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Conserved domains on  [gi|157412259|ref|NP_001094896|]
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D-ribitol-5-phosphate cytidylyltransferase isoform a [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ISPD_C pfam18706
D-ribitol-5-phosphate cytidylyltransferase C-terminal domain; This domain is located at the ...
 283-451 3.85e-108

D-ribitol-5-phosphate cytidylyltransferase C-terminal domain; This domain is located at the C-terminal region of ISPD (isoprenoid synthase domain containing protein, EC:2.7.7.40), pfam01128. Structural homologs can be found in two distinct alpha/beta protein families including the seven-stranded NAD(P) (H)-dependent short-chain dehydrogenases/reductases and five-stranded response regulator proteins involved in bacterial sensing systems.


:

Pssm-ID: 465843  Cd Length: 169  Bit Score: 316.98  E-value: 3.85e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412259  283 QEICVVMDTEEDNKHVGHLLEEVLKSELNHVKVTSEALGHAGRHLQQIILDQCYNFVCVNVTTSDFQETQKLLSMLEESS 362
Cdd:pfam18706   1 QEICVVTDTKEDAEHVGHLLEEVLKSELNHVKVTSTSLCPDGSDLQQIILEQCYNFICVNVKTSDFQETQKLVSMLEESN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412259  363 LCILYPVVVVSVHFLDFKLVPPSQKMENLMQIREFAKEVKERNILLYGLLISYPQDDQKLQESLRQGAIIIASLIKERNS 442
Cdd:pfam18706  81 LSILYPVVVVSVHLLDFKSVSFSQKMENLMAIREFAKEVKKRNILLYGLLINYSQDEQKLQESLRQGAAIIAALIKERNP 160


                  ....*....
gi 157412259  443 GLIGQLLIA 451
Cdd:pfam18706 161 ALVGQLLVA 169
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 47-273 3.21e-81

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: 250.13  E-value: 3.21e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412259  47 VAAVLPAGGCGERMGVPTPKQFCPILERPLISYTLQALERVCWIKDIVVAVTGENMEVMKSIIQKYQHKRISLVEAGVTR 126
Cdd:cd02516    1 VAAIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDIDLAKELAKYGLSKVVKIVEGGATR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412259 127 HRSIFNGLKALAEDqinsklsKPEVVIIHDAVRPFVEEGVLLKVVTAAKEHGAAGAIRPLVSTVVSPSADGCLDYSLERA 206
Cdd:cd02516   81 QDSVLNGLKALPDA-------DPDIVLIHDAARPFVSPELIDRLIDALKEYGAAIPAVPVTDTIKRVDDDGVVVETLDRE 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157412259 207 RHRASEMPQAFLFDVIYEAYQQCSDYDLEFgTECLQLALKyCCTKAKLVEGSPDLWKVTYKRDLYAA 273
Cdd:cd02516  154 KLWAAQTPQAFRLDLLLKAHRQASEEGEEF-TDDASLVEA-AGGKVALVEGSEDNIKITTPEDLALA 218
 
Name Accession Description Interval E-value
ISPD_C pfam18706
D-ribitol-5-phosphate cytidylyltransferase C-terminal domain; This domain is located at the ...
 283-451 3.85e-108

D-ribitol-5-phosphate cytidylyltransferase C-terminal domain; This domain is located at the C-terminal region of ISPD (isoprenoid synthase domain containing protein, EC:2.7.7.40), pfam01128. Structural homologs can be found in two distinct alpha/beta protein families including the seven-stranded NAD(P) (H)-dependent short-chain dehydrogenases/reductases and five-stranded response regulator proteins involved in bacterial sensing systems.


Pssm-ID: 465843  Cd Length: 169  Bit Score: 316.98  E-value: 3.85e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412259  283 QEICVVMDTEEDNKHVGHLLEEVLKSELNHVKVTSEALGHAGRHLQQIILDQCYNFVCVNVTTSDFQETQKLLSMLEESS 362
Cdd:pfam18706   1 QEICVVTDTKEDAEHVGHLLEEVLKSELNHVKVTSTSLCPDGSDLQQIILEQCYNFICVNVKTSDFQETQKLVSMLEESN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412259  363 LCILYPVVVVSVHFLDFKLVPPSQKMENLMQIREFAKEVKERNILLYGLLISYPQDDQKLQESLRQGAIIIASLIKERNS 442
Cdd:pfam18706  81 LSILYPVVVVSVHLLDFKSVSFSQKMENLMAIREFAKEVKKRNILLYGLLINYSQDEQKLQESLRQGAAIIAALIKERNP 160


                  ....*....
gi 157412259  443 GLIGQLLIA 451
Cdd:pfam18706 161 ALVGQLLVA 169
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 47-273 3.21e-81

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: 250.13  E-value: 3.21e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412259  47 VAAVLPAGGCGERMGVPTPKQFCPILERPLISYTLQALERVCWIKDIVVAVTGENMEVMKSIIQKYQHKRISLVEAGVTR 126
Cdd:cd02516    1 VAAIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDIDLAKELAKYGLSKVVKIVEGGATR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412259 127 HRSIFNGLKALAEDqinsklsKPEVVIIHDAVRPFVEEGVLLKVVTAAKEHGAAGAIRPLVSTVVSPSADGCLDYSLERA 206
Cdd:cd02516   81 QDSVLNGLKALPDA-------DPDIVLIHDAARPFVSPELIDRLIDALKEYGAAIPAVPVTDTIKRVDDDGVVVETLDRE 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157412259 207 RHRASEMPQAFLFDVIYEAYQQCSDYDLEFgTECLQLALKyCCTKAKLVEGSPDLWKVTYKRDLYAA 273
Cdd:cd02516  154 KLWAAQTPQAFRLDLLLKAHRQASEEGEEF-TDDASLVEA-AGGKVALVEGSEDNIKITTPEDLALA 218
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 50-280 4.75e-59

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: 193.04  E-value: 4.75e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412259  50 VLPAGGCGERMGVPTPKQFCPILERPLISYTLQALERVCWIKDIVVAVTGENMEVMKSIIQKYQ-HKRISLVEAGVTRHR 128
Cdd:COG1211    1 IIPAAGSGSRMGAGIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPDDIEYFEELLAKYGiDKPVRVVAGGATRQD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412259 129 SIFNGLKALAEDqinsklskPEVVIIHDAVRPFVEEGVLLKVVTAAKEHGAAGAIRPLVSTVVSPSADGCLDYSLERARH 208
Cdd:COG1211   81 SVRNGLEALPDD--------DDWVLVHDAARPLVSPELIDRVIEAAREYGAAIPALPVTDTIKRVDDDGRVTETVDRSGL 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157412259 209 RASEMPQAFLFDVIYEAYQQCSDYDLEFGTEClQLALKyCCTKAKLVEGSPDLWKVTYKRDLYAAESIIKER 280
Cdd:COG1211  153 WAAQTPQGFRLDLLLEAHEAAAADGLEFTDDA-SLVER-LGLPVRLVEGSEDNIKITTPEDLALAEALLRSR 222
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
44-281 5.21e-53

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 177.25  E-value: 5.21e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412259  44 PQAVAAVLPAGGCGERMGVPTPKQFCPILERPLISYTLQALERVCWIKDIVVAVTGENMEVMKSIIQKYqHKRISLVEAG 123
Cdd:PRK00155   1 MMMVYAIIPAAGKGSRMGADRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDRPDFAELLLAK-DPKVTVVAGG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412259 124 VTRHRSIFNGLKALAEDqinsklskpEVVIIHDAVRPFVEEGVLLKVVTAAKEHGAAGAIRPLVSTVVSPSADGCLDYSL 203
Cdd:PRK00155  80 AERQDSVLNGLQALPDD---------DWVLVHDAARPFLTPDDIDRLIEAAEETGAAILAVPVKDTIKRSDDGGGIVDTP 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157412259 204 ERARHRASEMPQAFLFDVIYEAYQQCSDYDLEFGTEClqLALKYCCTKAKLVEGSPDLWKVTYKRDLYAAESIIKERI 281
Cdd:PRK00155 151 DRSGLWAAQTPQGFRIELLREALARALAEGKTITDDA--SAVERLGKPVRLVEGRYDNIKITTPEDLALAEAILKRRI 226
ispD TIGR00453
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ...
 48-276 8.96e-45

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase, the IspD protein of the deoxyxylulose pathway of IPP biosynthesis. In about twenty percent of bacterial genomes, this protein occurs as IspDF, a bifunctional fusion protein. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 213532  Cd Length: 217  Bit Score: 155.52  E-value: 8.96e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412259   48 AAVLPAGGCGERMGVPTPKQFCPILERPLISYTLQALERVCWIKDIVVAVTGENMEVMKSIIQKYQHkrISLVEAGVTRH 127
Cdd:TIGR00453   1 SAVIPAAGRGTRFGSGVPKQYLELGGRPLLEHALDAFLAHPAIDEVVVVVSPDDTEFFQKYLVARAV--PKIVAGGDTRQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412259  128 RSIFNGLKALAEdqinsklskPEVVIIHDAVRPFVEEGVLLKVVTAAKEHGAAGAIRPLVSTVVSPSADGCLDYSLERAR 207
Cdd:TIGR00453  79 DSVRNGLKALKD---------AEFVLVHDAARPFVPKELLDRLLEALRKAGAAILALPVADTLKRVEADGFVVETVDREG 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157412259  208 HRASEMPQAFLFDVIYEAYQQCSDYDLEFGTEClqLALKYCCTKAKLVEGSPDLWKVTYKRDLYAAESI 276
Cdd:TIGR00453 150 LWAAQTPQAFRTELLKKALARAKLEGFEITDDA--SAVEKLGGKVQLVEGDALNFKITTPEDLALAEAL 216
IspD pfam01128
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ...
 49-279 6.35e-38

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes which catalyze the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from cytidine triphosphate and 2-C-methyl-D-erythritol 4-phosphate (MEP).


Pssm-ID: 460075  Cd Length: 219  Bit Score: 137.20  E-value: 6.35e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412259   49 AVLPAGGCGERMGVPTPKQFCPILERPLISYTLQALERVCWIKDIVVAVTGENMEVMKSIIqkyQHKRISLVEAGVTRHR 128
Cdd:pfam01128   1 AVIPAAGSGKRMGAGVPKQFLQLLGQPLLEHTVDAFLASPVVDRIVVAVSPDDTPEFRQLL---GDPSIQLVAGGDTRQD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412259  129 SIFNGLKALAEDQinsklskpEVVIIHDAVRPFVEEGVLLKVVTAAKEH--GAAGAIrPLVSTVVSPSADGCLDYSLERA 206
Cdd:pfam01128  78 SVLNGLKALAGTA--------KFVLVHDGARPCLPHADLARLLAALETGtqGAILAL-PVTDTIKRVEADGVVAGTPDRS 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157412259  207 RHRASEMPQAFLFDVIYEAYQQCSDYDLEFGTEClqLALKYCCTKAKLVEGSPDLWKVTYKRDLYAAESIIKE 279
Cdd:pfam01128 149 GLWAAQTPQGFRVDLLLAAHQRGDQPGAEITDDA--SLVEHAGGSVQVVPGRPDNLKITTPEDLALAEAILTR 219
 
Name Accession Description Interval E-value
ISPD_C pfam18706
D-ribitol-5-phosphate cytidylyltransferase C-terminal domain; This domain is located at the ...
 283-451 3.85e-108

D-ribitol-5-phosphate cytidylyltransferase C-terminal domain; This domain is located at the C-terminal region of ISPD (isoprenoid synthase domain containing protein, EC:2.7.7.40), pfam01128. Structural homologs can be found in two distinct alpha/beta protein families including the seven-stranded NAD(P) (H)-dependent short-chain dehydrogenases/reductases and five-stranded response regulator proteins involved in bacterial sensing systems.


Pssm-ID: 465843  Cd Length: 169  Bit Score: 316.98  E-value: 3.85e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412259  283 QEICVVMDTEEDNKHVGHLLEEVLKSELNHVKVTSEALGHAGRHLQQIILDQCYNFVCVNVTTSDFQETQKLLSMLEESS 362
Cdd:pfam18706   1 QEICVVTDTKEDAEHVGHLLEEVLKSELNHVKVTSTSLCPDGSDLQQIILEQCYNFICVNVKTSDFQETQKLVSMLEESN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412259  363 LCILYPVVVVSVHFLDFKLVPPSQKMENLMQIREFAKEVKERNILLYGLLISYPQDDQKLQESLRQGAIIIASLIKERNS 442
Cdd:pfam18706  81 LSILYPVVVVSVHLLDFKSVSFSQKMENLMAIREFAKEVKKRNILLYGLLINYSQDEQKLQESLRQGAAIIAALIKERNP 160


                  ....*....
gi 157412259  443 GLIGQLLIA 451
Cdd:pfam18706 161 ALVGQLLVA 169
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 47-273 3.21e-81

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: 250.13  E-value: 3.21e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412259  47 VAAVLPAGGCGERMGVPTPKQFCPILERPLISYTLQALERVCWIKDIVVAVTGENMEVMKSIIQKYQHKRISLVEAGVTR 126
Cdd:cd02516    1 VAAIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDIDLAKELAKYGLSKVVKIVEGGATR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412259 127 HRSIFNGLKALAEDqinsklsKPEVVIIHDAVRPFVEEGVLLKVVTAAKEHGAAGAIRPLVSTVVSPSADGCLDYSLERA 206
Cdd:cd02516   81 QDSVLNGLKALPDA-------DPDIVLIHDAARPFVSPELIDRLIDALKEYGAAIPAVPVTDTIKRVDDDGVVVETLDRE 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157412259 207 RHRASEMPQAFLFDVIYEAYQQCSDYDLEFgTECLQLALKyCCTKAKLVEGSPDLWKVTYKRDLYAA 273
Cdd:cd02516  154 KLWAAQTPQAFRLDLLLKAHRQASEEGEEF-TDDASLVEA-AGGKVALVEGSEDNIKITTPEDLALA 218
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 50-280 4.75e-59

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: 193.04  E-value: 4.75e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412259  50 VLPAGGCGERMGVPTPKQFCPILERPLISYTLQALERVCWIKDIVVAVTGENMEVMKSIIQKYQ-HKRISLVEAGVTRHR 128
Cdd:COG1211    1 IIPAAGSGSRMGAGIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPDDIEYFEELLAKYGiDKPVRVVAGGATRQD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412259 129 SIFNGLKALAEDqinsklskPEVVIIHDAVRPFVEEGVLLKVVTAAKEHGAAGAIRPLVSTVVSPSADGCLDYSLERARH 208
Cdd:COG1211   81 SVRNGLEALPDD--------DDWVLVHDAARPLVSPELIDRVIEAAREYGAAIPALPVTDTIKRVDDDGRVTETVDRSGL 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157412259 209 RASEMPQAFLFDVIYEAYQQCSDYDLEFGTEClQLALKyCCTKAKLVEGSPDLWKVTYKRDLYAAESIIKER 280
Cdd:COG1211  153 WAAQTPQGFRLDLLLEAHEAAAADGLEFTDDA-SLVER-LGLPVRLVEGSEDNIKITTPEDLALAEALLRSR 222
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
44-281 5.21e-53

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 177.25  E-value: 5.21e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412259  44 PQAVAAVLPAGGCGERMGVPTPKQFCPILERPLISYTLQALERVCWIKDIVVAVTGENMEVMKSIIQKYqHKRISLVEAG 123
Cdd:PRK00155   1 MMMVYAIIPAAGKGSRMGADRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDRPDFAELLLAK-DPKVTVVAGG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412259 124 VTRHRSIFNGLKALAEDqinsklskpEVVIIHDAVRPFVEEGVLLKVVTAAKEHGAAGAIRPLVSTVVSPSADGCLDYSL 203
Cdd:PRK00155  80 AERQDSVLNGLQALPDD---------DWVLVHDAARPFLTPDDIDRLIEAAEETGAAILAVPVKDTIKRSDDGGGIVDTP 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157412259 204 ERARHRASEMPQAFLFDVIYEAYQQCSDYDLEFGTEClqLALKYCCTKAKLVEGSPDLWKVTYKRDLYAAESIIKERI 281
Cdd:PRK00155 151 DRSGLWAAQTPQGFRIELLREALARALAEGKTITDDA--SAVERLGKPVRLVEGRYDNIKITTPEDLALAEAILKRRI 226
ispD TIGR00453
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ...
 48-276 8.96e-45

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase, the IspD protein of the deoxyxylulose pathway of IPP biosynthesis. In about twenty percent of bacterial genomes, this protein occurs as IspDF, a bifunctional fusion protein. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 213532  Cd Length: 217  Bit Score: 155.52  E-value: 8.96e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412259   48 AAVLPAGGCGERMGVPTPKQFCPILERPLISYTLQALERVCWIKDIVVAVTGENMEVMKSIIQKYQHkrISLVEAGVTRH 127
Cdd:TIGR00453   1 SAVIPAAGRGTRFGSGVPKQYLELGGRPLLEHALDAFLAHPAIDEVVVVVSPDDTEFFQKYLVARAV--PKIVAGGDTRQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412259  128 RSIFNGLKALAEdqinsklskPEVVIIHDAVRPFVEEGVLLKVVTAAKEHGAAGAIRPLVSTVVSPSADGCLDYSLERAR 207
Cdd:TIGR00453  79 DSVRNGLKALKD---------AEFVLVHDAARPFVPKELLDRLLEALRKAGAAILALPVADTLKRVEADGFVVETVDREG 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157412259  208 HRASEMPQAFLFDVIYEAYQQCSDYDLEFGTEClqLALKYCCTKAKLVEGSPDLWKVTYKRDLYAAESI 276
Cdd:TIGR00453 150 LWAAQTPQAFRTELLKKALARAKLEGFEITDDA--SAVEKLGGKVQLVEGDALNFKITTPEDLALAEAL 216
IspD pfam01128
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ...
 49-279 6.35e-38

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes which catalyze the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from cytidine triphosphate and 2-C-methyl-D-erythritol 4-phosphate (MEP).


Pssm-ID: 460075  Cd Length: 219  Bit Score: 137.20  E-value: 6.35e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412259   49 AVLPAGGCGERMGVPTPKQFCPILERPLISYTLQALERVCWIKDIVVAVTGENMEVMKSIIqkyQHKRISLVEAGVTRHR 128
Cdd:pfam01128   1 AVIPAAGSGKRMGAGVPKQFLQLLGQPLLEHTVDAFLASPVVDRIVVAVSPDDTPEFRQLL---GDPSIQLVAGGDTRQD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412259  129 SIFNGLKALAEDQinsklskpEVVIIHDAVRPFVEEGVLLKVVTAAKEH--GAAGAIrPLVSTVVSPSADGCLDYSLERA 206
Cdd:pfam01128  78 SVLNGLKALAGTA--------KFVLVHDGARPCLPHADLARLLAALETGtqGAILAL-PVTDTIKRVEADGVVAGTPDRS 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157412259  207 RHRASEMPQAFLFDVIYEAYQQCSDYDLEFGTEClqLALKYCCTKAKLVEGSPDLWKVTYKRDLYAAESIIKE 279
Cdd:pfam01128 149 GLWAAQTPQGFRVDLLLAAHQRGDQPGAEITDDA--SLVEHAGGSVQVVPGRPDNLKITTPEDLALAEAILTR 219
ispDF PRK09382
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ...
 47-274 6.35e-31

bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase protein; Provisional


Pssm-ID: 236492 [Multi-domain]  Cd Length: 378  Bit Score: 122.65  E-value: 6.35e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412259  47 VAAVLPAGGCGERMGVPTPKQFCPILERPLISYTLQALERVCWIKDIVVAVTGENMEVMKSIIQKYQHKRIslVEAGVTR 126
Cdd:PRK09382   6 ISLVIVAAGRSTRFSAEVKKQWLRIGGKPLWLHVLENLSSAPAFKEIVVVIHPDDIAYMKKALPEIKFVTL--VTGGATR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412259 127 HRSIFNGLKALAEdqinsklskpEVVIIHDAVRPFVEEGVLLKVVTAAKEHGAAGAIRPLVSTVVspSADGCLDysleRA 206
Cdd:PRK09382  84 QESVRNALEALDS----------EYVLIHDAARPFVPKELIDRLIEALDKADCVLPALPVADTLK--RANETVD----RE 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157412259 207 RHRASEMPQAFLFDVIYEAYQQcsdyDLEFGTEclQLALKYCCTKAKLVEGSPDLWKVTYKRDLYAAE 274
Cdd:PRK09382 148 GLKLIQTPQLSRTKTLKAAADG----RGDFTDD--SSAAEAAGGKVALVEGSEDLHKLTYKEDLKMAD 209
PLN02728 PLN02728
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
 45-285 9.29e-24

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase


Pssm-ID: 215387  Cd Length: 252  Bit Score: 99.81  E-value: 9.29e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412259  45 QAVAAVLPAGGCGERMGVPTPKQFCPILERPLISYTLQALERVCWIKDIVVAVTGENMEVMKSIIQKYqHKRISLVEAGV 124
Cdd:PLN02728  23 KSVSVILLAGGVGKRMGANMPKQYLPLLGQPIALYSLYTFARMPEVKEIVVVCDPSYRDVFEEAVENI-DVPLKFALPGK 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412259 125 TRHRSIFNGLKALAEDQinsklskpEVVIIHDAVRPFVEEGVLLKVVTAAKEHGAAGAIRPLVSTVVSPSADGCLDYSLE 204
Cdd:PLN02728 102 ERQDSVFNGLQEVDANS--------ELVCIHDSARPLVTSADIEKVLKDAAVHGAAVLGVPVKATIKEANSDSFVVKTLD 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412259 205 RARHRASEMPQAFLFDVIYEAYQQCSDYDLEFgTECLQL--ALKYcctKAKLVEGSPDLWKVTYKRDLYAAESIIKERIS 282
Cdd:PLN02728 174 RKRLWEMQTPQVIKPELLRRGFELVEREGLEV-TDDVSIveALKH---PVFITEGSYTNIKVTTPDDMLVAERILNERSD 249


                 ...
gi 157412259 283 QEI 285
Cdd:PLN02728 250 AEV 252
PRK13385 PRK13385
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Provisional
 48-284 4.57e-21

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Provisional


Pssm-ID: 184017  Cd Length: 230  Bit Score: 91.47  E-value: 4.57e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412259  48 AAVLPAGGCGERMGVPTPKQFCPILERPLISYTLQALERVCWIKDIVVAVTGENMEVMKSIIQKYQ--HKRISLVEAGVT 125
Cdd:PRK13385   4 ELIFLAAGQGKRMNAPLNKMWLDLVGEPIFIHALRPFLADNRCSKIIIVTQAQERKHVQDLMKQLNvaDQRVEVVKGGTE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412259 126 RHRSIFNGLkalaeDQINSKlskpEVVIIHDAVRPFVEEGVLLKVVTAAKEHGAAGAIRPLVSTVVSpSADGCLDYSLER 205
Cdd:PRK13385  84 RQESVAAGL-----DRIGNE----DVILVHDGARPFLTQDIIDRLLEGVAKYGAAICAVEVKDTVKR-VKDKQVIETVDR 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157412259 206 ARHRASEMPQAFLFDVIYEAYQQCSDyDLEFGTECLQLALKYCCTkAKLVEGSPDLWKVTYKRDLYAAESIIKERISQE 284
Cdd:PRK13385 154 NELWQGQTPQAFELKILQKAHRLASE-QQFLGTDEASLVERSPHP-VKLVQGSYYNIKLTTPEDMPLAKAILQGDIADD 230
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
47-185 2.29e-07

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 50.93  E-value: 2.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412259  47 VAAVLPAGGCGERMGvpTPKQFCPILERPLISYTLQALERVCWikDIVVAVTGENMEvmkSIIQKYQHKRISLVEagVTR 126
Cdd:COG2068    4 VAAIILAAGASSRMG--RPKLLLPLGGKPLLERAVEAALAAGL--DPVVVVLGADAE---EVAAALAGLGVRVVV--NPD 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157412259 127 HR-----SIFNGLKALAEDqinsklskPEVVIIHDAVRPFVEEGVLLKVVTAAKEHGAAgAIRP 185
Cdd:COG2068   75 WEegmssSLRAGLAALPAD--------ADAVLVLLGDQPLVTAETLRRLLAAFRESPAS-IVAP 129
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 49-200 2.50e-07

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: 51.04  E-value: 2.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412259  49 AVLPAGGCGERMGvP----TPKQFCPILERPLISYTLQALERVcWIKDIVVAVTGenmevMKSIIQKY------QHKRIS 118
Cdd:cd04181    1 AVILAAGKGTRLR-PltdtRPKPLLPIAGKPILEYIIERLARA-GIDEIILVVGY-----LGEQIEEYfgdgskFGVNIE 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412259 119 LV---EAGVTRHrSIFNGLKALAEDqinsklskpEVVIIH-DAVrpFVEEgvLLKVVTAAKEHGAAGAIrpLVSTVVSPS 194
Cdd:cd04181   74 YVvqeEPLGTAG-AVRNAEDFLGDD---------DFLVVNgDVL--TDLD--LSELLRFHREKGADATI--AVKEVEDPS 137


                 ....*.
gi 157412259 195 ADGCLD 200
Cdd:cd04181  138 RYGVVE 143
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 49-97 1.99e-06

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: 48.61  E-value: 1.99e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 157412259  49 AVLPAGGCGERMGvP----TPKQFCPILERPLISYTLQALERvCWIKDIVVAV 97
Cdd:COG1208    2 AVILAGGLGTRLR-PltdtRPKPLLPVGGKPLLEHILERLAA-AGITEIVINV 52
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 49-115 1.18e-05

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: 46.11  E-value: 1.18e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412259  49 AVLPAGGCGERMGVPT---PKQFCPILERPLISYTLQALERVCwIKDIVVAVTGENMEVMKSIIQKYQHK 115
Cdd:cd04198    3 AVILAGGGGSRLYPLTdniPKALLPVANKPMIWYPLDWLEKAG-FEDVIVVVPEEEQAEISTYLRSFPLN 71
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
49-99 8.71e-05

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 43.69  E-value: 8.71e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 157412259  49 AVLPAGGCGERMGVPT---PKQFCPILERPLISYTLQALERVCwIKDIVVaVTG 99
Cdd:COG1213    2 AVILAAGRGSRLGPLTddiPKCLVEIGGKTLLERQLEALAAAG-IKDIVV-VTG 53
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 53-98 1.01e-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: 42.95  E-value: 1.01e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 157412259  53 AGGCGERMGvPTPKQFCPILERPLISYTLQALERVCwIKDIVVAVT 98
Cdd:COG2266    2 AGGKGTRLG-GGEKPLLEICGKPMIDRVIDALEESC-IDKIYVAVS 45
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 49-121 1.35e-04

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: 42.99  E-value: 1.35e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157412259  49 AVLPAGGCGERMGVPT---PKQFCPILERPLISYTLQALERvCWIKDIVVaVTGENMEVMKSIIQKYQHkrISLVE 121
Cdd:cd02523    1 AIILAAGRGSRLRPLTedrPKCLLEINGKPLLERQIETLKE-AGIDDIVI-VTGYKKEQIEELLKKYPN--IKFVY 72
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 49-121 8.26e-04

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: 40.70  E-value: 8.26e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157412259  49 AVLPAGGCGERMGVPT---PKQFCPILERPLISYTLQALERVCwIKDIVVAVTGENMEVMKSIIQKYQHKRISLVE 121
Cdd:cd02507    3 AVVLADGFGSRFLPLTsdiPKALLPVANVPLIDYTLEWLEKAG-VEEVFVVCCEHSQAIIEHLLKSKWSSLSSKMI 77
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 47-101 1.40e-03

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


Pssm-ID: 133025 [Multi-domain]  Cd Length: 186  Bit Score: 39.47  E-value: 1.40e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 157412259  47 VAAVLPAGGCGERMGvpTPKQFCPILERPLISYTLQALERVCwIKDIVVaVTGEN 101
Cdd:cd04182    1 IAAIILAAGRSSRMG--GNKLLLPLDGKPLLRHALDAALAAG-LSRVIV-VLGAE 51
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 49-99 1.67e-03

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: 1.67e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 157412259   49 AVLPAGGCGERMGvpTPKQFCPILERPLISYTLQALERVCwikDIVVAVTG 99
Cdd:pfam12804   1 AVILAGGRSSRMG--GDKALLPLGGKPLLERVLERLRPAG---DEVVVVAN 46
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 49-109 1.82e-03

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: 39.86  E-value: 1.82e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157412259  49 AVLPAGGCGERMGvP----TPKQFCPILERPLISYTLQALeRVCWIKDIVVaVTGENMEVMKSII 109
Cdd:cd04189    3 GLILAGGKGTRLR-PltytRPKQLIPVAGKPIIQYAIEDL-REAGIEDIGI-VVGPTGEEIKEAL 64
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 48-95 2.44e-03

Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; Molybdopterin-guanine dinucleotide biosynthesis protein A is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 440509 [Multi-domain]  Cd Length: 188  Bit Score: 39.02  E-value: 2.44e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 157412259  48 AAVLpAGGCGERMGVptPKQFCPILERPLISYTLQALERVCWikDIVV 95
Cdd:COG0746    7 GVIL-AGGRSRRMGQ--DKALLPLGGRPLLERVLERLRPQVD--EVVI 49
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 49-122 2.70e-03

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: 39.44  E-value: 2.70e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157412259  49 AVLPAGGCGERMgVP----TPKQFCPILERPLISYTLQ-ALErvCWIKDIVVaVTGENmevmKSIIQKYQHKRISLVEA 122
Cdd:cd02541    3 AVIPAAGLGTRF-LPatkaIPKEMLPIVDKPVIQYIVEeAVA--AGIEDIII-VTGRG----KRAIEDHFDRSYELEET 73
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 48-225 6.30e-03

MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme molybdopterin-guanine dinucleotide biosynthesis protein A (MobA). All mononuclear molybdoenzymes bind molybdenum in complex with an organic cofactor termed molybdopterin (MPT). In many bacteria, including Escherichia coli, molybdopterin can be further modified by attachment of a GMP group to the terminal phosphate of molybdopterin to form molybdopterin guanine dinucleotide (MGD). This GMP attachment step is catalyzed by MobA, by linking a guanosine 5'-phosphate to MPT forming molybdopterin guanine dinucleotide. This reaction requires GTP, MgCl2, and the MPT form of the cofactor. It is a reaction unique to prokaryotes, and therefore may represent a potential drug target.


Pssm-ID: 133000 [Multi-domain]  Cd Length: 181  Bit Score: 37.56  E-value: 6.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412259  48 AAVLpAGGCGERMGvpTPKQFCPILERPLISYTLQALERVCwikDIVVAVTGENmevmksiIQKYQHKRISLVE------ 121
Cdd:cd02503    3 GVIL-AGGKSRRMG--GDKALLELGGKPLLEHVLERLKPLV---DEVVISANRD-------QERYALLGVPVIPdeppgk 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412259 122 ---AGvtrhrsIFNGLKALAEDQInsklskpeVVIIHDAvrPFVEEGVLLKVVTAAKEHGAA------GAIRPLVStVVS 192
Cdd:cd02503   70 gplAG------ILAALRAAPADWV--------LVLACDM--PFLPPELLERLLAAAEEGADAvvpksgGRLQPLHA-LYH 132

                        170       180       190
                 ....*....|....*....|....*....|...
gi 157412259 193 PSADGCLDYSLERARHRasemPQAFLFDVIYEA 225
Cdd:cd02503  133 KSLLPALEELLEAGERR----LRRLLEKLGVQY 161
 
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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