|
Name |
Accession |
Description |
Interval |
E-value |
| GalU |
COG1210 |
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis]; |
1-290 |
0e+00 |
|
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440823 [Multi-domain] Cd Length: 288 Bit Score: 531.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 1 MKIRKAIIPAAGLGTRFLPATKAQPKEMLPIVDKPTIQYIVEEAVSSGIEDIIIVSGRGKHVIEDHFDKSYELEQTLFKK 80
Cdd:COG1210 1 MKIRKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVTGRGKRAIEDHFDRSYELEATLEAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 81 NKIKTLEDIECISNLANIHYIRQKEPKGLGHAIYCARRFIGEEPFAVLLGDDIVSSTYPCLKQLIDVYEEHHCSVVGVQR 160
Cdd:COG1210 81 GKEELLEEVRSISPLANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSEKPCLKQMIEVYEETGGSVIAVQE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 161 VLETEVSKYGIVKSanQNVNQSIIPISMLVEKPPLETAPSNLAIMGRYILKPDIFEVLKNLPVGSGGEIQLTDAINVLNK 240
Cdd:COG1210 161 VPPEEVSKYGIVDG--EEIEGGVYRVTGLVEKPAPEEAPSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDAIAALAK 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 446624876 241 QQKVLAFEFDGKRYDVGDKFGFIKATIDFALQRESLKEDVLSYLRNITRD 290
Cdd:COG1210 239 EEPVYAYEFEGKRYDCGDKLGYLKATVEFALKRPDLGEEFREYLKELLKE 288
|
|
| UGPase_prokaryotic |
cd02541 |
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ... |
4-272 |
1.01e-160 |
|
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: 447.75 E-value: 1.01e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 4 RKAIIPAAGLGTRFLPATKAQPKEMLPIVDKPTIQYIVEEAVSSGIEDIIIVSGRGKHVIEDHFDKSYELEQTLFKKNKI 83
Cdd:cd02541 1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRGKRAIEDHFDRSYELEETLEKKGKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 84 KTLEDIECISNLANIHYIRQKEPKGLGHAIYCARRFIGEEPFAVLLGDDIVSSTYPCLKQLIDVYEEHHCSVVGVQRVLE 163
Cdd:cd02541 81 DLLEEVRIISDLANIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLIDSKEPCLKQLIEAYEKTGASVIAVEEVPP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 164 TEVSKYGIVKSAnqNVNQSIIPISMLVEKPPLETAPSNLAIMGRYILKPDIFEVLKNLPVGSGGEIQLTDAINVLNKQQK 243
Cdd:cd02541 161 EDVSKYGIVKGE--KIDGDVFKVKGLVEKPKPEEAPSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTDAIAKLLEEEP 238
|
250 260
....*....|....*....|....*....
gi 446624876 244 VLAFEFDGKRYDVGDKFGFIKATIDFALQ 272
Cdd:cd02541 239 VYAYVFEGKRYDCGNKLGYLKATVEFALK 267
|
|
| galU |
TIGR01099 |
UTP--glucose-1-phosphate uridylyltransferase; Built to distinquish between the highly similar ... |
4-265 |
1.33e-145 |
|
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: 409.44 E-value: 1.33e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 4 RKAIIPAAGLGTRFLPATKAQPKEMLPIVDKPTIQYIVEEAVSSGIEDIIIVSGRGKHVIEDHFDKSYELEQTLFKKNKI 83
Cdd:TIGR01099 1 RKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYIVEEAVEAGIEEIVFVTGRGKRAIEDHFDYSYELEHQLEKRGKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 84 KTLEDIECISNLANIHYIRQKEPKGLGHAIYCARRFIGEEPFAVLLGDDIVSSTYPCLKQLIDVYEEHHCSVVGVQRVLE 163
Cdd:TIGR01099 81 ELLEEVRKISNLATIFYVRQKEQKGLGHAVLCARPFVGDEPFAVILGDDIVVNEEPALKQMIKAYEKTGCSIIAVQEVPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 164 TEVSKYGIVKSanQNVNQSIIPISMLVEKPPLETAPSNLAIMGRYILKPDIFEVLKNLPVGSGGEIQLTDAINVLNKQQK 243
Cdd:TIGR01099 161 EEVSKYGVIDG--EGIEKDLYKVKNMVEKPKPEEAPSNLAIVGRYILTPDIFDLLEETPPGKGGEIQLTDAINKLLENET 238
|
250 260
....*....|....*....|..
gi 446624876 244 VLAFEFDGKRYDVGDKFGFIKA 265
Cdd:TIGR01099 239 VLAYKFNGKRYDCGSKLGYLEA 260
|
|
| PRK13389 |
PRK13389 |
UTP--glucose-1-phosphate uridylyltransferase GalU; |
2-291 |
6.35e-82 |
|
UTP--glucose-1-phosphate uridylyltransferase GalU;
Pssm-ID: 184021 [Multi-domain] Cd Length: 302 Bit Score: 249.44 E-value: 6.35e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 2 KIRKAIIPAAGLGTRFLPATKAQPKEMLPIVDKPTIQYIVEEAVSSGIEDIIIVSGRGKHVIEDHFDKSYELEQTLFKKN 81
Cdd:PRK13389 7 KVKKAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFDTSFELEAMLEKRV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 82 KIKTLEDIECI-SNLANIHYIRQKEPKGLGHAIYCARRFIGEEPFAVLLGDDIVSSTYPCLKQ-----LIDVYEEHHCSV 155
Cdd:PRK13389 87 KRQLLDEVQSIcPPHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILDEYESDLSQdnlaeMIRRFDETGHSQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 156 VGVQRVleTEVSKYGIV--KSANQNVNQSiIPISMLVEKPPLETAPSNLAIMGRYILKPDIFEVLKNLPVGSGGEIQLTD 233
Cdd:PRK13389 167 IMVEPV--ADVTAYGVVdcKGVELAPGES-VPMVGVVEKPKADVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTD 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 446624876 234 AINVLNKQQKVLAFEFDGKRYDVGDKFGFIKATIDFALQRESLKEDVLSYLRNITRDK 291
Cdd:PRK13389 244 AIDMLIEKETVEAYHMKGKSHDCGNKLGYMQAFVEYGIRHNTLGTEFKAWLEEEMGIK 301
|
|
| PRK10122 |
PRK10122 |
UTP--glucose-1-phosphate uridylyltransferase GalF; |
5-278 |
4.79e-69 |
|
UTP--glucose-1-phosphate uridylyltransferase GalF;
Pssm-ID: 182252 [Multi-domain] Cd Length: 297 Bit Score: 216.29 E-value: 4.79e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 5 KAIIPAAGLGTRFLPATKAQPKEMLPIVDKPTIQYIVEEAVSSGIEDIIIVSGRGKHVIEDHFDKSYELEQTLFKKNKIK 84
Cdd:PRK10122 5 KAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAVENHFDTSYELESLLEQRVKRQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 85 TLEDIECISNLA-NIHYIRQKEPKGLGHAIYCARRFIGEEPFAVLLGDDIV--SSTYPC---LKQLIDVYEEHHCSVVGV 158
Cdd:PRK10122 85 LLAEVQSICPPGvTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPDVVIddASADPLrynLAAMIARFNETGRSQVLA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 159 QRvLETEVSKYGIVKSANQNVNQSIIP-ISMLVEKP--PlETAPSNLAIMGRYILKPDIFEVLKNLPVGSGGEIQLTDAI 235
Cdd:PRK10122 165 KR-MPGDLSEYSVIQTKEPLDREGKVSrIVEFIEKPdqP-QTLDSDLMAVGRYVLSADIWPELERTEPGAWGRIQLTDAI 242
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 446624876 236 NVLNKQQKVLAFEFDGKRYDVGDKFGFIKATIDFALQreSLKE 278
Cdd:PRK10122 243 AELAKKQSVDAMLMTGDSYDCGKKMGYMQAFVKYGLR--NLKE 283
|
|
| NTP_transferase |
cd04181 |
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ... |
6-257 |
7.54e-61 |
|
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: 192.41 E-value: 7.54e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 6 AIIPAAGLGTRFLPATKAQPKEMLPIVDKPTIQYIVEEAVSSGIEDIIIVSGRGKHVIEDHFDKSYELeqtlfkknkikt 85
Cdd:cd04181 1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGSKF------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 86 lediecisnLANIHYIRQKEPKGLGHAIYCARRFIGEEPFAVLLGDDIvssTYPCLKQLIDVYEEH-HCSVVGVQRVleT 164
Cdd:cd04181 69 ---------GVNIEYVVQEEPLGTAGAVRNAEDFLGDDDFLVVNGDVL---TDLDLSELLRFHREKgADATIAVKEV--E 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 165 EVSKYGIVKSANQNVnqsiipISMLVEKPPLEtaPSNLAIMGRYILKPDIFEVLKNLPvgSGGEIQLTDAINVLNKQQKV 244
Cdd:cd04181 135 DPSRYGVVELDDDGR------VTRFVEKPTLP--ESNLANAGIYIFEPEILDYIPEIL--PRGEDELTDAIPLLIEEGKV 204
|
250
....*....|...
gi 446624876 245 LAFEFDGKRYDVG 257
Cdd:cd04181 205 YGYPVDGYWLDIG 217
|
|
| G1P_TT_long |
cd04189 |
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ... |
5-265 |
6.47e-54 |
|
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: 175.45 E-value: 6.47e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 5 KAIIPAAGLGTRFLPATKAQPKEMLPIVDKPTIQYIVEEAVSSGIEDIIIVSGRGKHVIEDHFDKSYELEqtlfkknkik 84
Cdd:cd04189 2 KGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEALGDGSRFG---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 85 tlediecisnlANIHYIRQKEPKGLGHAIYCARRFIGEEPFAVLLGDDIVSSTypcLKQLIDVYEEHHCSV-VGVQRVle 163
Cdd:cd04189 72 -----------VRITYILQEEPLGLAHAVLAARDFLGDEPFVVYLGDNLIQEG---ISPLVRDFLEEDADAsILLAEV-- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 164 TEVSKYGIVK-SANQnvnqsiipISMLVEKPplETAPSNLAIMGRYILKPDIFEVLKNLPVGSGGEIQLTDAINVL-NKQ 241
Cdd:cd04189 136 EDPRRFGVAVvDDGR--------IVRLVEKP--KEPPSNLALVGVYAFTPAIFDAISRLKPSWRGELEITDAIQWLiDRG 205
|
250 260
....*....|....*....|....
gi 446624876 242 QKVLAFEFDGKRYDVGDKFGFIKA 265
Cdd:cd04189 206 RRVGYSIVTGWWKDTGTPEDLLEA 229
|
|
| RmlA1 |
COG1209 |
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis]; |
4-251 |
1.64e-50 |
|
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440822 [Multi-domain] Cd Length: 294 Bit Score: 168.34 E-value: 1.64e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 4 RKAIIPAAGLGTRFLPATKAQPKEMLPIVDKPTIQYIVEEAVSSGIEDIIIVSGrgkhviedhfdkSYELEQtlFKknki 83
Cdd:COG1209 1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIIST------------PEDGPQ--FE---- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 84 KTLEDiecISNL-ANIHYIRQKEPKGLGHAIYCARRFIGEEPFAVLLGDDIVSstYPCLKQLIDVYEEHHC-SVVGVQRV 161
Cdd:COG1209 63 RLLGD---GSQLgIKISYAVQPEPLGLAHAFIIAEDFIGGDPVALVLGDNIFY--GDGLSELLREAAARESgATIFGYKV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 162 leTEVSKYGIVK-SANQNVnqsiipISmLVEKPplETAPSNLAIMGRYILKPDIFEVLKNLPVGSGGEIQLTDAINV-LN 239
Cdd:COG1209 138 --EDPERYGVVEfDEDGRV------VS-LEEKP--KEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAyLE 206
|
250
....*....|..
gi 446624876 240 KQQKVLAFEFDG 251
Cdd:COG1209 207 RGKLVVELLGRG 218
|
|
| GCD1 |
COG1208 |
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ... |
5-257 |
9.48e-46 |
|
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: 154.16 E-value: 9.48e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 5 KAIIPAAGLGTRFLPATKAQPKEMLPIVDKPTIQYIVEEAVSSGIEDIIIVSGRGKHVIEDHFDKSYELEqtlfkknkik 84
Cdd:COG1208 1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRFG---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 85 tlediecisnlANIHYIRQKEPKGLGHAIYCARRFIGEEPFAVLLGDDIVSstyPCLKQLIDVYEEH--HCSVVGVQRvl 162
Cdd:COG1208 71 -----------VRITYVDEGEPLGTGGALKRALPLLGDEPFLVLNGDILTD---LDLAALLAFHREKgaDATLALVPV-- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 163 eTEVSKYGIVKSANQNVnqsiipISMLVEKPplETAPSNLAIMGRYILKPDIFEVLKnlpvgSGGEIQLTDAINVLNKQQ 242
Cdd:COG1208 135 -PDPSRYGVVELDGDGR------VTRFVEKP--EEPPSNLINAGIYVLEPEIFDYIP-----EGEPFDLEDLLPRLIAEG 200
|
250
....*....|....*
gi 446624876 243 KVLAFEFDGKRYDVG 257
Cdd:COG1208 201 RVYGYVHDGYWLDIG 215
|
|
| G1P_TT_short |
cd02538 |
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ... |
4-254 |
3.10e-28 |
|
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: 108.82 E-value: 3.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 4 RKAIIPAAGLGTRFLPATKAQPKEMLPIVDKPTIQYIVEEAVSSGIEDIIIVSGRGkhviedHFDKSYELeqtlfkknki 83
Cdd:cd02538 1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPE------DLPLFKEL---------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 84 ktLEDIeciSNLA-NIHYIRQKEPKGLGHAIYCARRFIGEEPFAVLLGDDIV--SSTYPCLKQlidVYEEHHCSVVGVQR 160
Cdd:cd02538 65 --LGDG---SDLGiRITYAVQPKPGGLAQAFIIGEEFIGDDPVCLILGDNIFygQGLSPILQR---AAAQKEGATVFGYE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 161 VLETEvsKYGIVKSANqnvNQSIIPIsmlVEKPplETAPSNLAIMGRYILKPDIFEVLKNLPVGSGGEIQLTDaINVLNK 240
Cdd:cd02538 137 VNDPE--RYGVVEFDE---NGRVLSI---EEKP--KKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITD-VNNEYL 205
|
250
....*....|....
gi 446624876 241 QQKVLAFEFDGKRY 254
Cdd:cd02538 206 EKGKLSVELLGRGF 219
|
|
| NTP_transferase |
pfam00483 |
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ... |
5-266 |
1.11e-27 |
|
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: 107.34 E-value: 1.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 5 KAIIPAAGLGTRFLPATKAQPKEMLPIVDK-PTIQYIVEEAVSSGIEDIIIVSG-RGKHVIEDHfdksyeleqtlfkknk 82
Cdd:pfam00483 1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTqEHRFMLNEL---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 83 iktLEDIECISNlaNIHYIRQKEPKGLGHAIYCARRFIGEEPFAVL-LGDDIVSStyPCLKQLIDVYEEHHCSV-VGVQR 160
Cdd:pfam00483 65 ---LGDGSKFGV--QITYALQPEGKGTAPAVALAADFLGDEKSDVLvLGGDHIYR--MDLEQAVKFHIEKAADAtVTFGI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 161 VLETEVSKYGIVKS-ANQNVNQsiipismLVEKPPLETApSNLAIMGRYILKPDIFE-VLKNLPVGSGGEIQLTDAINV- 237
Cdd:pfam00483 138 VPVEPPTGYGVVEFdDNGRVIR-------FVEKPKLPKA-SNYASMGIYIFNSGVLDfLAKYLEELKRGEDEITDILPKa 209
|
250 260 270
....*....|....*....|....*....|
gi 446624876 238 LNKQQKVLAFEFDGKR-YDVGDKFGFIKAT 266
Cdd:pfam00483 210 LEDGKLAYAFIFKGYAwLDVGTWDSLWEAN 239
|
|
| PRK15480 |
PRK15480 |
glucose-1-phosphate thymidylyltransferase RfbA; Provisional |
1-277 |
1.52e-22 |
|
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
Pssm-ID: 185377 [Multi-domain] Cd Length: 292 Bit Score: 94.74 E-value: 1.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 1 MKIRKAIIPAAGLGTRFLPATKAQPKEMLPIVDKPTIQYIVEEAVSSGIEDIIIVSGRgkhviedhfDKSYELEQTLFKK 80
Cdd:PRK15480 1 MKTRKGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTP---------QDTPRFQQLLGDG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 81 NKIKTlediecisnlaNIHYIRQKEPKGLGHAIYCARRFIGEEPFAVLLGDDIV-SSTYPCLKQLIdVYEEHHCSVVGVQ 159
Cdd:PRK15480 72 SQWGL-----------NLQYKVQPSPDGLAQAFIIGEEFIGGDDCALVLGDNIFyGHDLPKLMEAA-VNKESGATVFAYH 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 160 rvlETEVSKYGIVKSANQNVNQSIipismlvEKPPLETApSNLAIMGRYILKPDIFEVLKNLPVGSGGEIQLTDaINVLN 239
Cdd:PRK15480 140 ---VNDPERYGVVEFDQNGTAISL-------EEKPLQPK-SNYAVTGLYFYDNDVVEMAKNLKPSARGELEITD-INRIY 207
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 446624876 240 KQQKVLAFEFDGKRY---DVGDKFGFIKAT--IDFALQRESLK 277
Cdd:PRK15480 208 MEQGRLSVAMMGRGYawlDTGTHQSLIEASnfIATIEERQGLK 250
|
|
| NTP_transferase_WcbM_like |
cd06915 |
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ... |
6-257 |
1.70e-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: 1.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 6 AIIPAAGLGTRFLPATKAQPKEMLPIVDKPTIQYIVEEAVSSGIEDIIIVSGRGKHVIEDHFDKSYELeqtlfkknkikt 85
Cdd:cd06915 1 AVILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYLAEQIEEYFGDGYRG------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 86 lediecisnLANIHYIRQKEPKGLGHAIYCARRFIGEEPFAVLLGDdivsSTYPC-LKQLIDVYEEHHC-SVVGVQRVle 163
Cdd:cd06915 69 ---------GIRIYYVIEPEPLGTGGAIKNALPKLPEDQFLVLNGD----TYFDVdLLALLAALRASGAdATMALRRV-- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 164 TEVSKYGIVKSANQNVnqsiipISMLVEKPPleTAPSNLAIMGRYILKPDIFEVLKNLPVGSggeiqLTDAINVLNKQQK 243
Cdd:cd06915 134 PDASRYGNVTVDGDGR------VIAFVEKGP--GAAPGLINGGVYLLRKEILAEIPADAFSL-----EADVLPALVKRGR 200
|
250
....*....|....
gi 446624876 244 VLAFEFDGKRYDVG 257
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 ... |
6-257 |
3.32e-20 |
|
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: 86.80 E-value: 3.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 6 AIIPAAGLGTRFLPATKAQPKEMLPIVDKPTIQYIVEEAVSSGIEDIIIVSGRGKHVIEDHF-DKSyeleqtlfKKNkik 84
Cdd:cd06426 1 VVIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNYLAEMIEDYFgDGS--------KFG--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 85 tlediecisnlANIHYIRQKEPKGLGHAIYCARRFIgEEPFAVLLGDDIVSSTYpclKQLIDVYEEHHCSVVGVQRVLET 164
Cdd:cd06426 70 -----------VNISYVREDKPLGTAGALSLLPEKP-TDPFLVMNGDILTNLNY---EHLLDFHKENNADATVCVREYEV 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 165 EVSkYGIVKSANQNVNQsiipismLVEKPPLetapSNLAIMGRYILKPdifEVLKNLPVGSggEIQLTDAIN-VLNKQQK 243
Cdd:cd06426 135 QVP-YGVVETEGGRITS-------IEEKPTH----SFLVNAGIYVLEP---EVLDLIPKNE--FFDMPDLIEkLIKEGKK 197
|
250
....*....|....
gi 446624876 244 VLAFEFDGKRYDVG 257
Cdd:cd06426 198 VGVFPIHEYWLDIG 211
|
|
| M1P_guanylylT_B_like_N |
cd06425 |
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ... |
5-266 |
1.07e-17 |
|
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: 79.95 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 5 KAIIPAAGLGTRFLPATKAQPKEMLPIVDKPTIQYIVEEAVSSGIEDIIIVSGRGKHVIEDhFDKSYEleqtlfKKNKIK 84
Cdd:cd06425 2 KALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYRPEDMVP-FLKEYE------KKLGIK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 85 tlediecisnlanIHYIRQKEPKGLGHAIYCARRFIGE--EPFAVLLGDdiVSSTYPcLKQLIDVYEEHHCSVVgvqrVL 162
Cdd:cd06425 75 -------------ITFSIETEPLGTAGPLALARDLLGDddEPFFVLNSD--VICDFP-LAELLDFHKKHGAEGT----IL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 163 ETEV---SKYGIVKSANQNVNqsiipISMLVEKPplETAPSNLAIMGRYILKPDIFEVLKNLPVGSGGEIqltdaINVLN 239
Cdd:cd06425 135 VTKVedpSKYGVVVHDENTGR-----IERFVEKP--KVFVGNKINAGIYILNPSVLDRIPLRPTSIEKEI-----FPKMA 202
|
250 260
....*....|....*....|....*..
gi 446624876 240 KQQKVLAFEFDGKRYDVGDKFGFIKAT 266
Cdd:cd06425 203 SEGQLYAYELPGFWMDIGQPKDFLKGM 229
|
|
| GT2_GlmU_N_bac |
cd02540 |
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ... |
6-250 |
1.68e-15 |
|
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: 74.09 E-value: 1.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 6 AIIPAAGLGTRFlpatK-AQPKEMLPIVDKPTIQYIVEEAVSSGIEDIIIVSGRGKHVIEDHFDKSyeleqtlfkknkik 84
Cdd:cd02540 1 AVILAAGKGTRM----KsDLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVKKALANP-------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 85 tlediecisnlaNIHYIRQKEPKGLGHAIYCARRFIG--EEPFAVLLGDD--IVSSTypcLKQLIDVYEEHHCSVVgvqr 160
Cdd:cd02540 63 ------------NVEFVLQEEQLGTGHAVKQALPALKdfEGDVLVLYGDVplITPET---LQRLLEAHREAGADVT---- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 161 VLETEVSK---YG-IVKSANQNVnQSIIPismlvEKpplETAPSNLAI----MGRYILK-PDIFEVLKNL-PVGSGGEIQ 230
Cdd:cd02540 124 VLTAELEDptgYGrIIRDGNGKV-LRIVE-----EK---DATEEEKAIrevnAGIYAFDaEFLFEALPKLtNNNAQGEYY 194
|
250 260
....*....|....*....|.
gi 446624876 231 LTDAINVLNKQ-QKVLAFEFD 250
Cdd:cd02540 195 LTDIIALAVADgLKVAAVLAD 215
|
|
| PC_cytidylyltransferase |
cd02523 |
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ... |
6-221 |
2.65e-15 |
|
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: 73.42 E-value: 2.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 6 AIIPAAGLGTRFLPATKAQPKEMLPIVDKPTIQYIVEEAVSSGIEDIIIVSGRGKHVIEDHFDKSYELeqTLF------K 79
Cdd:cd02523 1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKKYPNI--KFVynpdyaE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 80 KNKIKTLediecisnlanihyirqkepkglghaiYCARRFIgEEPFAVLLGDDIVSSTypCLKQLIDVYEEhhcSVVGVQ 159
Cdd:cd02523 79 TNNIYSL---------------------------YLARDFL-DEDFLLLEGDVVFDPS--ILERLLSSPAD---NAILVD 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446624876 160 RVLETEVSKYGIVKSANQNVNQSIIpISMLVEKPPLETapsnlaiMGRYILKPDIFEVLKNL 221
Cdd:cd02523 126 KKTKEWEDEYVKDLDDAGVLLGIIS-KAKNLEEIQGEY-------VGISKFSPEDADRLAEA 179
|
|
| GlmU |
COG1207 |
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ... |
4-250 |
1.66e-14 |
|
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: 73.14 E-value: 1.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 4 RKAIIPAAGLGTRFLPATkaqPKEMLPIVDKPTIQYIVEEAVSSGIEDIIIVSGRGKHVIEDHFDKsyeleqtlfkknki 83
Cdd:COG1207 3 LAVVILAAGKGTRMKSKL---PKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVRAALAD-------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 84 ktlediecisnlANIHYIRQKEPKGLGHAIYCARRFIG--EEPFAVLLGDD--IVSSTypcLKQLIDVYEEHHCSVVgvq 159
Cdd:COG1207 66 ------------LDVEFVLQEEQLGTGHAVQQALPALPgdDGTVLVLYGDVplIRAET---LKALLAAHRAAGAAAT--- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 160 rVLETEV---SKYG-IVKSANQNVnQSIipismlVE-KpplETAPSNLAI----MGRYILK-PDIFEVLKNL-PVGSGGE 228
Cdd:COG1207 128 -VLTAELddpTGYGrIVRDEDGRV-LRI------VEeK---DATEEQRAIreinTGIYAFDaAALREALPKLsNDNAQGE 196
|
250 260
....*....|....*....|...
gi 446624876 229 IQLTDAINVLNKQ-QKVLAFEFD 250
Cdd:COG1207 197 YYLTDVIAIARADgLKVAAVQPE 219
|
|
| COG1213 |
COG1213 |
Choline kinase [Lipid transport and metabolism]; |
5-146 |
2.20e-14 |
|
Choline kinase [Lipid transport and metabolism];
Pssm-ID: 440826 [Multi-domain] Cd Length: 236 Bit Score: 71.04 E-value: 2.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 5 KAIIPAAGLGTRFLPATKAQPKEMLPIVDKPTIQYIVEEAVSSGIEDIIIVSGRGKHVIEDHFDKSYeleqtlfkknkik 84
Cdd:COG1213 1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEALARPG------------- 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446624876 85 tlEDIECISN----LANIhyirqkepkglGHAIYCARRFIGeEPFAVLLGDDIVSSTypCLKQLID 146
Cdd:COG1213 68 --PDVTFVYNpdydETNN-----------IYSLWLAREALD-EDFLLLNGDVVFDPA--ILKRLLA 117
|
|
| NTP_transferase_like_1 |
cd06422 |
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ... |
5-258 |
6.92e-13 |
|
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: 66.44 E-value: 6.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 5 KAIIPAAGLGTRFLPATKAQPKEMLPIVDKPTIQYIVEEAVSSGIEDIII-VSGRGKhVIEDHFdksyeleqtlfkKNKI 83
Cdd:cd06422 1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVnTHHLAD-QIEAHL------------GDSR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 84 KTLediecisnlaNIHYIRqkEPKGL---GHAIYCARRFIGEEPFAVLLGDDIvsstypCLKQLIDVYEEH----HCSVV 156
Cdd:cd06422 68 FGL----------RITISD--EPDELletGGGIKKALPLLGDEPFLVVNGDIL------WDGDLAPLLLLHawrmDALLL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 157 GVQRVLETEVSKYGIVksanqnvnqSIIPISMLVEKPPLETAPsnLAIMGRYILKPDIFEvlkNLPVGSGGeiqLTDAIN 236
Cdd:cd06422 130 LLPLVRNPGHNGVGDF---------SLDADGRLRRGGGGAVAP--FTFTGIQILSPELFA---GIPPGKFS---LNPLWD 192
|
250 260
....*....|....*....|..
gi 446624876 237 VLNKQQKVLAFEFDGKRYDVGD 258
Cdd:cd06422 193 RAIAAGRLFGLVYDGLWFDVGT 214
|
|
| M1P_guanylylT_A_like_N |
cd06428 |
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ... |
14-250 |
3.07e-12 |
|
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: 65.35 E-value: 3.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 14 GTRFLPATKAQPKEMLPIVDKPTIQYIVeEAVS--SGIEDIIIVSGrgkhviedhFDksyELEQTLFkknkiktLEDIEC 91
Cdd:cd06428 11 GTRFRPLSLDVPKPLFPVAGKPMIHHHI-EACAkvPDLKEVLLIGF---------YP---ESVFSDF-------ISDAQQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 92 ISNLaNIHYIRQKEPKGLGHAIYCARRFIGEEP---FAVLLGDdiVSSTYPcLKQLIDVYEEH--HCSVVGVqRVLETEV 166
Cdd:cd06428 71 EFNV-PIRYLQEYKPLGTAGGLYHFRDQILAGNpsaFFVLNAD--VCCDFP-LQELLEFHKKHgaSGTILGT-EASREQA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 167 SKYG-IVksANQNVNQsiipISMLVEKPplETAPSNLAIMGRYILKPDIFEVLKNLPVGSGGEIQLTDaINVLNKQQKVL 245
Cdd:cd06428 146 SNYGcIV--EDPSTGE----VLHYVEKP--ETFVSDLINCGVYLFSPEIFDTIKKAFQSRQQEAQLGD-DNNREGRAEVI 216
|
....*
gi 446624876 246 AFEFD 250
Cdd:cd06428 217 RLEQD 221
|
|
| glmU |
PRK14354 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
4-247 |
2.31e-11 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184643 [Multi-domain] Cd Length: 458 Bit Score: 63.70 E-value: 2.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 4 RKAIIPAAGLGTRFlpaTKAQPKEMLPIVDKPTIQYIVEEAVSSGIEDIIIVSGRGKHVIEdhfdksyeleqtlfkknki 83
Cdd:PRK14354 3 RYAIILAAGKGTRM---KSKLPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVGHGAEEVK------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 84 KTLEDiecisnlaNIHYIRQKEPKGLGHAIYCARRFIGEEP--FAVLLGDD--IVSSTypcLKQLIDVYEEHHCSVVgvq 159
Cdd:PRK14354 61 EVLGD--------RSEFALQEEQLGTGHAVMQAEEFLADKEgtTLVICGDTplITAET---LKNLIDFHEEHKAAAT--- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 160 rVLETEV---SKYG-IVKSANQNVnqsiipiSMLVEKPplETAPSNLAI----MGRYIL-KPDIFEVLKNL-PVGSGGEI 229
Cdd:PRK14354 127 -ILTAIAenpTGYGrIIRNENGEV-------EKIVEQK--DATEEEKQIkeinTGTYCFdNKALFEALKKIsNDNAQGEY 196
|
250
....*....|....*....
gi 446624876 230 QLTDAINVLNKQ-QKVLAF 247
Cdd:PRK14354 197 YLTDVIEILKNEgEKVGAY 215
|
|
| GT_2_like_f |
cd04182 |
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ... |
6-156 |
2.18e-10 |
|
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: 58.73 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 6 AIIPAAGLGTRFlpatkAQPKEMLPIVDKPTIQYIVEEAVSSGIEDIIIVSGrgkhviedhfdksyeleqtlFKKNKIKT 85
Cdd:cd04182 3 AIILAAGRSSRM-----GGNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLG--------------------AEADAVRA 57
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446624876 86 LEDIECISNLANIHYIRqkepkGLGHAIYCARRFIGEEP--FAVLLGD--DIVSSTYpclKQLIDVYEEHHCSVV 156
Cdd:cd04182 58 ALAGLPVVVVINPDWEE-----GMSSSLAAGLEALPADAdaVLILLADqpLVTAETL---RALIDAFREDGAGIV 124
|
|
| eIF-2B_gamma_N_like |
cd02507 |
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ... |
5-107 |
5.75e-10 |
|
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; N-terminal domain of eEIF-2B epsilon and gamma, subunits of eukaryotic translation initiators, is a subfamily of glycosyltranferase 2 and is predicted to have glycosyltranferase activity. eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit epsilon shares sequence similarity with gamma subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.
Pssm-ID: 133001 [Multi-domain] Cd Length: 216 Bit Score: 58.03 E-value: 5.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 5 KAIIPAAGLGTRFLPATKAQPKEMLPIVDKPTIQYIVEEAVSSGIEDIIIVSGRGKHVIEDHFDKSYELEQTLFKKNKIK 84
Cdd:cd02507 2 QAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQAIIEHLLKSKWSSLSSKMIVDVI 81
|
90 100
....*....|....*....|...
gi 446624876 85 TLEDIECISNLANIHYIRQKEPK 107
Cdd:cd02507 82 TSDLCESAGDALRLRDIRGLIRS 104
|
|
| MocA |
COG2068 |
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism]; |
6-156 |
2.61e-09 |
|
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
Pssm-ID: 441671 [Multi-domain] Cd Length: 195 Bit Score: 55.94 E-value: 2.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 6 AIIPAAGLGTRFlpatkAQPKEMLPIVDKPTIQYIVEEAVSSGIEDIIIVSGRGKHVIEDHFDKsyeleqtlfkknkikt 85
Cdd:COG2068 6 AIILAAGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADAEEVAAALAG---------------- 64
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446624876 86 lEDIECISNLaniHYIRqkepkGLGHAIYCARRFIGE--EPFAVLLGD--DIVSSTypcLKQLIDVYEEHHCSVV 156
Cdd:COG2068 65 -LGVRVVVNP---DWEE-----GMSSSLRAGLAALPAdaDAVLVLLGDqpLVTAET---LRRLLAAFRESPASIV 127
|
|
| glmU |
PRK14355 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
1-179 |
1.81e-08 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237685 [Multi-domain] Cd Length: 459 Bit Score: 55.13 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 1 MKIRKAIIPAAGLGTRFlpaTKAQPKEMLPIVDKPTIQYIVEEAVSSGIEDIIIVSGRGKHVIEDHFdksyeleqtlfkk 80
Cdd:PRK14355 1 MNNLAAIILAAGKGTRM---KSDLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHF------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 81 nkiktledieciSNLANIHYIRQKEPKGLGHAIYCARRFIGEEPFAVL-LGDDIVSSTYPCLKQLIDVYEEHHCSVVgvq 159
Cdd:PRK14355 65 ------------AGDGDVSFALQEEQLGTGHAVACAAPALDGFSGTVLiLCGDVPLLRAETLQGMLAAHRATGAAVT--- 129
|
170 180
....*....|....*....|....
gi 446624876 160 rVLETEVSK---YG-IVKSANQNV 179
Cdd:PRK14355 130 -VLTARLENpfgYGrIVRDADGRV 152
|
|
| LicC |
COG4750 |
CTP:phosphocholine cytidylyltransferase LicC [Cell wall/membrane/envelope biogenesis, Lipid ... |
4-57 |
3.14e-08 |
|
CTP:phosphocholine cytidylyltransferase LicC [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism];
Pssm-ID: 443784 [Multi-domain] Cd Length: 228 Bit Score: 53.30 E-value: 3.14e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 446624876 4 RKAIIPAAGLGTRFLPATKAQPKEMLPIVDKPTIQYIVEEAVSSGIEDIIIVSG 57
Cdd:COG4750 1 MNAIILAAGLGSRFAPITYETPKGLLKVNGEPLIERQIRQLHEAGITDITVVVG 54
|
|
| glmU |
PRK14357 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
5-240 |
3.41e-08 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237687 [Multi-domain] Cd Length: 448 Bit Score: 54.00 E-value: 3.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 5 KAIIPAAGLGTRFlpaTKAQPKEMLPIVDKPTIQYIVEEAVSSGIEdIIIVSGRGKHVIEDHFDKsyeleqtlfkknkik 84
Cdd:PRK14357 2 RALVLAAGKGTRM---KSKIPKVLHKISGKPMINWVIDTAKKVAQK-VGVVLGHEAELVKKLLPE--------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 85 tlediecisnlaNIHYIRQKEPKGLGHAIYCARRFIGEEPFAVLLGDDIVSSTYPCLKQLIDVYEEHHCSVVGVQRVLEt 164
Cdd:PRK14357 63 ------------WVKIFLQEEQLGTAHAVMCARDFIEPGDDLLILYGDVPLISENTLKRLIEEHNRKGADVTILVADLE- 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446624876 165 EVSKYG-IVKSANQnvnqsiIPISMLVEKPPLETAPSNLAiMGRYILKPD-IFEVLKNL-PVGSGGEIQLTDAINVLNK 240
Cdd:PRK14357 130 DPTGYGrIIRDGGK------YRIVEDKDAPEEEKKIKEIN-TGIYVFSGDfLLEVLPKIkNENAKGEYYLTDAVNFAEK 201
|
|
| eIF-2B_gamma_N |
cd04198 |
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ... |
5-107 |
4.98e-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: 52.28 E-value: 4.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 5 KAIIPAAGLGTRFLPATKAQPKEMLPIVDKPTIQYIVEEAVSSGIEDIIIV-SGRGKHVIEDHFDKSYEleqtlfkknKI 83
Cdd:cd04198 2 QAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVvPEEEQAEISTYLRSFPL---------NL 72
|
90 100 110
....*....|....*....|....*....|
gi 446624876 84 KTLEDIECISNLAN------IHYIRQKEPK 107
Cdd:cd04198 73 KQKLDEVTIVLDEDmgtadsLRHIRKKIKK 102
|
|
| eIF-2B_epsilon_N |
cd04197 |
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ... |
6-152 |
2.15e-07 |
|
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; N-terminal domain of epsilon subunit of the eukaryotic translation initiation factor 2B (eIF-2B): eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit epsilon shares sequence similarity with gamma subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.
Pssm-ID: 133040 [Multi-domain] Cd Length: 217 Bit Score: 50.68 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 6 AIIPAAGLGTRFLPATKAQPKEMLPIVDKPTIQYIVEEAVSSGIEDIIIVSGRGKHVIEDHFDKSyeleqtlfKKNKIKt 85
Cdd:cd04197 3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQIKEYIEKS--------KWSKPK- 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 86 ledieciSNLANIHYIRQKEPKGLGHA---IYCARRFIGeePFaVLLGDDIVSSTypclkQLIDVYEEHH 152
Cdd:cd04197 74 -------SSLMIVIIIMSEDCRSLGDAlrdLDAKGLIRG--DF-ILVSGDVVSNI-----DLKEILEEHK 128
|
|
| glgC |
PRK05293 |
glucose-1-phosphate adenylyltransferase; Provisional |
107-257 |
1.07e-06 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 179997 [Multi-domain] Cd Length: 380 Bit Score: 49.48 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 107 KGLGHAIYCARRFIGE-EPFAVLL--GDDIVSSTYpclKQLIDVYEEHHCSV-VGVQRVLETEVSKYGIVksaNQNVNQS 182
Cdd:PRK05293 99 KGTAHAIYQNIDYIDQyDPEYVLIlsGDHIYKMDY---DKMLDYHKEKEADVtIAVIEVPWEEASRFGIM---NTDENMR 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 183 IIPISmlvEKPplETAPSNLAIMGRYILKpdiFEVLKN-LPVGSGGEIQLTD----AI-NVLNKQQKVLAFEFDGKRYDV 256
Cdd:PRK05293 173 IVEFE---EKP--KNPKSNLASMGIYIFN---WKRLKEyLIEDEKNPNSSHDfgknVIpLYLEEGEKLYAYPFKGYWKDV 244
|
.
gi 446624876 257 G 257
Cdd:PRK05293 245 G 245
|
|
| NTP_transf_3 |
pfam12804 |
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ... |
6-156 |
4.18e-06 |
|
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine dinucleotide biosynthesis protein A). The family also includes a wide range of other NTP transferase domain.
Pssm-ID: 463715 [Multi-domain] Cd Length: 159 Bit Score: 46.03 E-value: 4.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 6 AIIPAAGLGTRFlpatkAQPKEMLPIVDKPTIQYIVEEAVSSGiEDIIIVSGRgkhviedhfdksyeleqtlfkknkikt 85
Cdd:pfam12804 1 AVILAGGRSSRM-----GGDKALLPLGGKPLLERVLERLRPAG-DEVVVVAND--------------------------- 47
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446624876 86 lEDIECISNLANIHYIRQKEP-KGLGHAIYCARRFIGE-EPFAVLLGD--DIVSSTypcLKQLIDVYEEHHCSVV 156
Cdd:pfam12804 48 -EEVLAALAGLGVPVVPDPDPgQGPLAGLLAALRAAPGaDAVLVLACDmpFLTPEL---LRRLLAAAEESGADIV 118
|
|
| glmU |
PRK14358 |
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ... |
7-181 |
6.26e-06 |
|
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase; Provisional
Pssm-ID: 237688 [Multi-domain] Cd Length: 481 Bit Score: 47.28 E-value: 6.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 7 IIPAAGLGTRFlpaTKAQPKEMLPIVDKPTIQYIVEEAVSSGIEDIIIVSGRGKhviedhfdksyeleqtlfkknkiktl 86
Cdd:PRK14358 11 VILAAGQGTRM---KSALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGA-------------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 87 EDIECISNLANIHYIRQKEPKGLGHAIYCARRFIGEE--PFAVLLGDDIVSSTyPCLKQLIDVYEEHHcsvvGVQRVLET 164
Cdd:PRK14358 62 EQVEAALQGSGVAFARQEQQLGTGDAFLSGASALTEGdaDILVLYGDTPLLRP-DTLRALVADHRAQG----SAMTILTG 136
|
170 180
....*....|....*....|.
gi 446624876 165 EV---SKYG-IVKSANQNVNQ 181
Cdd:PRK14358 137 ELpdaTGYGrIVRGADGAVER 157
|
|
| glmU |
PRK14353 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
6-131 |
6.41e-06 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184642 [Multi-domain] Cd Length: 446 Bit Score: 47.16 E-value: 6.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 6 AIIPAAGLGTRFLPATkaqPKEMLPIVDKPTIQYIVEEAVSSGIEDIIIVSGRGKHVIEDHFDKSYELEQTlfkknkikt 85
Cdd:PRK14353 8 AIILAAGEGTRMKSSL---PKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGPGAEAVAAAAAKIAPDAEI--------- 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 446624876 86 lediecisnlanihyIRQKEPKGLGHAIYCARRFI--GEEPFAVLLGD 131
Cdd:PRK14353 76 ---------------FVQKERLGTAHAVLAAREALagGYGDVLVLYGD 108
|
|
| CDP-ME_synthetase |
cd02516 |
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ... |
6-56 |
4.34e-05 |
|
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; 4-diphosphocytidyl-2-methyl-D-erythritol synthase (CDP-ME), also called 2C-methyl-d-erythritol 4-phosphate cytidylyltransferase catalyzes the third step in the alternative (non-mevalonate) pathway of Isopentenyl diphosphate (IPP) biosynthesis: the formation of 4-diphosphocytidyl-2C-methyl-D-erythritol from CTP and 2C-methyl-D-erythritol 4-phosphate. This mevalonate independent pathway that utilizes pyruvate and glyceraldehydes 3-phosphate as starting materials for production of IPP occurs in a variety of bacteria, archaea and plant cells, but is absent in mammals. Thus, CDP-ME synthetase is an attractive targets for the structure-based design of selective antibacterial, herbicidal and antimalarial drugs.
Pssm-ID: 133009 [Multi-domain] Cd Length: 218 Bit Score: 43.67 E-value: 4.34e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 446624876 6 AIIPAAGLGTRFLPATkaqPKEMLPIVDKPTIQYIVEEAVSSG-IEDIIIVS 56
Cdd:cd02516 3 AIILAAGSGSRMGADI---PKQFLELGGKPVLEHTLEAFLAHPaIDEIVVVV 51
|
|
| ispD |
TIGR00453 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ... |
6-55 |
5.03e-05 |
|
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: 43.43 E-value: 5.03e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 446624876 6 AIIPAAGLGTRFlpaTKAQPKEMLPIVDKPTIQYIVEEAVSS-GIEDIIIV 55
Cdd:TIGR00453 2 AVIPAAGRGTRF---GSGVPKQYLELGGRPLLEHALDAFLAHpAIDEVVVV 49
|
|
| ispD |
PRK00155 |
D-ribitol-5-phosphate cytidylyltransferase; |
6-55 |
3.79e-04 |
|
D-ribitol-5-phosphate cytidylyltransferase;
Pssm-ID: 234670 Cd Length: 227 Bit Score: 40.89 E-value: 3.79e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 446624876 6 AIIPAAGLGTRFlpatKA-QPKEMLPIVDKPTIQYIVEEAVSSG-IEDIIIV 55
Cdd:PRK00155 6 AIIPAAGKGSRM----GAdRPKQYLPLGGKPILEHTLEAFLAHPrIDEIIVV 53
|
|
| glmU |
PRK14360 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
8-250 |
4.00e-04 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184646 [Multi-domain] Cd Length: 450 Bit Score: 41.45 E-value: 4.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 8 IPAAGLGTRFlpaTKAQPKEMLPIVDKPTIQYIVEEAVSSGIEDIIIVSGRgkhviedhfdKSYELEQTLFKknkiktle 87
Cdd:PRK14360 6 ILAAGKGTRM---KSSLPKVLHPLGGKSLVERVLDSCEELKPDRRLVIVGH----------QAEEVEQSLAH-------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 88 diecisnLANIHYIRQKEPKGLGHAIY----CARRFIGEepFAVLLGDD--IVSSTypcLKQLIDVYEEHHCSVVgvqrV 161
Cdd:PRK14360 65 -------LPGLEFVEQQPQLGTGHAVQqllpVLKGFEGD--LLVLNGDVplLRPET---LEALLNTHRSSNADVT----L 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 162 LETEVSK---YGIVKSANQNVNQSIIPismlvEKPPLETAPSNLAI-MGRYILK-PDIFEVLKNL-PVGSGGEIQLTDAI 235
Cdd:PRK14360 129 LTARLPNpkgYGRVFCDGNNLVEQIVE-----DRDCTPAQRQNNRInAGIYCFNwPALAEVLPKLsSNNDQKEYYLTDTV 203
|
250
....*....|....*
gi 446624876 236 NVLNkqqKVLAFEFD 250
Cdd:PRK14360 204 SLLD---PVMAVEVE 215
|
|
| GT2_BcE_like |
cd04183 |
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ... |
7-73 |
7.17e-04 |
|
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; GT2_BcbE_like: The bcbE gene is one of the genes in the capsule biosynthetic locus of Pasteurella multocida. Its deducted product is likely involved in the biosynthesis of the polysaccharide capsule, which is found on surface of a wide range of bacteria. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.
Pssm-ID: 133026 [Multi-domain] Cd Length: 231 Bit Score: 40.31 E-value: 7.17e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446624876 7 IIPAAGLGTRFLPATKAQPKEMLPIVDKPTIQYIVEEAVSSGIEDIIIVSgRGKHVIEDHFDKSYEL 73
Cdd:cd04183 2 IIPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEWVIESLAKIFDSRFIFIC-RDEHNTKFHLDESLKL 67
|
|
| GDP-M1P_Guanylyltransferase |
cd02509 |
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ... |
5-198 |
8.36e-04 |
|
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: 40.25 E-value: 8.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 5 KAIIPAAGLGTRFLPA-TKAQPKEMLPIV-DKPTIQYIVEEAVS-SGIEDIIIVSGrgkhviEDHFDKSyeLEQtlfkkn 81
Cdd:cd02509 2 YPVILAGGSGTRLWPLsRESYPKQFLKLFgDKSLLQQTLDRLKGlVPPDRILVVTN------EEYRFLV--REQ------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446624876 82 kiktLEDIecisnLANIHYIRQKEPKGLGHAIYCARRFI----GEEPFAVLLGDDIVSST---YPCLKQLIDVYEEHHCS 154
Cdd:cd02509 68 ----LPEG-----LPEENIILEPEGRNTAPAIALAALYLakrdPDAVLLVLPSDHLIEDVeafLKAVKKAVEAAEEGYLV 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446624876 155 VVGVQ--RVlETEvskYGIVKsANQNVNQSIIPISMLVEKPPLETA 198
Cdd:cd02509 139 TFGIKptRP-ETG---YGYIE-AGEKLGGGVYRVKRFVEKPDLETA 179
|
|
| IspD |
COG1211 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ... |
7-55 |
1.15e-03 |
|
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440824 Cd Length: 224 Bit Score: 39.34 E-value: 1.15e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 446624876 7 IIPAAGLGTRFlpaTKAQPKEMLPIVDKPTIQYIVEEAVSSG-IEDIIIV 55
Cdd:COG1211 1 IIPAAGSGSRM---GAGIPKQFLPLGGKPVLEHTLEAFLAHPrIDEIVVV 47
|
|
| |
