*....|.
gi 1520517018 244 AQEFSGKRYDVGTKIGMLEAN 264
Cdd:COG1208 204 GYVHDGYWLDIGTPEDLLEAN 224
|
|
| NTP_transferase |
pfam00483 |
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ... |
5-264 |
1.45e-34 |
|
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: 125.44 E-value: 1.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 5 KAVIPAAGLGTRFLPATKAIAKEMLPIVDK-PTIQFIVEEAMASGIEDILVVTGKAKRP-IEDHFDANIELEqnlkstgk 82
Cdd:pfam00483 1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFmLNELLGDGSKFG-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 83 tdllklveettdINLHFVRQKRPLGLGHAILQAKAFVGDEPF-VVMLGDDITSnKIPLTKQLINDYEKTKASTLAVMPVP 161
Cdd:pfam00483 73 ------------VQITYALQPEGKGTAPAVALAADFLGDEKSdVLVLGGDHIY-RMDLEQAVKFHIEKAADATVTFGIVP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 162 HEETSKYGIIEPNGEiakglYDVNSFVEKPKpEQAPSNLAIIGRYLLTPEIFSLLEKQ-KPGKGGEIQLTDSIDE-LNKT 239
Cdd:pfam00483 140 VEPPTGYGVVEFDDN-----GRVIRFVEKPK-LPKASNYASMGIYIFNSGVLDFLAKYlEELKRGEDEITDILPKaLEDG 213
|
250 260
....*....|....*....|....*.
gi 1520517018 240 QRVFAQEFSGKR-YDVGTKIGMLEAN 264
Cdd:pfam00483 214 KLAYAFIFKGYAwLDVGTWDSLWEAN 239
|
|
| G1P_TT_short |
cd02538 |
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ... |
4-264 |
8.94e-30 |
|
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: 112.67 E-value: 8.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 4 RKAVIPAAGLGTRFLPATKAIAKEMLPIVDKPTIQFIVEEAMASGIEDILVVTGKakrpieDHFDANIELEQNLKSTGkt 83
Cdd:cd02538 1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTP------EDLPLFKELLGDGSDLG-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 84 dllklveettdINLHFVRQKRPLGLGHAILQAKAFVGDEPFVVMLGDDITSNKiPLTKQLINDYEKTKASTLAVMPVPHE 163
Cdd:cd02538 73 -----------IRITYAVQPKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQ-GLSPILQRAAAQKEGATVFGYEVNDP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 164 EtsKYGIIEPNGEiakglYDVNSFVEKPKpeQAPSNLAIIGRYLLTPEIFSLLEKQKPGKGGEIQLTDSIDE-LNKTQRV 242
Cdd:cd02538 141 E--RYGVVEFDEN-----GRVLSIEEKPK--KPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEyLEKGKLS 211
|
250 260
....*....|....*....|....*
gi 1520517018 243 FaqEFSGKRY---DVGTKIGMLEAN 264
Cdd:cd02538 212 V--ELLGRGFawlDTGTHESLLEAS 234
|
|
| PRK15480 |
PRK15480 |
glucose-1-phosphate thymidylyltransferase RfbA; Provisional |
1-264 |
1.19e-22 |
|
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
Pssm-ID: 185377 [Multi-domain] Cd Length: 292 Bit Score: 94.74 E-value: 1.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 1 MKVRKAVIPAAGLGTRFLPATKAIAKEMLPIVDKPTIQFIVEEAMASGIEDILVVTGKAKRPiedhfdaniELEQNLKST 80
Cdd:PRK15480 1 MKTRKGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTP---------RFQQLLGDG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 81 GKTDLlklveettdiNLHFVRQKRPLGLGHAILQAKAFVGDEPFVVMLGDDI-TSNKIP-LTKQLINdyektKASTLAVM 158
Cdd:PRK15480 72 SQWGL----------NLQYKVQPSPDGLAQAFIIGEEFIGGDDCALVLGDNIfYGHDLPkLMEAAVN-----KESGATVF 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 159 PVPHEETSKYGIIEpngeiakglYDVN--SFVEKPKPEQAPSNLAIIGRYLLTPEIFSLLEKQKPGKGGEIQLTDsIDEL 236
Cdd:PRK15480 137 AYHVNDPERYGVVE---------FDQNgtAISLEEKPLQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITD-INRI 206
|
250 260 270
....*....|....*....|....*....|.
gi 1520517018 237 NKTQRVFAQEFSGKRY---DVGTKIGMLEAN 264
Cdd:PRK15480 207 YMEQGRLSVAMMGRGYawlDTGTHQSLIEAS 237
|
|
| NTP_transferase_like_2 |
cd06426 |
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ... |
6-264 |
1.97e-21 |
|
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: 89.88 E-value: 1.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 6 AVIPAAGLGTRFLPATKAIAKEMLPIVDKPTIQFIVEEAMASGIEDILVVTGKAKRPIEDHFdanieleQNLKSTGktdl 85
Cdd:cd06426 1 VVIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNYLAEMIEDYF-------GDGSKFG---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 86 lklveettdINLHFVRQKRPLGLGHAILQAKAFVgDEPFVVMLGDDITSNKIpltKQLINDYEKTKAS-TLAV----MPV 160
Cdd:cd06426 70 ---------VNISYVREDKPLGTAGALSLLPEKP-TDPFLVMNGDILTNLNY---EHLLDFHKENNADaTVCVreyeVQV 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 161 PheetskYGIIEPNGEiakglyDVNSFVEKPKPEQapsnLAIIGRYLLTPEIFSLLEkqkpgKGGEIQLTDSID-ELNKT 239
Cdd:cd06426 137 P------YGVVETEGG------RITSIEEKPTHSF----LVNAGIYVLEPEVLDLIP-----KNEFFDMPDLIEkLIKEG 195
|
250 260
....*....|....*....|....*
gi 1520517018 240 QRVFAQEFSGKRYDVGTKIGMLEAN 264
Cdd:cd06426 196 KKVGVFPIHEYWLDIGRPEDYEKAN 220
|
|
| NTP_transferase_like_1 |
cd06422 |
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ... |
5-263 |
7.09e-18 |
|
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: 80.31 E-value: 7.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 5 KAVIPAAGLGTRFLPATKAIAKEMLPIVDKPTIQFIVEEAMASGIEDILVVTGKAKRPIEDHfdanieleqnlkstgktd 84
Cdd:cd06422 1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAH------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 85 llkLVEETTDINLHFVR-QKRPLGLGHAILQAKAFVGDEPFVVMLGDDITSnkIPLTKQLINDYEKTKASTLAVMPVPHe 163
Cdd:cd06422 63 ---LGDSRFGLRITISDePDELLETGGGIKKALPLLGDEPFLVVNGDILWD--GDLAPLLLLHAWRMDALLLLLPLVRN- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 164 etskygiiepNGEIAKGLYDVNSFVE-KPKPEQAPSNLAIIGRYLLTPEIFSLLEKqkpgkgGEIQLTDSIDELNKTQRV 242
Cdd:cd06422 137 ----------PGHNGVGDFSLDADGRlRRGGGGAVAPFTFTGIQILSPELFAGIPP------GKFSLNPLWDRAIAAGRL 200
|
250 260
....*....|....*....|.
gi 1520517018 243 FAQEFSGKRYDVGTKIGMLEA 263
Cdd:cd06422 201 FGLVYDGLWFDVGTPERLLAA 221
|
|
| NTP_transferase_WcbM_like |
cd06915 |
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ... |
6-221 |
1.54e-17 |
|
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: 79.52 E-value: 1.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 6 AVIPAAGLGTRFLPATKAIAKEMLPIVDKPTIQFIVEEAMASGIEDILVVTGKAKRPIEDHF-DANIELeqnlkstgktd 84
Cdd:cd06915 1 AVILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYLAEQIEEYFgDGYRGG----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 85 llklveettdINLHFVRQKRPLGLGHAILQAKAFVGDEPFVVMLGD-----DItsnkipltKQLINDYEKTKA-STLAVM 158
Cdd:cd06915 70 ----------IRIYYVIEPEPLGTGGAIKNALPKLPEDQFLVLNGDtyfdvDL--------LALLAALRASGAdATMALR 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1520517018 159 PVPHeeTSKYGIIEPNGEiakglYDVNSFVEkpKPEQAPSNLAIIGRYLLTPEIFSLLEKQKP 221
Cdd:cd06915 132 RVPD--ASRYGNVTVDGD-----GRVIAFVE--KGPGAAPGLINGGVYLLRKEILAEIPADAF 185
|
|
| M1P_guanylylT_B_like_N |
cd06425 |
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ... |
5-217 |
7.99e-16 |
|
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: 74.94 E-value: 7.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 5 KAVIPAAGLGTRFLPATKAIAKEMLPIVDKPTIQFIVEEAMASGIEDILVVTgkAKRPiedhfdANIELEqnlkstgktd 84
Cdd:cd06425 2 KALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAV--NYRP------EDMVPF---------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 85 lLKLVEETTDINLHFVRQKRPLGLGHAILQAKAFVG--DEPFVVmLGDDITSNkIPLtKQLINDYEKTKA-STLAVMPVp 161
Cdd:cd06425 64 -LKEYEKKLGIKITFSIETEPLGTAGPLALARDLLGddDEPFFV-LNSDVICD-FPL-AELLDFHKKHGAeGTILVTKV- 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1520517018 162 hEETSKYGII---EPNGEIAKglydvnsFVEKPKpeQAPSNLAIIGRYLLTPEIFSLLE 217
Cdd:cd06425 139 -EDPSKYGVVvhdENTGRIER-------FVEKPK--VFVGNKINAGIYILNPSVLDRIP 187
|
|
| GlmU |
COG1207 |
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ... |
4-179 |
2.30e-13 |
|
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: 69.67 E-value: 2.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 4 RKAVIPAAGLGTRF---LPatkaiaKEMLPIVDKPTIQFIVEEAMASGIEDILVVTGKAKRPIEDHFDanieleqnlkst 80
Cdd:COG1207 3 LAVVILAAGKGTRMkskLP------KVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVRAALA------------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 81 gktdllklveettDINLHFVRQKRPLGLGHAILQAKAFVG--DEPFVVMLGDditsnkIPLT-----KQLINDYEKTKAS 153
Cdd:COG1207 65 -------------DLDVEFVLQEEQLGTGHAVQQALPALPgdDGTVLVLYGD------VPLIraetlKALLAAHRAAGAA 125
|
170 180 190
....*....|....*....|....*....|.
gi 1520517018 154 -TL--AVMPVPHeetsKYG-II-EPNGEIAK 179
Cdd:COG1207 126 aTVltAELDDPT----GYGrIVrDEDGRVLR 152
|
|
| eIF-2B_gamma_N_like |
cd02507 |
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ... |
5-177 |
2.36e-11 |
|
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: 61.89 E-value: 2.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 5 KAVIPAAGLGTRFLPATKAIAKEMLPIVDKPTIQFIVEEAMASGIEDILVVTGKakrpiedHFDANIELEQNLKSTGKTD 84
Cdd:cd02507 2 QAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCE-------HSQAIIEHLLKSKWSSLSS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 85 LLKLVEETTDinlhfvrQKRPLGLGHAILQAKAFVgDEPFVVMLGDDITSnkIPLTKQLI--NDYEKTKASTLAVM---P 159
Cdd:cd02507 75 KMIVDVITSD-------LCESAGDALRLRDIRGLI-RSDFLLLSCDLVSN--IPLSELLEerRKKDKNAIATLTVLlasP 144
|
170
....*....|....*...
gi 1520517018 160 VPHEETSKYGIIEPNGEI 177
Cdd:cd02507 145 PVSTEQSKKTEEEDVIAV 162
|
|
| GT2_GlmU_N_bac |
cd02540 |
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ... |
6-179 |
5.07e-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: 5.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 6 AVIPAAGLGTRF---LPatkaiaKEMLPIVDKPTIQFIVEEAMASGIEDILVVTGKAKrpiedhfdanieleqnlkstgk 82
Cdd:cd02540 1 AVILAAGKGTRMksdLP------KVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGA---------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 83 tdllKLVEET-TDINLHFVRQKRPLGLGHAILQAKAFVGD--EPFVVMLGDD--ITSNKIpltKQLINDYEKTKAsTLAV 157
Cdd:cd02540 53 ----EQVKKAlANPNVEFVLQEEQLGTGHAVKQALPALKDfeGDVLVLYGDVplITPETL---QRLLEAHREAGA-DVTV 124
|
170 180
....*....|....*....|....
gi 1520517018 158 MPVPHEETSKYG--IIEPNGEIAK 179
Cdd:cd02540 125 LTAELEDPTGYGriIRDGNGKVLR 148
|
|
| COG1213 |
COG1213 |
Choline kinase [Lipid transport and metabolism]; |
5-68 |
1.10e-10 |
|
Choline kinase [Lipid transport and metabolism];
Pssm-ID: 440826 [Multi-domain] Cd Length: 236 Bit Score: 60.25 E-value: 1.10e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1520517018 5 KAVIPAAGLGTRFLPATKAIAKEMLPIVDKPTIQFIVEEAMASGIEDILVVTGKAKRPIEDHFD 68
Cdd:COG1213 1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEALA 64
|
|
| glmU |
PRK14354 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
4-179 |
1.23e-10 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184643 [Multi-domain] Cd Length: 458 Bit Score: 61.39 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 4 RKAVIPAAGLGTRF---LPatkaiaKEMLPIVDKPTIQFIVEEAMASGIEDILVVTGKAKrpiedhfdanieleqnlkst 80
Cdd:PRK14354 3 RYAIILAAGKGTRMkskLP------KVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVGHGA-------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 81 gktdllKLVEETTDINLHFVRQKRPLGLGHAILQAKAFVGDEPFVVML--GDD--ITSNKIpltKQLINDYEKTKAS-TL 155
Cdd:PRK14354 57 ------EEVKEVLGDRSEFALQEEQLGTGHAVMQAEEFLADKEGTTLVicGDTplITAETL---KNLIDFHEEHKAAaTI 127
|
170 180
....*....|....*....|....*...
gi 1520517018 156 --AVMPVPHeetsKYG-II-EPNGEIAK 179
Cdd:PRK14354 128 ltAIAENPT----GYGrIIrNENGEVEK 151
|
|
| GDP-M1P_Guanylyltransferase |
cd02509 |
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ... |
5-256 |
2.13e-10 |
|
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: 59.90 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 5 KAVIPAAGLGTRFLPA-TKAIAKEMLPIV-DKPTIQFIVEEAM-ASGIEDILVVTGkakrpiEDHFDanIELEQnlkstg 81
Cdd:cd02509 2 YPVILAGGSGTRLWPLsRESYPKQFLKLFgDKSLLQQTLDRLKgLVPPDRILVVTN------EEYRF--LVREQ------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 82 ktdllkLVEETTDINLHFVRQKR----PLGLGHAILQAKAfvGDEPFVVMLGDDITSNkipltkqlINDYEKT--KASTL 155
Cdd:cd02509 68 ------LPEGLPEENIILEPEGRntapAIALAALYLAKRD--PDAVLLVLPSDHLIED--------VEAFLKAvkKAVEA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 156 AVMP-------VPHEETSKYGIIEPNGEIAKGLYDVNSFVEKPKPEQAPSNLAiIGRYL-------------------LT 209
Cdd:cd02509 132 AEEGylvtfgiKPTRPETGYGYIEAGEKLGGGVYRVKRFVEKPDLETAKEYLE-SGNYLwnsgiflfraktfleelkkHA 210
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1520517018 210 PEIFSLLEKQKPGKGGEIQLTD-----------SID----ElnKTQRVFAQEFSGKRYDVGT 256
Cdd:cd02509 211 PDIYEALEKALAAAGTDDFLRLleeafakipsiSIDyavmE--KTKKVAVVPADFGWSDLGS 270
|
|
| PC_cytidylyltransferase |
cd02523 |
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ... |
6-74 |
3.96e-10 |
|
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: 58.78 E-value: 3.96e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1520517018 6 AVIPAAGLGTRFLPATKAIAKEMLPIVDKPTIQFIVEEAMASGIEDILVVTGKAKRPIEDHFDANIELE 74
Cdd:cd02523 1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKKYPNIK 69
|
|
| glgC |
PRK05293 |
glucose-1-phosphate adenylyltransferase; Provisional |
107-273 |
1.41e-09 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 179997 [Multi-domain] Cd Length: 380 Bit Score: 57.96 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 107 GLGHAILQAKAFVGD-EP-FVVML-GDDITsnKIPLTKQLinDYEKTK-AS-TLAVMPVPHEETSKYGII--EPNGEIak 179
Cdd:PRK05293 100 GTAHAIYQNIDYIDQyDPeYVLILsGDHIY--KMDYDKML--DYHKEKeADvTIAVIEVPWEEASRFGIMntDENMRI-- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 180 glydvNSFVEKPKpeQAPSNLAIIGRYlltpeIF--SLLEK------QKP------GKggeiqltDSIDE-LNKTQRVFA 244
Cdd:PRK05293 174 -----VEFEEKPK--NPKSNLASMGIY-----IFnwKRLKEyliedeKNPnsshdfGK-------NVIPLyLEEGEKLYA 234
|
170 180
....*....|....*....|....*....
gi 1520517018 245 QEFSGKRYDVGTKIGMLEANIEYGLQHPE 273
Cdd:PRK05293 235 YPFKGYWKDVGTIESLWEANMELLRPENP 263
|
|
| eIF-2B_gamma_N |
cd04198 |
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ... |
5-95 |
3.17e-08 |
|
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; N-terminal domain of gamma subunit of the eukaryotic translation initiation factor 2B (eIF-2B): eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit gamma shares sequence similarity with epsilon subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.
Pssm-ID: 133041 [Multi-domain] Cd Length: 214 Bit Score: 53.05 E-value: 3.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 5 KAVIPAAGLGTRFLPATKAIAKEMLPIVDKPTIQFIVEEAMASGIEDILVVTGKAKRP-IEDHFDAN---------IELE 74
Cdd:cd04198 2 QAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEEQAeISTYLRSFplnlkqkldEVTI 81
|
90 100
....*....|....*....|...
gi 1520517018 75 QNLKSTGKTDLLKLV--EETTDI 95
Cdd:cd04198 82 VLDEDMGTADSLRHIrkKIKKDF 104
|
|
| MocA |
COG2068 |
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism]; |
6-156 |
2.12e-07 |
|
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
Pssm-ID: 441671 [Multi-domain] Cd Length: 195 Bit Score: 50.16 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 6 AVIPAAGLGTRFlPATKAiakeMLPIVDKPTIQFIVEEAMASGIEDILVVTGKAKRPIEDHFDanieleqnlkstgktdl 85
Cdd:COG2068 6 AIILAAGASSRM-GRPKL----LLPLGGKPLLERAVEAALAAGLDPVVVVLGADAEEVAAALA----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 86 lklveettDINLHFVRQKRP-LGLGHAI------LQAKAfvgdEPFVVMLGD--DITSNKIpltKQLINDYEKTKASTLA 156
Cdd:COG2068 64 --------GLGVRVVVNPDWeEGMSSSLraglaaLPADA----DAVLVLLGDqpLVTAETL---RRLLAAFRESPASIVA 128
|
|
| glmU |
PRK14358 |
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ... |
7-231 |
2.53e-07 |
|
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase; Provisional
Pssm-ID: 237688 [Multi-domain] Cd Length: 481 Bit Score: 51.52 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 7 VIPAAGLGTRFlpaTKAIAKEMLPIVDKPTIQFIVEEAMASGIEDILVVTGKAKRpiedhfdaniELEQNLKSTGKTdll 86
Cdd:PRK14358 11 VILAAGQGTRM---KSALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGAE----------QVEAALQGSGVA--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 87 klveettdinlhFVRQKRPLGLGHAILQ-AKAF-VGDEPFVVMLGDdiTSNKIPLTKQLINDYEKTKASTLAVMPVPHEE 164
Cdd:PRK14358 75 ------------FARQEQQLGTGDAFLSgASALtEGDADILVLYGD--TPLLRPDTLRALVADHRAQGSAMTILTGELPD 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1520517018 165 TSKYGIIepngeiakgLYDVNSFVEKPKPEQA--PSNLAI----IGRYLL---TPEIFSLLEKQKPgkGGEIQLTD 231
Cdd:PRK14358 141 ATGYGRI---------VRGADGAVERIVEQKDatDAEKAIgefnSGVYVFdarAPELARRIGNDNK--AGEYYLTD 205
|
|
| glmU |
PRK14357 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
5-251 |
2.75e-07 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237687 [Multi-domain] Cd Length: 448 Bit Score: 51.30 E-value: 2.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 5 KAVIPAAGLGTRFlpaTKAIAKEMLPIVDKPTIQFIVEEAMASGIEDILVVTGKAkrpiedhfdanieleqnlkstgktd 84
Cdd:PRK14357 2 RALVLAAGKGTRM---KSKIPKVLHKISGKPMINWVIDTAKKVAQKVGVVLGHEA------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 85 llKLVEETTDINLHFVRQKRPLGLGHAILQAKAFVG-DEPFVVMLGDD--ITSNKIpltKQLINDYEKTKASTlAVMPVP 161
Cdd:PRK14357 54 --ELVKKLLPEWVKIFLQEEQLGTAHAVMCARDFIEpGDDLLILYGDVplISENTL---KRLIEEHNRKGADV-TILVAD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 162 HEETSKYG-IIEPNGEI-----------AKGLYDVNSFVEKPKPEQAPSNLAII------GRYLLTpEIFSLLEKQKpgk 223
Cdd:PRK14357 128 LEDPTGYGrIIRDGGKYrivedkdapeeEKKIKEINTGIYVFSGDFLLEVLPKIknenakGEYYLT-DAVNFAEKVR--- 203
|
250 260 270
....*....|....*....|....*....|..
gi 1520517018 224 ggeIQLTDSIDEL----NKTQRVFAQEFSGKR 251
Cdd:PRK14357 204 ---VVKTEDLLEItgvnTRIQLAWLEKQLRMR 232
|
|
| glmU |
PRK09451 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
6-178 |
4.08e-07 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 181867 [Multi-domain] Cd Length: 456 Bit Score: 50.80 E-value: 4.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 6 AVIPAAGLGTRF---LPatkaiaKEMLPIVDKPTIQFIVEEAMASGIEDILVVTGKAkrpiedhfdanieleqnlkstgk 82
Cdd:PRK09451 8 VVILAAGKGTRMysdLP------KVLHTLAGKPMVQHVIDAANELGAQHVHLVYGHG----------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 83 TDLLKlvEETTDINLHFVRQKRPLGLGHAILQAKAFVGDEPFVVML-GDditsnkIPL-TKQLINDYEKTK-ASTLAVMP 159
Cdd:PRK09451 59 GDLLK--QTLADEPLNWVLQAEQLGTGHAMQQAAPFFADDEDILMLyGD------VPLiSVETLQRLRDAKpQGGIGLLT 130
|
170 180
....*....|....*....|
gi 1520517018 160 VPHEETSKYG-IIEPNGEIA 178
Cdd:PRK09451 131 VKLDNPTGYGrITRENGKVV 150
|
|
| glmU |
PRK14355 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
6-171 |
2.33e-06 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237685 [Multi-domain] Cd Length: 459 Bit Score: 48.59 E-value: 2.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 6 AVIPAAGLGTRFlpaTKAIAKEMLPIVDKPTIQFIVEEAMASGIEDILVVTGKAKRPIEDHFdanieleqnlkstgktdl 85
Cdd:PRK14355 6 AIILAAGKGTRM---KSDLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHF------------------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 86 lklvEETTDINlhFVRQKRPLGLGHAILQA-KAFVGDEPFVVMLGDDITSNKIPLTKQLINDYEKTKAStLAVMPVPHEE 164
Cdd:PRK14355 65 ----AGDGDVS--FALQEEQLGTGHAVACAaPALDGFSGTVLILCGDVPLLRAETLQGMLAAHRATGAA-VTVLTARLEN 137
|
....*..
gi 1520517018 165 TSKYGII 171
Cdd:PRK14355 138 PFGYGRI 144
|
|
| GT_2_like_f |
cd04182 |
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ... |
6-156 |
2.01e-05 |
|
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: 44.09 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 6 AVIPAAGLGTRFlPATKAiakeMLPIVDKPTIQFIVEEAMASGIEDILVVTGkakrpiedhfDANIELEQNLKstgktdl 85
Cdd:cd04182 3 AIILAAGRSSRM-GGNKL----LLPLDGKPLLRHALDAALAAGLSRVIVVLG----------AEADAVRAALA------- 60
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1520517018 86 lklveettDINLHFVRQKRP-LGLGHAILQAKAFVGDEP--FVVMLGD--DITSNKIpltKQLINDYEKTKASTLA 156
Cdd:cd04182 61 --------GLPVVVVINPDWeEGMSSSLAAGLEALPADAdaVLILLADqpLVTAETL---RALIDAFREDGAGIVA 125
|
|
| M1P_guanylylT_A_like_N |
cd06428 |
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ... |
14-232 |
2.67e-05 |
|
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: 44.55 E-value: 2.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 14 GTRFLPATKAIAKEMLPIVDKPTIQFIVEE-AMASGIEDILVVTgkakrpiedhFDANIELEQNLKSTgktdllklvEET 92
Cdd:cd06428 11 GTRFRPLSLDVPKPLFPVAGKPMIHHHIEAcAKVPDLKEVLLIG----------FYPESVFSDFISDA---------QQE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 93 TDINLHFVRQKRPLGLGHAI--LQAKAFVGD-EPFVVMLGdDITSNkIPLtKQLINDYEKTKAS-TLAVMPVPHEETSKY 168
Cdd:cd06428 72 FNVPIRYLQEYKPLGTAGGLyhFRDQILAGNpSAFFVLNA-DVCCD-FPL-QELLEFHKKHGASgTILGTEASREQASNY 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1520517018 169 GIIEPNGEIAKGLYdvnsFVEkpKPEQAPSNLAIIGRYLLTPEIFSLLEKQKPGKGGEIQLTDS 232
Cdd:cd06428 149 GCIVEDPSTGEVLH----YVE--KPETFVSDLINCGVYLFSPEIFDTIKKAFQSRQQEAQLGDD 206
|
|
| glgC |
PRK00844 |
glucose-1-phosphate adenylyltransferase; Provisional |
111-212 |
3.11e-05 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 234846 [Multi-domain] Cd Length: 407 Bit Score: 44.82 E-value: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 111 AILQAKAFVGDE-P-FVVMLG-D-----DItsnkipltKQLINDYEKTKAS-TLAVMPVPHEETSKYGIIE--PNGEIAk 179
Cdd:PRK00844 104 AIYQSLNLIEDEdPdYVVVFGaDhvyrmDP--------RQMVDFHIESGAGvTVAAIRVPREEASAFGVIEvdPDGRIR- 174
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1520517018 180 glydvnSFVEKPK--------PEQApsnLAIIGRYLLTPEI 212
Cdd:PRK00844 175 ------GFLEKPAdppglpddPDEA---LASMGNYVFTTDA 206
|
|
| eIF-2B_epsilon_N |
cd04197 |
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ... |
6-158 |
5.18e-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: 43.37 E-value: 5.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 6 AVIPAAGLGTRFLPATKAIAKEMLPIVDKPTIQFIVEEAMASGIEDILVVTGKAKRPIEDHFdanieleQNLKSTGKTDL 85
Cdd:cd04197 3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQIKEYI-------EKSKWSKPKSS 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1520517018 86 LKLVeettdinlHFVRQKRPLGLGHAI--LQAKAFV-GDepFVVMLGDDITSnkIPLTKQLINDYEKTKASTLAVM 158
Cdd:cd04197 76 LMIV--------IIIMSEDCRSLGDALrdLDAKGLIrGD--FILVSGDVVSN--IDLKEILEEHKERRKKDKNAIM 139
|
|
| glgC |
PRK00725 |
glucose-1-phosphate adenylyltransferase; Provisional |
154-266 |
6.18e-05 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 234824 [Multi-domain] Cd Length: 425 Bit Score: 44.06 E-value: 6.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 154 TLAVMPVPHEETSKYGIIEPNGEiakglYDVNSFVEKPK-PEQAPSN----LAIIGRYLLTPE-IFSLLEK--QKP---- 221
Cdd:PRK00725 160 TVACLEVPREEASAFGVMAVDEN-----DRITAFVEKPAnPPAMPGDpdksLASMGIYVFNADyLYELLEEdaEDPnssh 234
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1520517018 222 --GKggeiqltDSIDELNKTQRVFAQEFS---------GKRY--DVGTKIGMLEANIE 266
Cdd:PRK00725 235 dfGK-------DIIPKIVEEGKVYAHPFSdscvrsdpeEEPYwrDVGTLDAYWQANLD 285
|
|
| glgC |
PRK02862 |
glucose-1-phosphate adenylyltransferase; Provisional |
141-271 |
1.79e-04 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 179486 [Multi-domain] Cd Length: 429 Bit Score: 42.56 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 141 KQLINDYEKTKAS-TLAVMPVPHEETSKYGIIEPNGEiakGLydVNSFVEKPK-----------------PEQAPSN--L 200
Cdd:PRK02862 133 RLFVQHHRETGADiTLAVLPVDEKDASGFGLMKTDDD---GR--ITEFSEKPKgdelkamavdtsrlglsPEEAKGKpyL 207
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1520517018 201 AIIGRYLLTPEI-FSLLEKQKPGK--GGEIqltdsIDELNKTQRVFAQEFSGKRYDVGTKIGMLEANIEYGLQH 271
Cdd:PRK02862 208 ASMGIYVFSRDVlFDLLNKNPEYTdfGKEI-----IPEAIRDYKVQSYLFDGYWEDIGTIEAFYEANLALTQQP 276
|
|
| glmU |
PRK14359 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
7-114 |
2.89e-03 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237689 [Multi-domain] Cd Length: 430 Bit Score: 38.82 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 7 VIPAAGLGTRFLPATkaiAKEMLPIVDKPTIQFIVEEAMASGiEDILVVTG----KAKRPIEDHFDANIELEQNLKS--- 79
Cdd:PRK14359 6 IILAAGKGTRMKSSL---PKVLHTICGKPMLFYILKEAFAIS-DDVHVVLHhqkeRIKEAVLEYFPGVIFHTQDLENypg 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1520517018 80 TG------------------------KTDLLKLVEETTDINLHFVRQKRPLGLGHAILQ 114
Cdd:PRK14359 82 TGgalmgiepkhervlilngdmplveKDELEKLLENDADIVMSVFHLADPKGYGRVVIE 140
|
|
| CDP-ME_synthetase |
cd02516 |
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ... |
6-90 |
6.86e-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: 6.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1520517018 6 AVIPAAGLGTRFlpaTKAIAKEMLPIVDKPTIQFIVEEAMASG-IEDILVVTGkakrpiEDHfdanIELEQNLKSTGKTD 84
Cdd:cd02516 3 AIILAAGSGSRM---GADIPKQFLELGGKPVLEHTLEAFLAHPaIDEIVVVVP------PDD----IDLAKELAKYGLSK 69
|
....*.
gi 1520517018 85 LLKLVE 90
Cdd:cd02516 70 VVKIVE 75
|
|
| ispD |
TIGR00453 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ... |
6-56 |
7.66e-03 |
|
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase, the IspD protein of the deoxyxylulose pathway of IPP biosynthesis. In about twenty percent of bacterial genomes, this protein occurs as IspDF, a bifunctional fusion protein. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 213532 Cd Length: 217 Bit Score: 36.88 E-value: 7.66e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1520517018 6 AVIPAAGLGTRFlpaTKAIAKEMLPIVDKPTIQFIVEEAMAS-GIEDILVVT 56
Cdd:TIGR00453 2 AVIPAAGRGTRF---GSGVPKQYLELGGRPLLEHALDAFLAHpAIDEVVVVV 50
|
|
| |
