|
Name |
Accession |
Description |
Interval |
E-value |
| GalU |
COG1210 |
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis]; |
1-287 |
1.87e-172 |
|
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440823 [Multi-domain] Cd Length: 288 Bit Score: 478.37 E-value: 1.87e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 1 MRPRKAVIPAGGWGTRFLPTTKSQPKEMLPLVDRPIIHYAVEEVVRCGAELVVIVSSLGKRAVEDYFDKNADLELFLERK 80
Cdd:COG1210 1 MKIRKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVTGRGKRAIEDHFDRSYELEATLEAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 81 GDTSLLHKVRQLADMADICYVRQKEQLGLGHAVLTAKQVVGNEPFMLVLPDDLFEQQERVLQRMADIFEQHQASVLAVRR 160
Cdd:COG1210 81 GKEELLEEVRSISPLANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSEKPCLKQMIEVYEETGGSVIAVQE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 161 VNEDQVSRYGIIEASSIGDRTYRVTSLVEKPKREEAPSNLAIMGRYILTPQVFEELENTSPGAGKEIQLTDGLRRLLSRQ 240
Cdd:COG1210 161 VPPEEVSKYGIVDGEEIEGGVYRVTGLVEKPAPEEAPSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDAIAALAKEE 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1490726163 241 AIYAYEVEGDYYDAGTPLGWIKATIALALKHPEMGPEIREYLKSLVS 287
Cdd:COG1210 241 PVYAYEFEGKRYDCGDKLGYLKATVEFALKRPDLGEEFREYLKELLK 287
|
|
| UGPase_prokaryotic |
cd02541 |
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ... |
4-270 |
9.40e-145 |
|
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: 407.30 E-value: 9.40e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 4 RKAVIPAGGWGTRFLPTTKSQPKEMLPLVDRPIIHYAVEEVVRCGAELVVIVSSLGKRAVEDYFDKNADLELFLERKGDT 83
Cdd:cd02541 1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRGKRAIEDHFDRSYELEETLEKKGKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 84 SLLHKVRQLADMADICYVRQKEQLGLGHAVLTAKQVVGNEPFMLVLPDDLFEQQERVLQRMADIFEQHQASVLAVRRVNE 163
Cdd:cd02541 81 DLLEEVRIISDLANIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLIDSKEPCLKQLIEAYEKTGASVIAVEEVPP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 164 DQVSRYGIIEASSIGDRTYRVTSLVEKPKREEAPSNLAIMGRYILTPQVFEELENTSPGAGKEIQLTDGLRRLLSRQAIY 243
Cdd:cd02541 161 EDVSKYGIVKGEKIDGDVFKVKGLVEKPKPEEAPSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTDAIAKLLEEEPVY 240
|
250 260
....*....|....*....|....*..
gi 1490726163 244 AYEVEGDYYDAGTPLGWIKATIALALK 270
Cdd:cd02541 241 AYVFEGKRYDCGNKLGYLKATVEFALK 267
|
|
| galU |
TIGR01099 |
UTP--glucose-1-phosphate uridylyltransferase; Built to distinquish between the highly similar ... |
4-263 |
9.39e-127 |
|
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: 361.67 E-value: 9.39e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 4 RKAVIPAGGWGTRFLPTTKSQPKEMLPLVDRPIIHYAVEEVVRCGAELVVIVSSLGKRAVEDYFDKNADLELFLERKGDT 83
Cdd:TIGR01099 1 RKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYIVEEAVEAGIEEIVFVTGRGKRAIEDHFDYSYELEHQLEKRGKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 84 SLLHKVRQLADMADICYVRQKEQLGLGHAVLTAKQVVGNEPFMLVLPDDLFEQQERVLQRMADIFEQHQASVLAVRRVNE 163
Cdd:TIGR01099 81 ELLEEVRKISNLATIFYVRQKEQKGLGHAVLCARPFVGDEPFAVILGDDIVVNEEPALKQMIKAYEKTGCSIIAVQEVPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 164 DQVSRYGIIEASSIGDRTYRVTSLVEKPKREEAPSNLAIMGRYILTPQVFEELENTSPGAGKEIQLTDGLRRLLSRQAIY 243
Cdd:TIGR01099 161 EEVSKYGVIDGEGIEKDLYKVKNMVEKPKPEEAPSNLAIVGRYILTPDIFDLLEETPPGKGGEIQLTDAINKLLENETVL 240
|
250 260
....*....|....*....|
gi 1490726163 244 AYEVEGDYYDAGTPLGWIKA 263
Cdd:TIGR01099 241 AYKFNGKRYDCGSKLGYLEA 260
|
|
| PRK13389 |
PRK13389 |
UTP--glucose-1-phosphate uridylyltransferase GalU; |
4-287 |
5.25e-70 |
|
UTP--glucose-1-phosphate uridylyltransferase GalU;
Pssm-ID: 184021 [Multi-domain] Cd Length: 302 Bit Score: 219.01 E-value: 5.25e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 4 RKAVIPAGGWGTRFLPTTKSQPKEMLPLVDRPIIHYAVEEVVRCGAELVVIVSSLGKRAVEDYFDKNADLELFLERKGDT 83
Cdd:PRK13389 9 KKAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFDTSFELEAMLEKRVKR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 84 SLLHKVRQLA-DMADICYVRQKEQLGLGHAVLTAKQVVGNEPFMLVLPDDLFEQQERVLQR-----MADIFEQHQASVLA 157
Cdd:PRK13389 89 QLLDEVQSICpPHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILDEYESDLSQdnlaeMIRRFDETGHSQIM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 158 VRRVneDQVSRYGIIEASSI----GDRTYRVtSLVEKPKREEAPSNLAIMGRYILTPQVFEELENTSPGAGKEIQLTDGL 233
Cdd:PRK13389 169 VEPV--ADVTAYGVVDCKGVelapGESVPMV-GVVEKPKADVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTDAI 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1490726163 234 RRLLSRQAIYAYEVEGDYYDAGTPLGWIKATIALALKHPEMGPEIREYLKSLVS 287
Cdd:PRK13389 246 DMLIEKETVEAYHMKGKSHDCGNKLGYMQAFVEYGIRHNTLGTEFKAWLEEEMG 299
|
|
| PRK10122 |
PRK10122 |
UTP--glucose-1-phosphate uridylyltransferase GalF; |
1-287 |
2.51e-63 |
|
UTP--glucose-1-phosphate uridylyltransferase GalF;
Pssm-ID: 182252 [Multi-domain] Cd Length: 297 Bit Score: 201.66 E-value: 2.51e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 1 MRPRKAVIPAGGWGTRFLPTTKSQPKEMLPLVDRPIIHYAVEEVVRCGAELVVIVSSLGKRAVEDYFDKNADLELFLERK 80
Cdd:PRK10122 1 MTNLKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAVENHFDTSYELESLLEQR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 81 GDTSLLHKVRQLADMA-DICYVRQKEQLGLGHAVLTAKQVVGNEPFMLVLPDDLFEQQ-----ERVLQRMADIFEQHQAS 154
Cdd:PRK10122 81 VKRQLLAEVQSICPPGvTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPDVVIDDAsadplRYNLAAMIARFNETGRS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 155 VLAVRRVNEDqVSRYGIIEASSIGDR---TYRVTSLVEKPKREEA-PSNLAIMGRYILTPQVFEELENTSPGAGKEIQLT 230
Cdd:PRK10122 161 QVLAKRMPGD-LSEYSVIQTKEPLDRegkVSRIVEFIEKPDQPQTlDSDLMAVGRYVLSADIWPELERTEPGAWGRIQLT 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1490726163 231 DGLRRLLSRQAIYAYEVEGDYYDAGTPLGWIKATIALALKHPEMGPEIREYLKSLVS 287
Cdd:PRK10122 240 DAIAELAKKQSVDAMLMTGDSYDCGKKMGYMQAFVKYGLRNLKEGAKFRKGIEKLLS 296
|
|
| NTP_transferase |
cd04181 |
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ... |
6-255 |
5.58e-58 |
|
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; Nucleotidyltransferases transfer nucleotides onto phosphosugars. The enzyme family includes Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase. The products are activated sugars that are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides.
Pssm-ID: 133024 [Multi-domain] Cd Length: 217 Bit Score: 185.09 E-value: 5.58e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 6 AVIPAGGWGTRFLPTTKSQPKEMLPLVDRPIIHYAVEEVVRCGAELVVIVSSLGKRAVEDYFdknadlelflerkGDTSL 85
Cdd:cd04181 1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYF-------------GDGSK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 86 LHKvrqladmaDICYVRQKEQLGLGHAVLTAKQVVGNEPFMLVLPDDLFEQQervLQRMADIFEQHQA-SVLAVRRVneD 164
Cdd:cd04181 68 FGV--------NIEYVVQEEPLGTAGAVRNAEDFLGDDDFLVVNGDVLTDLD---LSELLRFHREKGAdATIAVKEV--E 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 165 QVSRYGIIEassiGDRTYRVTSLVEKPKREEapSNLAIMGRYILTPQVFEELENTSPgaGKEIQLTDGLRRLLSRQAIYA 244
Cdd:cd04181 135 DPSRYGVVE----LDDDGRVTRFVEKPTLPE--SNLANAGIYIFEPEILDYIPEILP--RGEDELTDAIPLLIEEGKVYG 206
|
250
....*....|.
gi 1490726163 245 YEVEGDYYDAG 255
Cdd:cd04181 207 YPVDGYWLDIG 217
|
|
| G1P_TT_long |
cd04189 |
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ... |
5-263 |
7.49e-53 |
|
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: 172.37 E-value: 7.49e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 5 KAVIPAGGWGTRFLPTTKSQPKEMLPLVDRPIIHYAVEEVVRCGAELVVIVSSLGKRAVEDYFdknadlelflerkGDTS 84
Cdd:cd04189 2 KGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEAL-------------GDGS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 85 LLHkvrqladmADICYVRQKEQLGLGHAVLTAKQVVGNEPFMLVLPDDLFEQqerVLQRMADIFEQHQASV-LAVRRVne 163
Cdd:cd04189 69 RFG--------VRITYILQEEPLGLAHAVLAARDFLGDEPFVVYLGDNLIQE---GISPLVRDFLEEDADAsILLAEV-- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 164 DQVSRYGIIEASSigdrtYRVTSLVEKPKreEAPSNLAIMGRYILTPQVFEELENTSPGAGKEIQLTDGLRRLLSR-QAI 242
Cdd:cd04189 136 EDPRRFGVAVVDD-----GRIVRLVEKPK--EPPSNLALVGVYAFTPAIFDAISRLKPSWRGELEITDAIQWLIDRgRRV 208
|
250 260
....*....|....*....|.
gi 1490726163 243 YAYEVEGDYYDAGTPLGWIKA 263
Cdd:cd04189 209 GYSIVTGWWKDTGTPEDLLEA 229
|
|
| RmlA1 |
COG1209 |
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis]; |
4-257 |
5.35e-49 |
|
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440822 [Multi-domain] Cd Length: 294 Bit Score: 164.49 E-value: 5.35e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 4 RKAVIPAGGWGTRFLPTTKSQPKEMLPLVDRPIIHYAVEEVVRCGAELVVIVSSlgkravedyfdkNADLELFLERKGDT 83
Cdd:COG1209 1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIIST------------PEDGPQFERLLGDG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 84 SLLHkvrqladmADICYVRQKEQLGLGHAVLTAKQVVGNEPFMLVLPDDLFEQQErvLQRMADIFEQHQA-SVLAVRRVN 162
Cdd:COG1209 69 SQLG--------IKISYAVQPEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDG--LSELLREAAARESgATIFGYKVE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 163 EDQvsRYGIIEAssigDRTYRVTSLVEKPKreEAPSNLAIMGRYILTPQVFEELENTSPGAGKEIQLTDGLRRLLSR-QA 241
Cdd:COG1209 139 DPE--RYGVVEF----DEDGRVVSLEEKPK--EPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERgKL 210
|
250
....*....|....*..
gi 1490726163 242 IYAYEVEG-DYYDAGTP 257
Cdd:COG1209 211 VVELLGRGfAWLDTGTH 227
|
|
| GCD1 |
COG1208 |
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ... |
5-257 |
2.07e-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: 156.08 E-value: 2.07e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 5 KAVIPAGGWGTRFLPTTKSQPKEMLPLVDRPIIHYAVEEVVRCGA-ELVVIVSSLGKRaVEDYFDKNADLELflerkgdt 83
Cdd:COG1208 1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGItEIVINVGYLAEQ-IEEYFGDGSRFGV-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 84 sllhkvrqladmaDICYVRQKEQLGLGHAVLTAKQVVGNEPFMLVLPDDLFEQQervLQRMADIFEQHQASV-LAVRRVn 162
Cdd:COG1208 72 -------------RITYVDEGEPLGTGGALKRALPLLGDEPFLVLNGDILTDLD---LAALLAFHREKGADAtLALVPV- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 163 eDQVSRYGIIEASSIGdrtyRVTSLVEKPkrEEAPSNLAIMGRYILTPQVFEELEntspgAGKEIQLTDGLRRLLSRQAI 242
Cdd:COG1208 135 -PDPSRYGVVELDGDG----RVTRFVEKP--EEPPSNLINAGIYVLEPEIFDYIP-----EGEPFDLEDLLPRLIAEGRV 202
|
250
....*....|....*
gi 1490726163 243 YAYEVEGDYYDAGTP 257
Cdd:COG1208 203 YGYVHDGYWLDIGTP 217
|
|
| NTP_transferase |
pfam00483 |
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ... |
5-268 |
1.13e-29 |
|
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer nucleotides onto phosphosugars.
Pssm-ID: 425709 [Multi-domain] Cd Length: 243 Bit Score: 112.35 E-value: 1.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 5 KAVIPAGGWGTRFLPTTKSQPKEMLPLVDR-PIIHYAVEEVVRCGAELVVIVSSlgkravedyfdkNADLELFLERKGDT 83
Cdd:pfam00483 1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILT------------QEHRFMLNELLGDG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 84 SLLHkvrqladmADICYVRQKEQLGLGHAVLTAKQVVGNEPF-MLVLPDDLFEQQErvLQRMADIFEQHQASVLA-VRRV 161
Cdd:pfam00483 69 SKFG--------VQITYALQPEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMD--LEQAVKFHIEKAADATVtFGIV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 162 NEDQVSRYGIIEAssigDRTYRVTSLVEKPKREEApSNLAIMGRYILTPQVFEEL-ENTSPGAGKEIQLTDGLRRLLSR- 239
Cdd:pfam00483 139 PVEPPTGYGVVEF----DDNGRVIRFVEKPKLPKA-SNYASMGIYIFNSGVLDFLaKYLEELKRGEDEITDILPKALEDg 213
|
250 260 270
....*....|....*....|....*....|
gi 1490726163 240 QAIYAYEVEG-DYYDAGTPLGWIKATIALA 268
Cdd:pfam00483 214 KLAYAFIFKGyAWLDVGTWDSLWEANLFLL 243
|
|
| G1P_TT_short |
cd02538 |
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ... |
4-264 |
8.63e-27 |
|
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is the short form of glucose-1-phosphate thymidylyltransferase. Glucose-1-phosphate thymidylyltransferase catalyses the formation of dTDP-glucose, from dTTP and glucose 1-phosphate. It is the first enzyme in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme.There are two forms of Glucose-1-phosphate thymidylyltransferase in bacteria and archeae; short form and long form. The homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose. The long form, which has an extra 50 amino acids c-terminal, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced.
Pssm-ID: 133019 [Multi-domain] Cd Length: 240 Bit Score: 104.96 E-value: 8.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 4 RKAVIPAGGWGTRFLPTTKSQPKEMLPLVDRPIIHYAVEEVVRCGAELVVIVSSLGkravedyfdknaDLELFLERKGDT 83
Cdd:cd02538 1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPE------------DLPLFKELLGDG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 84 SLLHKvrqladmaDICYVRQKEQLGLGHAVLTAKQVVGNEPFMLVLPDDLFEQQErvLQRMADIFEQHQ--ASVLAVrRV 161
Cdd:cd02538 69 SDLGI--------RITYAVQPKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQG--LSPILQRAAAQKegATVFGY-EV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 162 NEDQvsRYGIIEAssigDRTYRVTSLVEKPKReeAPSNLAIMGRYILTPQVFEELENTSPGAGKEIQLTDgLRRLLSRQA 241
Cdd:cd02538 138 NDPE--RYGVVEF----DENGRVLSIEEKPKK--PKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITD-VNNEYLEKG 208
|
250 260
....*....|....*....|....*.
gi 1490726163 242 IYAYEVEGDYY---DAGTPLGWIKAT 264
Cdd:cd02538 209 KLSVELLGRGFawlDTGTHESLLEAS 234
|
|
| NTP_transferase_WcbM_like |
cd06915 |
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ... |
6-263 |
4.40e-23 |
|
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: 94.54 E-value: 4.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 6 AVIPAGGWGTRFLPTTKSQPKEMLPLVDRPIIHYAVEEVVRCGAELVVIvsSLGKRA--VEDYFDKNADLElflerkgdt 83
Cdd:cd06915 1 AVILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVL--SVGYLAeqIEEYFGDGYRGG--------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 84 sllhkvrqladmADICYVRQKEQLGLGHAVLTAKQVVGNEPFMLVLPDDLFEQQERVLQRMADifEQHQASVLAVRRVNE 163
Cdd:cd06915 70 ------------IRIYYVIEPEPLGTGGAIKNALPKLPEDQFLVLNGDTYFDVDLLALLAALR--ASGADATMALRRVPD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 164 dqVSRYGIIEAssigDRTYRVTSLVEkpKREEAPSNLAIMGRYILTPQVFEELENTSPGAgkeiqLTDGLRRLLSRQAIY 243
Cdd:cd06915 136 --ASRYGNVTV----DGDGRVIAFVE--KGPGAAPGLINGGVYLLRKEILAEIPADAFSL-----EADVLPALVKRGRLY 202
|
250 260
....*....|....*....|
gi 1490726163 244 AYEVEGDYYDAGTPLGWIKA 263
Cdd:cd06915 203 GFEVDGYFIDIGIPEDYARA 222
|
|
| M1P_guanylylT_B_like_N |
cd06425 |
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ... |
5-264 |
2.05e-21 |
|
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: 90.35 E-value: 2.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 5 KAVIPAGGWGTRFLPTTKSQPKEMLPLVDRPIIHYAVEEVVRCGAELVVIvsslgkrAVEDYFDknaDLELFLErkgDTS 84
Cdd:cd06425 2 KALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIIL-------AVNYRPE---DMVPFLK---EYE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 85 LLHKVRqladmadICYVRQKEQLGLGHAVLTAKQVVG--NEPFmLVLPDDLFeqQERVLQRMADIFEQHQA-SVLAVRRV 161
Cdd:cd06425 69 KKLGIK-------ITFSIETEPLGTAGPLALARDLLGddDEPF-FVLNSDVI--CDFPLAELLDFHKKHGAeGTILVTKV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 162 neDQVSRYGIIEASsigDRTYRVTSLVEKPKreEAPSNLAIMGRYILTPQVFE--ELENTSpgAGKEIqltdgLRRLLSR 239
Cdd:cd06425 139 --EDPSKYGVVVHD---ENTGRIERFVEKPK--VFVGNKINAGIYILNPSVLDriPLRPTS--IEKEI-----FPKMASE 204
|
250 260
....*....|....*....|....*
gi 1490726163 240 QAIYAYEVEGDYYDAGTPLGWIKAT 264
Cdd:cd06425 205 GQLYAYELPGFWMDIGQPKDFLKGM 229
|
|
| PRK15480 |
PRK15480 |
glucose-1-phosphate thymidylyltransferase RfbA; Provisional |
1-290 |
4.03e-20 |
|
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
Pssm-ID: 185377 [Multi-domain] Cd Length: 292 Bit Score: 87.81 E-value: 4.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 1 MRPRKAVIPAGGWGTRFLPTTKSQPKEMLPLVDRPIIHYAVEEVVRCGAELVVIVSSlgkravedyfdkNADLELFLERK 80
Cdd:PRK15480 1 MKTRKGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIIST------------PQDTPRFQQLL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 81 GDTS-----LLHKVRQLADmadicyvrqkeqlGLGHAVLTAKQVVGNEPFMLVLPDDLFEQQERVLQRMADIFEQHQASV 155
Cdd:PRK15480 69 GDGSqwglnLQYKVQPSPD-------------GLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 156 LAVrRVNEDQvsRYGIIEAssigDRTYRVTSLVEKPKreEAPSNLAIMGRYILTPQVFEELENTSPGAGKEIQLTDgLRR 235
Cdd:PRK15480 136 FAY-HVNDPE--RYGVVEF----DQNGTAISLEEKPL--QPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITD-INR 205
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1490726163 236 LLSRQAIYAYEVEGDYY---DAGTPLGWIKATIALALKHPEMG-----PEIREYLKSLVSVSR 290
Cdd:PRK15480 206 IYMEQGRLSVAMMGRGYawlDTGTHQSLIEASNFIATIEERQGlkvscPEEIAFRKGFIDAEQ 268
|
|
| 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-18 |
|
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: 81.02 E-value: 3.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 6 AVIPAGGWGTRFLPTTKSQPKEMLPLVDRPIIHYAVEEVVRCGAELVVI-VSSLGKRaVEDYFdknadlelflerkGDTS 84
Cdd:cd06426 1 VVIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYIsVNYLAEM-IEDYF-------------GDGS 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 85 llhkvrqlADMADICYVRQKEQLGLGHAV--LTAKQvvgNEPFmLVLPDDLFEQQErvLQRMADIFEQHQASVLAVRRVN 162
Cdd:cd06426 67 --------KFGVNISYVREDKPLGTAGALslLPEKP---TDPF-LVMNGDILTNLN--YEHLLDFHKENNADATVCVREY 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 163 EDQVSrYGIIEassIGDRtyRVTSLVEKPKReeapSNLAIMGRYILTPQVFEELENtspgaGKEIQLTDGLRRLLSR-QA 241
Cdd:cd06426 133 EVQVP-YGVVE---TEGG--RITSIEEKPTH----SFLVNAGIYVLEPEVLDLIPK-----NEFFDMPDLIEKLIKEgKK 197
|
250
....*....|....*.
gi 1490726163 242 IYAYEVEGDYYDAGTP 257
Cdd:cd06426 198 VGVFPIHEYWLDIGRP 213
|
|
| GlgC |
COG0448 |
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ... |
143-254 |
7.89e-14 |
|
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate transport and metabolism];
Pssm-ID: 440217 [Multi-domain] Cd Length: 377 Bit Score: 70.87 E-value: 7.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 143 RM--ADIFEQHQAS----VLAVRRVNEDQVSRYGIIEAssigDRTYRVTSLVEKPKREEapSNLAIMGRYILTPQVFEEL 216
Cdd:COG0448 128 KMdyRQMLDFHIESgadiTVACIEVPREEASRFGVMEV----DEDGRITEFEEKPKDPK--SALASMGIYVFNKDVLIEL 201
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1490726163 217 -----ENTSPGAGKEIqltdgLRRLLSRQAIYAYEVEG---------DYYDA 254
Cdd:COG0448 202 leedaPNSSHDFGKDI-----IPRLLDRGKVYAYEFDGywrdvgtidSYYEA 248
|
|
| NTP_transferase_like_1 |
cd06422 |
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ... |
5-257 |
2.39e-12 |
|
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.
Pssm-ID: 133044 [Multi-domain] Cd Length: 221 Bit Score: 64.90 E-value: 2.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 5 KAVIPAGGWGTRFLPTTKSQPKEMLPLVDRPIIHYAVEEVVRCGAELVVI-VSSLGKrAVEDYF-DKNADLELFL--ERk 80
Cdd:cd06422 1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVnTHHLAD-QIEAHLgDSRFGLRITIsdEP- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 81 gdtsllhkvrqladmadicyvrqKEQLGLGHAVLTAKQVVGNEPFMLVLPD-----DLFEQQERVLQRMAdifeqhqASV 155
Cdd:cd06422 79 -----------------------DELLETGGGIKKALPLLGDEPFLVVNGDilwdgDLAPLLLLHAWRMD-------ALL 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 156 LAVRRVNEDQVSRYGIIEASSIGDRTyrvtslvekPKREEAPSNLAIMGRYILTPQVFEELEntsPGAGKeiqLTDGLRR 235
Cdd:cd06422 129 LLLPLVRNPGHNGVGDFSLDADGRLR---------RGGGGAVAPFTFTGIQILSPELFAGIP---PGKFS---LNPLWDR 193
|
250 260
....*....|....*....|..
gi 1490726163 236 LLSRQAIYAYEVEGDYYDAGTP 257
Cdd:cd06422 194 AIAAGRLFGLVYDGLWFDVGTP 215
|
|
| GlmU |
COG1207 |
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ... |
2-173 |
5.66e-11 |
|
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: 62.74 E-value: 5.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 2 RPRKAVIPAGGWGTRFlpttKSQ-PKEMLPLVDRPIIHYAVEEVVRCGAELVVIVSSLGKRAVEDYFDKNadlelflerk 80
Cdd:COG1207 1 SPLAVVILAAGKGTRM----KSKlPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVRAALADL---------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 81 gdtsllhkvrqladmaDICYVRQKEQLGLGHAVLTAKQVVGNEP-FMLVLPDD--LFEQQErvLQRMADIFEQHQA--SV 155
Cdd:COG1207 67 ----------------DVEFVLQEEQLGTGHAVQQALPALPGDDgTVLVLYGDvpLIRAET--LKALLAAHRAAGAaaTV 128
|
170 180
....*....|....*....|....*....
gi 1490726163 156 LAVR-----------RVNEDQVSRygIIE 173
Cdd:COG1207 129 LTAElddptgygrivRDEDGRVLR--IVE 155
|
|
| PC_cytidylyltransferase |
cd02523 |
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ... |
6-250 |
8.19e-11 |
|
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family contains proteins similar to prokaryotic phosphocholine (P-cho) cytidylyltransferases. Phosphocholine (PC) cytidylyltransferases catalyze the transfer of a cytidine monophosphate from CTP to phosphocholine to form CDP-choline. PC is the most abundant phospholipid in eukaryotic membranes and it is also important in prokaryotic membranes. For pathogenic prokaryotes, the cell surface PC facilitates the interaction with host surface and induces attachment and invasion. In addition cell wall PC serves as scaffold for a group of choline-binding proteins that are secreted from the cells. Phosphocholine (PC) cytidylyltransferase is a key enzyme in the prokaryotic choline metabolism pathway. It has been hypothesized to consist of a choline transport system, a choline kinase, CTP:phosphocholine cytidylyltransferase, and a choline phosphotransferase that transfers P-Cho from CDP-Cho to either lipoteichoic acid or lipopolysaccharide.
Pssm-ID: 133014 [Multi-domain] Cd Length: 229 Bit Score: 60.71 E-value: 8.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 6 AVIPAGGWGTRFLPTTKSQPKEMLPLVDRPIIHYAVEEVVRCGAELVVIVSSLGKRAVEDYFDKNADLELFLERKGDT-- 83
Cdd:cd02523 1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKKYPNIKFVYNPDYAEtn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 84 ---SLlhkvrQLAdmadicyvrqKEQLglghavltakqvvgNEPFMLVLPDDLFEqqERVLQRMADIfeQHQASVLAVRR 160
Cdd:cd02523 81 niySL-----YLA----------RDFL--------------DEDFLLLEGDVVFD--PSILERLLSS--PADNAILVDKK 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 161 VNEDQvsrygiIEASSIGDRTYRVTSLVEKPKREEAPsNLAIMGRYILTPQ----VFEELENTSPGAGKEIQLTDGLRRL 236
Cdd:cd02523 128 TKEWE------DEYVKDLDDAGVLLGIISKAKNLEEI-QGEYVGISKFSPEdadrLAEALEELIEAGRVNLYYEDALQRL 200
|
250
....*....|....
gi 1490726163 237 LSRQAIYAYEVEGD 250
Cdd:cd02523 201 ISEEGVKVKDISDG 214
|
|
| glmU |
PRK14355 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
6-190 |
2.31e-10 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237685 [Multi-domain] Cd Length: 459 Bit Score: 60.91 E-value: 2.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 6 AVIPAGGWGTRFlpttKS-QPKEMLPLVDRPIIHYAVEEVVRCGAELVVIVSSLGKRAVEDYFdknadlelflerkgdts 84
Cdd:PRK14355 6 AIILAAGKGTRM----KSdLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHF----------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 85 llhkvrqlADMADICYVRQKEQLGLGHAVLTAKQVV-GNEPFMLVLPDDLFEQQERVLQRMADIFEQHQAsVLAVRRVNE 163
Cdd:PRK14355 65 --------AGDGDVSFALQEEQLGTGHAVACAAPALdGFSGTVLILCGDVPLLRAETLQGMLAAHRATGA-AVTVLTARL 135
|
170 180
....*....|....*....|....*..
gi 1490726163 164 DQVSRYGIIeassIGDRTYRVTSLVEK 190
Cdd:PRK14355 136 ENPFGYGRI----VRDADGRVLRIVEE 158
|
|
| GT2_GlmU_N_bac |
cd02540 |
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ... |
6-173 |
2.32e-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: 56.37 E-value: 2.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 6 AVIPAGGWGTRFlpttKSQ-PKEMLPLVDRPIIHYAVEEVVRCGAELVVIVSSLGKRAVEDYFDKNadlelflerkgdts 84
Cdd:cd02540 1 AVILAAGKGTRM----KSDlPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVKKALANP-------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 85 llhkvrqladmaDICYVRQKEQLGLGHAVLTAKQVVGN-EPFMLVLPDD--LFEQQerVLQRMADIFEQHQA--SVLAVR 159
Cdd:cd02540 63 ------------NVEFVLQEEQLGTGHAVKQALPALKDfEGDVLVLYGDvpLITPE--TLQRLLEAHREAGAdvTVLTAE 128
|
170 180
....*....|....*....|....*
gi 1490726163 160 -----------RVNEDQVSRygIIE 173
Cdd:cd02540 129 ledptgygriiRDGNGKVLR--IVE 151
|
|
| COG1213 |
COG1213 |
Choline kinase [Lipid transport and metabolism]; |
5-69 |
2.46e-08 |
|
Choline kinase [Lipid transport and metabolism];
Pssm-ID: 440826 [Multi-domain] Cd Length: 236 Bit Score: 53.71 E-value: 2.46e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1490726163 5 KAVIPAGGWGTRFLPTTKSQPKEMLPLVDRPIIHYAVEEVVRCGAELVVIVSSLGKRAVEDYFDK 69
Cdd:COG1213 1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEALAR 65
|
|
| GDP-M1P_Guanylyltransferase |
cd02509 |
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ... |
5-221 |
2.82e-08 |
|
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: 53.73 E-value: 2.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 5 KAVIPAGGWGTRFLP-TTKSQPKEMLPLV-DRPIIHYAVE---EVVRCGAELVVIVSSLGKRAVEDYFDKNADLELFLER 79
Cdd:cd02509 2 YPVILAGGSGTRLWPlSRESYPKQFLKLFgDKSLLQQTLDrlkGLVPPDRILVVTNEEYRFLVREQLPEGLPEENIILEP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 80 KG-DTsllhkvrqladMADICYvrqkeqlglghAVLTAKQVVGNEPfMLVLPDDLFEQQErvlqrmaDIFEQ--HQASVL 156
Cdd:cd02509 82 EGrNT-----------APAIAL-----------AALYLAKRDPDAV-LLVLPSDHLIEDV-------EAFLKavKKAVEA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 157 AvrrvNEDQV-----------SRYGIIEA-SSIGDRTYRVTSLVEKPKREEAPSNLAiMGRY-------ILTPQVF-EEL 216
Cdd:cd02509 132 A----EEGYLvtfgikptrpeTGYGYIEAgEKLGGGVYRVKRFVEKPDLETAKEYLE-SGNYlwnsgifLFRAKTFlEEL 206
|
....*
gi 1490726163 217 ENTSP 221
Cdd:cd02509 207 KKHAP 211
|
|
| eIF-2B_gamma_N_like |
cd02507 |
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ... |
5-66 |
3.19e-08 |
|
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: 53.03 E-value: 3.19e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1490726163 5 KAVIPAGGWGTRFLPTTKSQPKEMLPLVDRPIIHYAVEEVVRCGAELVVIVSSLGKRAVEDY 66
Cdd:cd02507 2 QAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQAIIEH 63
|
|
| glmU |
PRK14353 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
1-118 |
4.88e-08 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184642 [Multi-domain] Cd Length: 446 Bit Score: 53.71 E-value: 4.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 1 MRPRKAVIPAGGWGTRFlpttKSQ-PKEMLPLVDRPIIHYAVEEVVRCGAELVVIVSSLGKRAVEDYfdknadlelfler 79
Cdd:PRK14353 3 DRTCLAIILAAGEGTRM----KSSlPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGPGAEAVAAA------------- 65
|
90 100 110
....*....|....*....|....*....|....*....
gi 1490726163 80 kgdtsllhkVRQLADMADIcyVRQKEQLGLGHAVLTAKQ 118
Cdd:PRK14353 66 ---------AAKIAPDAEI--FVQKERLGTAHAVLAARE 93
|
|
| glmU |
PRK14358 |
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ... |
2-241 |
7.15e-08 |
|
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase; Provisional
Pssm-ID: 237688 [Multi-domain] Cd Length: 481 Bit Score: 53.06 E-value: 7.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 2 RPRKAVIPAGGWGTRFlptTKSQPKEMLPLVDRPIIHYAVEEVVRCGAELVVIVSSLGKRAVEDYfdknadlelfLERKG 81
Cdd:PRK14358 6 RPLDVVILAAGQGTRM---KSALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGAEQVEAA----------LQGSG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 82 dtsllhkvrqladmadICYVRQKEQLGLGHAVLTAKQVVGN-EPFMLVLPDDLFEQQERVLQRMADIFEQHqASVLAVRR 160
Cdd:PRK14358 73 ----------------VAFARQEQQLGTGDAFLSGASALTEgDADILVLYGDTPLLRPDTLRALVADHRAQ-GSAMTILT 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 161 VNEDQVSRYGIIEASSIGdrtyRVTSLVEkpKREEAPSNLAI----MGRYIL---TPQVFEELENTSPgAGkEIQLTD-- 231
Cdd:PRK14358 136 GELPDATGYGRIVRGADG----AVERIVE--QKDATDAEKAIgefnSGVYVFdarAPELARRIGNDNK-AG-EYYLTDll 207
|
250
....*....|
gi 1490726163 232 GLRRLLSRQA 241
Cdd:PRK14358 208 GLYRAGGAQV 217
|
|
| glmU |
PRK14354 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
4-155 |
8.96e-08 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184643 [Multi-domain] Cd Length: 458 Bit Score: 52.91 E-value: 8.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 4 RKAVIPAGGWGTRFlpttKSQ-PKEMLPLVDRPIIHYAVEEVVRCGAELVVIVssLGKRAvedyfdknadlELFLERKGD 82
Cdd:PRK14354 3 RYAIILAAGKGTRM----KSKlPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTV--VGHGA-----------EEVKEVLGD 65
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1490726163 83 TSLlhkvrqladmadicYVRQKEQLGLGHAVLTAKQVVGNEPFM-LVLPDD--LFEQQerVLQRMADIFEQHQASV 155
Cdd:PRK14354 66 RSE--------------FALQEEQLGTGHAVMQAEEFLADKEGTtLVICGDtpLITAE--TLKNLIDFHEEHKAAA 125
|
|
| G1P_cytidylyltransferase |
cd02524 |
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ... |
6-249 |
1.31e-07 |
|
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; Alpha-D-Glucose-1-phosphate Cytidylyltransferase catalyzes the production of CDP-D-Glucose from alpha-D-Glucose-1-phosphate and MgCTP as substrate. CDP-D-Glucose is the precursor for synthesizing four of the five naturally occurring 3,6-dideoxy sugars-abequose (3,6-dideoxy-D-Xylo-hexose), ascarylose (3,6-dideoxy-L-arabino-hexose), paratose (3,6-dideoxy-D-ribohexose), and tyvelose (3,6-dideoxy-D-arabino-hexose. Deoxysugars are ubiquitous in nature where they function in a variety of biological processes, including cell adhesion, immune response, determination of ABO blood groups, fertilization, antibiotic function, and microbial pathogenicity.
Pssm-ID: 133015 [Multi-domain] Cd Length: 253 Bit Score: 51.42 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 6 AVIPAGGWGTRFLPTTKSQPKEMLPLVDRPII--------HYAVEE-VVRCGAELVVIvsslgKRAVEDYFDKNADLeLF 76
Cdd:cd02524 1 VVILAGGLGTRLSEETELKPKPMVEIGGRPILwhimkiysHYGHNDfILCLGYKGHVI-----KEYFLNYFLHNSDV-TI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 77 LERKGDTSLLHkvrQLADMADICYVrqkeQLGL----GHAVLTAKQVVGN-EPFMLVLPDDLFEQQervlqrMADIFEQH 151
Cdd:cd02524 75 DLGTNRIELHN---SDIEDWKVTLV----DTGLntmtGGRLKRVRRYLGDdETFMLTYGDGVSDVN------INALIEFH 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 152 Q-----ASVLAVRrvnedQVSRYGIIEASSIGdrtyRVTSLVEKPKREEAPSNlaiMGRYILTPQVFEELENtspgaGKE 226
Cdd:cd02524 142 RshgklATVTAVH-----PPGRFGELDLDDDG----QVTSFTEKPQGDGGWIN---GGFFVLEPEVFDYIDG-----DDT 204
|
250 260
....*....|....*....|...
gi 1490726163 227 IQLTDGLRRLLSRQAIYAYEVEG 249
Cdd:cd02524 205 VFEREPLERLAKDGELMAYKHTG 227
|
|
| eIF-2B_epsilon_N |
cd04197 |
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ... |
6-69 |
3.39e-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: 49.91 E-value: 3.39e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1490726163 6 AVIPAGGWGTRFLPTTKSQPKEMLPLVDRPIIHYAVEEVVRCGAELVVIVSSLGKRAVEDYFDK 69
Cdd:cd04197 3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQIKEYIEK 66
|
|
| glmU |
PRK14357 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
5-231 |
7.91e-07 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237687 [Multi-domain] Cd Length: 448 Bit Score: 50.15 E-value: 7.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 5 KAVIPAGGWGTRFlpttKSQ-PKEMLPLVDRPIIHYAVEEVVRCGAELVVIVSSlGKRAVEDYFDKnaDLELFLerkgdt 83
Cdd:PRK14357 2 RALVLAAGKGTRM----KSKiPKVLHKISGKPMINWVIDTAKKVAQKVGVVLGH-EAELVKKLLPE--WVKIFL------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 84 sllhkvrqladmadicyvrQKEQLGLGHAVLTAKQVVGNEPFMLVLPDDLFEQQERVLQRMADIFEQHQASVLAVRRVNE 163
Cdd:PRK14357 69 -------------------QEEQLGTAHAVMCARDFIEPGDDLLILYGDVPLISENTLKRLIEEHNRKGADVTILVADLE 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1490726163 164 DQvSRYGIIeassIGDR-TYRVTSLVEKPKRE----EAPSNLAIM-GRYILtpQVFEELENTSpgAGKEIQLTD 231
Cdd:PRK14357 130 DP-TGYGRI----IRDGgKYRIVEDKDAPEEEkkikEINTGIYVFsGDFLL--EVLPKIKNEN--AKGEYYLTD 194
|
|
| eIF-2B_gamma_N |
cd04198 |
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ... |
5-55 |
1.19e-06 |
|
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: 48.42 E-value: 1.19e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1490726163 5 KAVIPAGGWGTRFLPTTKSQPKEMLPLVDRPIIHYAVEEVVRCGAELVVIV 55
Cdd:cd04198 2 QAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVV 52
|
|
| glgC |
PRK05293 |
glucose-1-phosphate adenylyltransferase; Provisional |
142-256 |
4.44e-06 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 179997 [Multi-domain] Cd Length: 380 Bit Score: 47.56 E-value: 4.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 142 QRMADIFEQHQASV-LAVRRVNEDQVSRYGIIEAssigDRTYRVTSLVEKPKREEapSNLAIMGRYILTPQVFEEL---- 216
Cdd:PRK05293 134 DKMLDYHKEKEADVtIAVIEVPWEEASRFGIMNT----DENMRIVEFEEKPKNPK--SNLASMGIYIFNWKRLKEYlied 207
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1490726163 217 ---ENTSPGAGKEI---QLTDGLRrllsrqaIYAYEVEGDYYDAGT 256
Cdd:PRK05293 208 eknPNSSHDFGKNViplYLEEGEK-------LYAYPFKGYWKDVGT 246
|
|
| glgC |
PRK02862 |
glucose-1-phosphate adenylyltransferase; Provisional |
141-227 |
2.00e-05 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 179486 [Multi-domain] Cd Length: 429 Bit Score: 45.65 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 141 LQRM--ADIFEQHQAS----VLAVRRVNEDQVSRYGIIEAssigDRTYRVTSLVEKPKRE-----------------EAP 197
Cdd:PRK02862 127 LYRMdyRLFVQHHRETgadiTLAVLPVDEKDASGFGLMKT----DDDGRITEFSEKPKGDelkamavdtsrlglspeEAK 202
|
90 100 110
....*....|....*....|....*....|....*
gi 1490726163 198 SN--LAIMGRYILTPQVFEELENTSPGA---GKEI 227
Cdd:PRK02862 203 GKpyLASMGIYVFSRDVLFDLLNKNPEYtdfGKEI 237
|
|
| CDP-ME_synthetase |
cd02516 |
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ... |
6-57 |
2.13e-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: 44.44 E-value: 2.13e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1490726163 6 AVIPAGGWGTRFlptTKSQPKEMLPLVDRPIIHYAVEEVVRCGA-ELVVIVSS 57
Cdd:cd02516 3 AIILAAGSGSRM---GADIPKQFLELGGKPVLEHTLEAFLAHPAiDEIVVVVP 52
|
|
| NTP_transf_3 |
pfam12804 |
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ... |
6-163 |
2.32e-05 |
|
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: 43.72 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 6 AVIPAGGWGTRFlpttkSQPKEMLPLVDRPIIHYAVEEVVRCGAELVVIVsslGKRAVEDYFDKnadlelflerkgdtsl 85
Cdd:pfam12804 1 AVILAGGRSSRM-----GGDKALLPLGGKPLLERVLERLRPAGDEVVVVA---NDEEVLAALAG---------------- 56
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1490726163 86 lHKVRQLADMAdicyvrqkEQLGLGHAVLTAKQVVGNEPFMLVLPDDLFEQQERVLQRMADIFEQHQASVLAVRRVNE 163
Cdd:pfam12804 57 -LGVPVVPDPD--------PGQGPLAGLLAALRAAPGADAVLVLACDMPFLTPELLRRLLAAAEESGADIVVPVYDGG 125
|
|
| ispD |
TIGR00453 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ... |
6-57 |
1.10e-04 |
|
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: 42.66 E-value: 1.10e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1490726163 6 AVIPAGGWGTRFlptTKSQPKEMLPLVDRPIIHYAVEEVVRCGA-ELVVIVSS 57
Cdd:TIGR00453 2 AVIPAAGRGTRF---GSGVPKQYLELGGRPLLEHALDAFLAHPAiDEVVVVVS 51
|
|
| glmU |
PRK14360 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
8-155 |
1.25e-04 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184646 [Multi-domain] Cd Length: 450 Bit Score: 42.99 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 8 IPAGGWGTRFlpttKSQ-PKEMLPLVDRPIihyaVEEVVRCGAEL-----VVIVSSLGKRaVEDYFDKNADLElflerkg 81
Cdd:PRK14360 6 ILAAGKGTRM----KSSlPKVLHPLGGKSL----VERVLDSCEELkpdrrLVIVGHQAEE-VEQSLAHLPGLE------- 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1490726163 82 dtsllhkvrqladmadicYVRQKEQLGLGHAVLTAKQVV-GNEPFMLVLPDDLFEQQERVLQRMADIFEQHQASV 155
Cdd:PRK14360 70 ------------------FVEQQPQLGTGHAVQQLLPVLkGFEGDLLVLNGDVPLLRPETLEALLNTHRSSNADV 126
|
|
| ispD |
PRK00155 |
D-ribitol-5-phosphate cytidylyltransferase; |
6-56 |
2.51e-04 |
|
D-ribitol-5-phosphate cytidylyltransferase;
Pssm-ID: 234670 Cd Length: 227 Bit Score: 41.66 E-value: 2.51e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1490726163 6 AVIPAGGWGTRFLPTtksQPKEMLPLVDRPIIHYAVEEVVRCGA--ELVVIVS 56
Cdd:PRK00155 6 AIIPAAGKGSRMGAD---RPKQYLPLGGKPILEHTLEAFLAHPRidEIIVVVP 55
|
|
| MocA |
COG2068 |
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism]; |
6-64 |
9.65e-04 |
|
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
Pssm-ID: 441671 [Multi-domain] Cd Length: 195 Bit Score: 39.37 E-value: 9.65e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1490726163 6 AVIPAGGWGTRFlpttkSQPKEMLPLVDRPIIHYAVEEVVRCGAELVVIVssLGKRAVE 64
Cdd:COG2068 6 AIILAAGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPVVVV--LGADAEE 57
|
|
| glgC |
PRK00725 |
glucose-1-phosphate adenylyltransferase; Provisional |
173-274 |
1.22e-03 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 234824 [Multi-domain] Cd Length: 425 Bit Score: 40.21 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 173 EASSIG----DRTYRVTSLVEKPKREEA-PSN----LAIMGRYILTPQV-FEELE------NTSPGAGKEIqltdgLRRL 236
Cdd:PRK00725 170 EASAFGvmavDENDRITAFVEKPANPPAmPGDpdksLASMGIYVFNADYlYELLEedaedpNSSHDFGKDI-----IPKI 244
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1490726163 237 LSRQAIYAY---------EVEGDYY--DAGTPLGWIKATIALALKHPEM 274
Cdd:PRK00725 245 VEEGKVYAHpfsdscvrsDPEEEPYwrDVGTLDAYWQANLDLASVTPEL 293
|
|
| GT2_BcE_like |
cd04183 |
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ... |
7-206 |
1.43e-03 |
|
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: 39.16 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 7 VIPAGGWGTRFLPTTKSQPKEMLPLVDRPIIHYAVEEVVR-CGAELVVIVSslgKRAVEDYFDKNAdlelflerkgdTSL 85
Cdd:cd04183 2 IIPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEWVIESLAKiFDSRFIFICR---DEHNTKFHLDES-----------LKL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 86 LHKVrqladmADIcYVRQKEQLGLGHAVLTA-KQVVGNEPFMLVLPDDLFEqqervlqrmADIFeqhqASVLAVRRVNED 164
Cdd:cd04183 68 LAPN------ATV-VELDGETLGAACTVLLAaDLIDNDDPLLIFNCDQIVE---------SDLL----AFLAAFRERDLD 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1490726163 165 QvsryGIIEASSIGDR-TYRVT---SLVEKPKREEAPSNLAIMGRY 206
Cdd:cd04183 128 G----GVLTFFSSHPRwSYVKLdenGRVIETAEKEPISDLATAGLY 169
|
|
| GT_2_like_f |
cd04182 |
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ... |
6-157 |
1.58e-03 |
|
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: 38.70 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726163 6 AVIPAGGWGTRFlpttkSQPKEMLPLVDRPIIHYAVEEVVRCGAELVVIVssLGKRAVEdyfdknadlelflerkgdtsl 85
Cdd:cd04182 3 AIILAAGRSSRM-----GGNKLLLPLDGKPLLRHALDAALAAGLSRVIVV--LGAEADA--------------------- 54
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1490726163 86 lhkVRQLADMADICYVRQKE-QLGLGHAVLTA-KQVVGNEPFMLVLPDDLFEQQERVLQRMADIFEQHQASVLA 157
Cdd:cd04182 55 ---VRAALAGLPVVVVINPDwEEGMSSSLAAGlEALPADADAVLILLADQPLVTAETLRALIDAFREDGAGIVA 125
|
|
| IspD |
COG1211 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ... |
7-56 |
2.39e-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: 38.57 E-value: 2.39e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1490726163 7 VIPAGGWGTRFlptTKSQPKEMLPLVDRPIIHYAVEEVVRCG--AELVVIVS 56
Cdd:COG1211 1 IIPAAGSGSRM---GAGIPKQFLPLGGKPVLEHTLEAFLAHPriDEIVVVVP 49
|
|
| |
