NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|446571459|ref|WP_000648805|]
View 

MULTISPECIES: glucose-1-phosphate cytidylyltransferase [Bacillus]

Protein Classification

glycosyltransferase family protein( domain architecture ID 27718)

glycosyltransferase family protein may synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Glyco_tranf_GTA_type super family cl11394
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
2-255 1.64e-180

Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold; Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases 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. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.


The actual alignment was detected with superfamily member TIGR02623:

Pssm-ID: 472172 [Multi-domain]  Cd Length: 254  Bit Score: 495.43  E-value: 1.64e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459    2 KAVILAGGYGTRIGEETHLKPKPMIEIGTKPILWHIMSLYSHYGITEFIICLGYKGYAIKEFFLNYNLHMSDFTIQLNDN 81
Cdd:TIGR02623   1 KAVILAGGLGTRISEETHLRPKPMVEIGGKPILWHIMKIYSHHGINDFIICCGYKGYVIKEYFANYFLHMSDVTFHMADN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459   82 TITSHSHRVEPWKVTLIDTGVNTETGGRVKKIQNYVGDEPFCLTYGDGLSNVNIKELITFHKKHGKMATVTAVQPPGRFG 161
Cdd:TIGR02623  81 TMEVHHKRVEPWRVTLVDTGESTQTGGRLKRVREYLDDEAFCFTYGDGVADIDIKALIAFHRKHGKKATVTAVQPPGRFG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459  162 SLILDKQSVTSFQEKPLGDGGWVNGGFFILNPEVFNYISGDKSVFETDSLVQLVNKNELAAYQHSGFWHPMDTLRDKNKL 241
Cdd:TIGR02623 161 ALDLEGEQVTSFQEKPLGDGGWINGGFFVLNPSVLDLIDGDATVWEQEPLETLAQRGELSAYEHSGFWQPMDTLRDKNYL 240
                         250
                  ....*....|....
gi 446571459  242 VELWESNNAPWKVW 255
Cdd:TIGR02623 241 EELWESGRAPWKVW 254
 
Name Accession Description Interval E-value
G1P_cyt_trans TIGR02623
glucose-1-phosphate cytidylyltransferase; Members of this family are the enzyme ...
2-255 1.64e-180

glucose-1-phosphate cytidylyltransferase; Members of this family are the enzyme glucose-1-phosphate cytidylyltransferase, also called CDP-glucose pyrophosphorylase, the product of the rfbF gene. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 131672 [Multi-domain]  Cd Length: 254  Bit Score: 495.43  E-value: 1.64e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459    2 KAVILAGGYGTRIGEETHLKPKPMIEIGTKPILWHIMSLYSHYGITEFIICLGYKGYAIKEFFLNYNLHMSDFTIQLNDN 81
Cdd:TIGR02623   1 KAVILAGGLGTRISEETHLRPKPMVEIGGKPILWHIMKIYSHHGINDFIICCGYKGYVIKEYFANYFLHMSDVTFHMADN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459   82 TITSHSHRVEPWKVTLIDTGVNTETGGRVKKIQNYVGDEPFCLTYGDGLSNVNIKELITFHKKHGKMATVTAVQPPGRFG 161
Cdd:TIGR02623  81 TMEVHHKRVEPWRVTLVDTGESTQTGGRLKRVREYLDDEAFCFTYGDGVADIDIKALIAFHRKHGKKATVTAVQPPGRFG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459  162 SLILDKQSVTSFQEKPLGDGGWVNGGFFILNPEVFNYISGDKSVFETDSLVQLVNKNELAAYQHSGFWHPMDTLRDKNKL 241
Cdd:TIGR02623 161 ALDLEGEQVTSFQEKPLGDGGWINGGFFVLNPSVLDLIDGDATVWEQEPLETLAQRGELSAYEHSGFWQPMDTLRDKNYL 240
                         250
                  ....*....|....
gi 446571459  242 VELWESNNAPWKVW 255
Cdd:TIGR02623 241 EELWESGRAPWKVW 254
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
3-253 7.23e-160

G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; Alpha-D-Glucose-1-phosphate Cytidylyltransferase catalyzes the production of CDP-D-Glucose from alpha-D-Glucose-1-phosphate and MgCTP as substrate. CDP-D-Glucose is the precursor for synthesizing four of the five naturally occurring 3,6-dideoxy sugars-abequose (3,6-dideoxy-D-Xylo-hexose), ascarylose (3,6-dideoxy-L-arabino-hexose), paratose (3,6-dideoxy-D-ribohexose), and tyvelose (3,6-dideoxy-D-arabino-hexose. Deoxysugars are ubiquitous in nature where they function in a variety of biological processes, including cell adhesion, immune response, determination of ABO blood groups, fertilization, antibiotic function, and microbial pathogenicity.


Pssm-ID: 133015 [Multi-domain]  Cd Length: 253  Bit Score: 443.17  E-value: 7.23e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459   3 AVILAGGYGTRIGEETHLKPKPMIEIGTKPILWHIMSLYSHYGITEFIICLGYKGYAIKEFFLNYNLHMSDFTIQLNDNT 82
Cdd:cd02524    1 VVILAGGLGTRLSEETELKPKPMVEIGGRPILWHIMKIYSHYGHNDFILCLGYKGHVIKEYFLNYFLHNSDVTIDLGTNR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459  83 ITSHSHRVEPWKVTLIDTGVNTETGGRVKKIQNYVGD-EPFCLTYGDGLSNVNIKELITFHKKHGKMATVTAVQPPGRFG 161
Cdd:cd02524   81 IELHNSDIEDWKVTLVDTGLNTMTGGRLKRVRRYLGDdETFMLTYGDGVSDVNINALIEFHRSHGKLATVTAVHPPGRFG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459 162 SLILDKQS-VTSFQEKPLGDGGWVNGGFFILNPEVFNYISGDKSVFETDSLVQLVNKNELAAYQHSGFWHPMDTLRDKNK 240
Cdd:cd02524  161 ELDLDDDGqVTSFTEKPQGDGGWINGGFFVLEPEVFDYIDGDDTVFEREPLERLAKDGELMAYKHTGFWQCMDTLRDKQT 240
                        250
                 ....*....|...
gi 446571459 241 LVELWESNNAPWK 253
Cdd:cd02524  241 LEELWNSGKAPWK 253
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
2-255 2.16e-99

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: 289.75  E-value: 2.16e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459   2 KAVILAGGYGTRIGEETHLKPKPMIEIGTKPILWHIMSLYSHYGITEFIICLGYKGYAIKEFFLNynlhMSDFtiqlndn 81
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGD----GSRF------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459  82 titshshrvePWKVTLIDTGVNTETGGRVKKIQNYVGDEPFCLTYGDGLSNVNIKELITFHKKHGKMATVTAV--QPPGR 159
Cdd:COG1208   70 ----------GVRITYVDEGEPLGTGGALKRALPLLGDEPFLVLNGDILTDLDLAALLAFHREKGADATLALVpvPDPSR 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459 160 FGSLILDKQS-VTSFQEKPLGD-GGWVNGGFFILNPEVFNYISGDKSVFETDSLVQLVNKNELAAYQHSGFWHPMDTLRD 237
Cdd:COG1208  140 YGVVELDGDGrVTRFVEKPEEPpSNLINAGIYVLEPEIFDYIPEGEPFDLEDLLPRLIAEGRVYGYVHDGYWLDIGTPED 219
                        250
                 ....*....|....*...
gi 446571459 238 KNKLVELWESNNAPWKVW 255
Cdd:COG1208  220 LLEANALLLSGKAPVVIW 237
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
2-234 5.55e-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: 96.55  E-value: 5.55e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459    2 KAVILAGGYGTRIGEETHLKPKPMIEIGTK-PILWHIMSLYSHYGITEFIICLGYKGYAIKEFFLNYNlhmSDFTIQLND 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDG---SKFGVQITY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459   81 ntitshshRVEPwkvtlidTGVNteTGGRVKKIQNYVGDEPFCLTY--GDGLSNVNIKELITFHKKHGKMATVT----AV 154
Cdd:pfam00483  78 --------ALQP-------EGKG--TAPAVALAADFLGDEKSDVLVlgGDHIYRMDLEQAVKFHIEKAADATVTfgivPV 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459  155 QPPGRFGSLILDKQS-VTSFQEKPLGD--GGWVNGGFFILNPEVFNYISGD------KSVFETDSLVQLVNKNELAAYQH 225
Cdd:pfam00483 141 EPPTGYGVVEFDDNGrVIRFVEKPKLPkaSNYASMGIYIFNSGVLDFLAKYleelkrGEDEITDILPKALEDGKLAYAFI 220

                  ....*....
gi 446571459  226 SGFWHPMDT 234
Cdd:pfam00483 221 FKGYAWLDV 229
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
3-67 3.48e-04

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 40.89  E-value: 3.48e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446571459   3 AVILAGGYGTRIGEEthlKPKPMIEIGTKPILWH-IMSLYSHYGITEFIICL--GYKGYAIKEFFLNY 67
Cdd:PRK00155   6 AIIPAAGKGSRMGAD---RPKQYLPLGGKPILEHtLEAFLAHPRIDEIIVVVppDDRPDFAELLLAKD 70
 
Name Accession Description Interval E-value
G1P_cyt_trans TIGR02623
glucose-1-phosphate cytidylyltransferase; Members of this family are the enzyme ...
2-255 1.64e-180

glucose-1-phosphate cytidylyltransferase; Members of this family are the enzyme glucose-1-phosphate cytidylyltransferase, also called CDP-glucose pyrophosphorylase, the product of the rfbF gene. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 131672 [Multi-domain]  Cd Length: 254  Bit Score: 495.43  E-value: 1.64e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459    2 KAVILAGGYGTRIGEETHLKPKPMIEIGTKPILWHIMSLYSHYGITEFIICLGYKGYAIKEFFLNYNLHMSDFTIQLNDN 81
Cdd:TIGR02623   1 KAVILAGGLGTRISEETHLRPKPMVEIGGKPILWHIMKIYSHHGINDFIICCGYKGYVIKEYFANYFLHMSDVTFHMADN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459   82 TITSHSHRVEPWKVTLIDTGVNTETGGRVKKIQNYVGDEPFCLTYGDGLSNVNIKELITFHKKHGKMATVTAVQPPGRFG 161
Cdd:TIGR02623  81 TMEVHHKRVEPWRVTLVDTGESTQTGGRLKRVREYLDDEAFCFTYGDGVADIDIKALIAFHRKHGKKATVTAVQPPGRFG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459  162 SLILDKQSVTSFQEKPLGDGGWVNGGFFILNPEVFNYISGDKSVFETDSLVQLVNKNELAAYQHSGFWHPMDTLRDKNKL 241
Cdd:TIGR02623 161 ALDLEGEQVTSFQEKPLGDGGWINGGFFVLNPSVLDLIDGDATVWEQEPLETLAQRGELSAYEHSGFWQPMDTLRDKNYL 240
                         250
                  ....*....|....
gi 446571459  242 VELWESNNAPWKVW 255
Cdd:TIGR02623 241 EELWESGRAPWKVW 254
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
3-253 7.23e-160

G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; Alpha-D-Glucose-1-phosphate Cytidylyltransferase catalyzes the production of CDP-D-Glucose from alpha-D-Glucose-1-phosphate and MgCTP as substrate. CDP-D-Glucose is the precursor for synthesizing four of the five naturally occurring 3,6-dideoxy sugars-abequose (3,6-dideoxy-D-Xylo-hexose), ascarylose (3,6-dideoxy-L-arabino-hexose), paratose (3,6-dideoxy-D-ribohexose), and tyvelose (3,6-dideoxy-D-arabino-hexose. Deoxysugars are ubiquitous in nature where they function in a variety of biological processes, including cell adhesion, immune response, determination of ABO blood groups, fertilization, antibiotic function, and microbial pathogenicity.


Pssm-ID: 133015 [Multi-domain]  Cd Length: 253  Bit Score: 443.17  E-value: 7.23e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459   3 AVILAGGYGTRIGEETHLKPKPMIEIGTKPILWHIMSLYSHYGITEFIICLGYKGYAIKEFFLNYNLHMSDFTIQLNDNT 82
Cdd:cd02524    1 VVILAGGLGTRLSEETELKPKPMVEIGGRPILWHIMKIYSHYGHNDFILCLGYKGHVIKEYFLNYFLHNSDVTIDLGTNR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459  83 ITSHSHRVEPWKVTLIDTGVNTETGGRVKKIQNYVGD-EPFCLTYGDGLSNVNIKELITFHKKHGKMATVTAVQPPGRFG 161
Cdd:cd02524   81 IELHNSDIEDWKVTLVDTGLNTMTGGRLKRVRRYLGDdETFMLTYGDGVSDVNINALIEFHRSHGKLATVTAVHPPGRFG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459 162 SLILDKQS-VTSFQEKPLGDGGWVNGGFFILNPEVFNYISGDKSVFETDSLVQLVNKNELAAYQHSGFWHPMDTLRDKNK 240
Cdd:cd02524  161 ELDLDDDGqVTSFTEKPQGDGGWINGGFFVLEPEVFDYIDGDDTVFEREPLERLAKDGELMAYKHTGFWQCMDTLRDKQT 240
                        250
                 ....*....|...
gi 446571459 241 LVELWESNNAPWK 253
Cdd:cd02524  241 LEELWNSGKAPWK 253
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
2-255 2.16e-99

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: 289.75  E-value: 2.16e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459   2 KAVILAGGYGTRIGEETHLKPKPMIEIGTKPILWHIMSLYSHYGITEFIICLGYKGYAIKEFFLNynlhMSDFtiqlndn 81
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGD----GSRF------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459  82 titshshrvePWKVTLIDTGVNTETGGRVKKIQNYVGDEPFCLTYGDGLSNVNIKELITFHKKHGKMATVTAV--QPPGR 159
Cdd:COG1208   70 ----------GVRITYVDEGEPLGTGGALKRALPLLGDEPFLVLNGDILTDLDLAALLAFHREKGADATLALVpvPDPSR 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459 160 FGSLILDKQS-VTSFQEKPLGD-GGWVNGGFFILNPEVFNYISGDKSVFETDSLVQLVNKNELAAYQHSGFWHPMDTLRD 237
Cdd:COG1208  140 YGVVELDGDGrVTRFVEKPEEPpSNLINAGIYVLEPEIFDYIPEGEPFDLEDLLPRLIAEGRVYGYVHDGYWLDIGTPED 219
                        250
                 ....*....|....*...
gi 446571459 238 KNKLVELWESNNAPWKVW 255
Cdd:COG1208  220 LLEANALLLSGKAPVVIW 237
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
3-233 8.68e-57

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: 180.47  E-value: 8.68e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459   3 AVILAGGYGTRIGEETHLKPKPMIEIGTKPILWHIMSLYSHYGITEFIICLGYKGYAIKEFFLN-YNLHMsdftiqlndn 81
Cdd:cd04181    1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDgSKFGV---------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459  82 titshshrvepwKVTLIDTGVNTETGGRVKKIQNYVGDEPFCLTYGDGLSNVNIKELITFHKKHGKMATVTA--VQPPGR 159
Cdd:cd04181   71 ------------NIEYVVQEEPLGTAGAVRNAEDFLGDDDFLVVNGDVLTDLDLSELLRFHREKGADATIAVkeVEDPSR 138
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446571459 160 FGSLILDKQS-VTSFQEKP-LGDGGWVNGGFFILNPEVFNYI---SGDKSVFETDSLVQLVNKNELAAYQHSGFWHPMD 233
Cdd:cd04181  139 YGVVELDDDGrVTRFVEKPtLPESNLANAGIYIFEPEILDYIpeiLPRGEDELTDAIPLLIEEGKVYGYPVDGYWLDIG 217
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
3-227 3.98e-42

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: 143.08  E-value: 3.98e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459   3 AVILAGGYGTRIGEETHLKPKPMIEIGTKPILWHIMSLYSHYGITEFIICLGYKGYAIKEFFLNynlhmsdftiqlndnt 82
Cdd:cd06915    1 AVILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYLAEQIEEYFGD---------------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459  83 itshshrvEPWKVTLIDTGVNTE---TGGRVKKIQNYVGDEPFCLTYGDGLSNVNIKELITFHKKHGKMATVTAVQPPG- 158
Cdd:cd06915   65 --------GYRGGIRIYYVIEPEplgTGGAIKNALPKLPEDQFLVLNGDTYFDVDLLALLAALRASGADATMALRRVPDa 136
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446571459 159 -RFGSLILDK-QSVTSFQEKPLGDG-GWVNGGFFILNPEVFNYISGDKSVFETDSLVQLVNKNELAAYQHSG 227
Cdd:cd06915  137 sRYGNVTVDGdGRVIAFVEKGPGAApGLINGGVYLLRKEILAEIPADAFSLEADVLPALVKRGRLYGFEVDG 208
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
3-229 1.04e-33

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: 121.46  E-value: 1.04e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459   3 AVILAGGYGTRIGEETHLKPKPMIEIGTKPILWHIMSLYSHYGITEFIICLGYKGYAIKEFFLNynlhMSDFtiqlndnt 82
Cdd:cd06426    1 VVIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNYLAEMIEDYFGD----GSKF-------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459  83 itshshrvepwkvtlidtGVNTE---------TGGRVKKIQNYVgDEPFCLTYGDGLSNVNIKELITFHKKHGKMATVTA 153
Cdd:cd06426   69 ------------------GVNISyvredkplgTAGALSLLPEKP-TDPFLVMNGDILTNLNYEHLLDFHKENNADATVCV 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459 154 ----VQPPgrFGSLILDKQSVTSFQEKPLGDgGWVNGGFFILNPEVFNYISGDKSVFETDSLVQLVNKNE-LAAYQHSGF 228
Cdd:cd06426  130 reyeVQVP--YGVVETEGGRITSIEEKPTHS-FLVNAGIYVLEPEVLDLIPKNEFFDMPDLIEKLIKEGKkVGVFPIHEY 206

                 .
gi 446571459 229 W 229
Cdd:cd06426  207 W 207
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
1-233 1.44e-33

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: 121.16  E-value: 1.44e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459   1 MKAVILAGGYGTRIGEETHLKPKPMIEIGTKPILWHIMSLYSHYGITEFIICLGYKGYAIKEFFLNYNLHmsdFTIQLnd 80
Cdd:cd06425    1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYRPEDMVPFLKEYEKK---LGIKI-- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459  81 ntitSHSHRVEPwkvtlidTGvnteTGGRVKKIQNYVG--DEPFCLTYGDGLSNVNIKELITFHKKHGKMAT--VTAVQP 156
Cdd:cd06425   76 ----TFSIETEP-------LG----TAGPLALARDLLGddDEPFFVLNSDVICDFPLAELLDFHKKHGAEGTilVTKVED 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459 157 PGRFGSLILDKQS--VTSFQEKPLG-DGGWVNGGFFILNPEVFNYISGDKSVFETDSLVQLVNKNELAAYQHSGFWhpMD 233
Cdd:cd06425  141 PSKYGVVVHDENTgrIERFVEKPKVfVGNKINAGIYILNPSVLDRIPLRPTSIEKEIFPKMASEGQLYAYELPGFW--MD 218
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
1-237 1.87e-24

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: 97.64  E-value: 1.87e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459   1 MKAVILAGGYGTRIGEETHLKPKPMIEIGTKPILWHIMSLYSHYGITEFIICLGYKGYAIKEFFLNynlhMSDFTIqlnd 80
Cdd:cd04189    1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEALGD----GSRFGV---- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459  81 ntitshshrvepwKVTLIDTGVNTETGGRVKKIQNYVGDEPFCLTYGDGLSNVNIKELITFHKKHGKMAT--VTAVQPPG 158
Cdd:cd04189   73 -------------RITYILQEEPLGLAHAVLAARDFLGDEPFVVYLGDNLIQEGISPLVRDFLEEDADASilLAEVEDPR 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459 159 RFGSLILDKQSVTSFQEKP---LGDGGWVngGFFILNPEVFNYISGDK-SV---FE-TDSLVQLVNKN-ELAAYQHSGFW 229
Cdd:cd04189  140 RFGVAVVDDGRIVRLVEKPkepPSNLALV--GVYAFTPAIFDAISRLKpSWrgeLEiTDAIQWLIDRGrRVGYSIVTGWW 217

                 ....*...
gi 446571459 230 HPMDTLRD 237
Cdd:cd04189  218 KDTGTPED 225
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
2-234 5.55e-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: 96.55  E-value: 5.55e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459    2 KAVILAGGYGTRIGEETHLKPKPMIEIGTK-PILWHIMSLYSHYGITEFIICLGYKGYAIKEFFLNYNlhmSDFTIQLND 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDG---SKFGVQITY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459   81 ntitshshRVEPwkvtlidTGVNteTGGRVKKIQNYVGDEPFCLTY--GDGLSNVNIKELITFHKKHGKMATVT----AV 154
Cdd:pfam00483  78 --------ALQP-------EGKG--TAPAVALAADFLGDEKSDVLVlgGDHIYRMDLEQAVKFHIEKAADATVTfgivPV 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459  155 QPPGRFGSLILDKQS-VTSFQEKPLGD--GGWVNGGFFILNPEVFNYISGD------KSVFETDSLVQLVNKNELAAYQH 225
Cdd:pfam00483 141 EPPTGYGVVEFDDNGrVIRFVEKPKLPkaSNYASMGIYIFNSGVLDFLAKYleelkrGEDEITDILPKALEDGKLAYAFI 220

                  ....*....
gi 446571459  226 SGFWHPMDT 234
Cdd:pfam00483 221 FKGYAWLDV 229
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
2-85 5.69e-19

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 82.98  E-value: 5.69e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459   2 KAVILAGGYGTRIGEETHLKPKPMIEIGTKPILWHIMSLYSHYGITEFIICLGYKGYAIKEFFLNYNLhmsDFTIQLND- 80
Cdd:COG1213    1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEALARPGP---DVTFVYNPd 77

                 ....*....
gi 446571459  81 ----NTITS 85
Cdd:COG1213   78 ydetNNIYS 86
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
2-237 9.62e-18

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: 79.15  E-value: 9.62e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459   2 KAVILAGGYGTRIGEETHLKPKPMIEIGTKPILWHIMSLYSHYGITEFIICLGYKGYAIKEFflnynLHMSDFTIQLndn 81
Cdd:cd06422    1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAH-----LGDSRFGLRI--- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459  82 tITSHshrvEPwKVTLidtgvntETGGRVKKIQNYVGDEPFCLTYGDGLSNVNIKELITFH--KKHGKMATVTAVQPPG- 158
Cdd:cd06422   73 -TISD----EP-DELL-------ETGGGIKKALPLLGDEPFLVVNGDILWDGDLAPLLLLHawRMDALLLLLPLVRNPGh 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459 159 -RFGSLILDKQSVTSFqEKPLGDGGWVNGGFFILNPEVFNYISGDKsvfetDSLV----QLVNKNELAAYQHSGFWHPMD 233
Cdd:cd06422  140 nGVGDFSLDADGRLRR-GGGGAVAPFTFTGIQILSPELFAGIPPGK-----FSLNplwdRAIAAGRLFGLVYDGLWFDVG 213

                 ....
gi 446571459 234 TLRD 237
Cdd:cd06422  214 TPER 217
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
2-177 4.98e-16

glucose-1-phosphate thymidylylransferase, long form; The family of known and putative glucose-1-phosphate thymidyltransferase (also called dTDP-glucose synthase) shows a deep split into a short form (see TIGR01207) and a long form described by this model. The homotetrameric short form is found in numerous bacterial species that incorporate dTDP-L-rhamnose, which it helps synthesize, into the cell wall. It is subject to feedback inhibition. This form, in contrast, 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. Alternate name: dTDP-D-glucose synthase


Pssm-ID: 273500 [Multi-domain]  Cd Length: 353  Bit Score: 76.29  E-value: 4.98e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459    2 KAVILAGGYGTRIGEETHLKPKPMIEIGTKPILWHIMSLYSHYGITEFIICLGYK-GYAIKEFFLNynlhMSDFTIqlnd 80
Cdd:TIGR01208   1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIGIVVGPVtGEEIKEIVGE----GERFGA---- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459   81 ntitshshrvepwKVTLIDTGVNTETGGRVKKIQNYVGDEPFCLTYGDGLSNVNIKELI-TFHKKH-GKMATVTAVQPPG 158
Cdd:TIGR01208  73 -------------KITYIVQGEPLGLAHAVYTARDFLGDDDFVVYLGDNLIQDGISRFVkSFEEKDyDALILLTKVRDPT 139
                         170       180
                  ....*....|....*....|
gi 446571459  159 RFGSLIL-DKQSVTSFQEKP 177
Cdd:TIGR01208 140 AFGVAVLeDGKRILKLVEKP 159
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
3-64 1.29e-15

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


Pssm-ID: 133014 [Multi-domain]  Cd Length: 229  Bit Score: 73.42  E-value: 1.29e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446571459   3 AVILAGGYGTRIGEETHLKPKPMIEIGTKPILWHIMSLYSHYGITEFIICLGYKGYAIKEFF 64
Cdd:cd02523    1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELL 62
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-177 5.19e-13

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 67.04  E-value: 5.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459   1 MKAVILAGGYGTRIGEETHLKPKPMIEIGTKPILWHIMSLYSHYGITEFIICLG-YKGYAIKEFFLNynlhMSDFTIQLn 79
Cdd:COG1209    1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTpEDGPQFERLLGD----GSQLGIKI- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459  80 dnTI--------TSHShrvepwkvtlidtgvntetggrVKKIQNYVGDEPFCLTYGDglsNV----NIKELITFHKKHGK 147
Cdd:COG1209   76 --SYavqpeplgLAHA----------------------FIIAEDFIGGDPVALVLGD---NIfygdGLSELLREAAARES 128
                        170       180       190
                 ....*....|....*....|....*....|...
gi 446571459 148 MATVTA--VQPPGRFGSLILDKQS-VTSFQEKP 177
Cdd:COG1209  129 GATIFGykVEDPERYGVVEFDEDGrVVSLEEKP 161
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
1-230 4.31e-12

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: 64.09  E-value: 4.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459   1 MKAVILAGGYGTRIGEETHLKPKPMIEIGTKPILWHIMSLYSHYGITEFIICLGYKGYAIKEFFlNYNLHMSDFTIQLND 80
Cdd:cd02541    1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRGKRAIEDHF-DRSYELEETLEKKGK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459  81 NT-ITSHSHRVEPWKVTLIDTGVNTETGGRVKKIQNYVGDEPFCLTYGDGL--SNV-NIKELITFHKKHGKmaTVTAVQ- 155
Cdd:cd02541   80 TDlLEEVRIISDLANIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLidSKEpCLKQLIEAYEKTGA--SVIAVEe 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459 156 -PP---GRFGSLILDKQ-----SVTSFQEKPLGDGGWVN---GGFFILNPEVFNYISGDKS-----VFETDSLVQLVNKN 218
Cdd:cd02541  158 vPPedvSKYGIVKGEKIdgdvfKVKGLVEKPKPEEAPSNlaiVGRYVLTPDIFDILENTKPgkggeIQLTDAIAKLLEEE 237
                        250
                 ....*....|..
gi 446571459 219 ELAAYQHSGFWH 230
Cdd:cd02541  238 PVYAYVFEGKRY 249
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
1-155 2.70e-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: 61.12  E-value: 2.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459   1 MKAVILAGGYGTRIGEETHLKPKPMIEIGTKPILWH-IMSLYSHyGITE-FIICLGYKG----YAIKEFFLNYNLHMSDF 74
Cdd:cd02507    1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYtLEWLEKA-GVEEvFVVCCEHSQaiieHLLKSKWSSLSSKMIVD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459  75 TIqlndntitshshrvepwkvtLIDTGVNTETGGRVKKIQNYVgDEPFCLTYGDGLSNVNIKELI-TFHKKH-GKMATVT 152
Cdd:cd02507   80 VI--------------------TSDLCESAGDALRLRDIRGLI-RSDFLLLSCDLVSNIPLSELLeERRKKDkNAIATLT 138

                 ...
gi 446571459 153 AVQ 155
Cdd:cd02507  139 VLL 141
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
3-229 1.53e-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: 59.57  E-value: 1.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459   3 AVILAGG--YGTRIGEETHLKPKPMIEIGTKPILWHIMSLYSHY-GITEfIICLGYkgYAIKEFFLNYNLHMSDFTIQLn 79
Cdd:cd06428    1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKVpDLKE-VLLIGF--YPESVFSDFISDAQQEFNVPI- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459  80 dntitshSHRVEPwkvTLIDTGvntetGGRVKKIQNYVGDEP--FCLTYGDGLSNVNIKELITFHKKHGKMATVTAVQPP 157
Cdd:cd06428   77 -------RYLQEY---KPLGTA-----GGLYHFRDQILAGNPsaFFVLNADVCCDFPLQELLEFHKKHGASGTILGTEAS 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459 158 G----RFGSLILDKQS--VTSFQEKPlgdGGWV----NGGFFILNPEVFNYIS---------------------GDKSVF 206
Cdd:cd06428  142 ReqasNYGCIVEDPSTgeVLHYVEKP---ETFVsdliNCGVYLFSPEIFDTIKkafqsrqqeaqlgddnnregrAEVIRL 218
                        250       260
                 ....*....|....*....|...
gi 446571459 207 ETDSLVQLVNKNELAAYQHSGFW 229
Cdd:cd06428  219 EQDVLTPLAGSGKLYVYKTDDFW 241
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
1-199 5.44e-09

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: 54.89  E-value: 5.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459   1 MKAVILAGGYGTRIGEETHLKPKPMIEIGTKPILWHIMSLYSHYGITEFIICLGYKgyaikefflnynlHMSDFTIQLND 80
Cdd:cd02538    1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPE-------------DLPLFKELLGD 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459  81 NtitshshrvEPWKVTlIDTGVNTETGGRVKKI---QNYVGDEPFCLTYGDGL-SNVNIKELITFHKKHGKMATVTA--V 154
Cdd:cd02538   68 G---------SDLGIR-ITYAVQPKPGGLAQAFiigEEFIGDDPVCLILGDNIfYGQGLSPILQRAAAQKEGATVFGyeV 137
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 446571459 155 QPPGRFGSLILDKQS-VTSFQEKPLGDGG-WVNGGFFILNPEVFNYI 199
Cdd:cd02538  138 NDPERYGVVEFDENGrVLSIEEKPKKPKSnYAVTGLYFYDNDVFEIA 184
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
1-154 2.49e-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: 52.66  E-value: 2.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459   1 MKAVILAGGYGTRIGEETHLKPKPMIEIGTKPILWHIMSLYSHYGITEFIICL-----GYKGYAIKEFFLNYNLHMSDFT 75
Cdd:cd04198    1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVpeeeqAEISTYLRSFPLNLKQKLDEVT 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446571459  76 IQLNDNTITSHSHRvepwKVTlidtgvntetggrvKKIQNYVgdepFCLTyGDGLSNVNIKELITFHKKHGkmATVTAV 154
Cdd:cd04198   81 IVLDEDMGTADSLR----HIR--------------KKIKKDF----LVLS-CDLITDLPLIELVDLHRSHD--ASLTVL 134
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
3-51 1.52e-06

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


Pssm-ID: 133009 [Multi-domain]  Cd Length: 218  Bit Score: 47.52  E-value: 1.52e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 446571459   3 AVILAGGYGTRIGEEThlkPKPMIEIGTKPILWH-IMSLYSHYGITEFII 51
Cdd:cd02516    3 AIILAAGSGSRMGADI---PKQFLELGGKPVLEHtLEAFLAHPAIDEIVV 49
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
3-70 1.49e-05

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 44.38  E-value: 1.49e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446571459   3 AVILAGGYGTRIGEethlkPKPMIEIGTKPILWHIMSLYSHYGITEFIICLGYKGYAIKEFFLNYNLH 70
Cdd:COG2068    6 AIILAAGASSRMGR-----PKLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADAEEVAAALAGLGVR 68
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
3-168 1.80e-05

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: 44.43  E-value: 1.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459   3 AVILAGGYGTRIGEEthlKPKPMIEIGTKPILWHIMSLYSHYGITEFIICLGYKGYAIKEFFLNYNLHmsdFTIQlndnt 82
Cdd:cd02540    1 AVILAAGKGTRMKSD---LPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVKKALANPNVE---FVLQ----- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459  83 itshshrvepwkvtlidtgvnTE---TGGRVK----KIQNYVGDepFCLTYGDG--LSNVNIKELITFHKKHGKMATV-T 152
Cdd:cd02540   70 ---------------------EEqlgTGHAVKqalpALKDFEGD--VLVLYGDVplITPETLQRLLEAHREAGADVTVlT 126
                        170
                 ....*....|....*..
gi 446571459 153 AVQP-PGRFGSLILDKQ 168
Cdd:cd02540  127 AELEdPTGYGRIIRDGN 143
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
2-230 3.34e-05

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


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 44.25  E-value: 3.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459   2 KAVILAGGYGTR-------IgeethlkPKPMIEIGTKPILwhimslysHY--------GITEFIICLGYKGYAIKEFF-L 65
Cdd:COG1210    5 KAVIPVAGLGTRflpatkaI-------PKEMLPIVDKPLI--------QYvveeavaaGIEEIIFVTGRGKRAIEDHFdR 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459  66 NYNLHMsdftiqlndntitshshrvepwkvTLIDTGvNTETGGRVKKIQNY------------------------VGDEP 121
Cdd:COG1210   70 SYELEA------------------------TLEAKG-KEELLEEVRSISPLanihyvrqkeplglghavlcarpfVGDEP 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459 122 FCLTYGDGL--SNV-NIKELITFHKKHGkmATVTAVQ--PP---GRFGSLILDKQS-----VTSFQEKP--------LGd 180
Cdd:COG1210  125 FAVLLGDDLidSEKpCLKQMIEVYEETG--GSVIAVQevPPeevSKYGIVDGEEIEggvyrVTGLVEKPapeeapsnLA- 201
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446571459 181 ggwVNGGfFILNPEVFNYI------SGDksvfE---TDSLVQLVNKNELAAYQHSGFWH 230
Cdd:COG1210  202 ---IVGR-YILTPEIFDILektkpgAGG----EiqlTDAIAALAKEEPVYAYEFEGKRY 252
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
4-53 3.50e-05

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: 43.58  E-value: 3.50e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446571459   4 VILAGGYGTRIGEEThlkPKPMIEIGTKPILWH-IMSLYSHYGITEFIICL 53
Cdd:COG1211    1 IIPAAGSGSRMGAGI---PKQFLPLGGKPVLEHtLEAFLAHPRIDEIVVVV 48
LicC COG4750
CTP:phosphocholine cytidylyltransferase LicC [Cell wall/membrane/envelope biogenesis, Lipid ...
1-64 8.56e-05

CTP:phosphocholine cytidylyltransferase LicC [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism];


Pssm-ID: 443784 [Multi-domain]  Cd Length: 228  Bit Score: 42.51  E-value: 8.56e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446571459   1 MKAVILAGGYGTRIGEETHLKPKPMIEIGTKP-ILWHIMSLYShYGITEFIICLGYKgyaiKEFF 64
Cdd:COG4750    1 MNAIILAAGLGSRFAPITYETPKGLLKVNGEPlIERQIRQLHE-AGITDITVVVGYL----KEQF 60
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
3-37 1.30e-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: 41.41  E-value: 1.30e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 446571459    3 AVILAGGYGTRIGEethlkPKPMIEIGTKPILWHI 37
Cdd:pfam12804   1 AVILAGGRSSRMGG-----DKALLPLGGKPLLERV 30
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
3-154 2.02e-04

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: 41.44  E-value: 2.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459   3 AVILAGGYGTRIGEETHLKPK--------PMIEigtkpilWHIMSLySHYGITE-FIICLGYKGyAIKEFFLNynlhmSD 73
Cdd:cd04197    3 AVVLADSFNRRFRPLTKEKPRcllplanvPLID-------YTLEFL-ALNGVEEvFVFCCSHSD-QIKEYIEK-----SK 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459  74 ftiqlndntitSHSHRVEPWKVTLIdTGVNTETGGRV-------KKIQNYvgdepFCLTYGDGLSNVNIKELITFHK--- 143
Cdd:cd04197   69 -----------WSKPKSSLMIVIII-MSEDCRSLGDAlrdldakGLIRGD-----FILVSGDVVSNIDLKEILEEHKerr 131
                        170
                 ....*....|.
gi 446571459 144 KHGKMATVTAV 154
Cdd:cd04197  132 KKDKNAIMTMV 142
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
3-67 3.48e-04

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 40.89  E-value: 3.48e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446571459   3 AVILAGGYGTRIGEEthlKPKPMIEIGTKPILWH-IMSLYSHYGITEFIICL--GYKGYAIKEFFLNY 67
Cdd:PRK00155   6 AIIPAAGKGSRMGAD---RPKQYLPLGGKPILEHtLEAFLAHPRIDEIIVVVppDDRPDFAELLLAKD 70
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
1-70 4.74e-04

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: 40.78  E-value: 4.74e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571459   1 MKAVILAGGYGTRIGEEThlkPKPMIEIGTKPILWHIMSLYSHYGITEFIICLGYKGYAIKEFFLNYNLH 70
Cdd:COG1207    3 LAVVILAAGKGTRMKSKL---PKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVRAALADLDVE 69
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
1-52 4.77e-04

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: 39.87  E-value: 4.77e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446571459   1 MKAVILAGGYGTRIGEethlkPKPMIEIGTKPILWHIMSLYSHYGITEFIIC 52
Cdd:cd02503    1 ITGVILAGGKSRRMGG-----DKALLELGGKPLLEHVLERLKPLVDEVVISA 47
mobA PRK00317
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
1-38 7.48e-04

molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed


Pssm-ID: 234725 [Multi-domain]  Cd Length: 193  Bit Score: 39.40  E-value: 7.48e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 446571459   1 MKAVILAGGYGTRIGEEthlkPKPMIEIGTKPILWHIM 38
Cdd:PRK00317   4 ITGVILAGGRSRRMGGV----DKGLQELNGKPLIQHVI 37
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
1-37 1.13e-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: 1.13e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 446571459   1 MKAVILAGGYGTRIGEethlkPKPMIEIGTKPILWHI 37
Cdd:COG0746    5 ITGVILAGGRSRRMGQ-----DKALLPLGGRPLLERV 36
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
4-67 9.82e-03

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 36.89  E-value: 9.82e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446571459   4 VILAGGYGTRIGEEThlkPKPMIEIGTKPILWHImsLYSHYGITEFI-ICLGYKGYAIKEFFLNY 67
Cdd:PRK14359   6 IILAAGKGTRMKSSL---PKVLHTICGKPMLFYI--LKEAFAISDDVhVVLHHQKERIKEAVLEY 65
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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