|
Name |
Accession |
Description |
Interval |
E-value |
| GalU |
COG1210 |
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis]; |
12-302 |
5.33e-176 |
|
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440823 [Multi-domain] Cd Length: 288 Bit Score: 487.62 E-value: 5.33e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 12 RKAVIPAAGLGTRFLPATKAMPKEMLPVVDRPAIEYVVTEARRAGLADVLMITGRNKRALEDHFDRHPALEAALEHKGDA 91
Cdd:COG1210 4 RKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVTGRGKRAIEDHFDRSYELEATLEAKGKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 92 KRLAQIHESDLVGDIHYVRQGEALGLGHAVNCARRHVGEEPFAVLLGDDIIGDGEALLERMIDVQQRLGGSVIALMEVPE 171
Cdd:COG1210 84 ELLEEVRSISPLANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSEKPCLKQMIEVYEETGGSVIAVQEVPP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 172 EAVSAYGVAAVQAVPGegdDVVRVTDLVEKPAREDAPSTLAIIGRYVLAPQVFDVLDETPPGRGGEIQLTDALQRLATEd 251
Cdd:COG1210 164 EEVSKYGIVDGEEIEG---GVYRVTGLVEKPAPEEAPSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDAIAALAKE- 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 896140700 252 gegRGVHAVVFDGRRYDTGDKLGYLQAVIEFGTRHEDLGADLRAWLREFTA 302
Cdd:COG1210 240 ---EPVYAYEFEGKRYDCGDKLGYLKATVEFALKRPDLGEEFREYLKELLK 287
|
|
| UGPase_prokaryotic |
cd02541 |
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ... |
12-283 |
1.95e-149 |
|
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: 419.63 E-value: 1.95e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 12 RKAVIPAAGLGTRFLPATKAMPKEMLPVVDRPAIEYVVTEARRAGLADVLMITGRNKRALEDHFDRHPALEAALEHKGDA 91
Cdd:cd02541 1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRGKRAIEDHFDRSYELEETLEKKGKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 92 KRLAQIHESDLVGDIHYVRQGEALGLGHAVNCARRHVGEEPFAVLLGDDIIGDGEALLERMIDVQQRLGGSVIALMEVPE 171
Cdd:cd02541 81 DLLEEVRIISDLANIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLIDSKEPCLKQLIEAYEKTGASVIAVEEVPP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 172 EAVSAYGVAAVQAVPgegDDVVRVTDLVEKPAREDAPSTLAIIGRYVLAPQVFDVLDETPPGRGGEIQLTDALQRLATEd 251
Cdd:cd02541 161 EDVSKYGIVKGEKID---GDVFKVKGLVEKPKPEEAPSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTDAIAKLLEE- 236
|
250 260 270
....*....|....*....|....*....|..
gi 896140700 252 gegRGVHAVVFDGRRYDTGDKLGYLQAVIEFG 283
Cdd:cd02541 237 ---EPVYAYVFEGKRYDCGNKLGYLKATVEFA 265
|
|
| galU |
TIGR01099 |
UTP--glucose-1-phosphate uridylyltransferase; Built to distinquish between the highly similar ... |
12-278 |
4.83e-124 |
|
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: 355.12 E-value: 4.83e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 12 RKAVIPAAGLGTRFLPATKAMPKEMLPVVDRPAIEYVVTEARRAGLADVLMITGRNKRALEDHFDRHPALEAALEHKGDA 91
Cdd:TIGR01099 1 RKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYIVEEAVEAGIEEIVFVTGRGKRAIEDHFDYSYELEHQLEKRGKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 92 KRLAQIHESDLVGDIHYVRQGEALGLGHAVNCARRHVGEEPFAVLLGDDIIGDGEALLERMIDVQQRLGGSVIALMEVPE 171
Cdd:TIGR01099 81 ELLEEVRKISNLATIFYVRQKEQKGLGHAVLCARPFVGDEPFAVILGDDIVVNEEPALKQMIKAYEKTGCSIIAVQEVPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 172 EAVSAYGVAAVQAVPgegDDVVRVTDLVEKPAREDAPSTLAIIGRYVLAPQVFDVLDETPPGRGGEIQLTDALQRLATED 251
Cdd:TIGR01099 161 EEVSKYGVIDGEGIE---KDLYKVKNMVEKPKPEEAPSNLAIVGRYILTPDIFDLLEETPPGKGGEIQLTDAINKLLENE 237
|
250 260
....*....|....*....|....*..
gi 896140700 252 gegrGVHAVVFDGRRYDTGDKLGYLQA 278
Cdd:TIGR01099 238 ----TVLAYKFNGKRYDCGSKLGYLEA 260
|
|
| PRK13389 |
PRK13389 |
UTP--glucose-1-phosphate uridylyltransferase GalU; |
10-299 |
1.16e-81 |
|
UTP--glucose-1-phosphate uridylyltransferase GalU;
Pssm-ID: 184021 [Multi-domain] Cd Length: 302 Bit Score: 249.05 E-value: 1.16e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 10 RTRKAVIPAAGLGTRFLPATKAMPKEMLPVVDRPAIEYVVTEARRAGLADVLMITGRNKRALEDHFDRHPALEAALEHKG 89
Cdd:PRK13389 7 KVKKAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFDTSFELEAMLEKRV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 90 DAKRLAQIHESDLVG-DIHYVRQGEALGLGHAVNCARRHVGEEPFAVLLGDDIIGDGEALLER-----MIDVQQRLGGSV 163
Cdd:PRK13389 87 KRQLLDEVQSICPPHvTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILDEYESDLSQdnlaeMIRRFDETGHSQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 164 IalMEVPEEAVSAYGVAAVQAVPGEGDDVVRVTDLVEKPAREDAPSTLAIIGRYVLAPQVFDVLDETPPGRGGEIQLTDA 243
Cdd:PRK13389 167 I--MVEPVADVTAYGVVDCKGVELAPGESVPMVGVVEKPKADVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTDA 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 896140700 244 LQRLAtedgEGRGVHAVVFDGRRYDTGDKLGYLQAVIEFGTRHEDLGADLRAWLRE 299
Cdd:PRK13389 245 IDMLI----EKETVEAYHMKGKSHDCGNKLGYMQAFVEYGIRHNTLGTEFKAWLEE 296
|
|
| PRK10122 |
PRK10122 |
UTP--glucose-1-phosphate uridylyltransferase GalF; |
13-294 |
7.05e-65 |
|
UTP--glucose-1-phosphate uridylyltransferase GalF;
Pssm-ID: 182252 [Multi-domain] Cd Length: 297 Bit Score: 205.89 E-value: 7.05e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 13 KAVIPAAGLGTRFLPATKAMPKEMLPVVDRPAIEYVVTEARRAGLADVLMITGRNKRALEDHFDRHPALEAALEHKGDAK 92
Cdd:PRK10122 5 KAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAVENHFDTSYELESLLEQRVKRQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 93 RLAQIHESDLVG-DIHYVRQGEALGLGHAVNCARRHVGEEPFAVLLGDDIIGDGEA-----LLERMIDVQQRLGGSVIAL 166
Cdd:PRK10122 85 LLAEVQSICPPGvTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPDVVIDDASAdplryNLAAMIARFNETGRSQVLA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 167 MEVPEEaVSAYGVAAVQAVPGEGDDVVRVTDLVEKPAREDA-PSTLAIIGRYVLAPQVFDVLDETPPGRGGEIQLTDALQ 245
Cdd:PRK10122 165 KRMPGD-LSEYSVIQTKEPLDREGKVSRIVEFIEKPDQPQTlDSDLMAVGRYVLSADIWPELERTEPGAWGRIQLTDAIA 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 896140700 246 RLAtedgEGRGVHAVVFDGRRYDTGDKLGYLQAVIEFGTRHEDLGADLR 294
Cdd:PRK10122 244 ELA----KKQSVDAMLMTGDSYDCGKKMGYMQAFVKYGLRNLKEGAKFR 288
|
|
| NTP_transferase |
cd04181 |
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ... |
14-270 |
3.42e-54 |
|
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: 175.85 E-value: 3.42e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 14 AVIPAAGLGTRFLPATKAMPKEMLPVVDRPAIEYVVTEARRAGLADVLMITGRNKRALEDHFDRHpaleaalehkgdakr 93
Cdd:cd04181 1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDG--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 94 laqiheSDLVGDIHYVRQGEALGLGHAVNCARRHVGEEPFAVLLGDDIIGDGealLERMIDVQQRLGG-SVIALMEVPEe 172
Cdd:cd04181 66 ------SKFGVNIEYVVQEEPLGTAGAVRNAEDFLGDDDFLVVNGDVLTDLD---LSELLRFHREKGAdATIAVKEVED- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 173 aVSAYGVAavqavpgEGDDVVRVTDLVEKParEDAPSTLAIIGRYVLAPQVFDVLDETPPgrGGEIQLTDALQRLAtedg 252
Cdd:cd04181 136 -PSRYGVV-------ELDDDGRVTRFVEKP--TLPESNLANAGIYIFEPEILDYIPEILP--RGEDELTDAIPLLI---- 199
|
250
....*....|....*...
gi 896140700 253 EGRGVHAVVFDGRRYDTG 270
Cdd:cd04181 200 EEGKVYGYPVDGYWLDIG 217
|
|
| G1P_TT_long |
cd04189 |
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ... |
13-279 |
1.11e-50 |
|
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: 167.36 E-value: 1.11e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 13 KAVIPAAGLGTRFLPATKAMPKEMLPVVDRPAIEYVVTEARRAGLADVLMITGRNKRALEDHFdrhpaleaalehkGDAK 92
Cdd:cd04189 2 KGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEAL-------------GDGS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 93 RLAQihesdlvgDIHYVRQGEALGLGHAVNCARRHVGEEPFAVLLGDDIIGDGEALLERmiDVQQRLGGSVIALMEVPEe 172
Cdd:cd04189 69 RFGV--------RITYILQEEPLGLAHAVLAARDFLGDEPFVVYLGDNLIQEGISPLVR--DFLEEDADASILLAEVED- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 173 aVSAYGVAAVqavpgEGDdvvRVTDLVEKPAREdaPSTLAIIGRYVLAPQVFDVLDETPPGRGGEIQLTDALQRLATedg 252
Cdd:cd04189 138 -PRRFGVAVV-----DDG---RIVRLVEKPKEP--PSNLALVGVYAFTPAIFDAISRLKPSWRGELEITDAIQWLID--- 203
|
250 260
....*....|....*....|....*..
gi 896140700 253 EGRGVHAVVFDGRRYDTGDKLGYLQAV 279
Cdd:cd04189 204 RGRRVGYSIVTGWWKDTGTPEDLLEAN 230
|
|
| RmlA1 |
COG1209 |
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis]; |
12-278 |
9.12e-47 |
|
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440822 [Multi-domain] Cd Length: 294 Bit Score: 159.10 E-value: 9.12e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 12 RKAVIPAAGLGTRFLPATKAMPKEMLPVVDRPAIEYVVTEARRAGLADVLMITGRNKRaledhfdrhPALEAALehkGDA 91
Cdd:COG1209 1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDG---------PQFERLL---GDG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 92 krlaqiheSDLVGDIHYVRQGEALGLGHAVNCARRHVGEEPFAVLLGDDII-GDG-EALLERmidVQQRLGGSVIALMEV 169
Cdd:COG1209 69 --------SQLGIKISYAVQPEPLGLAHAFIIAEDFIGGDPVALVLGDNIFyGDGlSELLRE---AAARESGATIFGYKV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 170 --PEeavsAYGVAAVqavpgegDDVVRVTDLVEKParEDAPSTLAIIGRYVLAPQVFDVLDETPPGRGGEIQLTDALQRL 247
Cdd:COG1209 138 edPE----RYGVVEF-------DEDGRVVSLEEKP--KEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAY 204
|
250 260 270
....*....|....*....|....*....|..
gi 896140700 248 ATedgEGRGVHAVVFDGRR-YDTGDKLGYLQA 278
Cdd:COG1209 205 LE---RGKLVVELLGRGFAwLDTGTHESLLEA 233
|
|
| GCD1 |
COG1208 |
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ... |
13-278 |
1.31e-41 |
|
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: 143.75 E-value: 1.31e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 13 KAVIPAAGLGTRFLPATKAMPKEMLPVVDRPAIEYVVTEARRAGLADVLMITGRNKRALEDHFdrhpaleaalehkGDAk 92
Cdd:COG1208 1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYF-------------GDG- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 93 rlaqiheSDLVGDIHYVRQGEALGLGHAVNCARRHVGEEPFAVLLGDDIIG-DgealLERMIDVQQRlGGSVIALMEVPE 171
Cdd:COG1208 67 -------SRFGVRITYVDEGEPLGTGGALKRALPLLGDEPFLVLNGDILTDlD----LAALLAFHRE-KGADATLALVPV 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 172 EAVSAYGVAAVqavpgegDDVVRVTDLVEKParEDAPSTLAIIGRYVLAPQVFDVLDEtppgrGGEIQLTDALQRLAtED 251
Cdd:COG1208 135 PDPSRYGVVEL-------DGDGRVTRFVEKP--EEPPSNLINAGIYVLEPEIFDYIPE-----GEPFDLEDLLPRLI-AE 199
|
250 260
....*....|....*....|....*..
gi 896140700 252 GEgrgVHAVVFDGRRYDTGDKLGYLQA 278
Cdd:COG1208 200 GR---VYGYVHDGYWLDIGTPEDLLEA 223
|
|
| NTP_transferase |
pfam00483 |
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ... |
13-278 |
1.50e-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: 1.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 13 KAVIPAAGLGTRFLPATKAMPKEMLPVVDR-PAIEYVVTEARRAGLADVLMITGrnkraledhfDRHPALeaALEHKGDA 91
Cdd:pfam00483 1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILT----------QEHRFM--LNELLGDG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 92 KRLAqihesdlvGDIHYVRQGEALGLGHAVNCARRHVGEEPFAVL-LGDD-IIGDG-EALLERMIDVQQRLGGSVIAlme 168
Cdd:pfam00483 69 SKFG--------VQITYALQPEGKGTAPAVALAADFLGDEKSDVLvLGGDhIYRMDlEQAVKFHIEKAADATVTFGI--- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 169 VPEEAVSAYGVAavqavpgEGDDVVRVTDLVEKPAREDApSTLAIIGRYVLAPQVFDVL--DETPPGRgGEIQLTDALQR 246
Cdd:pfam00483 138 VPVEPPTGYGVV-------EFDDNGRVIRFVEKPKLPKA-SNYASMGIYIFNSGVLDFLakYLEELKR-GEDEITDILPK 208
|
250 260 270
....*....|....*....|....*....|...
gi 896140700 247 lATEDGEGRGvhAVVFDGRR-YDTGDKLGYLQA 278
Cdd:pfam00483 209 -ALEDGKLAY--AFIFKGYAwLDVGTWDSLWEA 238
|
|
| G1P_TT_short |
cd02538 |
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ... |
12-242 |
6.83e-27 |
|
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is the short form of glucose-1-phosphate thymidylyltransferase. Glucose-1-phosphate thymidylyltransferase catalyses the formation of dTDP-glucose, from dTTP and glucose 1-phosphate. It is the first enzyme in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme.There are two forms of Glucose-1-phosphate thymidylyltransferase in bacteria and archeae; short form and long form. The homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose. The long form, which has an extra 50 amino acids c-terminal, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced.
Pssm-ID: 133019 [Multi-domain] Cd Length: 240 Bit Score: 105.35 E-value: 6.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 12 RKAVIPAAGLGTRFLPATKAMPKEMLPVVDRPAIEYVVTEARRAGLADVLMITGRnkraledhfdrhpaleaalEHKGDA 91
Cdd:cd02538 1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTP-------------------EDLPLF 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 92 KRLAQiHESDLVGDIHYVRQGEALGLGHAVNCARRHVGEEPFAVLLGDDII-GDG-EALLERmidVQQRLGGSVIALMEV 169
Cdd:cd02538 62 KELLG-DGSDLGIRITYAVQPKPGGLAQAFIIGEEFIGDDPVCLILGDNIFyGQGlSPILQR---AAAQKEGATVFGYEV 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896140700 170 --PEeavsAYGVAavqavpgEGDDVVRVTDLVEKParEDAPSTLAIIGRYVLAPQVFDVLDETPPGRGGEIQLTD 242
Cdd:cd02538 138 ndPE----RYGVV-------EFDENGRVLSIEEKP--KKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITD 199
|
|
| NTP_transferase_like_1 |
cd06422 |
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ... |
13-278 |
5.16e-16 |
|
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: 75.30 E-value: 5.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 13 KAVIPAAGLGTRFLPATKAMPKEMLPVVDRPAIEYVVTEARRAGLADVLMitgrNKRALEDhfdrhpALEAALEHKGDAK 92
Cdd:cd06422 1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVV----NTHHLAD------QIEAHLGDSRFGL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 93 RLAQIHESDlvgdihyvrqgEALGLGHAVNCARRHVGEEPFAVLLGDDI-IGDGEALLERMIDVQQRLGGsVIALMEVPE 171
Cdd:cd06422 71 RITISDEPD-----------ELLETGGGIKKALPLLGDEPFLVVNGDILwDGDLAPLLLLHAWRMDALLL-LLPLVRNPG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 172 EavsaygvaavqavPGEGDDVVRVTDLVeKPAREDAPSTLAIIGRYVLAPQVFDVLDEtppgrgGEIQLTDALQRLATed 251
Cdd:cd06422 139 H-------------NGVGDFSLDADGRL-RRGGGGAVAPFTFTGIQILSPELFAGIPP------GKFSLNPLWDRAIA-- 196
|
250 260
....*....|....*....|....*..
gi 896140700 252 gEGRgVHAVVFDGRRYDTGDKLGYLQA 278
Cdd:cd06422 197 -AGR-LFGLVYDGLWFDVGTPERLLAA 221
|
|
| NTP_transferase_WcbM_like |
cd06915 |
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ... |
14-232 |
2.85e-15 |
|
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: 73.36 E-value: 2.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 14 AVIPAAGLGTRFLPATKAMPKEMLPVVDRPAIEYVVTEARRAGLADVLMITGRNKRALEDHFDRHPALEAalehkgdakr 93
Cdd:cd06915 1 AVILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYLAEQIEEYFGDGYRGGI---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 94 laqihesdlvgDIHYVRQGEALGLGHAVNCARRHVGEEPFAVLLGDDIIgdgEALLERMIDVQQRLGG-SVIALMEVPEe 172
Cdd:cd06915 71 -----------RIYYVIEPEPLGTGGAIKNALPKLPEDQFLVLNGDTYF---DVDLLALLAALRASGAdATMALRRVPD- 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 173 aVSAYGVAAVqavpgegDDVVRVTDLVEKpaREDAPSTLAIIGRYVLAPQVFDVLDETPP 232
Cdd:cd06915 136 -ASRYGNVTV-------DGDGRVIAFVEK--GPGAAPGLINGGVYLLRKEILAEIPADAF 185
|
|
| NTP_transferase_like_2 |
cd06426 |
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ... |
14-247 |
9.16e-15 |
|
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: 71.77 E-value: 9.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 14 AVIPAAGLGTRFLPATKAMPKEMLPVVDRPAIEYVVTEARRAGLADVLMITGRNKRALEDHFdrhpaleaalehkGDAKR 93
Cdd:cd06426 1 VVIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNYLAEMIEDYF-------------GDGSK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 94 LaqihesdlvG-DIHYVRQGEALGLGHAVNCARRHVgEEPFAVLLGDDIIG-DGEALLERMIDvqqrlGGSVIAL----- 166
Cdd:cd06426 68 F---------GvNISYVREDKPLGTAGALSLLPEKP-TDPFLVMNGDILTNlNYEHLLDFHKE-----NNADATVcvrey 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 167 -MEVPeeavsaYGVaavqaVPGEGDdvvRVTDLVEKPARedapSTLAIIGRYVLAPqvfDVLDETPPGRggEIQLTDALQ 245
Cdd:cd06426 133 eVQVP------YGV-----VETEGG---RITSIEEKPTH----SFLVNAGIYVLEP---EVLDLIPKNE--FFDMPDLIE 189
|
..
gi 896140700 246 RL 247
Cdd:cd06426 190 KL 191
|
|
| PRK15480 |
PRK15480 |
glucose-1-phosphate thymidylyltransferase RfbA; Provisional |
10-278 |
3.51e-14 |
|
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
Pssm-ID: 185377 [Multi-domain] Cd Length: 292 Bit Score: 71.24 E-value: 3.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 10 RTRKAVIPAAGLGTRFLPATKAMPKEMLPVVDRPAIEYVVTEARRAGLADVLMITGRNkraledhfdrhpaleaalehkg 89
Cdd:PRK15480 2 KTRKGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQ---------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 90 DAKRLAQihesdLVGD-------IHYVRQGEALGLGHAVNCARRHVGEEPFAVLLGDDII--GDGEALLERMIDVQQrlG 160
Cdd:PRK15480 60 DTPRFQQ-----LLGDgsqwglnLQYKVQPSPDGLAQAFIIGEEFIGGDDCALVLGDNIFygHDLPKLMEAAVNKES--G 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 161 GSVIAL-MEVPEEavsaYGVAavqavpgEGDDVVRVTDLVEKPAreDAPSTLAIIGRYVLAPQVFDVLDETPPGRGGEIQ 239
Cdd:PRK15480 133 ATVFAYhVNDPER----YGVV-------EFDQNGTAISLEEKPL--QPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELE 199
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 896140700 240 LTDaLQRLATEDGEgrgvHAVVFDGRRY---DTGDKLGYLQA 278
Cdd:PRK15480 200 ITD-INRIYMEQGR----LSVAMMGRGYawlDTGTHQSLIEA 236
|
|
| PC_cytidylyltransferase |
cd02523 |
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ... |
14-252 |
1.40e-12 |
|
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: 65.72 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 14 AVIPAAGLGTRFLPATKAMPKEMLPVVDRPAIEYVVTEARRAGLADVLMITGRNKRALEDHFDRHPALEaalehkgdakr 93
Cdd:cd02523 1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKKYPNIK----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 94 laqIHESDlvgdiHYVRQGEAlglgHAVNCARRHVgEEPFAVLLGDDIIgdGEALLERMIDvqqrlggsvialmevpeea 173
Cdd:cd02523 70 ---FVYNP-----DYAETNNI----YSLYLARDFL-DEDFLLLEGDVVF--DPSILERLLS------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 174 VSAYGVAAVQAVPGEGDDVVRVTD---LVEKPAREDAPSTLAIIGRYV--------LAPQVFDVLDETPPGRGGEIQLTD 242
Cdd:cd02523 116 SPADNAILVDKKTKEWEDEYVKDLddaGVLLGIISKAKNLEEIQGEYVgiskfspeDADRLAEALEELIEAGRVNLYYED 195
|
250
....*....|
gi 896140700 243 ALQRLATEDG 252
Cdd:cd02523 196 ALQRLISEEG 205
|
|
| COG1213 |
COG1213 |
Choline kinase [Lipid transport and metabolism]; |
13-267 |
1.68e-11 |
|
Choline kinase [Lipid transport and metabolism];
Pssm-ID: 440826 [Multi-domain] Cd Length: 236 Bit Score: 62.95 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 13 KAVIPAAGLGTRFLPATKAMPKEMLPVVDRPAIEYVVTEARRAGLADVLMITGRNKRALEDHFDRHPaleaalehkgdak 92
Cdd:COG1213 1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEALARPG------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 93 rlaqihesdlvGDIHYV--RQGEALGLGHAVNCARRHVGeEPFAVLLGdDIIGDgEALLERMIDVQQRLggsVIAL---- 166
Cdd:COG1213 68 -----------PDVTFVynPDYDETNNIYSLWLAREALD-EDFLLLNG-DVVFD-PAILKRLLASDGDI---VLLVdrkw 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 167 MEVPEEAVSaygvaaVQAVPGEgddvvRVTDLVEKPAREDapstlaIIGRYV--------LAPQVFDVLDETPPGRGGEI 238
Cdd:COG1213 131 EKPLDEEVK------VRVDEDG-----RIVEIGKKLPPEE------ADGEYIgifkfsaeGAAALREALEALIDEGGPNL 193
|
250 260
....*....|....*....|....*....
gi 896140700 239 QLTDALQRLATEDGEgrgVHAVVFDGRRY 267
Cdd:COG1213 194 YYEDALQELIDEGGP---VKAVDIGGLPW 219
|
|
| GlmU |
COG1207 |
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ... |
10-139 |
4.78e-10 |
|
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440820 [Multi-domain] Cd Length: 457 Bit Score: 60.04 E-value: 4.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 10 RTRKAVIPAAGLGTRFlpatK-AMPKEMLPVVDRPAIEYVVTEARRAGLADVLMITGRNKRALEDHFDRHpaleaalehk 88
Cdd:COG1207 1 SPLAVVILAAGKGTRM----KsKLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVRAALADL---------- 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 896140700 89 gdakrlaqihesdlvgDIHYVRQGEALGLGHAVNCARRHVG--EEPFAVLLGD 139
Cdd:COG1207 67 ----------------DVEFVLQEEQLGTGHAVQQALPALPgdDGTVLVLYGD 103
|
|
| eIF-2B_gamma_N_like |
cd02507 |
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ... |
13-106 |
1.15e-09 |
|
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: 57.26 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 13 KAVIPAAGLGTRFLPATKAMPKEMLPVVDRPAIEYVVTEARRAGLADVLMITGRNKRALEDH------------FDRHPA 80
Cdd:cd02507 2 QAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQAIIEHllkskwsslsskMIVDVI 81
|
90 100 110
....*....|....*....|....*....|....*.
gi 896140700 81 LEAALEHKGDAKRLAQIH----------ESDLVGDI 106
Cdd:cd02507 82 TSDLCESAGDALRLRDIRglirsdflllSCDLVSNI 117
|
|
| eIF-2B_gamma_N |
cd04198 |
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ... |
13-74 |
1.23e-09 |
|
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; N-terminal domain of gamma subunit of the eukaryotic translation initiation factor 2B (eIF-2B): eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit gamma shares sequence similarity with epsilon subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.
Pssm-ID: 133041 [Multi-domain] Cd Length: 214 Bit Score: 57.28 E-value: 1.23e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896140700 13 KAVIPAAGLGTRFLPATKAMPKEMLPVVDRPAIEYVVTEARRAGLADVLMITGRNKRALEDH 74
Cdd:cd04198 2 QAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEEQAEIST 63
|
|
| glmU |
PRK14354 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
11-139 |
1.60e-09 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184643 [Multi-domain] Cd Length: 458 Bit Score: 58.30 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 11 TRKAVIPAAGLGTRFlpaTKAMPKEMLPVVDRPAIEYVVTEARRAGLADVLMITGRNKralEDhfdrhpaLEAALEHKGD 90
Cdd:PRK14354 2 NRYAIILAAGKGTRM---KSKLPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVGHGA---EE-------VKEVLGDRSE 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 896140700 91 akrlaqihesdlvgdihYVRQGEALGLGHAVNCARRHVGEEP--FAVLLGD 139
Cdd:PRK14354 69 -----------------FALQEEQLGTGHAVMQAEEFLADKEgtTLVICGD 102
|
|
| GT2_GlmU_N_bac |
cd02540 |
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ... |
14-139 |
5.71e-09 |
|
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: 55.21 E-value: 5.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 14 AVIPAAGLGTRflpatkaM----PKEMLPVVDRPAIEYVVTEARRAGLADVLMITGrnkraledhfdrHPA--LEAALEH 87
Cdd:cd02540 1 AVILAAGKGTR-------MksdlPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVG------------HGAeqVKKALAN 61
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 896140700 88 KgdakrlaqihesdlvgDIHYVRQGEALGLGHAVNCARRHVG--EEPFAVLLGD 139
Cdd:cd02540 62 P----------------NVEFVLQEEQLGTGHAVKQALPALKdfEGDVLVLYGD 99
|
|
| glmU |
PRK14358 |
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ... |
8-244 |
6.79e-09 |
|
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase; Provisional
Pssm-ID: 237688 [Multi-domain] Cd Length: 481 Bit Score: 56.53 E-value: 6.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 8 RPRTRKAVIPAAGLGTRFlpaTKAMPKEMLPVVDRPAIEYVVTEARRAGLADVLMITGRNKRaledhfdrhpALEAALEH 87
Cdd:PRK14358 4 QTRPLDVVILAAGQGTRM---KSALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGAE----------QVEAALQG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 88 KGdakrlaqihesdlvgdIHYVRQGEALGLGHAVNCARR--HVGEEPFAVLLGDDIIGDGEALLERMIDVQQRLGGSVIA 165
Cdd:PRK14358 71 SG----------------VAFARQEQQLGTGDAFLSGASalTEGDADILVLYGDTPLLRPDTLRALVADHRAQGSAMTIL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 166 LMEVPEeaVSAYGvaavQAVPGEGDDVVRVtdlVEKPAREDAPSTLAII--GRYVL---APQVFDVLDETPPgrGGEIQL 240
Cdd:PRK14358 135 TGELPD--ATGYG----RIVRGADGAVERI---VEQKDATDAEKAIGEFnsGVYVFdarAPELARRIGNDNK--AGEYYL 203
|
....
gi 896140700 241 TDAL 244
Cdd:PRK14358 204 TDLL 207
|
|
| glmU |
PRK14355 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
14-166 |
9.84e-09 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237685 [Multi-domain] Cd Length: 459 Bit Score: 55.91 E-value: 9.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 14 AVIPAAGLGTRFlpaTKAMPKEMLPVVDRPAIEYVVTEARRAGLADVLMITGRNKRALEDHFdrhpaleaalehKGDakr 93
Cdd:PRK14355 6 AIILAAGKGTRM---KSDLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHF------------AGD--- 67
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896140700 94 laqihesdlvGDIHYVRQGEALGLGHAVNCARRHVGEEPFAVLL--GDDIIGDGEAlLERMIDVQQRLGGSVIAL 166
Cdd:PRK14355 68 ----------GDVSFALQEEQLGTGHAVACAAPALDGFSGTVLIlcGDVPLLRAET-LQGMLAAHRATGAAVTVL 131
|
|
| glmU |
PRK14353 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
9-139 |
2.60e-08 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184642 [Multi-domain] Cd Length: 446 Bit Score: 54.48 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 9 PRTRKAVIPAAGLGTRFlpaTKAMPKEMLPVVDRPAIEYVVTEARRAGLADVLMITGRNkraledhfdrHPALEAALEhk 88
Cdd:PRK14353 3 DRTCLAIILAAGEGTRM---KSSLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGPG----------AEAVAAAAA-- 67
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 896140700 89 gdakrlaqihesDLVGDIHYVRQGEALGLGHAVNCARRHV--GEEPFAVLLGD 139
Cdd:PRK14353 68 ------------KIAPDAEIFVQKERLGTAHAVLAAREALagGYGDVLVLYGD 108
|
|
| M1P_guanylylT_B_like_N |
cd06425 |
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ... |
13-225 |
3.01e-08 |
|
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: 53.37 E-value: 3.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 13 KAVIPAAGLGTRFLPATKAMPKEMLPVVDRPAIEYVVTEARRAGLADVlmITGRNKraledhfdRHPALEAALehkgdak 92
Cdd:cd06425 2 KALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEI--ILAVNY--------RPEDMVPFL------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 93 rlaQIHESDLVGDIHYVRQGEALGLGHAVNCARRHVGE--EPFAVlLGDDIIGDGEalLERMIDVQQRLGG-SVIALMEV 169
Cdd:cd06425 65 ---KEYEKKLGIKITFSIETEPLGTAGPLALARDLLGDddEPFFV-LNSDVICDFP--LAELLDFHKKHGAeGTILVTKV 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 896140700 170 peEAVSAYGVAAVQAVPGegddvvRVTDLVEKParEDAPSTLAIIGRYVLAPQVFD 225
Cdd:cd06425 139 --EDPSKYGVVVHDENTG------RIERFVEKP--KVFVGNKINAGIYILNPSVLD 184
|
|
| GT_2_like_f |
cd04182 |
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ... |
14-165 |
8.44e-07 |
|
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: 48.33 E-value: 8.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 14 AVIPAAGLGTRFlpatkAMPKEMLPVVDRPAIEYVVTEARRAGLADVLMITGrnkraledhfDRHPALEAALehkgdakr 93
Cdd:cd04182 3 AIILAAGRSSRM-----GGNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLG----------AEADAVRAAL-------- 59
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 896140700 94 laqiheSDLVGDIHYVRQGEaLGLGHAVNCARRHVGEEP--FAVLLGD--DIigdGEALLERMIDVQQRLGGSVIA 165
Cdd:cd04182 60 ------AGLPVVVVINPDWE-EGMSSSLAAGLEALPADAdaVLILLADqpLV---TAETLRALIDAFREDGAGIVA 125
|
|
| MocA |
COG2068 |
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism]; |
14-165 |
1.01e-06 |
|
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
Pssm-ID: 441671 [Multi-domain] Cd Length: 195 Bit Score: 48.23 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 14 AVIPAAGLGTRFlpatkAMPKEMLPVVDRPAIEYVVTEARRAGLADVLMITGrnkraledhfDRHPALEAALEHKGdakr 93
Cdd:COG2068 6 AIILAAGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPVVVVLG----------ADAEEVAAALAGLG---- 66
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 896140700 94 laqihesdlvgdIHYVR-QGEALGLGHAVNCARRHVGE--EPFAVLLGD--DIigdGEALLERMIDVQQRLGGSVIA 165
Cdd:COG2068 67 ------------VRVVVnPDWEEGMSSSLRAGLAALPAdaDAVLVLLGDqpLV---TAETLRRLLAAFRESPASIVA 128
|
|
| glmU |
PRK14357 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
13-244 |
2.39e-06 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237687 [Multi-domain] Cd Length: 448 Bit Score: 48.61 E-value: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 13 KAVIPAAGLGTRFlpaTKAMPKEMLPVVDRPAIEYVVTEARRAGlADVLMITGrnkraledhfdrhpaleaaleHKgdak 92
Cdd:PRK14357 2 RALVLAAGKGTRM---KSKIPKVLHKISGKPMINWVIDTAKKVA-QKVGVVLG---------------------HE---- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 93 rlAQIHESDLVGDIHYVRQGEALGLGHAVNCARRHVGEEPFAVLLGDDIIGDGEALLERMIDVQQRLGGSVIALMEVPEE 172
Cdd:PRK14357 53 --AELVKKLLPEWVKIFLQEEQLGTAHAVMCARDFIEPGDDLLILYGDVPLISENTLKRLIEEHNRKGADVTILVADLED 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896140700 173 AvSAYGvaavQAVPGEGDdvVRVTDLVEKPAREDAPSTLAiIGRYVL-APQVFDVLDE-TPPGRGGEIQLTDAL 244
Cdd:PRK14357 131 P-TGYG----RIIRDGGK--YRIVEDKDAPEEEKKIKEIN-TGIYVFsGDFLLEVLPKiKNENAKGEYYLTDAV 196
|
|
| glmU |
PRK09451 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
14-178 |
2.50e-05 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 181867 [Multi-domain] Cd Length: 456 Bit Score: 45.40 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 14 AVIPAAGLGTRFLpatKAMPKEMLPVVDRPAIEYVVTEARRAGLADVLMITGrnkraledhfdrhpaleaaleHKGDakr 93
Cdd:PRK09451 8 VVILAAGKGTRMY---SDLPKVLHTLAGKPMVQHVIDAANELGAQHVHLVYG---------------------HGGD--- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896140700 94 LAQIHESDlvGDIHYVRQGEALGLGHAVNCARRHVG-EEPFAVLLGD-DIIgdGEALLERMIDVQQRLGgsvIALMEVPE 171
Cdd:PRK09451 61 LLKQTLAD--EPLNWVLQAEQLGTGHAMQQAAPFFAdDEDILMLYGDvPLI--SVETLQRLRDAKPQGG---IGLLTVKL 133
|
....*..
gi 896140700 172 EAVSAYG 178
Cdd:PRK09451 134 DNPTGYG 140
|
|
| GT2_BcE_like |
cd04183 |
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ... |
15-77 |
2.46e-04 |
|
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; GT2_BcbE_like: The bcbE gene is one of the genes in the capsule biosynthetic locus of Pasteurella multocida. Its deducted product is likely involved in the biosynthesis of the polysaccharide capsule, which is found on surface of a wide range of bacteria. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.
Pssm-ID: 133026 [Multi-domain] Cd Length: 231 Bit Score: 41.47 E-value: 2.46e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896140700 15 VIPAAGLGTRFLPATKAMPKEMLPVVDRPAIEYVVTEARRAGLADVLMITgrNKRALEDHFDR 77
Cdd:cd04183 2 IIPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEWVIESLAKIFDSRFIFIC--RDEHNTKFHLD 62
|
|
| glgC |
PRK00725 |
glucose-1-phosphate adenylyltransferase; Provisional |
164-229 |
8.86e-04 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 234824 [Multi-domain] Cd Length: 425 Bit Score: 40.59 E-value: 8.86e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896140700 164 IALMEVPEEAVSAYGVAAVqavpgegDDVVRVTDLVEKPAREDA----PST-LAIIGRYVLAPQV-FDVLDE 229
Cdd:PRK00725 161 VACLEVPREEASAFGVMAV-------DENDRITAFVEKPANPPAmpgdPDKsLASMGIYVFNADYlYELLEE 225
|
|
| eIF-2B_epsilon_N |
cd04197 |
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ... |
14-75 |
1.09e-03 |
|
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; N-terminal domain of epsilon subunit of the eukaryotic translation initiation factor 2B (eIF-2B): eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit epsilon shares sequence similarity with gamma subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.
Pssm-ID: 133040 [Multi-domain] Cd Length: 217 Bit Score: 39.51 E-value: 1.09e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896140700 14 AVIPAAGLGTRFLPATKAMPKEMLPVVDRPAIEYVVTEARRAGLADVLMITGRNKRALEDHF 75
Cdd:cd04197 3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQIKEYI 64
|
|
| CDP-ME_synthetase |
cd02516 |
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ... |
14-49 |
5.29e-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: 37.50 E-value: 5.29e-03
10 20 30
....*....|....*....|....*....|....*.
gi 896140700 14 AVIPAAGLGTRFlpaTKAMPKEMLPVVDRPAIEYVV 49
Cdd:cd02516 3 AIILAAGSGSRM---GADIPKQFLELGGKPVLEHTL 35
|
|
| |
