|
Name |
Accession |
Description |
Interval |
E-value |
| GalU |
COG1210 |
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis]; |
2-289 |
0e+00 |
|
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440823 [Multi-domain] Cd Length: 288 Bit Score: 552.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 2 KRVRKAIIPAAGLGTRFLPATKAMPKEMLPIVDKPTIQYIVEEAIKSGIEDIIIVTGKTKRSIEDHFDNAFELEQNLLEK 81
Cdd:COG1210 1 MKIRKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVTGRGKRAIEDHFDRSYELEATLEAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 82 KKYELLEKVQASSKMVDIHYIRQKEPKGLGHAVWCARKFIGDEPFAVLLGDDIVQAEKPCLRQLIEEYDKTLSSVIGVQT 161
Cdd:COG1210 81 GKEELLEEVRSISPLANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSEKPCLKQMIEVYEETGGSVIAVQE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 162 VPEDETHRYGIIDPLEQEGRRYQVRNFVEKPAAGTAPSNLAIMGRYVLTPEIFMFLEQQHVGAGGEIQLTDAIQNLNEIQ 241
Cdd:COG1210 161 VPPEEVSKYGIVDGEEIEGGVYRVTGLVEKPAPEEAPSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDAIAALAKEE 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1207742263 242 RVFAYDFEGKRYDVGEKLGFVQTTIEMALQHPELRDDMVPMMQKILEE 289
Cdd:COG1210 241 PVYAYEFEGKRYDCGDKLGYLKATVEFALKRPDLGEEFREYLKELLKE 288
|
|
| UGPase_prokaryotic |
cd02541 |
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ... |
5-271 |
8.62e-166 |
|
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: 460.46 E-value: 8.62e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 5 RKAIIPAAGLGTRFLPATKAMPKEMLPIVDKPTIQYIVEEAIKSGIEDIIIVTGKTKRSIEDHFDNAFELEQNLLEKKKY 84
Cdd:cd02541 1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRGKRAIEDHFDRSYELEETLEKKGKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 85 ELLEKVQASSKMVDIHYIRQKEPKGLGHAVWCARKFIGDEPFAVLLGDDIVQAEKPCLRQLIEEYDKTLSSVIGVQTVPE 164
Cdd:cd02541 81 DLLEEVRIISDLANIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLIDSKEPCLKQLIEAYEKTGASVIAVEEVPP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 165 DETHRYGIIDPLEQEGRRYQVRNFVEKPAAGTAPSNLAIMGRYVLTPEIFMFLEQQHVGAGGEIQLTDAIQNLNEIQRVF 244
Cdd:cd02541 161 EDVSKYGIVKGEKIDGDVFKVKGLVEKPKPEEAPSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTDAIAKLLEEEPVY 240
|
250 260
....*....|....*....|....*..
gi 1207742263 245 AYDFEGKRYDVGEKLGFVQTTIEMALQ 271
Cdd:cd02541 241 AYVFEGKRYDCGNKLGYLKATVEFALK 267
|
|
| galU |
TIGR01099 |
UTP--glucose-1-phosphate uridylyltransferase; Built to distinquish between the highly similar ... |
5-264 |
9.58e-156 |
|
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: 434.86 E-value: 9.58e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 5 RKAIIPAAGLGTRFLPATKAMPKEMLPIVDKPTIQYIVEEAIKSGIEDIIIVTGKTKRSIEDHFDNAFELEQNLLEKKKY 84
Cdd:TIGR01099 1 RKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYIVEEAVEAGIEEIVFVTGRGKRAIEDHFDYSYELEHQLEKRGKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 85 ELLEKVQASSKMVDIHYIRQKEPKGLGHAVWCARKFIGDEPFAVLLGDDIVQAEKPCLRQLIEEYDKTLSSVIGVQTVPE 164
Cdd:TIGR01099 81 ELLEEVRKISNLATIFYVRQKEQKGLGHAVLCARPFVGDEPFAVILGDDIVVNEEPALKQMIKAYEKTGCSIIAVQEVPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 165 DETHRYGIIDPLEQEGRRYQVRNFVEKPAAGTAPSNLAIMGRYVLTPEIFMFLEQQHVGAGGEIQLTDAIQNLNEIQRVF 244
Cdd:TIGR01099 161 EEVSKYGVIDGEGIEKDLYKVKNMVEKPKPEEAPSNLAIVGRYILTPDIFDLLEETPPGKGGEIQLTDAINKLLENETVL 240
|
250 260
....*....|....*....|
gi 1207742263 245 AYDFEGKRYDVGEKLGFVQT 264
Cdd:TIGR01099 241 AYKFNGKRYDCGSKLGYLEA 260
|
|
| PRK13389 |
PRK13389 |
UTP--glucose-1-phosphate uridylyltransferase GalU; |
2-289 |
1.54e-85 |
|
UTP--glucose-1-phosphate uridylyltransferase GalU;
Pssm-ID: 184021 [Multi-domain] Cd Length: 302 Bit Score: 258.68 E-value: 1.54e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 2 KRVRKAIIPAAGLGTRFLPATKAMPKEMLPIVDKPTIQYIVEEAIKSGIEDIIIVTGKTKRSIEDHFDNAFELEQNLLEK 81
Cdd:PRK13389 6 TKVKKAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFDTSFELEAMLEKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 82 KKYELLEKVQA-SSKMVDIHYIRQKEPKGLGHAVWCARKFIGDEPFAVLLGDDIVQA-----EKPCLRQLIEEYDKTLSS 155
Cdd:PRK13389 86 VKRQLLDEVQSiCPPHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILDEyesdlSQDNLAEMIRRFDETGHS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 156 VIGVQtvPEDETHRYGIIDPLEQE---GRRYQVRNFVEKPAAGTAPSNLAIMGRYVLTPEIFMFLEQQHVGAGGEIQLTD 232
Cdd:PRK13389 166 QIMVE--PVADVTAYGVVDCKGVElapGESVPMVGVVEKPKADVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTD 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1207742263 233 AIQNLNEIQRVFAYDFEGKRYDVGEKLGFVQTTIEMALQHPELRDDMVPMMQKILEE 289
Cdd:PRK13389 244 AIDMLIEKETVEAYHMKGKSHDCGNKLGYMQAFVEYGIRHNTLGTEFKAWLEEEMGI 300
|
|
| PRK10122 |
PRK10122 |
UTP--glucose-1-phosphate uridylyltransferase GalF; |
6-289 |
3.43e-73 |
|
UTP--glucose-1-phosphate uridylyltransferase GalF;
Pssm-ID: 182252 [Multi-domain] Cd Length: 297 Bit Score: 226.69 E-value: 3.43e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 6 KAIIPAAGLGTRFLPATKAMPKEMLPIVDKPTIQYIVEEAIKSGIEDIIIVTGKTKRSIEDHFDNAFELEQNLLEKKKYE 85
Cdd:PRK10122 5 KAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAVENHFDTSYELESLLEQRVKRQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 86 LLEKVQA-SSKMVDIHYIRQKEPKGLGHAVWCARKFIGDEPFAVLLGDDIVQAE-----KPCLRQLIEEYDKTLSSVIGV 159
Cdd:PRK10122 85 LLAEVQSiCPPGVTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPDVVIDDAsadplRYNLAAMIARFNETGRSQVLA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 160 QTVPEDEThRYGII---DPLEQEGRRYQVRNFVEKP-AAGTAPSNLAIMGRYVLTPEIFMFLEQQHVGAGGEIQLTDAIQ 235
Cdd:PRK10122 165 KRMPGDLS-EYSVIqtkEPLDREGKVSRIVEFIEKPdQPQTLDSDLMAVGRYVLSADIWPELERTEPGAWGRIQLTDAIA 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1207742263 236 NLNEIQRVFAYDFEGKRYDVGEKLGFVQTTIEMALQHPELRDDMVPMMQKILEE 289
Cdd:PRK10122 244 ELAKKQSVDAMLMTGDSYDCGKKMGYMQAFVKYGLRNLKEGAKFRKGIEKLLSE 297
|
|
| NTP_transferase |
cd04181 |
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ... |
7-256 |
1.29e-64 |
|
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: 202.04 E-value: 1.29e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 7 AIIPAAGLGTRFLPATKAMPKEMLPIVDKPTIQYIVEEAIKSGIEDIIIVTGKTKRSIEDHFDNAFELEqnllekkkyel 86
Cdd:cd04181 1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGSKFG----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 87 lekvqasskmVDIHYIRQKEPKGLGHAVWCARKFIGDEPFAVLLGDDIVQAEkpcLRQLIEEY-DKTLSSVIGVQTVPED 165
Cdd:cd04181 70 ----------VNIEYVVQEEPLGTAGAVRNAEDFLGDDDFLVVNGDVLTDLD---LSELLRFHrEKGADATIAVKEVEDP 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 166 EthRYGIIDpLEQEGRryqVRNFVEKPAAGtaPSNLAIMGRYVLTPEIFMFLEqqHVGAGGEIQLTDAIQNLNEIQRVFA 245
Cdd:cd04181 137 S--RYGVVE-LDDDGR---VTRFVEKPTLP--ESNLANAGIYIFEPEILDYIP--EILPRGEDELTDAIPLLIEEGKVYG 206
|
250
....*....|.
gi 1207742263 246 YDFEGKRYDVG 256
Cdd:cd04181 207 YPVDGYWLDIG 217
|
|
| RmlA1 |
COG1209 |
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis]; |
5-237 |
3.88e-54 |
|
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440822 [Multi-domain] Cd Length: 294 Bit Score: 177.59 E-value: 3.88e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 5 RKAIIPAAGLGTRFLPATKAMPKEMLPIVDKPTIQYIVEEAIKSGIEDIIIVTGKtkrsiedhfdnafeleqnllekkky 84
Cdd:COG1209 1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTP------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 85 ELLEKVQA-----SSKMVDIHYIRQKEPKGLGHAVWCARKFIGDEPFAVLLGDDIVQAekPCLRQLIEEYDK-TLSSVIG 158
Cdd:COG1209 56 EDGPQFERllgdgSQLGIKISYAVQPEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYG--DGLSELLREAAArESGATIF 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207742263 159 VQTVPEDEthRYGIIDpLEQEGRryqVRNFVEKPAagTAPSNLAIMGRYVLTPEIFMFLEQQHVGAGGEIQLTDAIQNL 237
Cdd:COG1209 134 GYKVEDPE--RYGVVE-FDEDGR---VVSLEEKPK--EPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAY 204
|
|
| G1P_TT_long |
cd04189 |
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ... |
6-256 |
5.74e-54 |
|
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family is the long form of Glucose-1-phosphate thymidylyltransferase. Glucose-1-phosphate thymidylyltransferase catalyses the formation of dTDP-glucose, from dTTP and glucose 1-phosphate. It is the first enzyme in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme.There are two forms of Glucose-1-phosphate thymidylyltransferase in bacteria and archeae; short form and long form. The long form, which has an extra 50 amino acids c-terminal, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced.The long from enzymes also have a left-handed parallel helix domain at the c-terminus, whereas, th eshort form enzymes do not have this domain. The homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose.
Pssm-ID: 133032 [Multi-domain] Cd Length: 236 Bit Score: 175.45 E-value: 5.74e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 6 KAIIPAAGLGTRFLPATKAMPKEMLPIVDKPTIQYIVEEAIKSGIEDIIIVTGKTKRSIEDHFDNafeleqnllekkkye 85
Cdd:cd04189 2 KGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEALGD--------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 86 llekvqASSKMVDIHYIRQKEPKGLGHAVWCARKFIGDEPFAVLLGDDIVQAEkpcLRQLIEEYDKTLSSV-IGVQTVPe 164
Cdd:cd04189 67 ------GSRFGVRITYILQEEPLGLAHAVLAARDFLGDEPFVVYLGDNLIQEG---ISPLVRDFLEEDADAsILLAEVE- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 165 dETHRYGIIDPleqEGRRyqVRNFVEKPAagTAPSNLAIMGRYVLTPEIFMFLEQQHVGAGGEIQLTDAIQNLNEI-QRV 243
Cdd:cd04189 137 -DPRRFGVAVV---DDGR--IVRLVEKPK--EPPSNLALVGVYAFTPAIFDAISRLKPSWRGELEITDAIQWLIDRgRRV 208
|
250
....*....|...
gi 1207742263 244 FAYDFEGKRYDVG 256
Cdd:cd04189 209 GYSIVTGWWKDTG 221
|
|
| GCD1 |
COG1208 |
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ... |
6-256 |
4.51e-51 |
|
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: 168.02 E-value: 4.51e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 6 KAIIPAAGLGTRFLPATKAMPKEMLPIVDKPTIQYIVEEAIKSGIEDIIIVTGKTKRSIEDHFDNAFELEqnllekkkye 85
Cdd:COG1208 1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRFG---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 86 llekvqasskmVDIHYIRQKEPKGLGHAVWCARKFIGDEPFAVLLGDDIVQAEkpcLRQLIEEYDKTlSSVIGVQTVPED 165
Cdd:COG1208 71 -----------VRITYVDEGEPLGTGGALKRALPLLGDEPFLVLNGDILTDLD---LAALLAFHREK-GADATLALVPVP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 166 ETHRYGIIDpLEQEGRryqVRNFVEKPAAgtAPSNLAIMGRYVLTPEIFMFLEqqhvgAGGEIQLTDAIQNLNEIQRVFA 245
Cdd:COG1208 136 DPSRYGVVE-LDGDGR---VTRFVEKPEE--PPSNLINAGIYVLEPEIFDYIP-----EGEPFDLEDLLPRLIAEGRVYG 204
|
250
....*....|.
gi 1207742263 246 YDFEGKRYDVG 256
Cdd:COG1208 205 YVHDGYWLDIG 215
|
|
| NTP_transferase |
pfam00483 |
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ... |
6-256 |
2.74e-36 |
|
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: 130.07 E-value: 2.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 6 KAIIPAAGLGTRFLPATKAMPKEMLPIVDK-PTIQYIVEEAIKSGIEDIIIVTGKTKRsiedhfdnaFELEQNLLEKKKY 84
Cdd:pfam00483 1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHR---------FMLNELLGDGSKF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 85 EllekvqasskmVDIHYIRQKEPKGLGHAVWCARKFIGDEPFAVL-LGDDIVQAE--KPCLRQLIEEYDKTLSSVIGVQT 161
Cdd:pfam00483 72 G-----------VQITYALQPEGKGTAPAVALAADFLGDEKSDVLvLGGDHIYRMdlEQAVKFHIEKAADATVTFGIVPV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 162 vpEDEThRYGIIDPlEQEGRryqVRNFVEKPAAGTApSNLAIMGRYVLTPEIFMFLEQQHVG-AGGEIQLTDAIQN-LNE 239
Cdd:pfam00483 141 --EPPT-GYGVVEF-DDNGR---VIRFVEKPKLPKA-SNYASMGIYIFNSGVLDFLAKYLEElKRGEDEITDILPKaLED 212
|
250
....*....|....*...
gi 1207742263 240 IQRVFAYDFEGKR-YDVG 256
Cdd:pfam00483 213 GKLAYAFIFKGYAwLDVG 230
|
|
| G1P_TT_short |
cd02538 |
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ... |
5-232 |
1.01e-28 |
|
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is the short form of glucose-1-phosphate thymidylyltransferase. Glucose-1-phosphate thymidylyltransferase catalyses the formation of dTDP-glucose, from dTTP and glucose 1-phosphate. It is the first enzyme in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme.There are two forms of Glucose-1-phosphate thymidylyltransferase in bacteria and archeae; short form and long form. The homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose. The long form, which has an extra 50 amino acids c-terminal, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced.
Pssm-ID: 133019 [Multi-domain] Cd Length: 240 Bit Score: 109.97 E-value: 1.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 5 RKAIIPAAGLGTRFLPATKAMPKEMLPIVDKPTIQYIVEEAIKSGIEDIIIVTGKtkrsieDHFDNAFELEQNllekkky 84
Cdd:cd02538 1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTP------EDLPLFKELLGD------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 85 ellekvqASSKMVDIHYIRQKEPKGLGHAVWCARKFIGDEPFAVLLGDDIVqaEKPCLRQLIEEY-DKTLSSVIGVQTVP 163
Cdd:cd02538 68 -------GSDLGIRITYAVQPKPGGLAQAFIIGEEFIGDDPVCLILGDNIF--YGQGLSPILQRAaAQKEGATVFGYEVN 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207742263 164 EDEthRYGIIDpLEQEGRryqVRNFVEKPAAgtAPSNLAIMGRYVLTPEIFMFLEQQHVGAGGEIQLTD 232
Cdd:cd02538 139 DPE--RYGVVE-FDENGR---VLSIEEKPKK--PKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITD 199
|
|
| NTP_transferase_WcbM_like |
cd06915 |
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ... |
7-220 |
1.60e-19 |
|
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: 84.91 E-value: 1.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 7 AIIPAAGLGTRFLPATKAMPKEMLPIVDKPTIQYIVEEAIKSGIEDIIIVTGKTKRSIEDHFDNAFELEqnllekkkyel 86
Cdd:cd06915 1 AVILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYLAEQIEEYFGDGYRGG----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 87 lekvqasskmVDIHYIRQKEPKGLGHAVWCARKFIGDEPFAVLLGDDIVQAEkpcLRQLIEEYDKTlSSVIGVQTVPEDE 166
Cdd:cd06915 70 ----------IRIYYVIEPEPLGTGGAIKNALPKLPEDQFLVLNGDTYFDVD---LLALLAALRAS-GADATMALRRVPD 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1207742263 167 THRYGIIDpLEQEGRryqVRNFVEKPAagTAPSNLAIMGRYVLTPEIFMFLEQQ 220
Cdd:cd06915 136 ASRYGNVT-VDGDGR---VIAFVEKGP--GAAPGLINGGVYLLRKEILAEIPAD 183
|
|
| NTP_transferase_like_2 |
cd06426 |
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ... |
7-257 |
6.65e-19 |
|
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.
Pssm-ID: 133048 [Multi-domain] Cd Length: 220 Bit Score: 82.94 E-value: 6.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 7 AIIPAAGLGTRFLPATKAMPKEMLPIVDKPTIQYIVEEAIKSGIEDIIIVTGKTKRSIEDHFDNafeleqnllekkkyel 86
Cdd:cd06426 1 VVIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNYLAEMIEDYFGD---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 87 lekvqASSKMVDIHYIRQKEPKGLGHAVWCARKFIgDEPFAVLLGDDIVQAEkpcLRQLIEEYDKTlSSVIGVQTVPEDE 166
Cdd:cd06426 65 -----GSKFGVNISYVREDKPLGTAGALSLLPEKP-TDPFLVMNGDILTNLN---YEHLLDFHKEN-NADATVCVREYEV 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 167 THRYGIIdplEQEGRRyqVRNFVEKPAAgtapSNLAIMGRYVLTPEIFmfleqQHVGAGGEIQLTDAIQNL-NEIQRVFA 245
Cdd:cd06426 135 QVPYGVV---ETEGGR--ITSIEEKPTH----SFLVNAGIYVLEPEVL-----DLIPKNEFFDMPDLIEKLiKEGKKVGV 200
|
250
....*....|..
gi 1207742263 246 YDFEGKRYDVGE 257
Cdd:cd06426 201 FPIHEYWLDIGR 212
|
|
| M1P_guanylylT_B_like_N |
cd06425 |
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ... |
6-261 |
4.69e-18 |
|
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: 81.10 E-value: 4.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 6 KAIIPAAGLGTRFLPATKAMPKEMLPIVDKPTIQYIVEEAIKSGIEDIIIvtgktkrsiedhfdnAFELEQNLLEKKKYE 85
Cdd:cd06425 2 KALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIIL---------------AVNYRPEDMVPFLKE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 86 LLEKVQasskmVDIHYIRQKEPKGLGHAVWCARKFIG--DEPFAVLLGDDIvqAEKPcLRQLIEEYDKTLS-SVIGVQTV 162
Cdd:cd06425 67 YEKKLG-----IKITFSIETEPLGTAGPLALARDLLGddDEPFFVLNSDVI--CDFP-LAELLDFHKKHGAeGTILVTKV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 163 peDETHRYGIIDPLEQEGRryqVRNFVEKPAAGTapSNLAIMGRYVLTPEIFMFLEQQHVGAGGEIqltdaIQNLNEIQR 242
Cdd:cd06425 139 --EDPSKYGVVVHDENTGR---IERFVEKPKVFV--GNKINAGIYILNPSVLDRIPLRPTSIEKEI-----FPKMASEGQ 206
|
250
....*....|....*....
gi 1207742263 243 VFAYDFEGKRYDVGEKLGF 261
Cdd:cd06425 207 LYAYELPGFWMDIGQPKDF 225
|
|
| NTP_transferase_like_1 |
cd06422 |
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ... |
6-256 |
2.98e-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: 75.69 E-value: 2.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 6 KAIIPAAGLGTRFLPATKAMPKEMLPIVDKPTIQYIVEEAIKSGIEDIIIVTGKTKRSIEDHFdnafeleqnllekkkye 85
Cdd:cd06422 1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHL----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 86 llekvQASSKMVDIHYIRqkEPKGL---GHAVWCARKFIGDEPFAVLLGdDIVQAEKPC--LRQLIEEYDKTLSSVIGVQ 160
Cdd:cd06422 64 -----GDSRFGLRITISD--EPDELletGGGIKKALPLLGDEPFLVVNG-DILWDGDLAplLLLHAWRMDALLLLLPLVR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 161 TVPEdetHRYGIIDpLEQEGRRyqvrnfveKPAAGTAPSNLAIMGRYVLTPEIFMFLEqqhvgaggeiqltDAIQNLNEI 240
Cdd:cd06422 136 NPGH---NGVGDFS-LDADGRL--------RRGGGGAVAPFTFTGIQILSPELFAGIP-------------PGKFSLNPL 190
|
250 260
....*....|....*....|...
gi 1207742263 241 -------QRVFAYDFEGKRYDVG 256
Cdd:cd06422 191 wdraiaaGRLFGLVYDGLWFDVG 213
|
|
| PRK15480 |
PRK15480 |
glucose-1-phosphate thymidylyltransferase RfbA; Provisional |
3-232 |
3.22e-16 |
|
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
Pssm-ID: 185377 [Multi-domain] Cd Length: 292 Bit Score: 77.02 E-value: 3.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 3 RVRKAIIPAAGLGTRFLPATKAMPKEMLPIVDKPTIQYIVEEAIKSGIEDIIIVTGKtkrsiedhfDNAFELEQNLLEKK 82
Cdd:PRK15480 2 KTRKGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTP---------QDTPRFQQLLGDGS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 83 KYELlekvqasskmvDIHYIRQKEPKGLGHAVWCARKFIGDEPFAVLLGDDIVQAEKpcLRQLIE-EYDKTLSSVIGVQT 161
Cdd:PRK15480 73 QWGL-----------NLQYKVQPSPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHD--LPKLMEaAVNKESGATVFAYH 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207742263 162 VPEDEthRYGIIDpLEQEGRRYQVRnfvEKPAagTAPSNLAIMGRYVLTPEIFMFLEQQHVGAGGEIQLTD 232
Cdd:PRK15480 140 VNDPE--RYGVVE-FDQNGTAISLE---EKPL--QPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITD 202
|
|
| PC_cytidylyltransferase |
cd02523 |
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ... |
7-147 |
1.17e-15 |
|
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family contains proteins similar to prokaryotic phosphocholine (P-cho) cytidylyltransferases. Phosphocholine (PC) cytidylyltransferases catalyze the transfer of a cytidine monophosphate from CTP to phosphocholine to form CDP-choline. PC is the most abundant phospholipid in eukaryotic membranes and it is also important in prokaryotic membranes. For pathogenic prokaryotes, the cell surface PC facilitates the interaction with host surface and induces attachment and invasion. In addition cell wall PC serves as scaffold for a group of choline-binding proteins that are secreted from the cells. Phosphocholine (PC) cytidylyltransferase is a key enzyme in the prokaryotic choline metabolism pathway. It has been hypothesized to consist of a choline transport system, a choline kinase, CTP:phosphocholine cytidylyltransferase, and a choline phosphotransferase that transfers P-Cho from CDP-Cho to either lipoteichoic acid or lipopolysaccharide.
Pssm-ID: 133014 [Multi-domain] Cd Length: 229 Bit Score: 74.19 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 7 AIIPAAGLGTRFLPATKAMPKEMLPIVDKPTIQYIVEEAIKSGIEDIIIVTGKTKrsieDHFDNAFEleqnllekkkyel 86
Cdd:cd02523 1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKK----EQIEELLK------------- 63
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207742263 87 lekvqassKMVDIHYIRQKEP--KGLGHAVWCARKFIgDEPFAVLLGDDIVqaEKPCLRQLIE 147
Cdd:cd02523 64 --------KYPNIKFVYNPDYaeTNNIYSLYLARDFL-DEDFLLLEGDVVF--DPSILERLLS 115
|
|
| COG1213 |
COG1213 |
Choline kinase [Lipid transport and metabolism]; |
6-167 |
2.09e-15 |
|
Choline kinase [Lipid transport and metabolism];
Pssm-ID: 440826 [Multi-domain] Cd Length: 236 Bit Score: 73.74 E-value: 2.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 6 KAIIPAAGLGTRFLPATKAMPKEMLPIVDKPTIQYIVEEAIKSGIEDIIIVTGKTKRSIEDHFDnafeleqnllekkkye 85
Cdd:COG1213 1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEALA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 86 llekvqasSKMVDIHYIRQKEPK--GLGHAVWCARKFIgDEPFAVLLGDDIVqaEKPCLRQLIEEYDktlSSVIGVQTVP 163
Cdd:COG1213 65 --------RPGPDVTFVYNPDYDetNNIYSLWLAREAL-DEDFLLLNGDVVF--DPAILKRLLASDG---DIVLLVDRKW 130
|
....
gi 1207742263 164 EDET 167
Cdd:COG1213 131 EKPL 134
|
|
| GT2_GlmU_N_bac |
cd02540 |
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ... |
7-174 |
1.45e-13 |
|
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: 68.31 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 7 AIIPAAGLGTRflpatkaM----PKEMLPIVDKPTIQYIVEEAIKSGIEDIIIVTGKTKrsiedhfdnafeleqnllekk 82
Cdd:cd02540 1 AVILAAGKGTR-------MksdlPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGA--------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 83 kyellEKVQASSKMVDIHYIRQKEPKGLGHAVWCARKFIGD--EPFAVLLGD-DIVQAEKpcLRQLIEEYDKTLSSVIGV 159
Cdd:cd02540 53 -----EQVKKALANPNVEFVLQEEQLGTGHAVKQALPALKDfeGDVLVLYGDvPLITPET--LQRLLEAHREAGADVTVL 125
|
170
....*....|....*..
gi 1207742263 160 QTVPEDEThRYG--IID 174
Cdd:cd02540 126 TAELEDPT-GYGriIRD 141
|
|
| GlmU |
COG1207 |
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ... |
5-173 |
4.27e-13 |
|
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440820 [Multi-domain] Cd Length: 457 Bit Score: 68.90 E-value: 4.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 5 RKAIIPAAGLGTRFlpatK-AMPKEMLPIVDKPTIQYIVEEAIKSGIEDIIIVTGKTKrsiedhfdnafeleqnllekkk 83
Cdd:COG1207 3 LAVVILAAGKGTRM----KsKLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGA---------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 84 yellEKVQASSKMVDIHYIRQKEPKGLGHAVWCARKFIG--DEPFAVLLGDD-IVQAEKpcLRQLIEEYDKTLSSViGVQ 160
Cdd:COG1207 57 ----EQVRAALADLDVEFVLQEEQLGTGHAVQQALPALPgdDGTVLVLYGDVpLIRAET--LKALLAAHRAAGAAA-TVL 129
|
170
....*....|....*
gi 1207742263 161 TV-PEDEThRYG-II 173
Cdd:COG1207 130 TAeLDDPT-GYGrIV 143
|
|
| eIF-2B_gamma_N_like |
cd02507 |
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ... |
6-108 |
1.58e-11 |
|
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; N-terminal domain of eEIF-2B epsilon and gamma, subunits of eukaryotic translation initiators, is a subfamily of glycosyltranferase 2 and is predicted to have glycosyltranferase activity. eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit epsilon shares sequence similarity with gamma subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.
Pssm-ID: 133001 [Multi-domain] Cd Length: 216 Bit Score: 62.66 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 6 KAIIPAAGLGTRFLPATKAMPKEMLPIVDKPTIQYIVEEAIKSGIEDIIIVTGKTKRSIEDHFDNAFELEQN-LLEKKKY 84
Cdd:cd02507 2 QAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQAIIEHLLKSKWSSLSsKMIVDVI 81
|
90 100
....*....|....*....|....
gi 1207742263 85 ELLEKVQASSKMVDIHyIRQKEPK 108
Cdd:cd02507 82 TSDLCESAGDALRLRD-IRGLIRS 104
|
|
| GlgC |
COG0448 |
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ... |
157-293 |
7.90e-11 |
|
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate transport and metabolism];
Pssm-ID: 440217 [Multi-domain] Cd Length: 377 Bit Score: 62.01 E-value: 7.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 157 IGVQTVPEDETHRYGIIDpLEQEGRryqVRNFVEKPAagTAPSNLAIMGRYVLTPEIFMFLEQQHVGAGGEIQLTDAIQN 236
Cdd:COG0448 147 VACIEVPREEASRFGVME-VDEDGR---ITEFEEKPK--DPKSALASMGIYVFNKDVLIELLEEDAPNSSHDFGKDIIPR 220
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207742263 237 LNEIQRVFAYDFEGkrY--DVGeklgfvqtTIE------MALQHPELRDDMVPMMQKIleeYTKQ 293
Cdd:COG0448 221 LLDRGKVYAYEFDG--YwrDVG--------TIDsyyeanMDLLDPEPEFNLYDPEWPI---YTKQ 272
|
|
| glmU |
PRK14355 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
7-173 |
1.10e-10 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237685 [Multi-domain] Cd Length: 459 Bit Score: 61.68 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 7 AIIPAAGLGTRFlpaTKAMPKEMLPIVDKPTIQYIVEEAIKSGIEDIIIVTGKTKRSIEDHFDNAfeleqnllekkkyel 86
Cdd:PRK14355 6 AIILAAGKGTRM---KSDLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHFAGD--------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 87 lekvqasskmVDIHYIRQKEPKGLGHAVWCARKFIGDEPFAVL-LGDDIVQAEKPCLRQLIEEYDKTlSSVIGVQTVPED 165
Cdd:PRK14355 68 ----------GDVSFALQEEQLGTGHAVACAAPALDGFSGTVLiLCGDVPLLRAETLQGMLAAHRAT-GAAVTVLTARLE 136
|
....*...
gi 1207742263 166 ETHRYGII 173
Cdd:PRK14355 137 NPFGYGRI 144
|
|
| eIF-2B_gamma_N |
cd04198 |
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ... |
6-73 |
1.58e-10 |
|
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: 59.59 E-value: 1.58e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207742263 6 KAIIPAAGLGTRFLPATKAMPKEMLPIVDKPTIQYIVEEAIKSGIEDIIIVTGKT-KRSIEDHFDNAFE 73
Cdd:cd04198 2 QAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEeQAEISTYLRSFPL 70
|
|
| LicC |
COG4750 |
CTP:phosphocholine cytidylyltransferase LicC [Cell wall/membrane/envelope biogenesis, Lipid ... |
5-58 |
2.90e-10 |
|
CTP:phosphocholine cytidylyltransferase LicC [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism];
Pssm-ID: 443784 [Multi-domain] Cd Length: 228 Bit Score: 59.07 E-value: 2.90e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1207742263 5 RKAIIPAAGLGTRFLPATKAMPKEMLPIVDKPTIQYIVEEAIKSGIEDIIIVTG 58
Cdd:COG4750 1 MNAIILAAGLGSRFAPITYETPKGLLKVNGEPLIERQIRQLHEAGITDITVVVG 54
|
|
| glmU |
PRK14354 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
5-132 |
7.96e-10 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184643 [Multi-domain] Cd Length: 458 Bit Score: 59.07 E-value: 7.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 5 RKAIIPAAGLGTRFlpaTKAMPKEMLPIVDKPTIQYIVEEAIKSGIEDIIIVTGKTKRSIEDHfdnafeleqnllekkky 84
Cdd:PRK14354 3 RYAIILAAGKGTRM---KSKLPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVGHGAEEVKEV----------------- 62
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1207742263 85 eLLEKVQasskmvdihYIRQKEPKGLGHAVWCARKFIGDEP--FAVLLGD 132
Cdd:PRK14354 63 -LGDRSE---------FALQEEQLGTGHAVMQAEEFLADKEgtTLVICGD 102
|
|
| glmU |
PRK14357 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
6-289 |
2.56e-09 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237687 [Multi-domain] Cd Length: 448 Bit Score: 57.47 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 6 KAIIPAAGLGTRFlpaTKAMPKEMLPIVDKPTIQYIVEEAIKSGIEdIIIVTGKtkrsiedhfdnafeleqnllekkKYE 85
Cdd:PRK14357 2 RALVLAAGKGTRM---KSKIPKVLHKISGKPMINWVIDTAKKVAQK-VGVVLGH-----------------------EAE 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 86 LLEKVQASskmvDIHYIRQKEPKGLGHAVWCARKFIGDEPFAVLLGDDIVQAEKPCLRQLIEEYDKTLSSVIGVQTVPED 165
Cdd:PRK14357 55 LVKKLLPE----WVKIFLQEEQLGTAHAVMCARDFIEPGDDLLILYGDVPLISENTLKRLIEEHNRKGADVTILVADLED 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 166 ETHrYGIIdplEQEGRRYQVRNFVEKP----AAGTAPSNLAIM-GRYVLtpEIFMFLEQQHvgAGGEIQLTDAiqnLNEI 240
Cdd:PRK14357 131 PTG-YGRI---IRDGGKYRIVEDKDAPeeekKIKEINTGIYVFsGDFLL--EVLPKIKNEN--AKGEYYLTDA---VNFA 199
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1207742263 241 QRVFAYDFEgkryDVGEKLGfVQTTIEMALQHPELRddmvpmmQKILEE 289
Cdd:PRK14357 200 EKVRVVKTE----DLLEITG-VNTRIQLAWLEKQLR-------MRILEE 236
|
|
| GDP-M1P_Guanylyltransferase |
cd02509 |
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ... |
6-216 |
6.60e-09 |
|
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: 55.66 E-value: 6.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 6 KAIIPAAGLGTRFLPA-TKAMPKEMLPIV-DKPTIQYIVEEAIK-SGIEDIIIVTGKtkrsiedhfdnafeleqnllekk 82
Cdd:cd02509 2 YPVILAGGSGTRLWPLsRESYPKQFLKLFgDKSLLQQTLDRLKGlVPPDRILVVTNE----------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 83 KYELLEKVQASSKMVDIHYIRQKEPKG----LGHAVWCARKFIGDEPFAVLLGDDIVQAEkpclrqliEEYDKTLSS--- 155
Cdd:cd02509 59 EYRFLVREQLPEGLPEENIILEPEGRNtapaIALAALYLAKRDPDAVLLVLPSDHLIEDV--------EAFLKAVKKave 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207742263 156 --------VIGVQ-TVPEDEthrYGIIDPLEQEGRR-YQVRNFVEKPAAGTAPSNLAiMGRYVLTPEIFMF 216
Cdd:cd02509 131 aaeegylvTFGIKpTRPETG---YGYIEAGEKLGGGvYRVKRFVEKPDLETAKEYLE-SGNYLWNSGIFLF 197
|
|
| GT_2_like_f |
cd04182 |
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ... |
7-157 |
1.11e-08 |
|
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: 53.72 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 7 AIIPAAGLGTRFlpatkAMPKEMLPIVDKPTIQYIVEEAIKSGIEDIIIVTGktkrsiedHFDNAFELEQNLLekkkyel 86
Cdd:cd04182 3 AIILAAGRSSRM-----GGNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLG--------AEADAVRAALAGL------- 62
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207742263 87 lekvqasskmvDIHYIRQKEP-KGLGHAVWCARKFIGDEP--FAVLLGDDI-VQAEKpcLRQLIEEYDKTLSSVI 157
Cdd:cd04182 63 -----------PVVVVINPDWeEGMSSSLAAGLEALPADAdaVLILLADQPlVTAET--LRALIDAFREDGAGIV 124
|
|
| M1P_guanylylT_A_like_N |
cd06428 |
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ... |
15-219 |
4.62e-08 |
|
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose pyrophosphorylase; N-terminal domain of the M1P-guanylyltransferase A-isoform like proteins: The proteins of this family are likely to be a isoform of GDP-mannose pyrophosphorylase. Their sequences are highly conserved with mannose-1-phosphate guanyltransferase, but generally about 40-60 bases longer. GDP-mannose pyrophosphorylase (GTP: alpha-d-mannose-1-phosphate guanyltransferase) catalyzes the formation of GDP-d-mannose from GTP and alpha-d-mannose-1-Phosphate. It contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain. GDP-d-mannose is the activated form of mannose for formation of cell wall lipoarabinomannan and various mannose-containing glycolipids and polysaccharides. The function of GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability. Repression of GDP-mannose pyrophosphorylase in yeast leads to phenotypes including cell lysis, defective cell wall, and failure of polarized growth and cell separation.
Pssm-ID: 133050 [Multi-domain] Cd Length: 257 Bit Score: 53.03 E-value: 4.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 15 GTRFLPATKAMPKEMLPIVDKPTIQYIVEEAIK-SGIEDIIIVTGKTKRSIEDhfdnafeleqnllekkkyeLLEKVQAS 93
Cdd:cd06428 11 GTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKvPDLKEVLLIGFYPESVFSD-------------------FISDAQQE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 94 SKmVDIHYIRQKEPKGLGHAVWCARKFI---GDEPFAVLLGDdiVQAEKPcLRQLIEEYDK-TLSSVIGVQTVPEDETHR 169
Cdd:cd06428 72 FN-VPIRYLQEYKPLGTAGGLYHFRDQIlagNPSAFFVLNAD--VCCDFP-LQELLEFHKKhGASGTILGTEASREQASN 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1207742263 170 YGIIDPLEQEGRryqVRNFVEKPaaGTAPSNLAIMGRYVLTPEIFMFLEQ 219
Cdd:cd06428 148 YGCIVEDPSTGE---VLHYVEKP--ETFVSDLINCGVYLFSPEIFDTIKK 192
|
|
| glmU |
PRK14353 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
1-234 |
4.71e-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: 4.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 1 MKRVRKAIIPAAGLGTRFlpaTKAMPKEMLPIVDKPTIQYIVEEAIKSGIEDIIIVTGKTKRSIEDHfdnafeleqnlle 80
Cdd:PRK14353 2 TDRTCLAIILAAGEGTRM---KSSLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGPGAEAVAAA------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 81 kkkyellekvqASSKMVDIHYIRQKEPKGLGHAVWCAR----KFIGDepFAVLLGDD-IVQAEKpcLRQLIEEY-DKTLS 154
Cdd:PRK14353 66 -----------AAKIAPDAEIFVQKERLGTAHAVLAARealaGGYGD--VLVLYGDTpLITAET--LARLRERLaDGADV 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 155 SVIGVQTvpeDETHRYGIIdpLEQEGRRYQVRNFVEKPAAGTAPS--N---LAIMGRYVLTpeifmFLEQqhVG---AGG 226
Cdd:PRK14353 131 VVLGFRA---ADPTGYGRL--IVKGGRLVAIVEEKDASDEERAITlcNsgvMAADGADALA-----LLDR--VGndnAKG 198
|
....*...
gi 1207742263 227 EIQLTDAI 234
Cdd:PRK14353 199 EYYLTDIV 206
|
|
| MocA |
COG2068 |
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism]; |
1-70 |
6.72e-08 |
|
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
Pssm-ID: 441671 [Multi-domain] Cd Length: 195 Bit Score: 51.70 E-value: 6.72e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 1 MKRVRkAIIPAAGLGTRFlpatkAMPKEMLPIVDKPTIQYIVEEAIKSGIEDIIIVTGKTKRSIEDHFDN 70
Cdd:COG2068 1 MSKVA-AIILAAGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADAEEVAAALAG 64
|
|
| G1P_cytidylyltransferase |
cd02524 |
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ... |
7-214 |
2.96e-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: 50.65 E-value: 2.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 7 AIIPAAGLGTRFLPATKAMPKEMLPIVDKPTIQYIVEEAIKSGIEDIIIVTGKTKRSIEDHFDNAFELEQNL---LEKKK 83
Cdd:cd02524 1 VVILAGGLGTRLSEETELKPKPMVEIGGRPILWHIMKIYSHYGHNDFILCLGYKGHVIKEYFLNYFLHNSDVtidLGTNR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 84 YELLEKVQASSK--MVDihyirqkepKGL----GHAVWCARKFIGD-EPFAVLLGD---DIVqaekpcLRQLIEEY--DK 151
Cdd:cd02524 81 IELHNSDIEDWKvtLVD---------TGLntmtGGRLKRVRRYLGDdETFMLTYGDgvsDVN------INALIEFHrsHG 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207742263 152 TLSSVIGVQTvpedeTHRYGIIDpLEQEGrryQVRNFVEKPAAGTAPSNlaiMGRYVLTPEIF 214
Cdd:cd02524 146 KLATVTAVHP-----PGRFGELD-LDDDG---QVTSFTEKPQGDGGWIN---GGFFVLEPEVF 196
|
|
| eIF-2B_epsilon_N |
cd04197 |
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ... |
7-70 |
5.45e-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: 49.53 E-value: 5.45e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207742263 7 AIIPAAGLGTRFLPATKAMPKEMLPIVDKPTIQYIVEEAIKSGIEDIIIVTGKTKRSIEDHFDN 70
Cdd:cd04197 3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQIKEYIEK 66
|
|
| glmU |
PRK14358 |
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ... |
2-232 |
1.86e-06 |
|
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase; Provisional
Pssm-ID: 237688 [Multi-domain] Cd Length: 481 Bit Score: 48.82 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 2 KRVRKAIIPAAGLGTRFlpaTKAMPKEMLPIVDKPTIQYIVEEAIKSGIEDIIIVTGKTKrsiedhfdnafeleqnllek 81
Cdd:PRK14358 5 TRPLDVVILAAGQGTRM---KSALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGA-------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 82 kkyellEKVQASSKMVDIHYIRQKEPKGLGHAVWCARKFI--GDEPFAVLLGDD-IVQAEKpcLRQLIEEYdKTLSSVIG 158
Cdd:PRK14358 62 ------EQVEAALQGSGVAFARQEQQLGTGDAFLSGASALteGDADILVLYGDTpLLRPDT--LRALVADH-RAQGSAMT 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 159 VQTVPEDETHRYGIIdpLEQEGRryQVRNFVEKPAAgtAPSNLAI----MGRYVL---TPEIFMFLEQQHvgAGGEIQLT 231
Cdd:PRK14358 133 ILTGELPDATGYGRI--VRGADG--AVERIVEQKDA--TDAEKAIgefnSGVYVFdarAPELARRIGNDN--KAGEYYLT 204
|
.
gi 1207742263 232 D 232
Cdd:PRK14358 205 D 205
|
|
| CDP-ME_synthetase |
cd02516 |
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ... |
7-83 |
5.25e-06 |
|
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: 46.36 E-value: 5.25e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207742263 7 AIIPAAGLGTRFlpaTKAMPKEMLPIVDKPTIQYIVEEAIKSG-IEDIIIVTGktkrsiEDHFDNAFELEQNLLEKKK 83
Cdd:cd02516 3 AIILAAGSGSRM---GADIPKQFLELGGKPVLEHTLEAFLAHPaIDEIVVVVP------PDDIDLAKELAKYGLSKVV 71
|
|
| glgC |
PRK05293 |
glucose-1-phosphate adenylyltransferase; Provisional |
108-256 |
1.17e-05 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 179997 [Multi-domain] Cd Length: 380 Bit Score: 46.40 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 108 KGLGHAVWCARKFIGD-EPFAVLL--GDDIVQAEkpclrqlieeYDKTL--------SSVIGVQTVPEDETHRYGIIDPL 176
Cdd:PRK05293 99 KGTAHAIYQNIDYIDQyDPEYVLIlsGDHIYKMD----------YDKMLdyhkekeaDVTIAVIEVPWEEASRFGIMNTD 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 177 EqEGRRYQvrnFVEKPAagTAPSNLAIMGRYVLT-PEIFMFLEQqhvGAGGEIQLTDAIQN-----LNEIQRVFAYDFEG 250
Cdd:PRK05293 169 E-NMRIVE---FEEKPK--NPKSNLASMGIYIFNwKRLKEYLIE---DEKNPNSSHDFGKNviplyLEEGEKLYAYPFKG 239
|
....*.
gi 1207742263 251 KRYDVG 256
Cdd:PRK05293 240 YWKDVG 245
|
|
| GT2_BcE_like |
cd04183 |
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ... |
8-136 |
1.01e-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: 42.63 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 8 IIPAAGLGTRFLPATKAMPKEMLPIVDKPTIQYIVEEAIKSGIEDIIIVTGKtkrsieDHFDnafeleqnllekkKYELL 87
Cdd:cd04183 2 IIPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEWVIESLAKIFDSRFIFICRD------EHNT-------------KFHLD 62
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1207742263 88 EKVQASSKMVDIhYIRQKEPKGLGHAVWCARKFI-GDEPFAVLLGDDIVQ 136
Cdd:cd04183 63 ESLKLLAPNATV-VELDGETLGAACTVLLAADLIdNDDPLLIFNCDQIVE 111
|
|
| IspD |
COG1211 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ... |
8-59 |
1.78e-04 |
|
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: 42.04 E-value: 1.78e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1207742263 8 IIPAAGLGTRFlpaTKAMPKEMLPIVDKPTIQYIVEEAIKSG-IEDIIIVTGK 59
Cdd:COG1211 1 IIPAAGSGSRM---GAGIPKQFLPLGGKPVLEHTLEAFLAHPrIDEIVVVVPP 50
|
|
| ispD |
PRK00155 |
D-ribitol-5-phosphate cytidylyltransferase; |
7-57 |
1.99e-04 |
|
D-ribitol-5-phosphate cytidylyltransferase;
Pssm-ID: 234670 Cd Length: 227 Bit Score: 41.66 E-value: 1.99e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1207742263 7 AIIPAAGLGTRFlpatKA-MPKEMLPIVDKPTIQYIVEEAIKSG-IEDIIIVT 57
Cdd:PRK00155 6 AIIPAAGKGSRM----GAdRPKQYLPLGGKPILEHTLEAFLAHPrIDEIIVVV 54
|
|
| ispD |
TIGR00453 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ... |
7-57 |
2.84e-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: 41.12 E-value: 2.84e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1207742263 7 AIIPAAGLGTRFlpaTKAMPKEMLPIVDKPTIQYIVEEAIKS-GIEDIIIVT 57
Cdd:TIGR00453 2 AVIPAAGRGTRF---GSGVPKQYLELGGRPLLEHALDAFLAHpAIDEVVVVV 50
|
|
| glmU |
PRK14359 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
8-78 |
7.12e-04 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237689 [Multi-domain] Cd Length: 430 Bit Score: 40.74 E-value: 7.12e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207742263 8 IIPAAGLGTRFLPATkamPKEMLPIVDKPTIQYIVEEAIKSGiEDIIIVTG----KTKRSIEDHFDNAFELEQNL 78
Cdd:PRK14359 6 IILAAGKGTRMKSSL---PKVLHTICGKPMLFYILKEAFAIS-DDVHVVLHhqkeRIKEAVLEYFPGVIFHTQDL 76
|
|
| glgC |
PRK00844 |
glucose-1-phosphate adenylyltransferase; Provisional |
162-256 |
2.07e-03 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 234846 [Multi-domain] Cd Length: 407 Bit Score: 39.42 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 162 VPEDETHRYGIIDPlEQEGRryqVRNFVEKPAAGTA-PSN----LAIMGRYVLTPEIFMflEQQHVGA---------GGE 227
Cdd:PRK00844 154 VPREEASAFGVIEV-DPDGR---IRGFLEKPADPPGlPDDpdeaLASMGNYVFTTDALV--DALRRDAadedsshdmGGD 227
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1207742263 228 IqltdaIQNLNEIQRVFAYDF----------EGKRY--DVG 256
Cdd:PRK00844 228 I-----IPRLVERGRAYVYDFstnevpgateRDRGYwrDVG 263
|
|
| glgC |
PRK00725 |
glucose-1-phosphate adenylyltransferase; Provisional |
157-275 |
8.21e-03 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 234824 [Multi-domain] Cd Length: 425 Bit Score: 37.51 E-value: 8.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207742263 157 IGVQTVPEDETHRYGIIDPLEQegrrYQVRNFVEKPA-----AGTAPSNLAIMGRYVLTPEiFMF--LEQQHVGAG---- 225
Cdd:PRK00725 161 VACLEVPREEASAFGVMAVDEN----DRITAFVEKPAnppamPGDPDKSLASMGIYVFNAD-YLYelLEEDAEDPNsshd 235
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207742263 226 -GEiqltDAIQNLNEIQRVFAYDF---------EGKRY--DVGEKLGFVQTTIEMALQHPEL 275
Cdd:PRK00725 236 fGK----DIIPKIVEEGKVYAHPFsdscvrsdpEEEPYwrDVGTLDAYWQANLDLASVTPEL 293
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