NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1174887083|ref|WP_081563219|]
View 

MULTISPECIES: UTP--glucose-1-phosphate uridylyltransferase GalU [Acetobacteraceae]

Protein Classification

UTP--glucose-1-phosphate uridylyltransferase( domain architecture ID 10003115)

UTP--glucose-1-phosphate uridylyltransferase catalyzes the formation of UDP-glucose from glucose-1-phosphate and UTP, which is an intermediate step in the biosynthesis of diglucosyl-diacylglycerol (Glc2-DAG)

CATH:  3.90.550.10
EC:  2.7.7.9
Gene Ontology:  GO:0009225|GO:0003983
PubMed:  15020755

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
3-289 5.67e-175

UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 484.54  E-value: 5.67e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083   3 KPLKKAVLPVAGLGTRFLPATKAMPKEMLPVVDKPLIQYAIDEARAAGIEEFCLVTARGKDNLIDYFDIAYELESTLRER 82
Cdd:COG1210     1 MKIRKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVTGRGKRAIEDHFDRSYELEATLEAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083  83 KKISAIKALESSSvEAGSLVAVRQQNPLGLGHAIWCARNFIGNDPFAILLPDDIVQGGRSCVAQLADVYHQTGGNVVAVD 162
Cdd:COG1210    81 GKEELLEEVRSIS-PLANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSEKPCLKQMIEVYEETGGSVIAVQ 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083 163 EVPREWTDRYGILKIGEDDGRKVEVKGLVEKPAPADAPSNLAIIGRYVLTADVLKPLSALKTGVGGEVQLTDAMAEMIGK 242
Cdd:COG1210   160 EVPPEEVSKYGIVDGEEIEGGVYRVTGLVEKPAPEEAPSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDAIAALAKE 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1174887083 243 VPFHGLRYEGTRFDCGSKLGFLEAQVALALQREDLEDDVRAFLKKYA 289
Cdd:COG1210   240 EPVYAYEFEGKRYDCGDKLGYLKATVEFALKRPDLGEEFREYLKELL 286
 
Name Accession Description Interval E-value
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
3-289 5.67e-175

UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 484.54  E-value: 5.67e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083   3 KPLKKAVLPVAGLGTRFLPATKAMPKEMLPVVDKPLIQYAIDEARAAGIEEFCLVTARGKDNLIDYFDIAYELESTLRER 82
Cdd:COG1210     1 MKIRKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVTGRGKRAIEDHFDRSYELEATLEAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083  83 KKISAIKALESSSvEAGSLVAVRQQNPLGLGHAIWCARNFIGNDPFAILLPDDIVQGGRSCVAQLADVYHQTGGNVVAVD 162
Cdd:COG1210    81 GKEELLEEVRSIS-PLANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSEKPCLKQMIEVYEETGGSVIAVQ 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083 163 EVPREWTDRYGILKIGEDDGRKVEVKGLVEKPAPADAPSNLAIIGRYVLTADVLKPLSALKTGVGGEVQLTDAMAEMIGK 242
Cdd:COG1210   160 EVPPEEVSKYGIVDGEEIEGGVYRVTGLVEKPAPEEAPSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDAIAALAKE 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1174887083 243 VPFHGLRYEGTRFDCGSKLGFLEAQVALALQREDLEDDVRAFLKKYA 289
Cdd:COG1210   240 EPVYAYEFEGKRYDCGDKLGYLKATVEFALKRPDLGEEFREYLKELL 286
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 6-273 1.46e-144

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: 406.53  E-value: 1.46e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083   6 KKAVLPVAGLGTRFLPATKAMPKEMLPVVDKPLIQYAIDEARAAGIEEFCLVTARGKDNLIDYFDIAYELESTLRERKKI 85
Cdd:cd02541     1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRGKRAIEDHFDRSYELEETLEKKGKT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083  86 SAIKALESSSVEAgSLVAVRQQNPLGLGHAIWCARNFIGNDPFAILLPDDIVQGGRSCVAQLADVYHQTGGNVVAVDEVP 165
Cdd:cd02541    81 DLLEEVRIISDLA-NIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLIDSKEPCLKQLIEAYEKTGASVIAVEEVP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083 166 REWTDRYGILKIGEDDGRKVEVKGLVEKPAPADAPSNLAIIGRYVLTADVLKPLSALKTGVGGEVQLTDAMAEMIGKVPF 245
Cdd:cd02541   160 PEDVSKYGIVKGEKIDGDVFKVKGLVEKPKPEEAPSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTDAIAKLLEEEPV 239

                         250       260
                  ....*....|....*....|....*...
gi 1174887083 246 HGLRYEGTRFDCGSKLGFLEAQVALALQ 273
Cdd:cd02541   240 YAYVFEGKRYDCGNKLGYLKATVEFALK 267
galU TIGR01099
UTP--glucose-1-phosphate uridylyltransferase; Built to distinquish between the highly similar ...
 6-266 2.14e-119

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: 342.80  E-value: 2.14e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083   6 KKAVLPVAGLGTRFLPATKAMPKEMLPVVDKPLIQYAIDEARAAGIEEFCLVTARGKDNLIDYFDIAYELESTLRERKKI 85
Cdd:TIGR01099   1 RKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYIVEEAVEAGIEEIVFVTGRGKRAIEDHFDYSYELEHQLEKRGKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083  86 SAIKALESSSvEAGSLVAVRQQNPLGLGHAIWCARNFIGNDPFAILLPDDIVQGGRSCVAQLADVYHQTGGNVVAVDEVP 165
Cdd:TIGR01099  81 ELLEEVRKIS-NLATIFYVRQKEQKGLGHAVLCARPFVGDEPFAVILGDDIVVNEEPALKQMIKAYEKTGCSIIAVQEVP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083 166 REWTDRYGILKIGEDDGRKVEVKGLVEKPAPADAPSNLAIIGRYVLTADVLKPLSALKTGVGGEVQLTDAMAEMIGKVPF 245
Cdd:TIGR01099 160 KEEVSKYGVIDGEGIEKDLYKVKNMVEKPKPEEAPSNLAIVGRYILTPDIFDLLEETPPGKGGEIQLTDAINKLLENETV 239

                         250       260
                  ....*....|....*....|.
gi 1174887083 246 HGLRYEGTRFDCGSKLGFLEA 266
Cdd:TIGR01099 240 LAYKFNGKRYDCGSKLGYLEA 260
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
3-286 1.24e-74

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 230.56  E-value: 1.24e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083   3 KPLKKAVLPVAGLGTRFLPATKAMPKEMLPVVDKPLIQYAIDEARAAGIEEFCLVTARGKDNLIDYFDIAYELESTLRER 82
Cdd:PRK13389    6 TKVKKAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFDTSFELEAMLEKR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083  83 KKISAIKALESSSVEAGSLVAVRQQNPLGLGHAIWCARNFIGNDPFAILLPDDIVQGGRS-----CVAQLADVYHQTGGN 157
Cdd:PRK13389   86 VKRQLLDEVQSICPPHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILDEYESdlsqdNLAEMIRRFDETGHS 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083 158 VVAVDevPREWTDRYGILK---IGEDDGRKVEVKGLVEKPAPADAPSNLAIIGRYVLTADVLKPLSALKTGVGGEVQLTD 234
Cdd:PRK13389  166 QIMVE--PVADVTAYGVVDckgVELAPGESVPMVGVVEKPKADVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTD 243

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1174887083 235 AMAEMIGKVPFHGLRYEGTRFDCGSKLGFLEAQVALALQREDLEDDVRAFLK 286
Cdd:PRK13389  244 AIDMLIEKETVEAYHMKGKSHDCGNKLGYMQAFVEYGIRHNTLGTEFKAWLE 295
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 7-216 2.09e-20

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: 87.69  E-value: 2.09e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083   7 KAVLPVAGLGTRFLPATKAMPKEMLPVVDK-PLIQYAIDEARAAGIEEFCLVTArgkdnlidYFDiAYELESTLRERKKI 85
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILT--------QEH-RFMLNELLGDGSKF 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083  86 SaikalesssveaGSLVAVRQQNPLGLGHAIWCARNFIGNDPFAIL-LPDDIVQGGRscVAQLADVYHQTGGNV-VAVDE 163
Cdd:pfam00483  72 G------------VQITYALQPEGKGTAPAVALAADFLGDEKSDVLvLGGDHIYRMD--LEQAVKFHIEKAADAtVTFGI 137

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1174887083 164 VPREWTDRYGILKIGEDDgrkvEVKGLVEKPAPADApSNLAIIGRYVLTADVL 216
Cdd:pfam00483 138 VPVEPPTGYGVVEFDDNG----RVIRFVEKPKLPKA-SNYASMGIYIFNSGVL 185
 
Name Accession Description Interval E-value
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
3-289 5.67e-175

UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 484.54  E-value: 5.67e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083   3 KPLKKAVLPVAGLGTRFLPATKAMPKEMLPVVDKPLIQYAIDEARAAGIEEFCLVTARGKDNLIDYFDIAYELESTLRER 82
Cdd:COG1210     1 MKIRKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVTGRGKRAIEDHFDRSYELEATLEAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083  83 KKISAIKALESSSvEAGSLVAVRQQNPLGLGHAIWCARNFIGNDPFAILLPDDIVQGGRSCVAQLADVYHQTGGNVVAVD 162
Cdd:COG1210    81 GKEELLEEVRSIS-PLANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSEKPCLKQMIEVYEETGGSVIAVQ 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083 163 EVPREWTDRYGILKIGEDDGRKVEVKGLVEKPAPADAPSNLAIIGRYVLTADVLKPLSALKTGVGGEVQLTDAMAEMIGK 242
Cdd:COG1210   160 EVPPEEVSKYGIVDGEEIEGGVYRVTGLVEKPAPEEAPSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDAIAALAKE 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1174887083 243 VPFHGLRYEGTRFDCGSKLGFLEAQVALALQREDLEDDVRAFLKKYA 289
Cdd:COG1210   240 EPVYAYEFEGKRYDCGDKLGYLKATVEFALKRPDLGEEFREYLKELL 286
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 6-273 1.46e-144

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: 406.53  E-value: 1.46e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083   6 KKAVLPVAGLGTRFLPATKAMPKEMLPVVDKPLIQYAIDEARAAGIEEFCLVTARGKDNLIDYFDIAYELESTLRERKKI 85
Cdd:cd02541     1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRGKRAIEDHFDRSYELEETLEKKGKT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083  86 SAIKALESSSVEAgSLVAVRQQNPLGLGHAIWCARNFIGNDPFAILLPDDIVQGGRSCVAQLADVYHQTGGNVVAVDEVP 165
Cdd:cd02541    81 DLLEEVRIISDLA-NIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLIDSKEPCLKQLIEAYEKTGASVIAVEEVP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083 166 REWTDRYGILKIGEDDGRKVEVKGLVEKPAPADAPSNLAIIGRYVLTADVLKPLSALKTGVGGEVQLTDAMAEMIGKVPF 245
Cdd:cd02541   160 PEDVSKYGIVKGEKIDGDVFKVKGLVEKPKPEEAPSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTDAIAKLLEEEPV 239

                         250       260
                  ....*....|....*....|....*...
gi 1174887083 246 HGLRYEGTRFDCGSKLGFLEAQVALALQ 273
Cdd:cd02541   240 YAYVFEGKRYDCGNKLGYLKATVEFALK 267
galU TIGR01099
UTP--glucose-1-phosphate uridylyltransferase; Built to distinquish between the highly similar ...
 6-266 2.14e-119

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: 342.80  E-value: 2.14e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083   6 KKAVLPVAGLGTRFLPATKAMPKEMLPVVDKPLIQYAIDEARAAGIEEFCLVTARGKDNLIDYFDIAYELESTLRERKKI 85
Cdd:TIGR01099   1 RKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYIVEEAVEAGIEEIVFVTGRGKRAIEDHFDYSYELEHQLEKRGKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083  86 SAIKALESSSvEAGSLVAVRQQNPLGLGHAIWCARNFIGNDPFAILLPDDIVQGGRSCVAQLADVYHQTGGNVVAVDEVP 165
Cdd:TIGR01099  81 ELLEEVRKIS-NLATIFYVRQKEQKGLGHAVLCARPFVGDEPFAVILGDDIVVNEEPALKQMIKAYEKTGCSIIAVQEVP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083 166 REWTDRYGILKIGEDDGRKVEVKGLVEKPAPADAPSNLAIIGRYVLTADVLKPLSALKTGVGGEVQLTDAMAEMIGKVPF 245
Cdd:TIGR01099 160 KEEVSKYGVIDGEGIEKDLYKVKNMVEKPKPEEAPSNLAIVGRYILTPDIFDLLEETPPGKGGEIQLTDAINKLLENETV 239

                         250       260
                  ....*....|....*....|.
gi 1174887083 246 HGLRYEGTRFDCGSKLGFLEA 266
Cdd:TIGR01099 240 LAYKFNGKRYDCGSKLGYLEA 260
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
3-286 1.24e-74

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 230.56  E-value: 1.24e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083   3 KPLKKAVLPVAGLGTRFLPATKAMPKEMLPVVDKPLIQYAIDEARAAGIEEFCLVTARGKDNLIDYFDIAYELESTLRER 82
Cdd:PRK13389    6 TKVKKAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFDTSFELEAMLEKR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083  83 KKISAIKALESSSVEAGSLVAVRQQNPLGLGHAIWCARNFIGNDPFAILLPDDIVQGGRS-----CVAQLADVYHQTGGN 157
Cdd:PRK13389   86 VKRQLLDEVQSICPPHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILDEYESdlsqdNLAEMIRRFDETGHS 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083 158 VVAVDevPREWTDRYGILK---IGEDDGRKVEVKGLVEKPAPADAPSNLAIIGRYVLTADVLKPLSALKTGVGGEVQLTD 234
Cdd:PRK13389  166 QIMVE--PVADVTAYGVVDckgVELAPGESVPMVGVVEKPKADVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTD 243

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1174887083 235 AMAEMIGKVPFHGLRYEGTRFDCGSKLGFLEAQVALALQREDLEDDVRAFLK 286
Cdd:PRK13389  244 AIDMLIEKETVEAYHMKGKSHDCGNKLGYMQAFVEYGIRHNTLGTEFKAWLE 295
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
7-287 5.95e-72

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 223.61  E-value: 5.95e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083   7 KAVLPVAGLGTRFLPATKAMPKEMLPVVDKPLIQYAIDEARAAGIEEFCLVTARGKDNLIDYFDIAYELESTLRERKKIS 86
Cdd:PRK10122    5 KAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAVENHFDTSYELESLLEQRVKRQ 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083  87 AIKALESSSVEAGSLVAVRQQNPLGLGHAIWCARNFIGNDPFAILLPDDIVQGG-----RSCVAQLADVYHQTGGNVVAV 161
Cdd:PRK10122   85 LLAEVQSICPPGVTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPDVVIDDAsadplRYNLAAMIARFNETGRSQVLA 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083 162 DEVPREWTDrYGILKIGE---DDGRKVEVKGLVEKP-APADAPSNLAIIGRYVLTADVLKPLSALKTGVGGEVQLTDAMA 237
Cdd:PRK10122  165 KRMPGDLSE-YSVIQTKEpldREGKVSRIVEFIEKPdQPQTLDSDLMAVGRYVLSADIWPELERTEPGAWGRIQLTDAIA 243

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1174887083 238 EMIGKVPFHGLRYEGTRFDCGSKLGFLEAQVALAL----QREDLEDDVRAFLKK 287
Cdd:PRK10122  244 ELAKKQSVDAMLMTGDSYDCGKKMGYMQAFVKYGLrnlkEGAKFRKGIEKLLSE 297
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 8-258 6.09e-49

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: 161.59  E-value: 6.09e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083   8 AVLPVAGLGTRFLPATKAMPKEMLPVVDKPLIQYAIDEARAAGIEEFCLVTARGKDNLIDYFDIAYelestlRERKKISa 87
Cdd:cd04181     1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGS------KFGVNIE- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083  88 ikalesssveagslvAVRQQNPLGLGHAIWCARNFIGNDPFAILLPDDIVQGGRScvAQLADVYHQTGGNVVAVDEVPRE 167
Cdd:cd04181    74 ---------------YVVQEEPLGTAGAVRNAEDFLGDDDFLVVNGDVLTDLDLS--ELLRFHREKGADATIAVKEVEDP 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083 168 WtdRYGILKIgEDDGRkveVKGLVEKpaPADAPSNLAIIGRYVLTADVLKPLSalKTGVGGEVQLTDAMAEMIGKVPFHG 247
Cdd:cd04181   137 S--RYGVVEL-DDDGR---VTRFVEK--PTLPESNLANAGIYIFEPEILDYIP--EILPRGEDELTDAIPLLIEEGKVYG 206

                         250
                  ....*....|.
gi 1174887083 248 LRYEGTRFDCG 258
Cdd:cd04181   207 YPVDGYWLDIG 217
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 6-266 2.15e-47

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: 158.50  E-value: 2.15e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083   6 KKAVLPVAGLGTRFLPATKAMPKEMLPVVDKPLIQYAIDEARAAGIEEFCLVTARGKDNLIDYFDiayelestlrerkki 85
Cdd:cd04189     1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEALG--------------- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083  86 saikaleSSSVEAGSLVAVRQQNPLGLGHAIWCARNFIGNDPFAILLPDDIVQGGrscVAQLADVYHQTGGNV-VAVDEV 164
Cdd:cd04189    66 -------DGSRFGVRITYILQEEPLGLAHAVLAARDFLGDEPFVVYLGDNLIQEG---ISPLVRDFLEEDADAsILLAEV 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083 165 --PRewtdRYGILKIgeDDGRkveVKGLVEKpaPADAPSNLAIIGRYVLTADVLKPLSALKTGVGGEVQLTDAMAEMI-- 240
Cdd:cd04189   136 edPR----RFGVAVV--DDGR---IVRLVEK--PKEPPSNLALVGVYAFTPAIFDAISRLKPSWRGELEITDAIQWLIdr 204

                         250       260
                  ....*....|....*....|....*..
gi 1174887083 241 -GKVPFHglRYEGTRFDCGSKLGFLEA 266
Cdd:cd04189   205 gRRVGYS--IVTGWWKDTGTPEDLLEA 229
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
7-266 9.88e-43

dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 147.93  E-value: 9.88e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083   7 KAVLPVAGLGTRFLPATKAMPKEMLPVVDKPLIQYAIDEARAAGIEEFCLVTargkdnlidyfdiayelesTLRERKKIs 86
Cdd:COG1209     2 KGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIIS-------------------TPEDGPQF- 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083  87 aIKALESSSVEAGSLVAVRQQNPLGLGHAIWCARNFIGNDPFAILLPDDIVQGGrSCVAQLADVYHQTGGNVVAVDEV-- 164
Cdd:COG1209    62 -ERLLGDGSQLGIKISYAVQPEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGD-GLSELLREAAARESGATIFGYKVed 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083 165 PRewtdRYGILKIGEdDGRkveVKGLVEKpaPADAPSNLAIIGRYVLTADVLKPLSALKTGVGGEVQLTDAMAEMI--GK 242
Cdd:COG1209   140 PE----RYGVVEFDE-DGR---VVSLEEK--PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLerGK 209

                         250       260
                  ....*....|....*....|....*
gi 1174887083 243 VpFHGLRYEGTR-FDCGSKLGFLEA 266
Cdd:COG1209   210 L-VVELLGRGFAwLDTGTHESLLEA 233
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 7-271 9.49e-36

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: 128.35  E-value: 9.49e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083   7 KAVLPVAGLGTRFLPATKAMPKEMLPVVDKPLIQYAIDEARAAGIEEFCLVTARGKDNLIDYFdiayelESTLRERKKIS 86
Cdd:COG1208     1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYF------GDGSRFGVRIT 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083  87 aikalesssveagslvAVRQQNPLGLGHAIWCARNFIGNDPFAILLPDDIVqggRSCVAQLADvYHQTGGNVVAVDEVPR 166
Cdd:COG1208    75 ----------------YVDEGEPLGTGGALKRALPLLGDEPFLVLNGDILT---DLDLAALLA-FHREKGADATLALVPV 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083 167 EWTDRYGILKIgEDDGRkveVKGLVEKpaPADAPSNLAIIGRYVLTADVLKPLSAlktgvGGEVQLTDAMAEMIGKVPFH 246
Cdd:COG1208   135 PDPSRYGVVEL-DGDGR---VTRFVEK--PEEPPSNLINAGIYVLEPEIFDYIPE-----GEPFDLEDLLPRLIAEGRVY 203

                         250       260
                  ....*....|....*....|....*
gi 1174887083 247 GLRYEGTRFDCGSKLGFLEAQVALA 271
Cdd:COG1208   204 GYVHDGYWLDIGTPEDLLEANALLL 228
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 6-266 6.28e-23

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: 94.18  E-value: 6.28e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083   6 KKAVLPVAGLGTRFLPATKAMPKEMLPVVDKPLIQYAIDEARAAGIEEFCLVTARGKdnlIDYFdiayelestlrerkki 85
Cdd:cd02538     1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPED---LPLF---------------- 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083  86 saIKALESssveaGSLVAVR-----QQNPLGLGHAIWCARNFIGNDPFAILLPDDIVQGGrSCVAQLADVYHQTGGNVVA 160
Cdd:cd02538    62 --KELLGD-----GSDLGIRityavQPKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQ-GLSPILQRAAAQKEGATVF 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083 161 VDEV--PRewtdRYGILKIgEDDGRkveVKGLVEKpaPADAPSNLAIIGRYVLTADVLKPLSALKTGVGGEVQLTDAMAE 238
Cdd:cd02538   134 GYEVndPE----RYGVVEF-DENGR---VLSIEEK--PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNE 203

                         250       260       270
                  ....*....|....*....|....*....|
gi 1174887083 239 MI--GKVPFHGLRYEGTRFDCGSKLGFLEA 266
Cdd:cd02538   204 YLekGKLSVELLGRGFAWLDTGTHESLLEA 233
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 7-216 2.09e-20

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: 87.69  E-value: 2.09e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083   7 KAVLPVAGLGTRFLPATKAMPKEMLPVVDK-PLIQYAIDEARAAGIEEFCLVTArgkdnlidYFDiAYELESTLRERKKI 85
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILT--------QEH-RFMLNELLGDGSKF 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083  86 SaikalesssveaGSLVAVRQQNPLGLGHAIWCARNFIGNDPFAIL-LPDDIVQGGRscVAQLADVYHQTGGNV-VAVDE 163
Cdd:pfam00483  72 G------------VQITYALQPEGKGTAPAVALAADFLGDEKSDVLvLGGDHIYRMD--LEQAVKFHIEKAADAtVTFGI 137

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1174887083 164 VPREWTDRYGILKIGEDDgrkvEVKGLVEKPAPADApSNLAIIGRYVLTADVL 216
Cdd:pfam00483 138 VPVEPPTGYGVVEFDDNG----RVIRFVEKPKLPKA-SNYASMGIYIFNSGVL 185
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 6-234 6.98e-15

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 73.17  E-value: 6.98e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083   6 KKAVLPVAGLGTRFLPATKAMPKEMLPVVDKPLIQYAIDEARAAGIEEFCLVtargkdnlidyfdiayeleSTLRERKKI 85
Cdd:PRK15480    4 RKGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILII-------------------STPQDTPRF 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083  86 SAIkaLESSSVEAGSLVAVRQQNPLGLGHAIWCARNFIGNDPFAILLPDDIVQGGRSCVAQLADVYHQTGGNVVAVDEVP 165
Cdd:PRK15480   65 QQL--LGDGSQWGLNLQYKVQPSPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVND 142

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1174887083 166 REwtdRYGILKIgEDDGRKVEVKglvEKPApaDAPSNLAIIGRYVLTADVLKPLSALKTGVGGEVQLTD 234
Cdd:PRK15480  143 PE---RYGVVEF-DQNGTAISLE---EKPL--QPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITD 202
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 8-210 2.59e-14

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: 70.34  E-value: 2.59e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083   8 AVLPVAGLGTRFLPATKAMPKEMLPVVDKPLIQYAIDEARAAGIEEFCLVTARGKDNLIDYFDIAYELESTLRERKKisa 87
Cdd:cd02523     1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKKYPNIKFVYNPDYA--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083  88 ikalesSSVEAGSLvavrqqnplglghaiWCARNFIGNDpfAILLPDDIVQgGRSCVAQLADVyhqTGGNVVAVDEVPRE 167
Cdd:cd02523    78 ------ETNNIYSL---------------YLARDFLDED--FLLLEGDVVF-DPSILERLLSS---PADNAILVDKKTKE 130

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1174887083 168 WTDRYgilkigedDGRKVEVKGLVEKPAPADAPSNlaIIGRYV 210
Cdd:cd02523   131 WEDEY--------VKDLDDAGVLLGIISKAKNLEE--IQGEYV 163
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
7-188 6.62e-12

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 63.72  E-value: 6.62e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083   7 KAVLPVAGLGTRFLPATKAMPKEMLPVVDKPLIQYAIDEARAAGIEEFCLVTARGKDNLIDYFDiayelestlRERKKIS 86
Cdd:COG1213     1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEALA---------RPGPDVT 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083  87 AIKalesssveagslvavrqqNPL----GLGHAIWCARNFIgNDPFAILLPDDIVQggRSCVAQLADVYHqtgGNVVAVD 162
Cdd:COG1213    72 FVY------------------NPDydetNNIYSLWLAREAL-DEDFLLLNGDVVFD--PAILKRLLASDG---DIVLLVD 127

                         170       180
                  ....*....|....*....|....*.
gi 1174887083 163 evpREWtdrygilKIGEDDGRKVEVK 188
Cdd:COG1213   128 ---RKW-------EKPLDEEVKVRVD 143
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 7-134 1.11e-11

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: 62.97  E-value: 1.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083   7 KAVLPVAGLGTRFLPATKAMPKEMLPVVDKPLIQYAIDEARAAGIEEFCLVTArgkdnlidYFdiAYELESTLRERKKIS 86
Cdd:cd06422     1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTH--------HL--ADQIEAHLGDSRFGL 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1174887083  87 AIkaleSSSVEAGSLvavrqqnpLGLGHAIWCARNFIGNDPFAILLPD 134
Cdd:cd06422    71 RI----TISDEPDEL--------LETGGGIKKALPLLGDEPFLVVNGD 106
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 8-217 1.31e-11

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: 62.53  E-value: 1.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083   8 AVLPVAGLGTRFLPATKAMPKEMLPVVDKPLIQYAIDEARAAGIEEFCLVTARGKDNLIDYF--------DIAYelestL 79
Cdd:cd06426     1 VVIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNYLAEMIEDYFgdgskfgvNISY-----V 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083  80 RERKkisaikalesssveagslvavrqqnPLGLGHAIWCARNFIgNDPFaILLPDDIVQGGRscVAQLADvYHQTGGNVV 159
Cdd:cd06426    76 REDK-------------------------PLGTAGALSLLPEKP-TDPF-LVMNGDILTNLN--YEHLLD-FHKENNADA 125

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1174887083 160 AVDEVPREWTDRYGILKIgeDDGRkveVKGLVEKPapadAPSNLAIIGRYVLTADVLK 217
Cdd:cd06426   126 TVCVREYEVQVPYGVVET--EGGR---ITSIEEKP----THSFLVNAGIYVLEPEVLD 174
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 7-216 3.84e-11

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: 61.46  E-value: 3.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083   7 KAVLPVAGLGTRFLPATKAMPKEMLPVVDKPLIQYAIDEARAAGIEEFCLVtargkdnlidyfdIAYELESTLRERKKIS 86
Cdd:cd06425     2 KALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILA-------------VNYRPEDMVPFLKEYE 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083  87 AIKALE-SSSVEagslvavrqQNPLGLGHAIWCARNFIG--NDPFAILLPDDIvqggrsC---VAQLADVYHQTGGN--- 157
Cdd:cd06425    69 KKLGIKiTFSIE---------TEPLGTAGPLALARDLLGddDEPFFVLNSDVI------CdfpLAELLDFHKKHGAEgti 133

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083 158 -VVAVDEvPRewtdRYGILKIGEDDGRkveVKGLVEKpaPADAPSNLAIIGRYVLTADVL 216
Cdd:cd06425   134 lVTKVED-PS----KYGVVVHDENTGR---IERFVEK--PKVFVGNKINAGIYILNPSVL 183
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 7-132 1.82e-10

The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; N-terminal domain of eEIF-2B epsilon and gamma, subunits of eukaryotic translation initiators, is a subfamily of glycosyltranferase 2 and is predicted to have glycosyltranferase activity. eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit epsilon shares sequence similarity with gamma subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.


Pssm-ID: 133001 [Multi-domain]  Cd Length: 216  Bit Score: 59.57  E-value: 1.82e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083   7 KAVLPVAGLGTRFLPATKAMPKEMLPVVDKPLIQYAIDEARAAGIEEFCLVTARGKDNLIDYfdiaYELESTLRERKKIS 86
Cdd:cd02507     2 QAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQAIIEH----LLKSKWSSLSSKMI 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1174887083  87 AIKALESSSVEAGSLVAVRQQNPLGLGHAIWCARNFIGNDPFAILL 132
Cdd:cd02507    78 VDVITSDLCESAGDALRLRDIRGLIRSDFLLLSCDLVSNIPLSELL 123
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 8-223 1.12e-09

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: 57.18  E-value: 1.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083   8 AVLPVAGLGTRFLPATKAMPKEMLPVVDKPLIQYAIDEARAAGIEEFCLVTARGKDNLIDYFDIAYELESTLRerkkisa 87
Cdd:cd06915     1 AVILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYLAEQIEEYFGDGYRGGIRIY------- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083  88 ikalesssveagslvAVRQQNPLGLGHAIWCARNFIGNDPFAIL-----LPDDIvqggrscvAQLADVYHQTGG-NVVAV 161
Cdd:cd06915    74 ---------------YVIEPEPLGTGGAIKNALPKLPEDQFLVLngdtyFDVDL--------LALLAALRASGAdATMAL 130

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1174887083 162 DEVPRewTDRYGILKIgEDDGRKVevkGLVEKpaPADAPSNLAIIGRYVLTADVLKPLSALK 223
Cdd:cd06915   131 RRVPD--ASRYGNVTV-DGDGRVI---AFVEK--GPGAAPGLINGGVYLLRKEILAEIPADA 184
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 7-137 2.24e-09

The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; N-terminal domain of gamma subunit of the eukaryotic translation initiation factor 2B (eIF-2B): eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit gamma shares sequence similarity with epsilon subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.


Pssm-ID: 133041 [Multi-domain]  Cd Length: 214  Bit Score: 56.13  E-value: 2.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083   7 KAVLPVAGLGTRFLPATKAMPKEMLPVVDKPLIQYAIDEARAAGIEEFCLVTARGKDNLIDyfdiaYELESTLRErKKIS 86
Cdd:cd04198     2 QAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEEQAEIS-----TYLRSFPLN-LKQK 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1174887083  87 AIKALESSSVEAGSLVAVRqqnplglghAIwcaRNFIGNDpfAILLPDDIV 137
Cdd:cd04198    76 LDEVTIVLDEDMGTADSLR---------HI---RKKIKKD--FLVLSCDLI 112
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 13-126 2.91e-08

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: 54.26  E-value: 2.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083  13 AGLGTRFlpatK-AMPKEMLPVVDKPLIQYAIDEARAAGIEEFCLVTARGKDnlidyfdiayELESTLRERKkisaikal 91
Cdd:COG1207    10 AGKGTRM----KsKLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAE----------QVRAALADLD-------- 67

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1174887083  92 esssveagsLVAVRQQNPLGLGHAIWCARNFIGND 126
Cdd:COG1207    68 ---------VEFVLQEEQLGTGHAVQQALPALPGD 93
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 13-126 1.12e-06

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: 48.67  E-value: 1.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083  13 AGLGTRflpatkaM----PKEMLPVVDKPLIQYAIDEARAAGIEEFCLVTARGKDnlidyfdiayELEstlrerkkisai 88
Cdd:cd02540     6 AGKGTR-------MksdlPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAE----------QVK------------ 56

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1174887083  89 KALESSSVEagslvAVRQQNPLGLGHAIWCARNFIGND 126
Cdd:cd02540    57 KALANPNVE-----FVLQEEQLGTGHAVKQALPALKDF 89
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 3-236 1.41e-06

bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase; Provisional


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 49.21  E-value: 1.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083   3 KPLKKAVLpVAGLGTRFlpaTKAMPKEMLPVVDKPLIQYAIDEARAAGIEEFCLVTARGkdnlidyfdiAYELEStlrer 82
Cdd:PRK14358    6 RPLDVVIL-AAGQGTRM---KSALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHG----------AEQVEA----- 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083  83 kkisaikALESSSVEAGslvavRQQNPLGLGHAIWCARNFI--GNDPFAILLPDDIVQGGRSCVAQLADVYHQTGGNVVA 160
Cdd:PRK14358   67 -------ALQGSGVAFA-----RQEQQLGTGDAFLSGASALteGDADILVLYGDTPLLRPDTLRALVADHRAQGSAMTIL 134

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1174887083 161 VDEVPrewtDRYGILKIGEDDGRKVEvkGLVEKPAPADAPSNLAIIGRYVLTADVLKPLSALKTG---VGGEVQLTDAM 236
Cdd:PRK14358  135 TGELP----DATGYGRIVRGADGAVE--RIVEQKDATDAEKAIGEFNSGVYVFDARAPELARRIGndnKAGEYYLTDLL 207
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 7-243 2.82e-06

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 48.22  E-value: 2.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083   7 KAVLPVAGLGTRFlpaTKAMPKEMLPVVDKPLIQYAIDEARAAGiEEFCLVTARGKDnlidyfdiayELESTLRERKKIs 86
Cdd:PRK14357    2 RALVLAAGKGTRM---KSKIPKVLHKISGKPMINWVIDTAKKVA-QKVGVVLGHEAE----------LVKKLLPEWVKI- 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083  87 aikalesssveagslvaVRQQNPLGLGHAIWCARNFIGNDPFAILLPDDIVQGGRSCVAQLADvYHQTGGNVVAVDEVPR 166
Cdd:PRK14357   67 -----------------FLQEEQLGTAHAVMCARDFIEPGDDLLILYGDVPLISENTLKRLIE-EHNRKGADVTILVADL 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083 167 EWTDRYGILKIGEDDGRKVEVKglvekpapaDAPSNLAII-----GRYVLTAD-VLKPLSALKT-GVGGEVQLTDA--MA 237
Cdd:PRK14357  129 EDPTGYGRIIRDGGKYRIVEDK---------DAPEEEKKIkeintGIYVFSGDfLLEVLPKIKNeNAKGEYYLTDAvnFA 199


                  ....*.
gi 1174887083 238 EMIGKV 243
Cdd:PRK14357  200 EKVRVV 205
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 6-125 1.37e-05

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 45.98  E-value: 1.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083   6 KKAVLPVAGLGTRFlpaTKAMPKEMLPVVDKPLIQYAIDEARAAGIEEFCLVTARGKDnlidyfdiayELESTLRERKKI 85
Cdd:PRK14354    3 RYAIILAAGKGTRM---KSKLPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVGHGAE----------EVKEVLGDRSEF 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1174887083  86 saikalesssveagslvaVRQQNPLGLGHAIWCARNFIGN 125
Cdd:PRK14354   70 ------------------ALQEEQLGTGHAVMQAEEFLAD 91
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
 9-75 2.54e-05

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: 44.55  E-value: 2.54e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1174887083   9 VLPVAGLGTRFLPATKAMPKEMLPVVDKPLIQYAIDEARAAGIEEFCLVtARGKDNLIDYFDIAYEL 75
Cdd:cd04183     2 IIPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEWVIESLAKIFDSRFIFI-CRDEHNTKFHLDESLKL 67
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 8-69 2.78e-05

The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; N-terminal domain of epsilon subunit of the eukaryotic translation initiation factor 2B (eIF-2B): eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit epsilon shares sequence similarity with gamma subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.


Pssm-ID: 133040 [Multi-domain]  Cd Length: 217  Bit Score: 44.14  E-value: 2.78e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1174887083   8 AVLPVAGLGTRFLPATKAMPKEMLPVVDKPLIQYAIDEARAAGIEEFCLVTARGKDNLIDYF 69
Cdd:cd04197     3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQIKEYI 64
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 8-58 2.27e-04

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: 41.01  E-value: 2.27e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1174887083   8 AVLPVAGLGTRFlpatkAMPKEMLPVVDKPLIQYAIDEARAAGIEEFCLVT 58
Cdd:cd04182     3 AIILAAGRSSRM-----GGNKLLLPLDGKPLLRHALDAALAAGLSRVIVVL 48
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 8-120 2.30e-04

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 42.16  E-value: 2.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083   8 AVLPVAGLGTRFlpaTKAMPKEMLPVVDKPLIQYAIDEARAAGIEEFCLVTARGKDNLidyfdiayelestlrerkkisa 87
Cdd:PRK14353    8 AIILAAGEGTRM---KSSLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGPGAEAV---------------------- 62

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1174887083  88 IKALESSSVEAgslVAVRQQNPLGLGHAIWCAR 120
Cdd:PRK14353   63 AAAAAKIAPDA---EIFVQKERLGTAHAVLAAR 92
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 8-193 3.33e-04

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 41.65  E-value: 3.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083   8 AVLPVAGLGTRFlpaTKAMPKEMLPVVDKPLIQYAIDEARAAGIEEFCLVTARGKDNLIDYFDiayelestlrerkkisa 87
Cdd:PRK14355    6 AIILAAGKGTRM---KSDLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHFA----------------- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083  88 ikalesssvEAGSLVAVRQQNPLGLGHAIWCARNFIgnDPFA----ILLPDDIVQGGRSCVAQLAdvYHQTGGNVVAVDE 163
Cdd:PRK14355   66 ---------GDGDVSFALQEEQLGTGHAVACAAPAL--DGFSgtvlILCGDVPLLRAETLQGMLA--AHRATGAAVTVLT 132

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1174887083 164 VPREWTDRYG-ILKigEDDGRkveVKGLVEK 193
Cdd:PRK14355  133 ARLENPFGYGrIVR--DADGR---VLRIVEE 158
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
8-58 3.74e-04

CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 40.53  E-value: 3.74e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1174887083   8 AVLPVAGLGTRFlpatkAMPKEMLPVVDKPLIQYAIDEARAAGIEEFCLVT 58
Cdd:COG2068     6 AIILAAGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPVVVVL 51
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
 159-219 4.83e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 41.36  E-value: 4.83e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1174887083 159 VAVDEVPREWTDRYGILKIGEDDgrkvEVKGLVEKPA-----PADAPSNLAIIGRYVLTADVLKPL 219
Cdd:PRK00725  161 VACLEVPREEASAFGVMAVDEND----RITAFVEKPAnppamPGDPDKSLASMGIYVFNADYLYEL 222
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 8-234 7.95e-04

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: 40.31  E-value: 7.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083   8 AVLPVAG--LGTRFLPATKAMPKEMLPVVDKPLIQYAIDE-ARAAGIEEFClvtargkdnLIDYFDIAyELESTLRERKK 84
Cdd:cd06428     1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEAcAKVPDLKEVL---------LIGFYPES-VFSDFISDAQQ 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174887083  85 IS--AIKALesssveagslvavRQQNPLGLGHAIWCARNFI-GNDPFAILlpddIVQGGRSC---VAQLADVYHQTGGNV 158
Cdd:cd06428    71 EFnvPIRYL-------------QEYKPLGTAGGLYHFRDQIlAGNPSAFF----VLNADVCCdfpLQELLEFHKKHGASG 133

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1174887083 159 V-AVDEVPREWTDRYGILKIGEDDGrkvEVKGLVEKpaPADAPSNLAIIGRYVLTADVLKPLSALKTGVGGEVQLTD 234
Cdd:cd06428   134 TiLGTEASREQASNYGCIVEDPSTG---EVLHYVEK--PETFVSDLINCGVYLFSPEIFDTIKKAFQSRQQEAQLGD 205
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 8-61 2.69e-03

CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; 4-diphosphocytidyl-2-methyl-D-erythritol synthase (CDP-ME), also called 2C-methyl-d-erythritol 4-phosphate cytidylyltransferase catalyzes the third step in the alternative (non-mevalonate) pathway of Isopentenyl diphosphate (IPP) biosynthesis: the formation of 4-diphosphocytidyl-2C-methyl-D-erythritol from CTP and 2C-methyl-D-erythritol 4-phosphate. This mevalonate independent pathway that utilizes pyruvate and glyceraldehydes 3-phosphate as starting materials for production of IPP occurs in a variety of bacteria, archaea and plant cells, but is absent in mammals. Thus, CDP-ME synthetase is an attractive targets for the structure-based design of selective antibacterial, herbicidal and antimalarial drugs.


Pssm-ID: 133009 [Multi-domain]  Cd Length: 218  Bit Score: 38.27  E-value: 2.69e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1174887083   8 AVLPVAGLGTRFlpaTKAMPKEMLPVVDKPLIQYAIDE-ARAAGIEEFCLVTARG 61
Cdd:cd02516     3 AIILAAGSGSRM---GADIPKQFLELGGKPVLEHTLEAfLAHPAIDEIVVVVPPD 54
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 151-217 3.89e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 38.31  E-value: 3.89e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1174887083 151 YH-QTGGNV-VAVDEVPREWTDRYGILKIgEDDGRKVEVKglvEKpaPADAPSNLAIIGRYVLTADVLK 217
Cdd:PRK05293  139 YHkEKEADVtIAVIEVPWEEASRFGIMNT-DENMRIVEFE---EK--PKNPKSNLASMGIYIFNWKRLK 201
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 144-216 7.85e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 37.50  E-value: 7.85e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1174887083 144 VAQLADVYHQTGGNV-VAVDEVPREWTDRYGILKIGEDdGRkveVKGLVEKPA-----PADAPSNLAIIGRYVLTADVL 216
Cdd:PRK00844  133 PRQMVDFHIESGAGVtVAAIRVPREEASAFGVIEVDPD-GR---IRGFLEKPAdppglPDDPDEALASMGNYVFTTDAL 207
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH