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Conserved domains on  [gi|1036601530|gb|OBA09640|]
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glucose-1-phosphate cytidylyltransferase [Bacillus subtilis]

Protein Classification

glucose-1-phosphate cytidylyltransferase( domain architecture ID 10118576)

glucose-1-phosphate cytidylyltransferase catalyzes the transfer of a CMP moiety from CTP to glucose 1-phosphate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
 3-252 4.90e-137

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: 385.39  E-value: 4.90e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530   3 AVILCGGKGTRMSEVTNDIPKPLAMIGGKPILWHIMKIYQYYGVNEFILLLGYKGEKIKEYFLDYEWKHNSLTLDSSTGE 82
Cdd:cd02524     1 VVILAGGLGTRLSEETELKPKPMVEIGGRPILWHIMKIYSHYGHNDFILCLGYKGHVIKEYFLNYFLHNSDVTIDLGTNR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530  83 VQMLGQ-PETWKITFLETGEDTLTAGRILQAKDYIGD-ETFLLTYGDGLANINLFHLISFHQAKGAAATVTGIDKVSQFG 160
Cdd:cd02524    81 IELHNSdIEDWKVTLVDTGLNTMTGGRLKRVRRYLGDdETFMLTYGDGVSDVNINALIEFHRSHGKLATVTAVHPPGRFG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530 161 TLTV-EDGMAKTFSEKTSSD-GIINGGFFVLSPKVFDYLPkNGNAMFEDEPLKNLAKDGELAVYRHYGFWTAIDTYKNLL 238
Cdd:cd02524   161 ELDLdDDGQVTSFTEKPQGDgGWINGGFFVLEPEVFDYID-GDDTVFEREPLERLAKDGELMAYKHTGFWQCMDTLRDKQ 239

                         250
                  ....*....|....
gi 1036601530 239 EVNKMWDQGQQVWK 252
Cdd:cd02524   240 TLEELWNSGKAPWK 253
 
Name Accession Description Interval E-value
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
 3-252 4.90e-137

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: 385.39  E-value: 4.90e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530   3 AVILCGGKGTRMSEVTNDIPKPLAMIGGKPILWHIMKIYQYYGVNEFILLLGYKGEKIKEYFLDYEWKHNSLTLDSSTGE 82
Cdd:cd02524     1 VVILAGGLGTRLSEETELKPKPMVEIGGRPILWHIMKIYSHYGHNDFILCLGYKGHVIKEYFLNYFLHNSDVTIDLGTNR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530  83 VQMLGQ-PETWKITFLETGEDTLTAGRILQAKDYIGD-ETFLLTYGDGLANINLFHLISFHQAKGAAATVTGIDKVSQFG 160
Cdd:cd02524    81 IELHNSdIEDWKVTLVDTGLNTMTGGRLKRVRRYLGDdETFMLTYGDGVSDVNINALIEFHRSHGKLATVTAVHPPGRFG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530 161 TLTV-EDGMAKTFSEKTSSD-GIINGGFFVLSPKVFDYLPkNGNAMFEDEPLKNLAKDGELAVYRHYGFWTAIDTYKNLL 238
Cdd:cd02524   161 ELDLdDDGQVTSFTEKPQGDgGWINGGFFVLEPEVFDYID-GDDTVFEREPLERLAKDGELMAYKHTGFWQCMDTLRDKQ 239

                         250
                  ....*....|....
gi 1036601530 239 EVNKMWDQGQQVWK 252
Cdd:cd02524   240 TLEELWNSGKAPWK 253
G1P_cyt_trans TIGR02623
glucose-1-phosphate cytidylyltransferase; Members of this family are the enzyme ...
 2-254 2.43e-91

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: 269.70  E-value: 2.43e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530   2 KAVILCGGKGTRMSEVTNDIPKPLAMIGGKPILWHIMKIYQYYGVNEFILLLGYKGEKIKEYFLDYEWKHNSLTLDSSTG 81
Cdd:TIGR02623   1 KAVILAGGLGTRISEETHLRPKPMVEIGGKPILWHIMKIYSHHGINDFIICCGYKGYVIKEYFANYFLHMSDVTFHMADN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530  82 EVQMLG-QPETWKITFLETGEDTLTAGRILQAKDYIGDETFLLTYGDGLANINLFHLISFHQAKGAAATVTGIDKVSQFG 160
Cdd:TIGR02623  81 TMEVHHkRVEPWRVTLVDTGESTQTGGRLKRVREYLDDEAFCFTYGDGVADIDIKALIAFHRKHGKKATVTAVQPPGRFG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530 161 TLTVEDGMAKTFSEKTSSD-GIINGGFFVLSPKVFDYLpKNGNAMFEDEPLKNLAKDGELAVYRHYGFWTAIDTY--KNL 237
Cdd:TIGR02623 161 ALDLEGEQVTSFQEKPLGDgGWINGGFFVLNPSVLDLI-DGDATVWEQEPLETLAQRGELSAYEHSGFWQPMDTLrdKNY 239

                         250
                  ....*....|....*..
gi 1036601530 238 LEvnKMWDQGQQVWKVW 254
Cdd:TIGR02623 240 LE--ELWESGRAPWKVW 254
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 2-254 3.00e-89

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: 263.94  E-value: 3.00e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530   2 KAVILCGGKGTRMSEVTNDIPKPLAMIGGKPILWHIMKIYQYYGVNEFILLLGYKGEKIKEYFLDyewkhnsltldsstg 81
Cdd:COG1208     1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGD--------------- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530  82 evqmlGQPETWKITFLETGEDTLTAGRILQAKDYIGDETFLLTYGDGLANINLFHLISFHQAKGAAATVTGI--DKVSQF 159
Cdd:COG1208    66 -----GSRFGVRITYVDEGEPLGTGGALKRALPLLGDEPFLVLNGDILTDLDLAALLAFHREKGADATLALVpvPDPSRY 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530 160 GTLTV-EDGMAKTFSEK--TSSDGIINGGFFVLSPKVFDYLPKNGNAMFEDePLKNLAKDGELAVYRHYGFWTAIDTYKN 236
Cdd:COG1208   141 GVVELdGDGRVTRFVEKpeEPPSNLINAGIYVLEPEIFDYIPEGEPFDLED-LLPRLIAEGRVYGYVHDGYWLDIGTPED 219

                         250
                  ....*....|....*...
gi 1036601530 237 LLEVNKMWDQGQQVWKVW 254
Cdd:COG1208   220 LLEANALLLSGKAPVVIW 237
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-241 3.28e-20

Nucleotidyl transferase; This family includes a wide range of enzymes which transfer nucleotides onto phosphosugars.


Pssm-ID: 425709 [Multi-domain]  Cd Length: 243  Bit Score: 86.15  E-value: 3.28e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530   2 KAVILCGGKGTRMSEVTNDIPKPLAMIGGK-PILWHIMKIYQYYGVNEFILLLG-YKGEKIKEYFLD-YEWKHNsltlds 78
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTqEHRFMLNELLGDgSKFGVQ------ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530  79 stgevqmlgqpetwkITFLETGEDTLTAGRILQAKDYIGDE--TFLLTYGDGLANINLFHLISFHQAKGAAATVTGI--- 153
Cdd:pfam00483  75 ---------------ITYALQPEGKGTAPAVALAADFLGDEksDVLVLGGDHIYRMDLEQAVKFHIEKAADATVTFGivp 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530 154 -DKVSQFGTLTVED-GMAKTFSEK----TSSDgIINGGFFVLSPKVFDYLPKNGNAMFEDEP-----LKNLAKDGELAVY 222
Cdd:pfam00483 140 vEPPTGYGVVEFDDnGRVIRFVEKpklpKASN-YASMGIYIFNSGVLDFLAKYLEELKRGEDeitdiLPKALEDGKLAYA 218

                         250       260
                  ....*....|....*....|..
gi 1036601530 223 ---RHYgFWTAIDTYKNLLEVN 241
Cdd:pfam00483 219 fifKGY-AWLDVGTWDSLWEAN 239
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-150 2.23e-09

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 57.15  E-value: 2.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530   3 AVILCGGKGTRMsevTNDIPKPLAMIGGKPILWHIMKIYQYYGVNEFILLLGYKGEKIKEyfldyewkhnslTLDSSTG- 81
Cdd:PRK14354    5 AIILAAGKGTRM---KSKLPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVGHGAEEVKE------------VLGDRSEf 69

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1036601530  82 ---EVQmLGqpetwkitfletgedtlTAGRILQAKDYIGDE--TFLLTYGDG--LANINLFHLISFHQAKGAAATV 150
Cdd:PRK14354   70 alqEEQ-LG-----------------TGHAVMQAEEFLADKegTTLVICGDTplITAETLKNLIDFHEEHKAAATI 127
 
Name Accession Description Interval E-value
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
 3-252 4.90e-137

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: 385.39  E-value: 4.90e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530   3 AVILCGGKGTRMSEVTNDIPKPLAMIGGKPILWHIMKIYQYYGVNEFILLLGYKGEKIKEYFLDYEWKHNSLTLDSSTGE 82
Cdd:cd02524     1 VVILAGGLGTRLSEETELKPKPMVEIGGRPILWHIMKIYSHYGHNDFILCLGYKGHVIKEYFLNYFLHNSDVTIDLGTNR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530  83 VQMLGQ-PETWKITFLETGEDTLTAGRILQAKDYIGD-ETFLLTYGDGLANINLFHLISFHQAKGAAATVTGIDKVSQFG 160
Cdd:cd02524    81 IELHNSdIEDWKVTLVDTGLNTMTGGRLKRVRRYLGDdETFMLTYGDGVSDVNINALIEFHRSHGKLATVTAVHPPGRFG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530 161 TLTV-EDGMAKTFSEKTSSD-GIINGGFFVLSPKVFDYLPkNGNAMFEDEPLKNLAKDGELAVYRHYGFWTAIDTYKNLL 238
Cdd:cd02524   161 ELDLdDDGQVTSFTEKPQGDgGWINGGFFVLEPEVFDYID-GDDTVFEREPLERLAKDGELMAYKHTGFWQCMDTLRDKQ 239

                         250
                  ....*....|....
gi 1036601530 239 EVNKMWDQGQQVWK 252
Cdd:cd02524   240 TLEELWNSGKAPWK 253
G1P_cyt_trans TIGR02623
glucose-1-phosphate cytidylyltransferase; Members of this family are the enzyme ...
 2-254 2.43e-91

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: 269.70  E-value: 2.43e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530   2 KAVILCGGKGTRMSEVTNDIPKPLAMIGGKPILWHIMKIYQYYGVNEFILLLGYKGEKIKEYFLDYEWKHNSLTLDSSTG 81
Cdd:TIGR02623   1 KAVILAGGLGTRISEETHLRPKPMVEIGGKPILWHIMKIYSHHGINDFIICCGYKGYVIKEYFANYFLHMSDVTFHMADN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530  82 EVQMLG-QPETWKITFLETGEDTLTAGRILQAKDYIGDETFLLTYGDGLANINLFHLISFHQAKGAAATVTGIDKVSQFG 160
Cdd:TIGR02623  81 TMEVHHkRVEPWRVTLVDTGESTQTGGRLKRVREYLDDEAFCFTYGDGVADIDIKALIAFHRKHGKKATVTAVQPPGRFG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530 161 TLTVEDGMAKTFSEKTSSD-GIINGGFFVLSPKVFDYLpKNGNAMFEDEPLKNLAKDGELAVYRHYGFWTAIDTY--KNL 237
Cdd:TIGR02623 161 ALDLEGEQVTSFQEKPLGDgGWINGGFFVLNPSVLDLI-DGDATVWEQEPLETLAQRGELSAYEHSGFWQPMDTLrdKNY 239

                         250
                  ....*....|....*..
gi 1036601530 238 LEvnKMWDQGQQVWKVW 254
Cdd:TIGR02623 240 LE--ELWESGRAPWKVW 254
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 2-254 3.00e-89

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: 263.94  E-value: 3.00e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530   2 KAVILCGGKGTRMSEVTNDIPKPLAMIGGKPILWHIMKIYQYYGVNEFILLLGYKGEKIKEYFLDyewkhnsltldsstg 81
Cdd:COG1208     1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGD--------------- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530  82 evqmlGQPETWKITFLETGEDTLTAGRILQAKDYIGDETFLLTYGDGLANINLFHLISFHQAKGAAATVTGI--DKVSQF 159
Cdd:COG1208    66 -----GSRFGVRITYVDEGEPLGTGGALKRALPLLGDEPFLVLNGDILTDLDLAALLAFHREKGADATLALVpvPDPSRY 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530 160 GTLTV-EDGMAKTFSEK--TSSDGIINGGFFVLSPKVFDYLPKNGNAMFEDePLKNLAKDGELAVYRHYGFWTAIDTYKN 236
Cdd:COG1208   141 GVVELdGDGRVTRFVEKpeEPPSNLINAGIYVLEPEIFDYIPEGEPFDLED-LLPRLIAEGRVYGYVHDGYWLDIGTPED 219

                         250
                  ....*....|....*...
gi 1036601530 237 LLEVNKMWDQGQQVWKVW 254
Cdd:COG1208   220 LLEANALLLSGKAPVVIW 237
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 3-228 6.31e-56

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: 178.54  E-value: 6.31e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530   3 AVILCGGKGTRMSEVTNDIPKPLAMIGGKPILWHIMKIYQYYGVNEFILLLGYKGEKIKEYFLDYEWKHNsltldsstge 82
Cdd:cd04181     1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGSKFGV---------- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530  83 vqmlgqpetwKITFLETGEDTLTAGRILQAKDYIGDETFLLTYGDGLANINLFHLISFHQAKGAAATVTGI--DKVSQFG 160
Cdd:cd04181    71 ----------NIEYVVQEEPLGTAGAVRNAEDFLGDDDFLVVNGDVLTDLDLSELLRFHREKGADATIAVKevEDPSRYG 140

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1036601530 161 TLTVED-GMAKTFSEKTSSDG--IINGGFFVLSPKVFDYLPKN--GNAMFEDEPLKNLAKDGELAVYRHYGFW 228
Cdd:cd04181   141 VVELDDdGRVTRFVEKPTLPEsnLANAGIYIFEPEILDYIPEIlpRGEDELTDAIPLLIEEGKVYGYPVDGYW 213
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 3-222 4.69e-49

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: 160.80  E-value: 4.69e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530   3 AVILCGGKGTRMSEVTNDIPKPLAMIGGKPILWHIMKIYQYYGVNEFILLLGYKGEKIKEYFLDYEWKhnSLTLDSSTGE 82
Cdd:cd06915     1 AVILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYLAEQIEEYFGDGYRG--GIRIYYVIEP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530  83 VQmLGqpetwkitfletgedtlTAGRILQAKDYIGDETFLLTYGDGLANINLFHLISFHQAKGAAATVTGID--KVSQFG 160
Cdd:cd06915    79 EP-LG-----------------TGGAIKNALPKLPEDQFLVLNGDTYFDVDLLALLAALRASGADATMALRRvpDASRYG 140

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1036601530 161 TLTVEDGMAKT-FSEKTSSD--GIINGGFFVLSPKVFDYLPKNgNAMFEDEPLKNLAKDGELAVY 222
Cdd:cd06915   141 NVTVDGDGRVIaFVEKGPGAapGLINGGVYLLRKEILAEIPAD-AFSLEADVLPALVKRGRLYGF 204
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 3-231 1.98e-43

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: 146.50  E-value: 1.98e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530   3 AVILCGGKGTRMSEVTNDIPKPLAMIGGKPILWHIMKIYQYYGVNEFILLLGYKGEKIKEYFldyewkhnsltldsstge 82
Cdd:cd06426     1 VVIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNYLAEMIEDYF------------------ 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530  83 vqmlGQPETW--KITFLETGEDTLTAGRILQAKDYIgDETFLLTYGDGLANINLFHLISFHQAKGAAATVTGIDKVSQ-- 158
Cdd:cd06426    63 ----GDGSKFgvNISYVREDKPLGTAGALSLLPEKP-TDPFLVMNGDILTNLNYEHLLDFHKENNADATVCVREYEVQvp 137

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1036601530 159 FGTLTVEDGMAKTFSEKTSSDGIINGGFFVLSPKVFDYLPKNGNAMFEDEPLKNLAKDGELAVYRHYGFWTAI 231
Cdd:cd06426   138 YGVVETEGGRITSIEEKPTHSFLVNAGIYVLEPEVLDLIPKNEFFDMPDLIEKLIKEGKKVGVFPIHEYWLDI 210
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 1-243 1.18e-38

UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The MJ_1101 protein from Methanococcus jannaschii has been characterized as the GlmU enzyme catalyzing the final two steps of UDP-GlcNAc biosynthesis. Many of the genes identified by this model are in proximity to the GlmS and GlmM genes and are also presumed to be GlmU. However, some archaeal genomes contain multiple closely-related homologs from this family and it is not clear what the substrate specificity is for each of them.


Pssm-ID: 274908 [Multi-domain]  Cd Length: 393  Bit Score: 138.50  E-value: 1.18e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530   1 MKAVILCGGKGTRMSEVTNDIPKPLAMIGGKPILWHIMKIYQYYGVNEFILLLGYKGEKIKEYFldyewkhnsltLDSST 80
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEKVREYF-----------GDGSR 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530  81 GEVqmlgqpetwKITFLETGEDTLTAGRILQAKDYIgDETFLLTYGDGLANINLF-HLISfhqAKGAAATVTGIDKVSQF 159
Cdd:TIGR03992  70 GGV---------PIEYVVQEEQLGTADALGSAKEYV-DDEFLVLNGDVLLDSDLLeRLIR---AEAPAIAVVEVDDPSDY 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530 160 GTLTVEDGMAKTFSEKTSS--DGIINGGFFVLSPKVFDYLPK-----NGNAMFEDEpLKNLAKDGELAVYRHYGFWTAID 232
Cdd:TIGR03992 137 GVVETDGGRVTGIVEKPENppSNLINAGIYLFSPEIFELLEKtklspRGEYELTDA-LQLLIDEGKVKAVELDGFWLDVG 215

                         250
                  ....*....|.
gi 1036601530 233 TYKNLLEVNKM 243
Cdd:TIGR03992 216 RPWDLLDANEA 226
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 1-242 1.95e-28

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: 108.04  E-value: 1.95e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530   1 MKAVILCGGKGTRMSEVTNDIPKPLAMIGGKPILWHIMKIYQYYGVNEFILLLGYKGEKIKEYFldyewkhnsltldsst 80
Cdd:cd04189     1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEAL---------------- 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530  81 GEVQMLGQpetwKITFLETGEDTLTAGRILQAKDYIGDETFLLTYGDGLANINLFHLISFHQAKGAAAT--VTGIDKVSQ 158
Cdd:cd04189    65 GDGSRFGV----RITYILQEEPLGLAHAVLAARDFLGDEPFVVYLGDNLIQEGISPLVRDFLEEDADASilLAEVEDPRR 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530 159 FGTLTVEDGMAKTFSEK----TSSDGIIngGFFVLSPKVFDYL----P-KNGNAMFEDEPLKNLAKDGELAVYRHYGFWT 229
Cdd:cd04189   141 FGVAVVDDGRIVRLVEKpkepPSNLALV--GVYAFTPAIFDAIsrlkPsWRGELEITDAIQWLIDRGRRVGYSIVTGWWK 218

                         250
                  ....*....|...
gi 1036601530 230 AIDTYKNLLEVNK 242
Cdd:cd04189   219 DTGTPEDLLEANR 231
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 1-239 2.84e-28

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: 107.30  E-value: 2.84e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530   1 MKAVILCGGKGTRMSEVTNDIPKPLAMIGGKPILWHIMKIYQYYGVNEFILLLGYKGEKIKEYFLDYEWKHNSltldsst 80
Cdd:cd06425     1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYRPEDMVPFLKEYEKKLGI------- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530  81 gevqmlgqpetwKITF-LETgEDTLTAGRILQAKDYIG--DETFLLTYGDGLANINLFHLISFHQAKGAAAT--VTGIDK 155
Cdd:cd06425    74 ------------KITFsIET-EPLGTAGPLALARDLLGddDEPFFVLNSDVICDFPLAELLDFHKKHGAEGTilVTKVED 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530 156 VSQFGTLtVED---GMAKTFSEKTSS--DGIINGGFFVLSPKVFDYLPkNGNAMFEDEPLKNLAKDGELAVYRHYGFWTA 230
Cdd:cd06425   141 PSKYGVV-VHDentGRIERFVEKPKVfvGNKINAGIYILNPSVLDRIP-LRPTSIEKEIFPKMASEGQLYAYELPGFWMD 218


                  ....*....
gi 1036601530 231 IDTYKNLLE 239
Cdd:cd06425   219 IGQPKDFLK 227
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
2-244 4.33e-23

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 93.77  E-value: 4.33e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530   2 KAVILCGGKGTRMSEVTNDIPKPLAMIGGKPILWHIMKIYQYYGVNEFILLLGYKGEKIKEYFL------------DYEW 69
Cdd:COG1213     1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEALArpgpdvtfvynpDYDE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530  70 KHNSLTLdsstgevqmlgqpetwkitfletgedtltagriLQAKDYIGDEtFLLTYGDGLANINLFHLIsfhQAKGAAAT 149
Cdd:COG1213    81 TNNIYSL---------------------------------WLAREALDED-FLLLNGDVVFDPAILKRL---LASDGDIV 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530 150 VTgIDKVSQFG-----TLTVE-DGMAKTFSeKTSSDGIING---GFFVLSPKVFDYL---------PKNGNAMFEDePLK 211
Cdd:COG1213   124 LL-VDRKWEKPldeevKVRVDeDGRIVEIG-KKLPPEEADGeyiGIFKFSAEGAAALrealealidEGGPNLYYED-ALQ 200

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1036601530 212 NLAKDGEL--AVYRHYGFWTAIDTYKNLLEVNKMW 244
Cdd:COG1213   201 ELIDEGGPvkAVDIGGLPWVEIDTPEDLERAEELF 235
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 3-233 7.56e-21

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: 88.46  E-value: 7.56e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530   3 AVILCGG--KGTRMSEVTNDIPKPLAMIGGKPILWHIM-KIYQYYGVNEfILLLGYKGEKIKEYFLDYEwkHNSLTLdss 79
Cdd:cd06428     1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIeACAKVPDLKE-VLLIGFYPESVFSDFISDA--QQEFNV--- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530  80 tgevqmlgqpetwKITFLEtgEDTL--TAGRILQAKDYI---GDETFLLTYGDGLANINLFHLISFHQAKGAAATVTGI- 153
Cdd:cd06428    75 -------------PIRYLQ--EYKPlgTAGGLYHFRDQIlagNPSAFFVLNADVCCDFPLQELLEFHKKHGASGTILGTe 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530 154 ---DKVSQFGTLtVEDgmAKTFS-----EKTSS--DGIINGGFFVLSPKVFDYLPK------------NGNA-------- 203
Cdd:cd06428   140 asrEQASNYGCI-VED--PSTGEvlhyvEKPETfvSDLINCGVYLFSPEIFDTIKKafqsrqqeaqlgDDNNregraevi 216

                         250       260       270
                  ....*....|....*....|....*....|
gi 1036601530 204 MFEDEPLKNLAKDGELAVYRHYGFWTAIDT 233
Cdd:cd06428   217 RLEQDVLTPLAGSGKLYVYKTDDFWSQIKT 246
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 3-237 3.16e-20

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: 86.13  E-value: 3.16e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530   3 AVILCGGKGTRMSEVTNDIPKPLAMIGGKPILWHIMKIYQYYGVNEFILLLGYKGEKIKEYFLDYEwkhnsltldsstge 82
Cdd:cd02523     1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKKYP-------------- 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530  83 vqmlgqpetwKITFLETG--EDTLTAGRILQAKDYIgDETFLLTYGDGLANINLFH-LISFhqAKGAAATVTGIDKVSQ- 158
Cdd:cd02523    67 ----------NIKFVYNPdyAETNNIYSLYLARDFL-DEDFLLLEGDVVFDPSILErLLSS--PADNAILVDKKTKEWEd 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530 159 -FGTLTVEDGMAKTFSEKTSSDGIING---GFFVLSPKVFDYLPKNGNAMFEDEP--------LKNLAKDGELAVYR-HY 225
Cdd:cd02523   134 eYVKDLDDAGVLLGIISKAKNLEEIQGeyvGISKFSPEDADRLAEALEELIEAGRvnlyyedaLQRLISEEGVKVKDiSD 213

                         250
                  ....*....|..
gi 1036601530 226 GFWTAIDTYKNL 237
Cdd:cd02523   214 GFWYEIDDLEDL 225
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-241 3.28e-20

Nucleotidyl transferase; This family includes a wide range of enzymes which transfer nucleotides onto phosphosugars.


Pssm-ID: 425709 [Multi-domain]  Cd Length: 243  Bit Score: 86.15  E-value: 3.28e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530   2 KAVILCGGKGTRMSEVTNDIPKPLAMIGGK-PILWHIMKIYQYYGVNEFILLLG-YKGEKIKEYFLD-YEWKHNsltlds 78
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTqEHRFMLNELLGDgSKFGVQ------ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530  79 stgevqmlgqpetwkITFLETGEDTLTAGRILQAKDYIGDE--TFLLTYGDGLANINLFHLISFHQAKGAAATVTGI--- 153
Cdd:pfam00483  75 ---------------ITYALQPEGKGTAPAVALAADFLGDEksDVLVLGGDHIYRMDLEQAVKFHIEKAADATVTFGivp 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530 154 -DKVSQFGTLTVED-GMAKTFSEK----TSSDgIINGGFFVLSPKVFDYLPKNGNAMFEDEP-----LKNLAKDGELAVY 222
Cdd:pfam00483 140 vEPPTGYGVVEFDDnGRVIRFVEKpklpKASN-YASMGIYIFNSGVLDFLAKYLEELKRGEDeitdiLPKALEDGKLAYA 218

                         250       260
                  ....*....|....*....|..
gi 1036601530 223 ---RHYgFWTAIDTYKNLLEVN 241
Cdd:pfam00483 219 fifKGY-AWLDVGTWDSLWEAN 239
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
 2-243 6.51e-18

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: 81.68  E-value: 6.51e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530   2 KAVILCGGKGTRMSEVTNDIPKPLAMIGGKPILWHIMKIYQYYGVNEFILLLGYK-GEKIKEYfldyewkhnsltldsst 80
Cdd:TIGR01208   1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIGIVVGPVtGEEIKEI----------------- 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530  81 gevqmLGQPETW--KITFLETGEDTLTAGRILQAKDYIGDETFLLTYGDglaniNLF------HLISFHQAKGAAAT-VT 151
Cdd:TIGR01208  64 -----VGEGERFgaKITYIVQGEPLGLAHAVYTARDFLGDDDFVVYLGD-----NLIqdgisrFVKSFEEKDYDALIlLT 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530 152 GIDKVSQFGTLTVEDG-MAKTFSEK----TSSDGIIngGFFVLSPKVFDYL----PKNGNAMFEDEPLKNLAKDGELAVY 222
Cdd:TIGR01208 134 KVRDPTAFGVAVLEDGkRILKLVEKpkepPSNLAVV--GLYMFRPLIFEAIknikPSWRGELEITDAIQWLIEKGYKVGG 211

                         250       260
                  ....*....|....*....|..
gi 1036601530 223 -RHYGFWTAIDTYKNLLEVNKM 243
Cdd:TIGR01208 212 sKVTGWWKDTGKPEDLLDANRL 233
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 2-239 7.77e-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: 79.54  E-value: 7.77e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530   2 KAVILCGGKGTRMSEVTNDIPKPLAMIGGKP-ILWHIMKIYQyYGVNEFILLLGYKGEKIKEYFLDyewKHNSLTLDSSt 80
Cdd:cd06422     1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPlIDHALDRLAA-AGIRRIVVNTHHLADQIEAHLGD---SRFGLRITIS- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530  81 gevqmlgqPETWKItfLETGedtltaGRILQAKDYIGDETFLLTYGDGLANINLFHLISFHQAKGAAA-----TVTGIDK 155
Cdd:cd06422    76 --------DEPDEL--LETG------GGIKKALPLLGDEPFLVVNGDILWDGDLAPLLLLHAWRMDALllllpLVRNPGH 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530 156 VSQF-------GTLTVEDGMAK---TFSektssdgiingGFFVLSPKVFDYLPK---NGNAMFEDeplknLAKDGELAVY 222
Cdd:cd06422   140 NGVGdfsldadGRLRRGGGGAVapfTFT-----------GIQILSPELFAGIPPgkfSLNPLWDR-----AIAAGRLFGL 203

                         250
                  ....*....|....*..
gi 1036601530 223 RHYGFWTAIDTYKNLLE 239
Cdd:cd06422   204 VYDGLWFDVGTPERLLA 220
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 1-151 3.45e-16

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: 74.98  E-value: 3.45e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530   1 MKAVILCGGKGTRMSEVTNDIPKPLAMIGGKPILWHIMKIYQYYGVNEFILLLGYKGEKIKEYFLDYEWKHnsltlDSST 80
Cdd:cd02507     1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQAIIEHLLKSKWSS-----LSSK 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1036601530  81 GEVQmlgqpetwKITFLETgEDTLTAGRILQAKDYI-GDetFLLTYGDGLANINLFHLI--SFHQAKGAAATVT 151
Cdd:cd02507    76 MIVD--------VITSDLC-ESAGDALRLRDIRGLIrSD--FLLLSCDLVSNIPLSELLeeRRKKDKNAIATLT 138
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 1-150 4.57e-14

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: 71.21  E-value: 4.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530   1 MKAVILCGGKGTRM-SevtnDIPKPLAMIGGKPILWHIMKIYQYYGVNEFILLLGYKGEKIKEYFLDY--EWKHNSltld 77
Cdd:COG1207     3 LAVVILAAGKGTRMkS----KLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVRAALADLdvEFVLQE---- 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1036601530  78 sstgevQMLGqpetwkitfletgedtlTAGRILQAKDYIG--DETFLLTYGDG--LANINLFHLISFHQAKGAAATV 150
Cdd:COG1207    75 ------EQLG-----------------TGHAVQQALPALPgdDGTVLVLYGDVplIRAETLKALLAAHRAAGAAATV 128
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-175 7.09e-14

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 69.73  E-value: 7.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530   1 MKAVILCGGKGTRMSEVTNDIPKPLAMIGGKPILWH----IMKIyqyyGVNEFILLLG-YKGEKIKEYfldyewkhnslt 75
Cdd:COG1209     1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYplstLMLA----GIREILIISTpEDGPQFERL------------ 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530  76 ldsstgevqmLGQPETW--KITFLETGEDTLTAGRILQAKDYIGDETFLLTYGDglaniNLFH------LISFHQAKGAA 147
Cdd:COG1209    65 ----------LGDGSQLgiKISYAVQPEPLGLAHAFIIAEDFIGGDPVALVLGD-----NIFYgdglseLLREAAARESG 129

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1036601530 148 ATVTGiDKV---SQFGTLTV-EDGMAKTFSEK 175
Cdd:COG1209   130 ATIFG-YKVedpERYGVVEFdEDGRVVSLEEK 160
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 3-150 9.77e-13

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: 65.61  E-value: 9.77e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530   3 AVILCGGKGTRM-SevtnDIPKPLAMIGGKPILWHIMKIYQYYGVNEFILLLGYKGEKIKEYFLDYewkhnsltldsstg 81
Cdd:cd02540     1 AVILAAGKGTRMkS----DLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVKKALANP-------------- 62

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1036601530  82 evqmlgqpetwKITFLETGEDTLTAGRILQAKDYIGD--ETFLLTYGDG--LANINLFHLISFHQAKGAAATV 150
Cdd:cd02540    63 -----------NVEFVLQEEQLGTGHAVKQALPALKDfeGDVLVLYGDVplITPETLQRLLEAHREAGADVTV 124
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 1-150 3.69e-11

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: 60.75  E-value: 3.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530   1 MKAVILCGGKGTRMSEVTNDIPKPLAMIGGKPILWHIMKIYQYYGVNEFILLLGYKGEKIKEYFLDYEWKHNSLTLDSST 80
Cdd:cd04198     1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEEQAEISTYLRSFPLNLKQKLDEVT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530  81 GEVQmlgqpetwkitfletgEDTLTAGRILQAKDYIgDETFLLTYGDGLANINLFHLISFHQAKGAAATV 150
Cdd:cd04198    81 IVLD----------------EDMGTADSLRHIRKKI-KKDFLVLSCDLITDLPLIELVDLHRSHDASLTV 133
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 1-197 1.42e-10

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: 59.85  E-value: 1.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530   1 MKAVILCGGKGTRMSEVTNDIPKPLAMIGGKPILWHIMKIYQYYGVNEFILLLGYKGEKIKEYF-LDYEWKHnslTLdSS 79
Cdd:cd02541     1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRGKRAIEDHFdRSYELEE---TL-EK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530  80 TGEVQMLGQ----PETWKITFLETGEdTLTAGR-ILQAKDYIGDETFLLTYGDGL---ANINLFHLISFHQAKGaaATVT 151
Cdd:cd02541    77 KGKTDLLEEvriiSDLANIHYVRQKE-PLGLGHaVLCAKPFIGDEPFAVLLGDDLidsKEPCLKQLIEAYEKTG--ASVI 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1036601530 152 GI-----DKVSQFGTLTVEDGMAKTFS-----EK------TSSDGIIngGFFVLSPKVFDYL 197
Cdd:cd02541   154 AVeevppEDVSKYGIVKGEKIDGDVFKvkglvEKpkpeeaPSNLAIV--GRYVLTPDIFDIL 213
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-150 2.23e-09

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 57.15  E-value: 2.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530   3 AVILCGGKGTRMsevTNDIPKPLAMIGGKPILWHIMKIYQYYGVNEFILLLGYKGEKIKEyfldyewkhnslTLDSSTG- 81
Cdd:PRK14354    5 AIILAAGKGTRM---KSKLPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVGHGAEEVKE------------VLGDRSEf 69

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1036601530  82 ---EVQmLGqpetwkitfletgedtlTAGRILQAKDYIGDE--TFLLTYGDG--LANINLFHLISFHQAKGAAATV 150
Cdd:PRK14354   70 alqEEQ-LG-----------------TGHAVMQAEEFLADKegTTLVICGDTplITAETLKNLIDFHEEHKAAATI 127
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 3-241 4.36e-09

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 56.24  E-value: 4.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530   3 AVILCGGKGTRMSEVTNDIPKPlAM-IGGK------PI--LWH--IMKI-----YQYYGVNEFIlllgYKGEkikeyfld 66
Cdd:COG0448     4 AIILAGGRGSRLGPLTKDRAKP-AVpFGGKyriidfPLsnCVNsgIRRVgvltqYKSHSLNDHI----GSGK-------- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530  67 yEWkhnslTLDSSTGEVQMLgQPETWKitfleTGED--TLTAGRILQAKDYIGD---ETFLLTYGDGLANINLFHLISFH 141
Cdd:COG0448    71 -PW-----DLDRKRGGVFIL-PPYQQR-----EGEDwyQGTADAVYQNLDFIERsdpDYVLILSGDHIYKMDYRQMLDFH 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530 142 QAKGAAATVTGI----DKVSQFGTLTV-EDGMAKTFSEKTSSDGIING--GFFVLSPKVF-DYL---PKNGNAMFEDEPL 210
Cdd:COG0448   139 IESGADITVACIevprEEASRFGVMEVdEDGRITEFEEKPKDPKSALAsmGIYVFNKDVLiELLeedAPNSSHDFGKDII 218

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1036601530 211 KNLAKDGELAVYRHYGFWTAIDTYKNLLEVN 241
Cdd:COG0448   219 PRLLDRGKVYAYEFDGYWRDVGTIDSYYEAN 249
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 3-150 6.07e-08

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: 51.84  E-value: 6.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530   3 AVILCGGKGTRMSEVTNDIPKPLAMIGGKPILWHIMKIYQYYGVNEFILLLGYKGEKIKEYFLDYEWkHNSLtldSSTGE 82
Cdd:cd04197     3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQIKEYIEKSKW-SKPK---SSLMI 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1036601530  83 VQMLgqpetwkitfleTGEDTLTAG---RILQAKDYI-GDetFLLTYGDGLANINLFHLISFHQA-----KGAAATV 150
Cdd:cd04197    79 VIII------------MSEDCRSLGdalRDLDAKGLIrGD--FILVSGDVVSNIDLKEILEEHKErrkkdKNAIMTM 141
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 3-39 2.16e-07

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: 50.21  E-value: 2.16e-07
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1036601530   3 AVILCGGKGTRMSevtNDIPKPLAMIGGKPILWHIMK 39
Cdd:cd02516     3 AIILAAGSGSRMG---ADIPKQFLELGGKPVLEHTLE 36
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-206 2.86e-07

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 50.90  E-value: 2.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530   3 AVILCGGKGTRMSevtNDIPKPLAMIGGKPIL-WHIMKIYQyYGVNEFILLLGYKGEKIKEYFldyewkhnsltldSSTG 81
Cdd:PRK14355    6 AIILAAGKGTRMK---SDLVKVMHPLAGRPMVsWPVAAARE-AGAGRIVLVVGHQAEKVREHF-------------AGDG 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530  82 EVQMLGQPETwkitfLETGEDTLTAGRILQAkdyiGDETFLLTYGDG--LANINLFHLISFHQAKGAAATVTGIDKVSQF 159
Cdd:PRK14355   69 DVSFALQEEQ-----LGTGHAVACAAPALDG----FSGTVLILCGDVplLRAETLQGMLAAHRATGAAVTVLTARLENPF 139

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1036601530 160 G---TLTVEDG-MAKTFSEKTSSD---GI--INGGFFVL-SPKVFDYLP--KNGNAMFE 206
Cdd:PRK14355  140 GygrIVRDADGrVLRIVEEKDATPeerSIreVNSGIYCVeAAFLFDAIGrlGNDNAQGE 198
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-251 4.70e-07

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 50.15  E-value: 4.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530   1 MKAVILCGGKGTRMSevtNDIPKPLAMIGGKPILWHIMKIYQYYGvNEFILLLGYKGEKIKEYFldyewkhnsltldsst 80
Cdd:PRK14357    1 MRALVLAAGKGTRMK---SKIPKVLHKISGKPMINWVIDTAKKVA-QKVGVVLGHEAELVKKLL---------------- 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530  81 gevqmlgqPETWKItFLETgEDTLTAGRILQAKDYIG-DETFLLTYGDG--LANINLFHLISFHQAKGAAATVTG--IDK 155
Cdd:PRK14357   61 --------PEWVKI-FLQE-EQLGTAHAVMCARDFIEpGDDLLILYGDVplISENTLKRLIEEHNRKGADVTILVadLED 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530 156 VSQFGTLTVEDGMAKTFSEKTSSDGI-----INGGFFVLSPK-VFDYLPKngnamfedepLKNLAKDGELAVYRHYGFWT 229
Cdd:PRK14357  131 PTGYGRIIRDGGKYRIVEDKDAPEEEkkikeINTGIYVFSGDfLLEVLPK----------IKNENAKGEYYLTDAVNFAE 200

                         250       260
                  ....*....|....*....|....
gi 1036601530 230 AIDTYK--NLLEVNKMWDQGQQVW 251
Cdd:PRK14357  201 KVRVVKteDLLEITGVNTRIQLAW 224
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
3-70 6.17e-07

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 48.62  E-value: 6.17e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1036601530   3 AVILCGGKGTRMSEvtndiPKPLAMIGGKPILWHIMKIYQYYGVNEFILLLGYKGEKIKEYFLDYEWK 70
Cdd:COG2068     6 AIILAAGASSRMGR-----PKLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADAEEVAAALAGLGVR 68
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
3-36 7.92e-07

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 48.59  E-value: 7.92e-07
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1036601530   3 AVILCGGKGTRMSEvtnDIPKPLAMIGGKPILWH 36
Cdd:PRK00155    6 AIIPAAGKGSRMGA---DRPKQYLPLGGKPILEH 36
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 3-37 1.68e-06

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: 46.80  E-value: 1.68e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1036601530   3 AVILCGGKGTRMSEvtndiPKPLAMIGGKPILWHI 37
Cdd:pfam12804   1 AVILAGGRSSRMGG-----DKALLPLGGKPLLERV 30
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 4-36 1.79e-06

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: 47.43  E-value: 1.79e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1036601530   4 VILCGGKGTRMSevtNDIPKPLAMIGGKPILWH 36
Cdd:COG1211     1 IIPAAGSGSRMG---AGIPKQFLPLGGKPVLEH 30
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-67 1.93e-06

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 48.06  E-value: 1.93e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1036601530   4 VILCGGKGTRMSEVTndiPKPLAMIGGKPILWHIMKiyQYYGVNEFI-LLLGYKGEKIKEYFLDY 67
Cdd:PRK14359    6 IILAAGKGTRMKSSL---PKVLHTICGKPMLFYILK--EAFAISDDVhVVLHHQKERIKEAVLEY 65
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 1-136 3.23e-06

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: 46.80  E-value: 3.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530   1 MKAVILCGGKGTRMSEVTNDIPKPLAMIGGKPILWHIMKIYQYYGVNEfILLLgykgekikeyfldyewkhnsltldsST 80
Cdd:cd02538     1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIRE-ILII-------------------------ST 54

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1036601530  81 GE-----VQMLGQPETWKITFLETGEDtlTAGRILQA----KDYIGDETFLLTYGDglaniNLFH 136
Cdd:cd02538    55 PEdlplfKELLGDGSDLGIRITYAVQP--KPGGLAQAfiigEEFIGDDPVCLILGD-----NIFY 112
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 1-37 5.25e-06

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: 45.64  E-value: 5.25e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1036601530   1 MKAVILCGGKGTRMSEvtndiPKPLAMIGGKPILWHI 37
Cdd:cd02503     1 ITGVILAGGKSRRMGG-----DKALLELGGKPLLEHV 32
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-66 5.36e-06

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 47.03  E-value: 5.36e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1036601530   3 AVILCGGKGTRMSevtNDIPKPLAMIGGKPILWHIMK-IYQYYGVNEFiLLLGYKGEKIKEYFLD 66
Cdd:PRK14356    8 ALILAAGKGTRMH---SDKPKVLQTLLGEPMLRFVYRaLRPLFGDNVW-TVVGHRADMVRAAFPD 68
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 1-37 8.42e-06

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: 45.18  E-value: 8.42e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1036601530   1 MKAVILCGGKGTRMSEvtndiPKPLAMIGGKPILWHI 37
Cdd:COG0746     5 ITGVILAGGRSRRMGQ-----DKALLPLGGRPLLERV 36
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-62 1.47e-05

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 45.40  E-value: 1.47e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1036601530   1 MKAVILCGGKGTRMsevTNDIPKPLAMIGGKPILWHIMKIYQYYGVNEFILLLGYKGEKIKE 62
Cdd:PRK09451    6 MSVVILAAGKGTRM---YSDLPKVLHTLAGKPMVQHVIDAANELGAQHVHLVYGHGGDLLKQ 64
mobA PRK00317
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
 1-38 2.19e-05

molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed


Pssm-ID: 234725 [Multi-domain]  Cd Length: 193  Bit Score: 44.02  E-value: 2.19e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1036601530   1 MKAVILCGGKGTRMSEVtndiPKPLAMIGGKPILWHIM 38
Cdd:PRK00317    4 ITGVILAGGRSRRMGGV----DKGLQELNGKPLIQHVI 37
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 6-37 2.89e-05

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


Pssm-ID: 441867 [Multi-domain]  Cd Length: 185  Bit Score: 43.34  E-value: 2.89e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1036601530   6 LCGGKGTRMsevtNDIPKPLAMIGGKPILWHI 37
Cdd:COG2266     1 MAGGKGTRL----GGGEKPLLEICGKPMIDRV 28
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-150 2.99e-05

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 44.53  E-value: 2.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530   1 MKAV-ILCGGKGTRMsevTNDIPKPLAMIGGKPILWHIMKIYQYYGVNEFILLLGYKGEKIKEyfldyEWKHNSltldss 79
Cdd:PRK14360    1 MLAVaILAAGKGTRM---KSSLPKVLHPLGGKSLVERVLDSCEELKPDRRLVIVGHQAEEVEQ-----SLAHLP------ 66

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1036601530  80 tgevqmlgqpetwKITFLETGEDTLTAGRILQ----AKDYIGDetFLLTYGDG--LANINLFHLISFHQAKGAAATV 150
Cdd:PRK14360   67 -------------GLEFVEQQPQLGTGHAVQQllpvLKGFEGD--LLVLNGDVplLRPETLEALLNTHRSSNADVTL 128
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 3-68 3.07e-05

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: 43.32  E-value: 3.07e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1036601530   3 AVILCGGKGTRMSEvtndiPKPLAMIGGKPILWHIMKIYQYYGVNEFILLLGYKGEKIKEYFLDYE 68
Cdd:cd04182     3 AIILAAGRSSRMGG-----NKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALAGLP 63
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
 3-150 3.09e-04

ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ADP-glucose pyrophosphorylase (glucose-1-phosphate adenylyltransferase) catalyzes a very important step in the biosynthesis of alpha 1,4-glucans (glycogen or starch) in bacteria and plants: synthesis of the activated glucosyl donor, ADP-glucose, from glucose-1-phosphate and ATP. ADP-glucose pyrophosphorylase is a tetrameric allosterically regulated enzyme. While a homotetramer in bacteria, in plant chloroplasts and amyloplasts, it is a heterotetramer of two different, yet evolutionary related, subunits. There are a number of conserved regions in the sequence of bacterial and plant ADP-glucose pyrophosphorylase subunits. It is a subfamily of a very diverse glycosy transferase family 2.


Pssm-ID: 133002 [Multi-domain]  Cd Length: 200  Bit Score: 40.60  E-value: 3.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530   3 AVILCGGKGTRMSEVTNDIPKPLAMIGGKPILW----------HIMKI-----YQYYGVNEFIlllgYKGekikeyfldY 67
Cdd:cd02508     1 AIILAGGEGTRLSPLTKKRAKPAVPFGGRYRLIdfplsnmvnsGIRNVgvltqYKSRSLNDHL----GSG---------K 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530  68 EWkhnslTLDSSTGEVQML----GQPETWKitfletgedTLTAGRILQAKDYIGD---ETFLLTYGDGLANINLFHLISF 140
Cdd:cd02508    68 EW-----DLDRKNGGLFILppqqRKGGDWY---------RGTADAIYQNLDYIERsdpEYVLILSGDHIYNMDYREMLDF 133

                         170
                  ....*....|
gi 1036601530 141 HQAKGAAATV 150
Cdd:cd02508   134 HIESGADITV 143
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-39 3.13e-04

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 41.39  E-value: 3.13e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1036601530   3 AVILCGGKGTRMSevtNDIPKPLAMIGGKPILWHIMK 39
Cdd:PRK14353    8 AIILAAGEGTRMK---SSLPKVLHPVAGRPMLAHVLA 41
PRK14489 PRK14489
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; ...
 3-39 6.56e-04

putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; Provisional


Pssm-ID: 237727 [Multi-domain]  Cd Length: 366  Bit Score: 40.51  E-value: 6.56e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1036601530   3 AVILCGGKGTRMsevtNDIPKPLAMIGGKPILWHIMK 39
Cdd:PRK14489    8 GVILAGGLSRRM----NGRDKALILLGGKPLIERVVD 40
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
 3-31 7.20e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 40.21  E-value: 7.20e-04
                          10        20
                  ....*....|....*....|....*....
gi 1036601530   3 AVILCGGKGTRMSEVTNDIPKPLAMIGGK 31
Cdd:PRK00725   18 ALILAGGRGSRLKELTDKRAKPAVYFGGK 46
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 1-31 1.28e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 39.47  E-value: 1.28e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1036601530   1 MKAVILCGGKGTRMSEVTNDIPKPLAMIGGK 31
Cdd:PRK05293    4 MLAMILAGGQGTRLGKLTKNIAKPAVPFGGK 34
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
 4-151 2.11e-03

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


Pssm-ID: 133026 [Multi-domain]  Cd Length: 231  Bit Score: 38.39  E-value: 2.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036601530   4 VILCGGKGTRMSEVTNDIPKPLAMIGGKPILWHIMKIYQYYGVNEFILLlgYKGEKIKEYFLDYEWK---HNS--LTLDS 78
Cdd:cd04183     2 IIPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEWVIESLAKIFDSRFIFI--CRDEHNTKFHLDESLKllaPNAtvVELDG 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1036601530  79 STgevqmLGQPETwkitfletgedtltagrILQAKDYI-GDETFLLTYGDGLANINLF-HLISFHQAKGAAATVT 151
Cdd:cd04183    80 ET-----LGAACT-----------------VLLAADLIdNDDPLLIFNCDQIVESDLLaFLAAFRERDLDGGVLT 132
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
2-64 2.98e-03

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 38.35  E-value: 2.98e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1036601530   2 KAVILCGGKGTRMSEVTNDIPKPLAMIGGKPILWHIMKIYQYYGVNEFILLLGYKGEKIKEYF 64
Cdd:PRK13389   10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHF 72
TIGR00454 TIGR00454
TIGR00454 family protein; At this time this gene appears to be present only in Archea ...
 3-63 3.45e-03

TIGR00454 family protein; At this time this gene appears to be present only in Archea [Hypothetical proteins, Conserved]


Pssm-ID: 200016  Cd Length: 175  Bit Score: 37.20  E-value: 3.45e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1036601530   3 AVILCGGKGTRMSEVTndipKPLAMIGGKPILWHIMKIYQYYGVNEFILLLGYKGEKIKEY 63
Cdd:TIGR00454   2 ALIMAGGKGTRLGGVE----KPLIEVCGRCLIDHVLSPLLKSKVNNIIIATSPHTPKTEEY 58
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 138-175 6.71e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 37.50  E-value: 6.71e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1036601530 138 ISFHQAKGAAATVTGI----DKVSQFGTLTV-EDGMAKTFSEK 175
Cdd:PRK00844  137 VDFHIESGAGVTVAAIrvprEEASAFGVIEVdPDGRIRGFLEK 179
 
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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