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Conserved domains on  [gi|446664303|ref|WP_000741649|]
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MULTISPECIES: 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Salmonella]

Protein Classification

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase( domain architecture ID 10011283)

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from 2-C-methyl-derythritol 4-phosphate and CTP

EC:  2.7.7.60
Gene Ontology:  GO:0050518|GO:0019288
PubMed:  12691742|9445404
SCOP:  4002789

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
8-232 1.18e-122

D-ribitol-5-phosphate cytidylyltransferase;


:

Pssm-ID: 234670  Cd Length: 227  Bit Score: 347.51  E-value: 1.18e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664303   8 VCAVVPAAGFGRRMQTECPKQYLSIGNKTILEHSVHALLAHPRVTRVVIAISPGDH-RFAQLPLANHPQITVVDGGNERA 86
Cdd:PRK00155   4 VYAIIPAAGKGSRMGADRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDRpDFAELLLAKDPKVTVVAGGAERQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664303  87 DSVLAGLQAVAKAQWVLVHDAARPCLHQDDLARLLAISENSrVGGILASPVRDTMKRGEPGKNaIAHTVERADLWHALTP 166
Cdd:PRK00155  84 DSVLNGLQALPDDDWVLVHDAARPFLTPDDIDRLIEAAEET-GAAILAVPVKDTIKRSDDGGG-IVDTPDRSGLWAAQTP 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446664303 167 QFFPRELLHDCLTRALNEGATITDEASALEYCGFHPALVEGRADNIKVTRPEDLALAEFYLTRTIH 232
Cdd:PRK00155 162 QGFRIELLREALARALAEGKTITDDASAVERLGKPVRLVEGRYDNIKITTPEDLALAEAILKRRIA 227
 
Name Accession Description Interval E-value
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
8-232 1.18e-122

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 347.51  E-value: 1.18e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664303   8 VCAVVPAAGFGRRMQTECPKQYLSIGNKTILEHSVHALLAHPRVTRVVIAISPGDH-RFAQLPLANHPQITVVDGGNERA 86
Cdd:PRK00155   4 VYAIIPAAGKGSRMGADRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDRpDFAELLLAKDPKVTVVAGGAERQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664303  87 DSVLAGLQAVAKAQWVLVHDAARPCLHQDDLARLLAISENSrVGGILASPVRDTMKRGEPGKNaIAHTVERADLWHALTP 166
Cdd:PRK00155  84 DSVLNGLQALPDDDWVLVHDAARPFLTPDDIDRLIEAAEET-GAAILAVPVKDTIKRSDDGGG-IVDTPDRSGLWAAQTP 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446664303 167 QFFPRELLHDCLTRALNEGATITDEASALEYCGFHPALVEGRADNIKVTRPEDLALAEFYLTRTIH 232
Cdd:PRK00155 162 QGFRIELLREALARALAEGKTITDDASAVERLGKPVRLVEGRYDNIKITTPEDLALAEAILKRRIA 227
IspD pfam01128
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ...
 10-229 1.83e-110

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: 316.31  E-value: 1.83e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664303   10 AVVPAAGFGRRMQTECPKQYLSIGNKTILEHSVHALLAHPRVTRVVIAISPGDH-RFAQLPLanHPQITVVDGGNERADS 88
Cdd:pfam01128   1 AVIPAAGSGKRMGAGVPKQFLQLLGQPLLEHTVDAFLASPVVDRIVVAVSPDDTpEFRQLLG--DPSIQLVAGGDTRQDS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664303   89 VLAGLQAVA-KAQWVLVHDAARPCLHQDDLARLLAISENSRVGGILASPVRDTMKRGEpGKNAIAHTVERADLWHALTPQ 167
Cdd:pfam01128  79 VLNGLKALAgTAKFVLVHDGARPCLPHADLARLLAALETGTQGAILALPVTDTIKRVE-ADGVVAGTPDRSGLWAAQTPQ 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446664303  168 FFPRELLHDCLTRALNEGATITDEASALEYCGFHPALVEGRADNIKVTRPEDLALAEFYLTR 229
Cdd:pfam01128 158 GFRVDLLLAAHQRGDQPGAEITDDASLVEHAGGSVQVVPGRPDNLKITTPEDLALAEAILTR 219
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 11-229 3.56e-101

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: 292.80  E-value: 3.56e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664303  11 VVPAAGFGRRMQTECPKQYLSIGNKTILEHSVHALLAHPRVTRVVIAISPGDHRFAQLPLAN---HPQITVVDGGNERAD 87
Cdd:COG1211    1 IIPAAGSGSRMGAGIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPDDIEYFEELLAKygiDKPVRVVAGGATRQD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664303  88 SVLAGLQAVAK-AQWVLVHDAARPCLHQDDLARLLAISENSrVGGILASPVRDTMKRGEPGkNAIAHTVERADLWHALTP 166
Cdd:COG1211   81 SVRNGLEALPDdDDWVLVHDAARPLVSPELIDRVIEAAREY-GAAIPALPVTDTIKRVDDD-GRVTETVDRSGLWAAQTP 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446664303 167 QFFPRELLHDCLTRALNEGATITDEASALEYCGFHPALVEGRADNIKVTRPEDLALAEFYLTR 229
Cdd:COG1211  159 QGFRLDLLLEAHEAAAADGLEFTDDASLVERLGLPVRLVEGSEDNIKITTPEDLALAEALLRS 221
ispD TIGR00453
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ...
 9-227 1.20e-100

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: 291.50  E-value: 1.20e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664303    9 CAVVPAAGFGRRMQTECPKQYLSIGNKTILEHSVHALLAHPRVTRVVIAISPGDHRFAQLPLANHPQITVVDGGNERADS 88
Cdd:TIGR00453   1 SAVIPAAGRGTRFGSGVPKQYLELGGRPLLEHALDAFLAHPAIDEVVVVVSPDDTEFFQKYLVARAVPKIVAGGDTRQDS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664303   89 VLAGLQAVAKAQWVLVHDAARPCLHQDDLARLLAISENSrVGGILASPVRDTMKRGEpGKNAIAHTVERADLWHALTPQF 168
Cdd:TIGR00453  81 VRNGLKALKDAEFVLVHDAARPFVPKELLDRLLEALRKA-GAAILALPVADTLKRVE-ADGFVVETVDREGLWAAQTPQA 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 446664303  169 FPRELLHDCLTRALNEGATITDEASALEYCGFHPALVEGRADNIKVTRPEDLALAEFYL 227
Cdd:TIGR00453 159 FRTELLKKALARAKLEGFEITDDASAVEKLGGKVQLVEGDALNFKITTPEDLALAEALL 217
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 8-223 3.87e-89

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: 262.07  E-value: 3.87e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664303   8 VCAVVPAAGFGRRMQTECPKQYLSIGNKTILEHSVHALLAHPRVTRVVIAISPGDHRFAQ--LPLANHPQITVVDGGNER 85
Cdd:cd02516    1 VAAIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDIDLAKelAKYGLSKVVKIVEGGATR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664303  86 ADSVLAGLQAV--AKAQWVLVHDAARPCLHQDDLARLLAISEnSRVGGILASPVRDTMKRGEpGKNAIAHTVERADLWHA 163
Cdd:cd02516   81 QDSVLNGLKALpdADPDIVLIHDAARPFVSPELIDRLIDALK-EYGAAIPAVPVTDTIKRVD-DDGVVVETLDREKLWAA 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664303 164 LTPQFFPRELLHDCLTRALNEGATITDEASALEYCGFHPALVEGRADNIKVTRPEDLALA 223
Cdd:cd02516  159 QTPQAFRLDLLLKAHRQASEEGEEFTDDASLVEAAGGKVALVEGSEDNIKITTPEDLALA 218
 
Name Accession Description Interval E-value
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
8-232 1.18e-122

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 347.51  E-value: 1.18e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664303   8 VCAVVPAAGFGRRMQTECPKQYLSIGNKTILEHSVHALLAHPRVTRVVIAISPGDH-RFAQLPLANHPQITVVDGGNERA 86
Cdd:PRK00155   4 VYAIIPAAGKGSRMGADRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDRpDFAELLLAKDPKVTVVAGGAERQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664303  87 DSVLAGLQAVAKAQWVLVHDAARPCLHQDDLARLLAISENSrVGGILASPVRDTMKRGEPGKNaIAHTVERADLWHALTP 166
Cdd:PRK00155  84 DSVLNGLQALPDDDWVLVHDAARPFLTPDDIDRLIEAAEET-GAAILAVPVKDTIKRSDDGGG-IVDTPDRSGLWAAQTP 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446664303 167 QFFPRELLHDCLTRALNEGATITDEASALEYCGFHPALVEGRADNIKVTRPEDLALAEFYLTRTIH 232
Cdd:PRK00155 162 QGFRIELLREALARALAEGKTITDDASAVERLGKPVRLVEGRYDNIKITTPEDLALAEAILKRRIA 227
IspD pfam01128
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ...
 10-229 1.83e-110

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: 316.31  E-value: 1.83e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664303   10 AVVPAAGFGRRMQTECPKQYLSIGNKTILEHSVHALLAHPRVTRVVIAISPGDH-RFAQLPLanHPQITVVDGGNERADS 88
Cdd:pfam01128   1 AVIPAAGSGKRMGAGVPKQFLQLLGQPLLEHTVDAFLASPVVDRIVVAVSPDDTpEFRQLLG--DPSIQLVAGGDTRQDS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664303   89 VLAGLQAVA-KAQWVLVHDAARPCLHQDDLARLLAISENSRVGGILASPVRDTMKRGEpGKNAIAHTVERADLWHALTPQ 167
Cdd:pfam01128  79 VLNGLKALAgTAKFVLVHDGARPCLPHADLARLLAALETGTQGAILALPVTDTIKRVE-ADGVVAGTPDRSGLWAAQTPQ 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446664303  168 FFPRELLHDCLTRALNEGATITDEASALEYCGFHPALVEGRADNIKVTRPEDLALAEFYLTR 229
Cdd:pfam01128 158 GFRVDLLLAAHQRGDQPGAEITDDASLVEHAGGSVQVVPGRPDNLKITTPEDLALAEAILTR 219
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 11-229 3.56e-101

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: 292.80  E-value: 3.56e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664303  11 VVPAAGFGRRMQTECPKQYLSIGNKTILEHSVHALLAHPRVTRVVIAISPGDHRFAQLPLAN---HPQITVVDGGNERAD 87
Cdd:COG1211    1 IIPAAGSGSRMGAGIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPDDIEYFEELLAKygiDKPVRVVAGGATRQD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664303  88 SVLAGLQAVAK-AQWVLVHDAARPCLHQDDLARLLAISENSrVGGILASPVRDTMKRGEPGkNAIAHTVERADLWHALTP 166
Cdd:COG1211   81 SVRNGLEALPDdDDWVLVHDAARPLVSPELIDRVIEAAREY-GAAIPALPVTDTIKRVDDD-GRVTETVDRSGLWAAQTP 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446664303 167 QFFPRELLHDCLTRALNEGATITDEASALEYCGFHPALVEGRADNIKVTRPEDLALAEFYLTR 229
Cdd:COG1211  159 QGFRLDLLLEAHEAAAADGLEFTDDASLVERLGLPVRLVEGSEDNIKITTPEDLALAEALLRS 221
ispD TIGR00453
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ...
 9-227 1.20e-100

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: 291.50  E-value: 1.20e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664303    9 CAVVPAAGFGRRMQTECPKQYLSIGNKTILEHSVHALLAHPRVTRVVIAISPGDHRFAQLPLANHPQITVVDGGNERADS 88
Cdd:TIGR00453   1 SAVIPAAGRGTRFGSGVPKQYLELGGRPLLEHALDAFLAHPAIDEVVVVVSPDDTEFFQKYLVARAVPKIVAGGDTRQDS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664303   89 VLAGLQAVAKAQWVLVHDAARPCLHQDDLARLLAISENSrVGGILASPVRDTMKRGEpGKNAIAHTVERADLWHALTPQF 168
Cdd:TIGR00453  81 VRNGLKALKDAEFVLVHDAARPFVPKELLDRLLEALRKA-GAAILALPVADTLKRVE-ADGFVVETVDREGLWAAQTPQA 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 446664303  169 FPRELLHDCLTRALNEGATITDEASALEYCGFHPALVEGRADNIKVTRPEDLALAEFYL 227
Cdd:TIGR00453 159 FRTELLKKALARAKLEGFEITDDASAVEKLGGKVQLVEGDALNFKITTPEDLALAEALL 217
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 8-223 3.87e-89

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: 262.07  E-value: 3.87e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664303   8 VCAVVPAAGFGRRMQTECPKQYLSIGNKTILEHSVHALLAHPRVTRVVIAISPGDHRFAQ--LPLANHPQITVVDGGNER 85
Cdd:cd02516    1 VAAIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDIDLAKelAKYGLSKVVKIVEGGATR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664303  86 ADSVLAGLQAV--AKAQWVLVHDAARPCLHQDDLARLLAISEnSRVGGILASPVRDTMKRGEpGKNAIAHTVERADLWHA 163
Cdd:cd02516   81 QDSVLNGLKALpdADPDIVLIHDAARPFVSPELIDRLIDALK-EYGAAIPAVPVTDTIKRVD-DDGVVVETLDREKLWAA 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664303 164 LTPQFFPRELLHDCLTRALNEGATITDEASALEYCGFHPALVEGRADNIKVTRPEDLALA 223
Cdd:cd02516  159 QTPQAFRLDLLLKAHRQASEEGEEFTDDASLVEAAGGKVALVEGSEDNIKITTPEDLALA 218
ispDF PRK09382
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ...
 5-229 8.19e-54

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: 177.35  E-value: 8.19e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664303   5 LLDVCAVVPAAGFGRRMQTECPKQYLSIGNKTILEHSVHALLAHPRVTRVVIAISPGDHRFAQLPLANHPQITVVDGGNE 84
Cdd:PRK09382   3 MSDISLVIVAAGRSTRFSAEVKKQWLRIGGKPLWLHVLENLSSAPAFKEIVVVIHPDDIAYMKKALPEIKFVTLVTGGAT 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664303  85 RADSVLAGLQAVaKAQWVLVHDAARPCLHQDDLARLLAISENSrvGGIL-ASPVRDTMKRGEPgknaiahTVERADLWHA 163
Cdd:PRK09382  83 RQESVRNALEAL-DSEYVLIHDAARPFVPKELIDRLIEALDKA--DCVLpALPVADTLKRANE-------TVDREGLKLI 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446664303 164 LTPQFFPRELlhdcLTRALNEGATITDEASALEYCGFHPALVEGRADNIKVTRPEDLALAEFYLTR 229
Cdd:PRK09382 153 QTPQLSRTKT----LKAAADGRGDFTDDSSAAEAAGGKVALVEGSEDLHKLTYKEDLKMADLLLSP 214
PRK13385 PRK13385
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Provisional
 14-223 2.59e-40

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


Pssm-ID: 184017  Cd Length: 230  Bit Score: 138.08  E-value: 2.59e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664303  14 AAGFGRRMQTECPKQYLSIGNKTILEHSVHALLAHPRVTRVVIA-----ISPGDHRFAQLPLANHpQITVVDGGNERADS 88
Cdd:PRK13385   9 AAGQGKRMNAPLNKMWLDLVGEPIFIHALRPFLADNRCSKIIIVtqaqeRKHVQDLMKQLNVADQ-RVEVVKGGTERQES 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664303  89 VLAGLQAVAKAQWVLVHDAARPCLHQDDLARLLAISENSRvGGILASPVRDTMKRGEPGKNAiaHTVERADLWHALTPQF 168
Cdd:PRK13385  88 VAAGLDRIGNEDVILVHDGARPFLTQDIIDRLLEGVAKYG-AAICAVEVKDTVKRVKDKQVI--ETVDRNELWQGQTPQA 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446664303 169 FPRELLHDCLTRALNEGATITDEASALEYCGFHPALVEGRADNIKVTRPEDLALA 223
Cdd:PRK13385 165 FELKILQKAHRLASEQQFLGTDEASLVERSPHPVKLVQGSYYNIKLTTPEDMPLA 219
PLN02728 PLN02728
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
 7-228 3.08e-34

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


Pssm-ID: 215387  Cd Length: 252  Bit Score: 122.92  E-value: 3.08e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664303   7 DVCAVVPAAGFGRRMQTECPKQYLSIGNKTILEHSVHALLAHPRVTRVVIAISP--------------GDHRFAqLPlan 72
Cdd:PLN02728  24 SVSVILLAGGVGKRMGANMPKQYLPLLGQPIALYSLYTFARMPEVKEIVVVCDPsyrdvfeeavenidVPLKFA-LP--- 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664303  73 hpqitvvdgGNERADSVLAGLQAV-AKAQWVLVHDAARPCLHQDDLARLLaiSENSRVGG-ILASPVRDTMKRGEPGkNA 150
Cdd:PLN02728 100 ---------GKERQDSVFNGLQEVdANSELVCIHDSARPLVTSADIEKVL--KDAAVHGAaVLGVPVKATIKEANSD-SF 167

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446664303 151 IAHTVERADLWHALTPQFFPRELLHDCLTRALNEGATITDEASALEYCGfHPA-LVEGRADNIKVTRPEDLALAEFYLT 228
Cdd:PLN02728 168 VVKTLDRKRLWEMQTPQVIKPELLRRGFELVEREGLEVTDDVSIVEALK-HPVfITEGSYTNIKVTTPDDMLVAERILN 245
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
8-135 3.80e-14

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 68.26  E-value: 3.80e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664303   8 VCAVVPAAGFGRRMQTecPKQYLSIGNKTILEHSVHALLAHpRVTRVVIAISPGDHRFAqlPLANHPQITVVDggNERAD 87
Cdd:COG2068    4 VAAIILAAGASSRMGR--PKLLLPLGGKPLLERAVEAALAA-GLDPVVVVLGADAEEVA--AALAGLGVRVVV--NPDWE 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446664303  88 -----SVLAGLQAV-AKAQWVLVHDAARPCLHQDDLARLLAISENSRvGGILAS 135
Cdd:COG2068   77 egmssSLRAGLAALpADADAVLVLLGDQPLVTAETLRRLLAAFRESP-ASIVAP 129
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 8-122 9.60e-12

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: 61.81  E-value: 9.60e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664303   8 VCAVVPAAGFGRRMQTecPKQYLSIGNKTILEHSVHALLAHpRVTRVVIAISPGDHRFAQLpLANHPQITVVdggNERA- 86
Cdd:cd04182    1 IAAIILAAGRSSRMGG--NKLLLPLDGKPLLRHALDAALAA-GLSRVIVVLGAEADAVRAA-LAGLPVVVVI---NPDWe 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 446664303  87 ----DSVLAGLQAV-AKAQWVLVHDAARPCLHQDDLARLLA 122
Cdd:cd04182   74 egmsSSLAAGLEALpADADAVLILLADQPLVTAETLRALID 114
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 10-146 1.49e-09

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: 54.89  E-value: 1.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664303   10 AVVPAAGFGRRMQTecPKQYLSIGNKTILEHSVHALLAHPRvtRVVIaISPGDHRFAQLPLANHPQITVVDGGNERADSV 89
Cdd:pfam12804   1 AVILAGGRSSRMGG--DKALLPLGGKPLLERVLERLRPAGD--EVVV-VANDEEVLAALAGLGVPVVPDPDPGQGPLAGL 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 446664303   90 LAGLQAVAKAQWVLVHDAARPCLHQDDLARLLAISENSRVGGILASPVRdtmKRGEP 146
Cdd:pfam12804  76 LAALRAAPGADAVLVLACDMPFLTPELLRRLLAAAEESGADIVVPVYDG---GRGHP 129
matur_MocA_YgfJ TIGR03310
molybdenum cofactor cytidylyltransferase; Members of this protein include MocA, which ...
 10-122 2.39e-09

molybdenum cofactor cytidylyltransferase; Members of this protein include MocA, which transfers cytosine from CTP to molybdopterin during molybdopterin cytosine dinucleotide (MCD) cofactor biosynthesis. It is distantly related to MobA, the GTP:molybdopterin guanylyltransferase. The MocA family is particularly closely related in phylogenetic distribution to other markers of selenium-dependent molybdenum hydroxylases (SDMH), suggesting most SDMH must use MCD rather than molybdopterin guanine dinucleotide.


Pssm-ID: 274516  Cd Length: 188  Bit Score: 55.04  E-value: 2.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664303   10 AVVPAAGFGRRMQTecPKQYLSIGNKTILEHSVHALLAHpRVTRVVIAISPgDHRFAQLPLANHPQITVVDGGNER---A 86
Cdd:TIGR03310   2 AIILAAGLSSRMGQ--NKLLLPYKGKTILEHVVDNALRL-FFDEVILVLGH-EADELVALLANHSNITLVHNPQYAegqS 77

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 446664303   87 DSVLAGLQAVAKAQWVLVHDAARPCLHQDDLARLLA 122
Cdd:TIGR03310  78 SSIKLGLELPVQSDGYLFLLGDQPFVTPDIIQLLLE 113
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
10-227 1.25e-08

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 53.71  E-value: 1.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664303  10 AVVPAAGFGRRMQ---TECPKQYLSIGNKTILEHSVHALLAHpRVTRVVIAISPGDHRFAQLPLANHPQITVVDggNERA 86
Cdd:COG1213    2 AVILAAGRGSRLGpltDDIPKCLVEIGGKTLLERQLEALAAA-GIKDIVVVTGYKAELIEEALARPGPDVTFVY--NPDY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664303  87 D------SVLAGLQAVAKAQWVL----VHDAArpclhqdDLARLLAISENSR--VGGILASPVRDTMK-RGEPGKN--AI 151
Cdd:COG1213   79 DetnniySLWLAREALDEDFLLLngdvVFDPA-------ILKRLLASDGDIVllVDRKWEKPLDEEVKvRVDEDGRivEI 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664303 152 AHTVERADLW------HALTPQFFP--RELLhDCLTRALNEGATITD--EASALEYCGFHPALVEGRA----DNikvtrP 217
Cdd:COG1213  152 GKKLPPEEADgeyigiFKFSAEGAAalREAL-EALIDEGGPNLYYEDalQELIDEGGPVKAVDIGGLPwveiDT-----P 225

                        250
                 ....*....|
gi 446664303 218 EDLALAEFYL 227
Cdd:COG1213  226 EDLERAEELF 235
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 10-65 4.85e-08

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: 51.81  E-value: 4.85e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446664303  10 AVVPAAGFGRRMQ--TE-CPKQYLSIGNKTILEHSVHALLAHPrVTRVVIAISPGDHRF 65
Cdd:cd04181    1 AVILAAGKGTRLRplTDtRPKPLLPIAGKPILEYIIERLARAG-IDEIILVVGYLGEQI 58
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 10-59 9.42e-08

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: 51.31  E-value: 9.42e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446664303  10 AVVPAAGFGRRMQ--TE-CPKQYLSIGNKTILEHSVHALLAHPrVTRVVIAIS 59
Cdd:COG1208    2 AVILAGGLGTRLRplTDtRPKPLLPVGGKPLLEHILERLAAAG-ITEIVINVG 53
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 10-88 3.98e-07

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: 49.15  E-value: 3.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664303  10 AVVPAAGFGRRMQT---ECPKQYLSIGNKTILEHSVHALLAHpRVTRVVIAISPGDHRFAQLpLANHPQITVVDggNERA 86
Cdd:cd02523    1 AIILAAGRGSRLRPlteDRPKCLLEINGKPLLERQIETLKEA-GIDDIVIVTGYKKEQIEEL-LKKYPNIKFVY--NPDY 76


                 ..
gi 446664303  87 DS 88
Cdd:cd02523   77 AE 78
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 7-128 6.28e-04

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 40.31  E-value: 6.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664303   7 DVCAVVPAAGFGRRMQTECPKQYLSIGNKTILEHSVHALLA-HPRvtRVVIAISPGDHRFAQLPLANHPQITVVD----G 81
Cdd:PRK14352   4 PTAVIVLAAGAGTRMRSDTPKVLHTLAGRSMLGHVLHAAAGlAPQ--HLVVVVGHDRERVAPAVAELAPEVDIAVqdeqP 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 446664303  82 GNERAdsVLAGLQAVAK--AQWVLVHDAARPCLHQDDLARLLAISENSR 128
Cdd:PRK14352  82 GTGHA--VQCALEALPAdfDGTVVVTAGDVPLLDGETLADLVATHTAEG 128
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 10-65 8.36e-04

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: 39.47  E-value: 8.36e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664303  10 AVVPAAGFGRRMQ----TEcPKQYLSIGNKTILEHSVHAlLAHPRVTRVVIAISPGDHRF 65
Cdd:cd04189    3 GLILAGGKGTRLRpltyTR-PKQLIPVAGKPIIQYAIED-LREAGIEDIGIVVGPTGEEI 60
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 10-79 1.42e-03

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: 38.65  E-value: 1.42e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664303  10 AVVPAAGFGRRMQTECPKQYLSIGNKTILEHSVHALLAHpRVTRVVIAISPGDHRFAQlpLANHPQITVV 79
Cdd:cd02540    1 AVILAAGKGTRMKSDLPKVLHPLAGKPMLEHVLDAARAL-GPDRIVVVVGHGAEQVKK--ALANPNVEFV 67
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 10-56 2.52e-03

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: 37.94  E-value: 2.52e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 446664303  10 AVVPAAGFGRRMQ--TE-CPKQYLSIGNKTILEHSVhALLAHPRVTRVVI 56
Cdd:cd06422    2 AMILAAGLGTRMRplTDtRPKPLVPVAGKPLIDHAL-DRLAAAGIRRIVV 50
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 10-63 3.39e-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: 37.90  E-value: 3.39e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446664303  10 AVVPAAGFGRRM--QTEC-PKQYLSIGNKTILEHSVHALLAhPRVTRVVIAISPG-----DH 63
Cdd:cd02541    3 AVIPAAGLGTRFlpATKAiPKEMLPIVDKPVIQYIVEEAVA-AGIEDIIIVTGRGkraieDH 63
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 10-59 3.51e-03

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: 37.58  E-value: 3.51e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446664303  10 AVVPAAGFGRRMQT---ECPKQYLSIGNKTILEHSVHALLAhPRVTRVVIAIS 59
Cdd:cd06425    3 ALILVGGYGTRLRPltlTVPKPLVEFCNKPMIEHQIEALAK-AGVKEIILAVN 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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