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Conserved domains on  [gi|1085499362|gb|OGW60295|]
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UTP--glucose-1-phosphate uridylyltransferase [Nitrospirae bacterium RIFCSPHIGHO2_02_FULL_42_12]

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

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List of domain hits

 Name Accession Description Interval E-value
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
4-287 0e+00

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


:

Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 547.71  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362   4 PVTKAVFPVAGLGTRFLPATKASPKEMLPLVDKPLIQYVIEEAISSGIEEVIIVTGRGKRAIEDHFDISYELEDLLRQKG 83
Cdd:COG1210     2 KIRKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVTGRGKRAIEDHFDRSYELEATLEAKG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362  84 KRKLLAEVQKISNMMNICYVRQKEPNGLGHAILCTKNLVKNEPFAVLLGDDIIDSDVPALKQMLDIYNTYSASIIAVQEV 163
Cdd:COG1210    82 KEELLEEVRSISPLANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSEKPCLKQMIEVYEETGGSVIAVQEV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362 164 DRSQVSNYGIIEATPIGDRVYKISDMVEKPGMEEAPSNLAIIGRYILTPGIIDLLEKTNPGSGKEIQLTDALKKLVKVSP 243
Cdd:COG1210   162 PPEEVSKYGIVDGEEIEGGVYRVTGLVEKPAPEEAPSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDAIAALAKEEP 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1085499362 244 VYGYKFKGTRYDAGDKLGFLKATVEFALKNKEFGKKFREYLKTL 287
Cdd:COG1210   242 VYAYEFEGKRYDCGDKLGYLKATVEFALKRPDLGEEFREYLKEL 285
 
Name Accession Description Interval E-value
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
4-287 0e+00

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


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 547.71  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362   4 PVTKAVFPVAGLGTRFLPATKASPKEMLPLVDKPLIQYVIEEAISSGIEEVIIVTGRGKRAIEDHFDISYELEDLLRQKG 83
Cdd:COG1210     2 KIRKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVTGRGKRAIEDHFDRSYELEATLEAKG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362  84 KRKLLAEVQKISNMMNICYVRQKEPNGLGHAILCTKNLVKNEPFAVLLGDDIIDSDVPALKQMLDIYNTYSASIIAVQEV 163
Cdd:COG1210    82 KEELLEEVRSISPLANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSEKPCLKQMIEVYEETGGSVIAVQEV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362 164 DRSQVSNYGIIEATPIGDRVYKISDMVEKPGMEEAPSNLAIIGRYILTPGIIDLLEKTNPGSGKEIQLTDALKKLVKVSP 243
Cdd:COG1210   162 PPEEVSKYGIVDGEEIEGGVYRVTGLVEKPAPEEAPSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDAIAALAKEEP 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1085499362 244 VYGYKFKGTRYDAGDKLGFLKATVEFALKNKEFGKKFREYLKTL 287
Cdd:COG1210   242 VYAYEFEGKRYDCGDKLGYLKATVEFALKRPDLGEEFREYLKEL 285
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 6-272 3.98e-167

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: 463.54  E-value: 3.98e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362   6 TKAVFPVAGLGTRFLPATKASPKEMLPLVDKPLIQYVIEEAISSGIEEVIIVTGRGKRAIEDHFDISYELEDLLRQKGKR 85
Cdd:cd02541     1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRGKRAIEDHFDRSYELEETLEKKGKT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362  86 KLLAEVQKISNMMNICYVRQKEPNGLGHAILCTKNLVKNEPFAVLLGDDIIDSDVPALKQMLDIYNTYSASIIAVQEVDR 165
Cdd:cd02541    81 DLLEEVRIISDLANIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLIDSKEPCLKQLIEAYEKTGASVIAVEEVPP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362 166 SQVSNYGIIEATPIGDRVYKISDMVEKPGMEEAPSNLAIIGRYILTPGIIDLLEKTNPGSGKEIQLTDALKKLVKVSPVY 245
Cdd:cd02541   161 EDVSKYGIVKGEKIDGDVFKVKGLVEKPKPEEAPSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTDAIAKLLEEEPVY 240

                         250       260
                  ....*....|....*....|....*..
gi 1085499362 246 GYKFKGTRYDAGDKLGFLKATVEFALK 272
Cdd:cd02541   241 AYVFEGKRYDCGNKLGYLKATVEFALK 267
galU TIGR01099
UTP--glucose-1-phosphate uridylyltransferase; Built to distinquish between the highly similar ...
 7-265 2.21e-148

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: 415.99  E-value: 2.21e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362   7 KAVFPVAGLGTRFLPATKASPKEMLPLVDKPLIQYVIEEAISSGIEEVIIVTGRGKRAIEDHFDISYELEDLLRQKGKRK 86
Cdd:TIGR01099   2 KAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYIVEEAVEAGIEEIVFVTGRGKRAIEDHFDYSYELEHQLEKRGKEE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362  87 LLAEVQKISNMMNICYVRQKEPNGLGHAILCTKNLVKNEPFAVLLGDDIIDSDVPALKQMLDIYNTYSASIIAVQEVDRS 166
Cdd:TIGR01099  82 LLEEVRKISNLATIFYVRQKEQKGLGHAVLCARPFVGDEPFAVILGDDIVVNEEPALKQMIKAYEKTGCSIIAVQEVPKE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362 167 QVSNYGIIEATPIGDRVYKISDMVEKPGMEEAPSNLAIIGRYILTPGIIDLLEKTNPGSGKEIQLTDALKKLVKVSPVYG 246
Cdd:TIGR01099 162 EVSKYGVIDGEGIEKDLYKVKNMVEKPKPEEAPSNLAIVGRYILTPDIFDLLEETPPGKGGEIQLTDAINKLLENETVLA 241

                         250
                  ....*....|....*....
gi 1085499362 247 YKFKGTRYDAGDKLGFLKA 265
Cdd:TIGR01099 242 YKFNGKRYDCGSKLGYLEA 260
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
3-287 1.51e-92

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 276.02  E-value: 1.51e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362   3 TPVTKAVFPVAGLGTRFLPATKASPKEMLPLVDKPLIQYVIEEAISSGIEEVIIVTGRGKRAIEDHFDISYELEDLLRQK 82
Cdd:PRK13389    6 TKVKKAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFDTSFELEAMLEKR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362  83 GKRKLLAEVQKI-SNMMNICYVRQKEPNGLGHAILCTKNLVKNEPFAVLLGDDIID---SDVPA--LKQMLDIYNTYSAS 156
Cdd:PRK13389   86 VKRQLLDEVQSIcPPHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILDeyeSDLSQdnLAEMIRRFDETGHS 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362 157 IIAVQEVDrsQVSNYGIIEATPI----GDRVYKISdMVEKPGMEEAPSNLAIIGRYILTPGIIDLLEKTNPGSGKEIQLT 232
Cdd:PRK13389  166 QIMVEPVA--DVTAYGVVDCKGVelapGESVPMVG-VVEKPKADVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLT 242

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1085499362 233 DALKKLVKVSPVYGYKFKGTRYDAGDKLGFLKATVEFALKNKEFGKKFREYLKTL 287
Cdd:PRK13389  243 DAIDMLIEKETVEAYHMKGKSHDCGNKLGYMQAFVEYGIRHNTLGTEFKAWLEEE 297
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 7-266 2.80e-24

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: 98.09  E-value: 2.80e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362   7 KAVFPVAGLGTRFLPATKASPKEMLPLVDK-PLIQYVIEEAISSGIEEVIIVTgrgkraiedhfdiSYELEDLLRQkgkr 85
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVIL-------------TQEHRFMLNE---- 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362  86 kLLAEVQKISnmMNICYVRQKEPNGLGHAILCTKNLVKNEPFAVL-LGDDIIDSDvpALKQMLDIYNTYSASIIA-VQEV 163
Cdd:pfam00483  64 -LLGDGSKFG--VQITYALQPEGKGTAPAVALAADFLGDEKSDVLvLGGDHIYRM--DLEQAVKFHIEKAADATVtFGIV 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362 164 DRSQVSNYGIIEATPIGdrvyKISDMVEKPGMEEApSNLAIIGRYILTPGIIDLLEKT-NPGSGKEIQLTDALKKLV-KV 241
Cdd:pfam00483 139 PVEPPTGYGVVEFDDNG----RVIRFVEKPKLPKA-SNYASMGIYIFNSGVLDFLAKYlEELKRGEDEITDILPKALeDG 213

                         250       260
                  ....*....|....*....|....*.
gi 1085499362 242 SPVYGYKFKGTR-YDAGDKLGFLKAT 266
Cdd:pfam00483 214 KLAYAFIFKGYAwLDVGTWDSLWEAN 239
 
Name Accession Description Interval E-value
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
4-287 0e+00

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


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 547.71  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362   4 PVTKAVFPVAGLGTRFLPATKASPKEMLPLVDKPLIQYVIEEAISSGIEEVIIVTGRGKRAIEDHFDISYELEDLLRQKG 83
Cdd:COG1210     2 KIRKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVTGRGKRAIEDHFDRSYELEATLEAKG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362  84 KRKLLAEVQKISNMMNICYVRQKEPNGLGHAILCTKNLVKNEPFAVLLGDDIIDSDVPALKQMLDIYNTYSASIIAVQEV 163
Cdd:COG1210    82 KEELLEEVRSISPLANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSEKPCLKQMIEVYEETGGSVIAVQEV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362 164 DRSQVSNYGIIEATPIGDRVYKISDMVEKPGMEEAPSNLAIIGRYILTPGIIDLLEKTNPGSGKEIQLTDALKKLVKVSP 243
Cdd:COG1210   162 PPEEVSKYGIVDGEEIEGGVYRVTGLVEKPAPEEAPSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDAIAALAKEEP 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1085499362 244 VYGYKFKGTRYDAGDKLGFLKATVEFALKNKEFGKKFREYLKTL 287
Cdd:COG1210   242 VYAYEFEGKRYDCGDKLGYLKATVEFALKRPDLGEEFREYLKEL 285
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 6-272 3.98e-167

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: 463.54  E-value: 3.98e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362   6 TKAVFPVAGLGTRFLPATKASPKEMLPLVDKPLIQYVIEEAISSGIEEVIIVTGRGKRAIEDHFDISYELEDLLRQKGKR 85
Cdd:cd02541     1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRGKRAIEDHFDRSYELEETLEKKGKT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362  86 KLLAEVQKISNMMNICYVRQKEPNGLGHAILCTKNLVKNEPFAVLLGDDIIDSDVPALKQMLDIYNTYSASIIAVQEVDR 165
Cdd:cd02541    81 DLLEEVRIISDLANIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLIDSKEPCLKQLIEAYEKTGASVIAVEEVPP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362 166 SQVSNYGIIEATPIGDRVYKISDMVEKPGMEEAPSNLAIIGRYILTPGIIDLLEKTNPGSGKEIQLTDALKKLVKVSPVY 245
Cdd:cd02541   161 EDVSKYGIVKGEKIDGDVFKVKGLVEKPKPEEAPSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTDAIAKLLEEEPVY 240

                         250       260
                  ....*....|....*....|....*..
gi 1085499362 246 GYKFKGTRYDAGDKLGFLKATVEFALK 272
Cdd:cd02541   241 AYVFEGKRYDCGNKLGYLKATVEFALK 267
galU TIGR01099
UTP--glucose-1-phosphate uridylyltransferase; Built to distinquish between the highly similar ...
 7-265 2.21e-148

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: 415.99  E-value: 2.21e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362   7 KAVFPVAGLGTRFLPATKASPKEMLPLVDKPLIQYVIEEAISSGIEEVIIVTGRGKRAIEDHFDISYELEDLLRQKGKRK 86
Cdd:TIGR01099   2 KAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYIVEEAVEAGIEEIVFVTGRGKRAIEDHFDYSYELEHQLEKRGKEE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362  87 LLAEVQKISNMMNICYVRQKEPNGLGHAILCTKNLVKNEPFAVLLGDDIIDSDVPALKQMLDIYNTYSASIIAVQEVDRS 166
Cdd:TIGR01099  82 LLEEVRKISNLATIFYVRQKEQKGLGHAVLCARPFVGDEPFAVILGDDIVVNEEPALKQMIKAYEKTGCSIIAVQEVPKE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362 167 QVSNYGIIEATPIGDRVYKISDMVEKPGMEEAPSNLAIIGRYILTPGIIDLLEKTNPGSGKEIQLTDALKKLVKVSPVYG 246
Cdd:TIGR01099 162 EVSKYGVIDGEGIEKDLYKVKNMVEKPKPEEAPSNLAIVGRYILTPDIFDLLEETPPGKGGEIQLTDAINKLLENETVLA 241

                         250
                  ....*....|....*....
gi 1085499362 247 YKFKGTRYDAGDKLGFLKA 265
Cdd:TIGR01099 242 YKFNGKRYDCGSKLGYLEA 260
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
3-287 1.51e-92

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 276.02  E-value: 1.51e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362   3 TPVTKAVFPVAGLGTRFLPATKASPKEMLPLVDKPLIQYVIEEAISSGIEEVIIVTGRGKRAIEDHFDISYELEDLLRQK 82
Cdd:PRK13389    6 TKVKKAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFDTSFELEAMLEKR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362  83 GKRKLLAEVQKI-SNMMNICYVRQKEPNGLGHAILCTKNLVKNEPFAVLLGDDIID---SDVPA--LKQMLDIYNTYSAS 156
Cdd:PRK13389   86 VKRQLLDEVQSIcPPHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILDeyeSDLSQdnLAEMIRRFDETGHS 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362 157 IIAVQEVDrsQVSNYGIIEATPI----GDRVYKISdMVEKPGMEEAPSNLAIIGRYILTPGIIDLLEKTNPGSGKEIQLT 232
Cdd:PRK13389  166 QIMVEPVA--DVTAYGVVDCKGVelapGESVPMVG-VVEKPKADVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLT 242

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1085499362 233 DALKKLVKVSPVYGYKFKGTRYDAGDKLGFLKATVEFALKNKEFGKKFREYLKTL 287
Cdd:PRK13389  243 DAIDMLIEKETVEAYHMKGKSHDCGNKLGYMQAFVEYGIRHNTLGTEFKAWLEEE 297
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
7-287 1.23e-83

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 253.27  E-value: 1.23e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362   7 KAVFPVAGLGTRFLPATKASPKEMLPLVDKPLIQYVIEEAISSGIEEVIIVTGRGKRAIEDHFDISYELEDLLRQKGKRK 86
Cdd:PRK10122    5 KAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAVENHFDTSYELESLLEQRVKRQ 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362  87 LLAEVQKIS----NMMNicyVRQKEPNGLGHAILCTKNLVKNEPFAVLLGDDIID-SDVPALKqmldiYNtYSASIIAVQ 161
Cdd:PRK10122   85 LLAEVQSICppgvTIMN---VRQGQPLGLGHSILCARPAIGDNPFVVVLPDVVIDdASADPLR-----YN-LAAMIARFN 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362 162 EVDRSQV---------SNYGIIEATPIGDR---VYKISDMVEKPGMEEA-PSNLAIIGRYILTPGIIDLLEKTNPGSGKE 228
Cdd:PRK10122  156 ETGRSQVlakrmpgdlSEYSVIQTKEPLDRegkVSRIVEFIEKPDQPQTlDSDLMAVGRYVLSADIWPELERTEPGAWGR 235

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1085499362 229 IQLTDALKKLVKVSPVYGYKFKGTRYDAGDKLGFLKATVEFALKNKEFGKKFREYLKTL 287
Cdd:PRK10122  236 IQLTDAIAELAKKQSVDAMLMTGDSYDCGKKMGYMQAFVKYGLRNLKEGAKFRKGIEKL 294
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 8-257 2.11e-60

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: 191.25  E-value: 2.11e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362   8 AVFPVAGLGTRFLPATKASPKEMLPLVDKPLIQYVIEEAISSGIEEVIIVTGRGKRAIEDHFDISYELEdllrqkgkrkl 87
Cdd:cd04181     1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGSKFG----------- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362  88 laevqkisnmMNICYVRQKEPNGLGHAILCTKNLVKNEPFAVLLGDDIIDSDvpaLKQMLDIYNTYSA-SIIAVQEVDRs 166
Cdd:cd04181    70 ----------VNIEYVVQEEPLGTAGAVRNAEDFLGDDDFLVVNGDVLTDLD---LSELLRFHREKGAdATIAVKEVED- 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362 167 qVSNYGIIEatpiGDRVYKISDMVEKPgmEEAPSNLAIIGRYILTPGIIDLLEKTNPgsGKEIQLTDALKKLVKVSPVYG 246
Cdd:cd04181   136 -PSRYGVVE----LDDDGRVTRFVEKP--TLPESNLANAGIYIFEPEILDYIPEILP--RGEDELTDAIPLLIEEGKVYG 206

                         250
                  ....*....|.
gi 1085499362 247 YKFKGTRYDAG 257
Cdd:cd04181   207 YPVDGYWLDIG 217
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 7-265 3.36e-46

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: 155.42  E-value: 3.36e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362   7 KAVFPVAGLGTRFLPATKASPKEMLPLVDKPLIQYVIEEAISSGIEEVIIVTGRGKRAIEDHFDISYELEdllrqkgkrk 86
Cdd:cd04189     2 KGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEALGDGSRFG---------- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362  87 llaevqkisnmMNICYVRQKEPNGLGHAILCTKNLVKNEPFAVLLGDDII-DSDVPALKQMLDiyNTYSASiIAVQEVDr 165
Cdd:cd04189    72 -----------VRITYILQEEPLGLAHAVLAARDFLGDEPFVVYLGDNLIqEGISPLVRDFLE--EDADAS-ILLAEVE- 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362 166 sQVSNYGIIEatPIGDRVYKIsdmVEKPgmEEAPSNLAIIGRYILTPGIIDLLEKTNPGSGKEIQLTDALKKLV-KVSPV 244
Cdd:cd04189   137 -DPRRFGVAV--VDDGRIVRL---VEKP--KEPPSNLALVGVYAFTPAIFDAISRLKPSWRGELEITDAIQWLIdRGRRV 208

                         250       260
                  ....*....|....*....|.
gi 1085499362 245 YGYKFKGTRYDAGDKLGFLKA 265
Cdd:cd04189   209 GYSIVTGWWKDTGTPEDLLEA 229
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 7-257 1.07e-43

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: 148.76  E-value: 1.07e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362   7 KAVFPVAGLGTRFLPATKASPKEMLPLVDKPLIQYVIEEAISSGIEEVIIVTGRGKRAIEDHFdisyeledllrQKGKRK 86
Cdd:COG1208     1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYF-----------GDGSRF 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362  87 LLaevqkisnmmNICYVRQKEPNGLGHAILCTKNLVKNEPFAVLLGDDIIDSDvpaLKQMLDIYNTYSASI-IAVqeVDR 165
Cdd:COG1208    70 GV----------RITYVDEGEPLGTGGALKRALPLLGDEPFLVLNGDILTDLD---LAALLAFHREKGADAtLAL--VPV 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362 166 SQVSNYGIIEATPIGdrvyKISDMVEKPgmEEAPSNLAIIGRYILTPGIIDLLEKtnpgsGKEIQLTDALKKLVKVSPVY 245
Cdd:COG1208   135 PDPSRYGVVELDGDG----RVTRFVEKP--EEPPSNLINAGIYVLEPEIFDYIPE-----GEPFDLEDLLPRLIAEGRVY 203

                         250
                  ....*....|..
gi 1085499362 246 GYKFKGTRYDAG 257
Cdd:COG1208   204 GYVHDGYWLDIG 215
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
7-240 1.96e-41

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 144.46  E-value: 1.96e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362   7 KAVFPVAGLGTRFLPATKASPKEMLPLVDKPLIQYVIEEAISSGIEEV-IIVTGRGKRAIEDHF-DISyeledllrQKGk 84
Cdd:COG1209     2 KGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREIlIISTPEDGPQFERLLgDGS--------QLG- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362  85 rkllaevqkisnmMNICYVRQKEPNGLGHAILCTKNLVKNEPFAVLLGDDIIDSDvpALKQMLDIYNTYSA-SIIAVQEV 163
Cdd:COG1209    73 -------------IKISYAVQPEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGD--GLSELLREAAARESgATIFGYKV 137

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1085499362 164 DRSQvsNYGIIEAtpigDRVYKISDMVEKPgmEEAPSNLAIIGRYILTPGIIDLLEKTNPGSGKEIQLTDALKKLVK 240
Cdd:COG1209   138 EDPE--RYGVVEF----DEDGRVVSLEEKP--KEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLE 206
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 7-266 2.80e-24

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: 98.09  E-value: 2.80e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362   7 KAVFPVAGLGTRFLPATKASPKEMLPLVDK-PLIQYVIEEAISSGIEEVIIVTgrgkraiedhfdiSYELEDLLRQkgkr 85
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVIL-------------TQEHRFMLNE---- 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362  86 kLLAEVQKISnmMNICYVRQKEPNGLGHAILCTKNLVKNEPFAVL-LGDDIIDSDvpALKQMLDIYNTYSASIIA-VQEV 163
Cdd:pfam00483  64 -LLGDGSKFG--VQITYALQPEGKGTAPAVALAADFLGDEKSDVLvLGGDHIYRM--DLEQAVKFHIEKAADATVtFGIV 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362 164 DRSQVSNYGIIEATPIGdrvyKISDMVEKPGMEEApSNLAIIGRYILTPGIIDLLEKT-NPGSGKEIQLTDALKKLV-KV 241
Cdd:pfam00483 139 PVEPPTGYGVVEFDDNG----RVIRFVEKPKLPKA-SNYASMGIYIFNSGVLDFLAKYlEELKRGEDEITDILPKALeDG 213

                         250       260
                  ....*....|....*....|....*.
gi 1085499362 242 SPVYGYKFKGTR-YDAGDKLGFLKAT 266
Cdd:pfam00483 214 KLAYAFIFKGYAwLDVGTWDSLWEAN 239
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 7-233 8.65e-21

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: 88.40  E-value: 8.65e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362   7 KAVFPVAGLGTRFLPATKASPKEMLPLVDKPLIQYVIEEAISSGIEEVIIVTGRgkraiedhfdisyelEDLLRQKgkrK 86
Cdd:cd02538     2 KGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTP---------------EDLPLFK---E 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362  87 LLAEVQKISnmMNICYVRQKEPNGLGHAILCTKNLVKNEPFAVLLGDDII-DSDvpaLKQMLDIYNTYS--ASIIAVQEV 163
Cdd:cd02538    64 LLGDGSDLG--IRITYAVQPKPGGLAQAFIIGEEFIGDDPVCLILGDNIFyGQG---LSPILQRAAAQKegATVFGYEVN 138

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362 164 DRSQvsnYGIIEAtpigDRVYKISDMVEKPgmEEAPSNLAIIGRYILTPGIIDLLEKTNPGSGKEIQLTD 233
Cdd:cd02538   139 DPER---YGVVEF----DENGRVLSIEEKP--KKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITD 199
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 7-266 1.66e-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: 82.26  E-value: 1.66e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362   7 KAVFPVAGLGTRFLPATKASPKEMLPLVDKPLIQYVIEEAISSGIEEVIIVtgrgkraiedhfdISYELEDLLRqkgkrk 86
Cdd:cd06425     2 KALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILA-------------VNYRPEDMVP------ 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362  87 llaEVQKISNM--MNICYVRQKEPNGLGHAILCTKNLVK--NEPFAVlLGDDIIdSDVPaLKQMLDIYNTYSA-SIIAVQ 161
Cdd:cd06425    63 ---FLKEYEKKlgIKITFSIETEPLGTAGPLALARDLLGddDEPFFV-LNSDVI-CDFP-LAELLDFHKKHGAeGTILVT 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362 162 EVDRSqvSNYGIIEATPigdRVYKISDMVEKPgmEEAPSNLAIIGRYILTPGIIDLLEKTNPGSGKEIqltdaLKKLVKV 241
Cdd:cd06425   137 KVEDP--SKYGVVVHDE---NTGRIERFVEKP--KVFVGNKINAGIYILNPSVLDRIPLRPTSIEKEI-----FPKMASE 204

                         250       260
                  ....*....|....*....|....*
gi 1085499362 242 SPVYGYKFKGTRYDAGDKLGFLKAT 266
Cdd:cd06425   205 GQLYAYELPGFWMDIGQPKDFLKGM 229
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 14-247 1.98e-17

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: 79.09  E-value: 1.98e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362  14 GLGTRFLPATKASPKEMLPLVDKPLIQYVIEEAISSGIEEVIIVTGRGKRAIEDHFdisyeledllrQKGKRKllaevqk 93
Cdd:cd06426     7 GKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNYLAEMIEDYF-----------GDGSKF------- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362  94 isnMMNICYVRQKEPNGLGHAI-LCTKNLvkNEPFAVLLGDDIIDSDvpaLKQMLDIYNTYSASI-IAVQEVDrSQVSnY 171
Cdd:cd06426    69 ---GVNISYVREDKPLGTAGALsLLPEKP--TDPFLVMNGDILTNLN---YEHLLDFHKENNADAtVCVREYE-VQVP-Y 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362 172 GIIEatpIGDRvyKISDMVEKPGMeeapSNLAIIGRYILTPGIIDLLEKtnpgsGKEIQLTDALKKL------VKVSPVY 245
Cdd:cd06426   139 GVVE---TEGG--RITSIEEKPTH----SFLVNAGIYVLEPEVLDLIPK-----NEFFDMPDLIEKLikegkkVGVFPIH 204


                  ..
gi 1085499362 246 GY 247
Cdd:cd06426   205 EY 206
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 14-257 4.97e-16

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: 75.28  E-value: 4.97e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362  14 GLGTRFLPATKASPKEMLPLVDKPLIQYVIEEAISSGIEEVIIVTGRGKRAIEDHFdisyeledllrQKGKRKLlaevqk 93
Cdd:cd06915     7 GLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYLAEQIEEYF-----------GDGYRGG------ 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362  94 isnmMNICYVRQKEPNGLGHAILCTKNLVKNEPFAVLLGDDIIDSDvpaLKQMLDIYNTYSASI-IAVQEVDRSqvSNYG 172
Cdd:cd06915    70 ----IRIYYVIEPEPLGTGGAIKNALPKLPEDQFLVLNGDTYFDVD---LLALLAALRASGADAtMALRRVPDA--SRYG 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362 173 IIEAtpigDRVYKISDMVEK-PGMEEAPSNLAIigrYILTPGIIDLLEKTNPGSgkeiqLTDALKKLVKVSPVYGYKFKG 251
Cdd:cd06915   141 NVTV----DGDGRVIAFVEKgPGAAPGLINGGV---YLLRKEILAEIPADAFSL-----EADVLPALVKRGRLYGFEVDG 208


                  ....*.
gi 1085499362 252 TRYDAG 257
Cdd:cd06915   209 YFIDIG 214
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 7-233 3.32e-14

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 71.24  E-value: 3.32e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362   7 KAVFPVAGLGTRFLPATKASPKEMLPLVDKPLIQYVIEEAISSGIEEVIIVTGRgkraiedhfdisyelEDLLRQKgkrK 86
Cdd:PRK15480    5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTP---------------QDTPRFQ---Q 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362  87 LLAEVQKISnmMNICYVRQKEPNGLGHAILCTKNLVKNEPFAVLLGDDII-DSDVPALkqMLDIYNTYSASIIAVQEVDR 165
Cdd:PRK15480   67 LLGDGSQWG--LNLQYKVQPSPDGLAQAFIIGEEFIGGDDCALVLGDNIFyGHDLPKL--MEAAVNKESGATVFAYHVND 142

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1085499362 166 SQvsNYGIIEATPIGDRVykisDMVEKPgmEEAPSNLAIIGRYILTPGIIDLLEKTNPGSGKEIQLTD 233
Cdd:PRK15480  143 PE--RYGVVEFDQNGTAI----SLEEKP--LQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITD 202
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 8-76 2.33e-12

Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family contains proteins similar to prokaryotic phosphocholine (P-cho) cytidylyltransferases. Phosphocholine (PC) cytidylyltransferases catalyze the transfer of a cytidine monophosphate from CTP to phosphocholine to form CDP-choline. PC is the most abundant phospholipid in eukaryotic membranes and it is also important in prokaryotic membranes. For pathogenic prokaryotes, the cell surface PC facilitates the interaction with host surface and induces attachment and invasion. In addition cell wall PC serves as scaffold for a group of choline-binding proteins that are secreted from the cells. Phosphocholine (PC) cytidylyltransferase is a key enzyme in the prokaryotic choline metabolism pathway. It has been hypothesized to consist of a choline transport system, a choline kinase, CTP:phosphocholine cytidylyltransferase, and a choline phosphotransferase that transfers P-Cho from CDP-Cho to either lipoteichoic acid or lipopolysaccharide.


Pssm-ID: 133014 [Multi-domain]  Cd Length: 229  Bit Score: 64.95  E-value: 2.33e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1085499362   8 AVFPVAGLGTRFLPATKASPKEMLPLVDKPLIQYVIEEAISSGIEEVIIVTGRGKRAIEDHFDISYELE 76
Cdd:cd02523     1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKKYPNIK 69
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
7-70 1.52e-11

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 62.95  E-value: 1.52e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1085499362   7 KAVFPVAGLGTRFLPATKASPKEMLPLVDKPLIQYVIEEAISSGIEEVIIVTGRGKRAIEDHFD 70
Cdd:COG1213     1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEALA 64
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 13-150 2.55e-11

Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 63.51  E-value: 2.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362  13 AGLGTRFLPATkasPKEMLPLVDKPLIQYVIEEAISSGIEEVIIVTGRGKRAIEDHfdisyeledllrqkgkrklLAEVq 92
Cdd:COG1207    10 AGKGTRMKSKL---PKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVRAA-------------------LADL- 66

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1085499362  93 kisnmmNICYVRQKEPNGLGHAILCTKNLVKNEPFAVLlgddIIDSDVP-----ALKQMLDIY 150
Cdd:COG1207    67 ------DVEFVLQEEQLGTGHAVQQALPALPGDDGTVL----VLYGDVPliraeTLKALLAAH 119
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 7-162 7.19e-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: 60.73  E-value: 7.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362   7 KAVFPVAGLGTRFLPATKASPKEMLPLVDKPLIQYVIEEAISSGIEEVIIVTGRGKRAIEDHFDISYELEDLLRQKgkrk 86
Cdd:cd02507     2 QAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQAIIEHLLKSKWSSLSSKMI---- 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1085499362  87 llaeVQKISNMmnicyvrQKEPNGLGHAILCTKNLVKNePFAVLLGDDIIDSD-VPALKQMLDIYNTYSASIIAVQE 162
Cdd:cd02507    78 ----VDVITSD-------LCESAGDALRLRDIRGLIRS-DFLLLSCDLVSNIPlSELLEERRKKDKNAIATLTVLLA 142
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 16-221 1.08e-10

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: 60.73  E-value: 1.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362  16 GTRFLPATKASPKEMLPLVDKPLIQYVIeEAIS--SGIEEVIIVTGrgkraiedhfdisYELEDLlrqkgkRKLLAEVQK 93
Cdd:cd06428    11 GTRFRPLSLDVPKPLFPVAGKPMIHHHI-EACAkvPDLKEVLLIGF-------------YPESVF------SDFISDAQQ 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362  94 ISNmMNICYVRqkEPNGLGHA---------ILctknlvKNEP--FAVLLGDdiIDSDVPaLKQMLDIYNTYSASI-IAVQ 161
Cdd:cd06428    71 EFN-VPIRYLQ--EYKPLGTAgglyhfrdqIL------AGNPsaFFVLNAD--VCCDFP-LQELLEFHKKHGASGtILGT 138

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1085499362 162 EVDRSQVSNYGIIEATPIGDRV--YkisdmVEKPgmEEAPSNLAIIGRYILTPGIIDLLEKT 221
Cdd:cd06428   139 EASREQASNYGCIVEDPSTGEVlhY-----VEKP--ETFVSDLINCGVYLFSPEIFDTIKKA 193
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 13-157 1.40e-10

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: 59.84  E-value: 1.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362  13 AGLGTRFlpatKAS-PKEMLPLVDKPLIQYVIEEAISSGIEEVIIVTGRGKraiedhfdisyeledllrqkgkrkllAEV 91
Cdd:cd02540     6 AGKGTRM----KSDlPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGA--------------------------EQV 55

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1085499362  92 QKISNMMNICYVRQKEPNGLGHAILCTKNLVK--NEPFAVLLGD-DIIDSDvpALKQMLDIYNTYSASI 157
Cdd:cd02540    56 KKALANPNVEFVLQEEQLGTGHAVKQALPALKdfEGDVLVLYGDvPLITPE--TLQRLLEAHREAGADV 122
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 7-79 2.74e-10

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: 59.12  E-value: 2.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362   7 KAVFPVAGLGTRFLPATKASPKEMLPLVDKPLIQYVIEEAISSGIEEVIIVTGRGKRAIEDHF---------DISYELED 77
Cdd:cd06422     1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHLgdsrfglriTISDEPDE 80


                  ..
gi 1085499362  78 LL 79
Cdd:cd06422    81 LL 82
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 8-69 5.16e-09

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: 55.31  E-value: 5.16e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1085499362   8 AVFPVAGLGTRFLPATKASPKEMLPLVDKPLIQYVIEEAISSGIEEVIIVTGRGKRAIEDHF 69
Cdd:cd04197     3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQIKEYI 64
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 143-251 1.05e-08

Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate transport and metabolism];


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 55.47  E-value: 1.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362 143 LKQMLDIYNTYSASI-IAVQEVDRSQVSNYGIIEATPIGdrvyKISDMVEKPgmEEAPSNLAIIGRYILTPGI-IDLLEK 220
Cdd:COG0448   131 YRQMLDFHIESGADItVACIEVPREEASRFGVMEVDEDG----RITEFEEKP--KDPKSALASMGIYVFNKDVlIELLEE 204

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1085499362 221 TNPGS----GKEIqltdaLKKLVKVSPVYGYKFKG 251
Cdd:COG0448   205 DAPNSshdfGKDI-----IPRLLDRGKVYAYEFDG 234
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 7-160 1.43e-08

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


Pssm-ID: 133041 [Multi-domain]  Cd Length: 214  Bit Score: 53.82  E-value: 1.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362   7 KAVFPVAGLGTRFLPATKASPKEMLPLVDKPLIQYVIEEAISSGIEEVIIVTGRgkraiEDHFDISYEL-EDLLRQKGKR 85
Cdd:cd04198     2 QAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPE-----EEQAEISTYLrSFPLNLKQKL 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1085499362  86 KLLAEVqkisnmmnicyvrQKEPNGLGHAILCTKNLVKNEpfAVLLGDDIIdSDVPALKqMLDIYNTYSASIIAV 160
Cdd:cd04198    77 DEVTIV-------------LDEDMGTADSLRHIRKKIKKD--FLVLSCDLI-TDLPLIE-LVDLHRSHDASLTVL 134
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
13-70 2.86e-08

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 52.86  E-value: 2.86e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1085499362  13 AGLGTRFlpatkASPKEMLPLVDKPLIQYVIEEAISSGIEEVIIVTGRGKRAIEDHFD 70
Cdd:COG2068    11 AGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADAEEVAAALA 63
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 13-70 2.28e-07

GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133025 [Multi-domain]  Cd Length: 186  Bit Score: 49.87  E-value: 2.28e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1085499362  13 AGLGTRFlpatkASPKEMLPLVDKPLIQYVIEEAISSGIEEVIIVTGRGKRAIEDHFD 70
Cdd:cd04182     8 AGRSSRM-----GGNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALA 60
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-133 4.75e-06

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 47.55  E-value: 4.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362   1 MATPVTKAVFPVAGLGTRFlpatKAS-PKEMLPLVDKPLIQYVIEEAISSGIEEVIIVTGRGKRAIEdhfdisyeledll 79
Cdd:PRK14353    1 MTDRTCLAIILAAGEGTRM----KSSlPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGPGAEAVA------------- 63

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1085499362  80 rqkgkrkllAEVQKISNMMNIcyVRQKEPNGLGHAILCTKNLVKNEP--FAVLLGD 133
Cdd:PRK14353   64 ---------AAAAKIAPDAEI--FVQKERLGTAHAVLAAREALAGGYgdVLVLYGD 108
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 8-192 1.48e-05

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 45.89  E-value: 1.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362   8 AVFPVAGLGTRFlpaTKASPKEMLPLVDKPLIQYVIEEAISSGIEEVIIVTGRGKRAIEDHFdisyeledllrqkgkrkl 87
Cdd:PRK14355    6 AIILAAGKGTRM---KSDLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHF------------------ 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362  88 laevqkiSNMMNICYVRQKEPNGLGHAILCTKNLVKNEPFAVLlgddIIDSDVP-----ALKQMLDiYNTYSASIIAVQE 162
Cdd:PRK14355   65 -------AGDGDVSFALQEEQLGTGHAVACAAPALDGFSGTVL----ILCGDVPllraeTLQGMLA-AHRATGAAVTVLT 132

                         170       180       190
                  ....*....|....*....|....*....|
gi 1085499362 163 VDRSQVSNYGIIeatpIGDRVYKISDMVEK 192
Cdd:PRK14355  133 ARLENPFGYGRI----VRDADGRVLRIVEE 158
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 7-244 1.60e-05

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 45.91  E-value: 1.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362   7 KAVFPVAGLGTRFlpaTKASPKEMLPLVDKPLIQYVIEEAISSGiEEVIIVTGRGKRAIedhfdisyeledllrqkgkRK 86
Cdd:PRK14357    2 RALVLAAGKGTRM---KSKIPKVLHKISGKPMINWVIDTAKKVA-QKVGVVLGHEAELV-------------------KK 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362  87 LLAEVQKIsnmmnicyVRQKEPNGLGHAILCTKNLV-KNEPFAVLLGddiidsDVP-----ALKQMLDIYNTySASIIAV 160
Cdd:PRK14357   59 LLPEWVKI--------FLQEEQLGTAHAVMCARDFIePGDDLLILYG------DVPlisenTLKRLIEEHNR-KGADVTI 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362 161 QEVDRSQVSNYGIIEATPIGDRVYKISDMVEK-PGMEEAPSNLAII-GRYILTpgiiDLLEKTNPGSGKEIQLTDALKKL 238
Cdd:PRK14357  124 LVADLEDPTGYGRIIRDGGKYRIVEDKDAPEEeKKIKEINTGIYVFsGDFLLE----VLPKIKNENAKGEYYLTDAVNFA 199


                  ....*.
gi 1085499362 239 VKVSPV 244
Cdd:PRK14357  200 EKVRVV 205
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 8-158 1.82e-05

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 45.59  E-value: 1.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362   8 AVFPVAGLGTRFlpatKAS-PKEMLPLVDKPLIQYVIEEAISSGIEEVIIVTGRGKRAIEDHfdisyeLEDLLRqkgkrk 86
Cdd:PRK14354    5 AIILAAGKGTRM----KSKlPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVGHGAEEVKEV------LGDRSE------ 68

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1085499362  87 llaevqkisnmmnicYVRQKEPNGLGHAILCTKNLVKNEPFAVLlgddIIDSDVP-----ALKQMLDIYNT--YSASII 158
Cdd:PRK14354   69 ---------------FALQEEQLGTGHAVMQAEEFLADKEGTTL----VICGDTPlitaeTLKNLIDFHEEhkAAATIL 128
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 114-250 3.23e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 41.74  E-value: 3.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362 114 AILCTKNLVKNE-P--FAVLLGDDIIDSDVpalKQMLD--IYNTYSASIIAVqEVDRSQVSNYGIIEATPIGdrvyKISD 188
Cdd:PRK00844  104 AIYQSLNLIEDEdPdyVVVFGADHVYRMDP---RQMVDfhIESGAGVTVAAI-RVPREEASAFGVIEVDPDG----RIRG 175

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1085499362 189 MVEKP----GMEEAPSN-LAIIGRYILTPGI-IDLLEK--TNPGS----GKEIqltdaLKKLVKVSPVYGYKFK 250
Cdd:PRK00844  176 FLEKPadppGLPDDPDEaLASMGNYVFTTDAlVDALRRdaADEDSshdmGGDI-----IPRLVERGRAYVYDFS 244
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 14-58 3.74e-04

GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP:adenosylcobinamide-phosphate guanylyltransferase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441867 [Multi-domain]  Cd Length: 185  Bit Score: 40.64  E-value: 3.74e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1085499362  14 GLGTRFLPATKAspkeMLPLVDKPLIQYVIEEAISSGIEEVIIVT 58
Cdd:COG2266     4 GKGTRLGGGEKP----LLEICGKPMIDRVIDALEESCIDKIYVAV 44
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
 9-208 4.07e-04

GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; GT2_BcbE_like: The bcbE gene is one of the genes in the capsule biosynthetic locus of Pasteurella multocida. Its deducted product is likely involved in the biosynthesis of the polysaccharide capsule, which is found on surface of a wide range of bacteria. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.


Pssm-ID: 133026 [Multi-domain]  Cd Length: 231  Bit Score: 40.70  E-value: 4.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362   9 VFPVAGLGTRFLPATKASPKEMLPLVDKPLIQYVIEEAISSGIEEVIIVTgrgkraiedhfdisyeledllrqkgkRKLL 88
Cdd:cd04183     2 IIPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEWVIESLAKIFDSRFIFIC--------------------------RDEH 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362  89 AEVQKISNMmnicyVRQKEPNGlghAILCTKNLVKNEPFAVLLGDDIIDSDVPALKQMLDIY--NTYSASIIAVQEVDRS 166
Cdd:cd04183    56 NTKFHLDES-----LKLLAPNA---TVVELDGETLGAACTVLLAADLIDNDDPLLIFNCDQIveSDLLAFLAAFRERDLD 127

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1085499362 167 QvsnyGIIEATPIGDRvY---KISD--MVEKPGMEEAPSNLAIIGRY 208
Cdd:cd04183   128 G----GVLTFFSSHPR-WsyvKLDEngRVIETAEKEPISDLATAGLY 169
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 9-117 7.54e-04

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 40.73  E-value: 7.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085499362   9 VFPVAGLGTRFlpaTKASPKEMLPLVDKPLIQYVIEEAISSGIEEVIIVTGRGKRaiedhfdisyELEDLLRQKGkrkll 88
Cdd:PRK14358   11 VILAAGQGTRM---KSALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGAE----------QVEAALQGSG----- 72

                          90       100
                  ....*....|....*....|....*....
gi 1085499362  89 aevqkisnmmnICYVRQKEPNGLGHAILC 117
Cdd:PRK14358   73 -----------VAFARQEQQLGTGDAFLS 90
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 13-60 9.31e-04

MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine dinucleotide biosynthesis protein A). The family also includes a wide range of other NTP transferase domain.


Pssm-ID: 463715 [Multi-domain]  Cd Length: 159  Bit Score: 39.10  E-value: 9.31e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1085499362  13 AGLGTRFlpatkASPKEMLPLVDKPLIQYVIEEAISSGiEEVIIVTGR 60
Cdd:pfam12804   6 GGRSSRM-----GGDKALLPLGGKPLLERVLERLRPAG-DEVVVVAND 47
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 13-88 1.70e-03

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440824  Cd Length: 224  Bit Score: 38.96  E-value: 1.70e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1085499362  13 AGLGTRFlpaTKASPKEMLPLVDKPLIQYVIEEAISSG-IEEVIIVTGRGkraiedhfDISYeLEDLLRQKGKRKLL 88
Cdd:COG1211     5 AGSGSRM---GAGIPKQFLPLGGKPVLEHTLEAFLAHPrIDEIVVVVPPD--------DIEY-FEELLAKYGIDKPV 69
CMP-NeuAc_Synthase cd02513
CMP-NeuAc_Synthase activates N-acetylneuraminic acid by adding CMP moiety; ...
 28-58 2.47e-03

CMP-NeuAc_Synthase activates N-acetylneuraminic acid by adding CMP moiety; CMP-N-acetylneuraminic acid synthetase (CMP-NeuAc synthetase) or acylneuraminate cytidylyltransferase catalyzes the transfer the CMP moiety of CTP to the anomeric hydroxyl group of NeuAc in the presence of Mg++. It is the second to last step in the sialylation of the oligosaccharide component of glycoconjugates by providing the activated sugar-nucleotide cytidine 5'-monophosphate N-acetylneuraminic acid (CMP-Neu5Ac), the substrate for sialyltransferases. Eukaryotic CMP-NeuAc synthetases are predominantly located in the nucleus. The activated CMP-Neu5Ac diffuses from the nucleus into the cytoplasm.


Pssm-ID: 133006  Cd Length: 223  Bit Score: 38.29  E-value: 2.47e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1085499362  28 KEMLPLVDKPLIQYVIEEAISSGIEEVIIVT 58
Cdd:cd02513    18 KNIRPLGGKPLIAWTIEAALESKLFDRVVVS 48
NeuA COG1083
CMP-N-acetylneuraminic acid synthetase, NeuA/PseF family [Cell wall/membrane/envelope ...
 28-58 9.42e-03

CMP-N-acetylneuraminic acid synthetase, NeuA/PseF family [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440700  Cd Length: 228  Bit Score: 36.68  E-value: 9.42e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1085499362  28 KEMLPLVDKPLIQYVIEEAISSG-IEEVIIVT 58
Cdd:COG1083    19 KNIRPLAGKPLIAYSIEAALKSGlFDRVVVST 50
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
8-58 9.46e-03

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 36.65  E-value: 9.46e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1085499362   8 AVFPVAGLGTRFlpatKAS-PKEMLPLVDKPLIQYVIEEAISSG-IEEVIIVT 58
Cdd:PRK00155    6 AIIPAAGKGSRM----GADrPKQYLPLGGKPILEHTLEAFLAHPrIDEIIVVV 54
 
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.
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