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Conserved domains on  [gi|785769739|gb|AJZ75657|]
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mannose-1-phosphate guanyltransferase [Candidatus Nitrosotenuis cloacae]

Protein Classification

nucleotidyltransferase family protein( domain architecture ID 10135418)

nucleotidyltransferase family protein such as mucleotidyltransferases which transfer nucleotides onto phosphosugars, or nucleoside-diphosphate-sugar pyrophosphorylases

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
3-214 1.38e-48

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: 158.90  E-value: 1.38e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739   3 AVILAGGKGTRAKPFTDYFPKAMIPVDGKPLIAYTIQHLLSFDfISEITIVCDLKgfGGQIKNYFAES----KKIKFV-Q 77
Cdd:cd04181    1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAG-IDEIILVVGYL--GEQIEEYFGDGskfgVNIEYVvQ 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739  78 DSSSGTAGDLMHLK-IAKNEPFFLWFADNLCALDLRKMLKHYTNKNSLACIATRQF-RKEETGFAQVKD-GVVSQFIEKP 154
Cdd:cd04181   78 EEPLGTAGAVRNAEdFLGDDDFLVVNGDVLTDLDLSELLRFHREKGADATIAVKEVeDPSRYGVVELDDdGRVTRFVEKP 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739 155 LIKMEDCECTGIYVLSGKILDVIRSKAKKNLNLSYDILQELSKKDLVSSFDIgKTPWVDV 214
Cdd:cd04181  158 TLPESNLANAGIYIFEPEILDYIPEILPRGEDELTDAIPLLIEEGKVYGYPV-DGYWLDI 216
 
Name Accession Description Interval E-value
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
3-214 1.38e-48

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: 158.90  E-value: 1.38e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739   3 AVILAGGKGTRAKPFTDYFPKAMIPVDGKPLIAYTIQHLLSFDfISEITIVCDLKgfGGQIKNYFAES----KKIKFV-Q 77
Cdd:cd04181    1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAG-IDEIILVVGYL--GEQIEEYFGDGskfgVNIEYVvQ 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739  78 DSSSGTAGDLMHLK-IAKNEPFFLWFADNLCALDLRKMLKHYTNKNSLACIATRQF-RKEETGFAQVKD-GVVSQFIEKP 154
Cdd:cd04181   78 EEPLGTAGAVRNAEdFLGDDDFLVVNGDVLTDLDLSELLRFHREKGADATIAVKEVeDPSRYGVVELDDdGRVTRFVEKP 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739 155 LIKMEDCECTGIYVLSGKILDVIRSKAKKNLNLSYDILQELSKKDLVSSFDIgKTPWVDV 214
Cdd:cd04181  158 TLPESNLANAGIYIFEPEILDYIPEILPRGEDELTDAIPLLIEEGKVYGYPV-DGYWLDI 216
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
2-218 5.06e-48

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: 158.01  E-value: 5.06e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739   2 KAVILAGGKGTRAKPFTDYFPKAMIPVDGKPLIAYTIQHLLSFDfISEITIVCdlkG-FGGQIKNYFAESK----KIKFV 76
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAG-ITEIVINV---GyLAEQIEEYFGDGSrfgvRITYV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739  77 -QDSSSGTAGDLMH-LKIAKNEPFFLWFADNLCALDLRKMLKHYTNKNSLACIATRQF-RKEETGFAQV-KDGVVSQFIE 152
Cdd:COG1208   77 dEGEPLGTGGALKRaLPLLGDEPFLVLNGDILTDLDLAALLAFHREKGADATLALVPVpDPSRYGVVELdGDGRVTRFVE 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 785769739 153 KPLIKMEDCECTGIYVLSGKILDVIRSKAKKNLNlsyDILQELSKKDLVSSFDIgKTPWVDVESPA 218
Cdd:COG1208  157 KPEEPPSNLINAGIYVLEPEIFDYIPEGEPFDLE---DLLPRLIAEGRVYGYVH-DGYWLDIGTPE 218
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
2-214 5.42e-21

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: 88.08  E-value: 5.42e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739    2 KAVILAGGKGTRAKPFTDYFPKAMIPV-DGKPLIAYTIQHLLSFDfISEITIVC---------DLKGFGGQIKNyfaesk 71
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVgGKYPLIDYPLSRLANAG-IREIIVILtqehrfmlnELLGDGSKFGV------ 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739   72 KIKF-VQDSSSGTAGD--LMHLKIAKNEPFFLWFADN-LCALDLRKMLKHYTNKNSLA---CIATRqfRKEETGFAQVK- 143
Cdd:pfam00483  74 QITYaLQPEGKGTAPAvaLAADFLGDEKSDVLVLGGDhIYRMDLEQAVKFHIEKAADAtvtFGIVP--VEPPTGYGVVEf 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 785769739  144 --DGVVSQFIEKPLI-KMEDCECTGIYVLSGKILDvIRSKAKKNLN----LSYDILQE-LSKKDLVSSFDIGKTPWVDV 214
Cdd:pfam00483 152 ddNGRVIRFVEKPKLpKASNYASMGIYIFNSGVLD-FLAKYLEELKrgedEITDILPKaLEDGKLAYAFIFKGYAWLDV 229
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
3-79 2.77e-13

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 66.70  E-value: 2.77e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739   3 AVILAGGKGTRAKpfTDyFPKAMIPVDGKPLIAYTIQHLLSFDFISEITIVCDLKGFGGQIKNYFAESKKIKFV------ 76
Cdd:PRK00155   6 AIIPAAGKGSRMG--AD-RPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDRPDFAELLLAKDPKVTVVaggaer 82

                 ...
gi 785769739  77 QDS 79
Cdd:PRK00155  83 QDS 85
 
Name Accession Description Interval E-value
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
3-214 1.38e-48

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: 158.90  E-value: 1.38e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739   3 AVILAGGKGTRAKPFTDYFPKAMIPVDGKPLIAYTIQHLLSFDfISEITIVCDLKgfGGQIKNYFAES----KKIKFV-Q 77
Cdd:cd04181    1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAG-IDEIILVVGYL--GEQIEEYFGDGskfgVNIEYVvQ 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739  78 DSSSGTAGDLMHLK-IAKNEPFFLWFADNLCALDLRKMLKHYTNKNSLACIATRQF-RKEETGFAQVKD-GVVSQFIEKP 154
Cdd:cd04181   78 EEPLGTAGAVRNAEdFLGDDDFLVVNGDVLTDLDLSELLRFHREKGADATIAVKEVeDPSRYGVVELDDdGRVTRFVEKP 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739 155 LIKMEDCECTGIYVLSGKILDVIRSKAKKNLNLSYDILQELSKKDLVSSFDIgKTPWVDV 214
Cdd:cd04181  158 TLPESNLANAGIYIFEPEILDYIPEILPRGEDELTDAIPLLIEEGKVYGYPV-DGYWLDI 216
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
2-218 5.06e-48

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: 158.01  E-value: 5.06e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739   2 KAVILAGGKGTRAKPFTDYFPKAMIPVDGKPLIAYTIQHLLSFDfISEITIVCdlkG-FGGQIKNYFAESK----KIKFV 76
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAG-ITEIVINV---GyLAEQIEEYFGDGSrfgvRITYV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739  77 -QDSSSGTAGDLMH-LKIAKNEPFFLWFADNLCALDLRKMLKHYTNKNSLACIATRQF-RKEETGFAQV-KDGVVSQFIE 152
Cdd:COG1208   77 dEGEPLGTGGALKRaLPLLGDEPFLVLNGDILTDLDLAALLAFHREKGADATLALVPVpDPSRYGVVELdGDGRVTRFVE 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 785769739 153 KPLIKMEDCECTGIYVLSGKILDVIRSKAKKNLNlsyDILQELSKKDLVSSFDIgKTPWVDVESPA 218
Cdd:COG1208  157 KPEEPPSNLINAGIYVLEPEIFDYIPEGEPFDLE---DLLPRLIAEGRVYGYVH-DGYWLDIGTPE 218
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
3-222 3.90e-30

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: 111.45  E-value: 3.90e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739   3 AVILAGGKGTRAKPFTDYFPKAMIPVDGKPLIAYTIQHLLSFDFiSEITIVCDLKgfGGQIKNYFAESKK----IKFVQ- 77
Cdd:cd06426    1 VVIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGF-RNFYISVNYL--AEMIEDYFGDGSKfgvnISYVRe 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739  78 DSSSGTAGDLMHLKIAKNEPFFLWFADNLCALDLRKMLKHYTNKNSLACIATRQFRKE-ETGFAQVKDGVVSQFIEKP-- 154
Cdd:cd06426   78 DKPLGTAGALSLLPEKPTDPFLVMNGDILTNLNYEHLLDFHKENNADATVCVREYEVQvPYGVVETEGGRITSIEEKPth 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 785769739 155 --LIKmedcecTGIYVLSGKILDVIRSkakknlNLSYD----ILQELSKKDLVSSFDIGKTpWVDVESPAVLER 222
Cdd:cd06426  158 sfLVN------AGIYVLEPEVLDLIPK------NEFFDmpdlIEKLIKEGKKVGVFPIHEY-WLDIGRPEDYEK 218
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
1-179 1.61e-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: 107.65  E-value: 1.61e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739   1 MKAVILAGGKGTRAKPFTDYFPKAMIPVDGKPLIAYTIQHLLSFDfISEITIVCDlkGFGGQIKNYFAESK----KIKFV 76
Cdd:cd04189    1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAG-IEDIGIVVG--PTGEEIKEALGDGSrfgvRITYI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739  77 -QDSSSGTAgdlmH-LKIAK----NEPFFLWFADNLCALDLRKMLKHYTNKNSLACIAT------RQFrkeetGFAQVKD 144
Cdd:cd04189   78 lQEEPLGLA----HaVLAARdflgDEPFVVYLGDNLIQEGISPLVRDFLEEDADASILLaevedpRRF-----GVAVVDD 148
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 785769739 145 GVVSQFIEKPLIKMEDCECTGIYVLSGKILDVIRS 179
Cdd:cd04189  149 GRIVRLVEKPKEPPSNLALVGVYAFTPAIFDAISR 183
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
2-222 4.16e-27

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 103.78  E-value: 4.16e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739   2 KAVILAGGKGTRAKPFTDYFPKAMIPVDGKPLIAYTIQHLLSFDfISEITIVCdlkGF-GGQIKNYFAESK-KIKFVQDS 79
Cdd:COG1213    1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAG-IKDIVVVT---GYkAELIEEALARPGpDVTFVYNP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739  80 SSGTAGDLMHLKIAK---NEPFFLWFADNLC-ALDLRKMLKHytNKNSLACIATRQFRK--EETGFAQVKDGVVSQFIEK 153
Cdd:COG1213   77 DYDETNNIYSLWLARealDEDFLLLNGDVVFdPAILKRLLAS--DGDIVLLVDRKWEKPldEEVKVRVDEDGRIVEIGKK 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 785769739 154 PLIKMEDCECTGIYVLSGKILDVIRS-----KAKKNLNLSY-DILQELSKKDL-VSSFDIGKTPWVDVESPAVLER 222
Cdd:COG1213  155 LPPEEADGEYIGIFKFSAEGAAALREalealIDEGGPNLYYeDALQELIDEGGpVKAVDIGGLPWVEIDTPEDLER 230
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
3-222 1.91e-26

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: 101.93  E-value: 1.91e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739   3 AVILAGGKGTRAKPFTDYFPKAMIPVDGKPLIAYTIQHLLSFDfISEITIVCdlkGFGG-QIKNYFAESKKIKFV---QD 78
Cdd:cd02523    1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAG-IDDIVIVT---GYKKeQIEELLKKYPNIKFVynpDY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739  79 SSSGTAGDLMHLKIAKNEPFFLWFADNLCALDLRKMLKHYTNKNSLACIATRQFRKEETGFAQVKDGVVSQFIEKPLIKM 158
Cdd:cd02523   77 AETNNIYSLYLARDFLDEDFLLLEGDVVFDPSILERLLSSPADNAILVDKKTKEWEDEYVKDLDDAGVLLGIISKAKNLE 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 785769739 159 E-DCECTGIYVLSGKILDVIRSKAKK-----NLNLSY-DILQELSKKDLVSSFDIGKTPWVDVESPAVLER 222
Cdd:cd02523  157 EiQGEYVGISKFSPEDADRLAEALEElieagRVNLYYeDALQRLISEEGVKVKDISDGFWYEIDDLEDLER 227
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
3-222 6.79e-22

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: 89.92  E-value: 6.79e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739   3 AVILAGGKGTRAKPFTDYFPKAMIPVDGKPLIAYTIQHLLSFDFiSEITIvcdLKGFGG-QIKNYFAESK----KIKFV- 76
Cdd:cd06915    1 AVILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGI-SRIVL---SVGYLAeQIEEYFGDGYrggiRIYYVi 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739  77 QDSSSGTAGDLMH-LKIAKNEPFFLWFADNLCALDLRKMLKHYTNKNSLACIA-TRQFRKEETGFAQV-KDGVVSQFIEK 153
Cdd:cd06915   77 EPEPLGTGGAIKNaLPKLPEDQFLVLNGDTYFDVDLLALLAALRASGADATMAlRRVPDASRYGNVTVdGDGRVIAFVEK 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 785769739 154 PLIKMEDCECTGIYVLSGKILDVIrskAKKNLNLSYDILQELSKKDLVSSFdIGKTPWVDVESPAVLER 222
Cdd:cd06915  157 GPGAAPGLINGGVYLLRKEILAEI---PADAFSLEADVLPALVKRGRLYGF-EVDGYFIDIGIPEDYAR 221
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
2-214 5.42e-21

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: 88.08  E-value: 5.42e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739    2 KAVILAGGKGTRAKPFTDYFPKAMIPV-DGKPLIAYTIQHLLSFDfISEITIVC---------DLKGFGGQIKNyfaesk 71
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVgGKYPLIDYPLSRLANAG-IREIIVILtqehrfmlnELLGDGSKFGV------ 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739   72 KIKF-VQDSSSGTAGD--LMHLKIAKNEPFFLWFADN-LCALDLRKMLKHYTNKNSLA---CIATRqfRKEETGFAQVK- 143
Cdd:pfam00483  74 QITYaLQPEGKGTAPAvaLAADFLGDEKSDVLVLGGDhIYRMDLEQAVKFHIEKAADAtvtFGIVP--VEPPTGYGVVEf 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 785769739  144 --DGVVSQFIEKPLI-KMEDCECTGIYVLSGKILDvIRSKAKKNLN----LSYDILQE-LSKKDLVSSFDIGKTPWVDV 214
Cdd:pfam00483 152 ddNGRVIRFVEKPKLpKASNYASMGIYIFNSGVLD-FLAKYLEELKrgedEITDILPKaLEDGKLAYAFIFKGYAWLDV 229
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
2-222 3.30e-19

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: 82.62  E-value: 3.30e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739   2 KAVILAGGKGTRAKPFTDYFPKAMIPVDGKPLIAYTIQHLLSfdfiSEIT-IVCDLKGFGGQIKNYFAESKK---IKFVQ 77
Cdd:cd06422    1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAA----AGIRrIVVNTHHLADQIEAHLGDSRFglrITISD 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739  78 DSSS--GTAGDLMH-LKIAKNEPFFLWFADNLCALDLRKMLKHYTNK--NSLACIAT-RQFRKEETG-FAQVKDGVVSQF 150
Cdd:cd06422   77 EPDEllETGGGIKKaLPLLGDEPFLVVNGDILWDGDLAPLLLLHAWRmdALLLLLPLvRNPGHNGVGdFSLDADGRLRRG 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 785769739 151 IEKPLIKmedCECTGIYVLSGKILDVIRSKaKKNLNLSYDILQElsKKDLVSSFDIGKtpWVDVESPAVLER 222
Cdd:cd06422  157 GGGAVAP---FTFTGIQILSPELFAGIPPG-KFSLNPLWDRAIA--AGRLFGLVYDGL--WFDVGTPERLLA 220
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-179 1.04e-18

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 82.45  E-value: 1.04e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739   1 MKAVILAGGKGTRAKPFTDYFPKAMIPVDGKPLIAYTIQHLLSFDfISEITIVCDLKgFGGQIKNYFAESKK--IKF--- 75
Cdd:COG1209    1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAG-IREILIISTPE-DGPQFERLLGDGSQlgIKIsya 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739  76 VQDSSSGTAgdlmH-LKIAK----NEPFFLWFADNLC-ALDLRKMLKHYTNKNSLACIatrqfrkeetgFA-QVKD---- 144
Cdd:COG1209   79 VQPEPLGLA----HaFIIAEdfigGDPVALVLGDNIFyGDGLSELLREAAARESGATI-----------FGyKVEDpery 143
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 785769739 145 GVVS--------QFIEKPLIKMEDCECTGIYVLSGKILDVIRS 179
Cdd:COG1209  144 GVVEfdedgrvvSLEEKPKEPKSNLAVTGLYFYDNDVVEIAKN 186
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
3-184 5.69e-18

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: 79.99  E-value: 5.69e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739   3 AVILAGG--KGTRAKPFTDYFPKAMIPVDGKPLIAYTIQHLLSFDFISEITIVC-----DLKGFGGQIKNYFAESkkIKF 75
Cdd:cd06428    1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKVPDLKEVLLIGfypesVFSDFISDAQQEFNVP--IRY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739  76 VQ-DSSSGTAGDLMHLK--IAKNEP--FFLWFADNLCALDLRKMLKHYTNKNSLACI-ATRQFRKEETGF----AQVKDG 145
Cdd:cd06428   79 LQeYKPLGTAGGLYHFRdqILAGNPsaFFVLNADVCCDFPLQELLEFHKKHGASGTIlGTEASREQASNYgcivEDPSTG 158
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 785769739 146 VVSQFIEKPLIKMEDCECTGIYVLSGKILDVIRSKAKKN 184
Cdd:cd06428  159 EVLHYVEKPETFVSDLINCGVYLFSPEIFDTIKKAFQSR 197
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
1-193 1.45e-17

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: 78.08  E-value: 1.45e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739   1 MKAVILAGGKGTRAKPFTDYFPKAMIPVDGKPLIAYTIQHLLSFDFiSEITIVCdLKGFGGQIKNYFAESKK-------- 72
Cdd:cd04198    1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGF-EDVIVVV-PEEEQAEISTYLRSFPLnlkqklde 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739  73 IKFVQDSSSGTAGDLMHLKIAKNEPFFLWFADNLCALDL-RKMLKHYTNKNSLACIATRQFRKEETGFAQVKdgvvSQFI 151
Cdd:cd04198   79 VTIVLDEDMGTADSLRHIRKKIKKDFLVLSCDLITDLPLiELVDLHRSHDASLTVLLYPPPVSSEQKGGKGK----SKKA 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 785769739 152 EKPlIKMEDCECTGIYVLSGKILDVirskaKKNLNLSYDILQ 193
Cdd:cd04198  155 DER-DVIGLDEKTQRLLFITSEEDL-----DEDLELRKSLLK 190
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
1-180 4.07e-17

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: 77.25  E-value: 4.07e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739   1 MKAVILAGGKGTRAKPFTDYFPKAMIPVDGKPLIAYTIQHLLSFDFISEITIVC----DLKGFggqIKNYfaESK---KI 73
Cdd:cd06425    1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNyrpeDMVPF---LKEY--EKKlgiKI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739  74 KF-VQDSSSGTAGDlmhLKIAKN------EPFFLWFADNLCALDLRKMLKHYTNKNSLACIATRQFrkEETGFAQV---- 142
Cdd:cd06425   76 TFsIETEPLGTAGP---LALARDllgdddEPFFVLNSDVICDFPLAELLDFHKKHGAEGTILVTKV--EDPSKYGVvvhd 150
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 785769739 143 -KDGVVSQFIEKPLIKMEDCECTGIYVLSGKILDVIRSK 180
Cdd:cd06425  151 eNTGRIERFVEKPKVFVGNKINAGIYILNPSVLDRIPLR 189
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
1-129 2.54e-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: 74.60  E-value: 2.54e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739   1 MKAVILAGGKGTRAKPFTDYFPKAMIPVDGKPLIAYTIQHLLSFDFiSEITIVCDLKgfGGQIKNYFAESKK-------- 72
Cdd:cd02507    1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGV-EEVFVVCCEH--SQAIIEHLLKSKWsslsskmi 77
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739  73 ---IKFVQDSSSGTAGDLMHLKIAKNEPFFLWFADNLCALDLRKMLKHYTNKNSLAcIAT 129
Cdd:cd02507   78 vdvITSDLCESAGDALRLRDIRGLIRSDFLLLSCDLVSNIPLSELLEERRKKDKNA-IAT 136
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
3-79 2.77e-13

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 66.70  E-value: 2.77e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739   3 AVILAGGKGTRAKpfTDyFPKAMIPVDGKPLIAYTIQHLLSFDFISEITIVCDLKGFGGQIKNYFAESKKIKFV------ 76
Cdd:PRK00155   6 AIIPAAGKGSRMG--AD-RPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDRPDFAELLLAKDPKVTVVaggaer 82

                 ...
gi 785769739  77 QDS 79
Cdd:PRK00155  83 QDS 85
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
3-79 4.83e-12

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: 62.93  E-value: 4.83e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739   3 AVILAGGKGTRAKPFTdyfPKAMIPVDGKPLIAYTIQHLLSFDFISEITIVC--DLKGFGGQIKNYFAeSKKIKFV---- 76
Cdd:cd02516    3 AIILAAGSGSRMGADI---PKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVppDDIDLAKELAKYGL-SKVVKIVegga 78

                 ....*
gi 785769739  77 --QDS 79
Cdd:cd02516   79 trQDS 83
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
3-178 1.12e-11

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: 62.59  E-value: 1.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739   3 AVILAGGKGTRAKPFTDYFPKAMIPVDGKPLIAYTIQHLLSF---DFIseitIVCDLKGFggQIKNYFA----------- 68
Cdd:cd02524    1 VVILAGGLGTRLSEETELKPKPMVEIGGRPILWHIMKIYSHYghnDFI----LCLGYKGH--VIKEYFLnyflhnsdvti 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739  69 --------------ESKKIKFVQD-SSSGTAGDLMHLK--IAKNEPFFLWFADNLCALDLRKMLKHYTNKNSLACIATRQ 131
Cdd:cd02524   75 dlgtnrielhnsdiEDWKVTLVDTgLNTMTGGRLKRVRryLGDDETFMLTYGDGVSDVNINALIEFHRSHGKLATVTAVH 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 785769739 132 frkEETGFAQVK---DGVVSQFIEKP-----LIKmedcecTGIYVLSGKILDVIR 178
Cdd:cd02524  155 ---PPGRFGELDlddDGQVTSFTEKPqgdggWIN------GGFFVLEPEVFDYID 200
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
1-178 1.49e-11

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: 62.16  E-value: 1.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739   1 MKAVILAGGKGTRAKPFTDYFPKAMIPVDGKPLIAYTIQHLLSFDfISEITIVCdlkGFGGQ-IKNYF------------ 67
Cdd:cd02541    1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAG-IEDIIIVT---GRGKRaIEDHFdrsyeleetlek 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739  68 -------------AESKKIKFV-QDSSSGTaGD--LMHLKIAKNEPFFLWFADNLCALD---LRKMLKHYtNKNSLACIA 128
Cdd:cd02541   77 kgktdlleevriiSDLANIHYVrQKEPLGL-GHavLCAKPFIGDEPFAVLLGDDLIDSKepcLKQLIEAY-EKTGASVIA 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 785769739 129 TRQFRKEET---GFAQVKDGV-----VSQFIEKPliKMEDC----ECTGIYVLSGKILDVIR 178
Cdd:cd02541  155 VEEVPPEDVskyGIVKGEKIDgdvfkVKGLVEKP--KPEEApsnlAIVGRYVLTPDIFDILE 214
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
4-79 3.05e-11

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: 60.91  E-value: 3.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739   4 VILAGGKGTRAKPFTdyfPKAMIPVDGKPLIAYTIQHLLSFDFISEITIVC---DLKGFGGQIKNYFAeSKKIKFV---- 76
Cdd:COG1211    1 IIPAAGSGSRMGAGI---PKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVppdDIEYFEELLAKYGI-DKPVRVVagga 76

                 ....*
gi 785769739  77 --QDS 79
Cdd:COG1211   77 trQDS 81
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
3-118 3.93e-10

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: 57.62  E-value: 3.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739   3 AVILAGGKGTRAKPFTDYFPKAMIPVDGKPLIAYTIqHLLSFDFISEITIVCDLKgfGGQIKNYFAESKK---------I 73
Cdd:cd04197    3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTL-EFLALNGVEEVFVFCCSH--SDQIKEYIEKSKWskpksslmiV 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 785769739  74 KFVQDSSSGTAGDLMHLKIAK---NEPFFLWFADNLCALDLRKMLKHY 118
Cdd:cd04197   80 IIIMSEDCRSLGDALRDLDAKgliRGDFILVSGDVVSNIDLKEILEEH 127
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
3-133 2.04e-09

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


Pssm-ID: 463715 [Multi-domain]  Cd Length: 159  Bit Score: 54.51  E-value: 2.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739    3 AVILAGGKGTRakpftdyF--PKAMIPVDGKPLIAYTIQHLLSfdFISEITIVCDlkgfGGQIKNYFAESkKIKFVQDSS 80
Cdd:pfam12804   1 AVILAGGRSSR-------MggDKALLPLGGKPLLERVLERLRP--AGDEVVVVAN----DEEVLAALAGL-GVPVVPDPD 66
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 785769739   81 SGT-------AGdLMHLKIAknEPFFLWFAD--NLCALDLRKMLKHYTNKNSLACIATRQFR 133
Cdd:pfam12804  67 PGQgplagllAA-LRAAPGA--DAVLVLACDmpFLTPELLRRLLAAAEESGADIVVPVYDGG 125
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
1-179 3.73e-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: 55.27  E-value: 3.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739   1 MKAVILAGGKGTRAKPFTDYFPKAMIPVDGKPLIAYTIQHLLSFDfISEITIVC---------DLKGFGGQIknyfaeSK 71
Cdd:cd02538    1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAG-IREILIIStpedlplfkELLGDGSDL------GI 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739  72 KIKF-VQDSSSGTAGDLMhlkIAK----NEPFFLWFADNLCA-LDLRKMLKHYTNKNSLACIATRQFRK-EETGFAQV-K 143
Cdd:cd02538   74 RITYaVQPKPGGLAQAFI---IGEefigDDPVCLILGDNIFYgQGLSPILQRAAAQKEGATVFGYEVNDpERYGVVEFdE 150
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 785769739 144 DGVVSQFIEKPLIKMEDCECTGIYVLSGKILDVIRS 179
Cdd:cd02538  151 NGRVLSIEEKPKKPKSNYAVTGLYFYDNDVFEIAKQ 186
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
3-174 1.89e-08

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: 52.90  E-value: 1.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739   3 AVILAGGKGTRAKpfTDYfPKAMIPVDGKPLIAYTIQHLLSFdFISEITIVCdlkGFGG-QIKNYFAEsKKIKFV-QDSS 80
Cdd:cd02540    1 AVILAAGKGTRMK--SDL-PKVLHPLAGKPMLEHVLDAARAL-GPDRIVVVV---GHGAeQVKKALAN-PNVEFVlQEEQ 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739  81 SGTAGDLM----HLKiAKNEPFFLWFADN--LCALDLRKMLKHYTNKNSLACIATrqFRKEE-TGFAQV---KDGVVSQF 150
Cdd:cd02540   73 LGTGHAVKqalpALK-DFEGDVLVLYGDVplITPETLQRLLEAHREAGADVTVLT--AELEDpTGYGRIirdGNGKVLRI 149
                        170       180       190
                 ....*....|....*....|....*....|...
gi 785769739 151 IEKplikmEDC--------EC-TGIYVLSGKIL 174
Cdd:cd02540  150 VEE-----KDAteeekairEVnAGIYAFDAEFL 177
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
1-206 5.54e-08

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 52.46  E-value: 5.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739   1 MKAVILAGGKGTRAKpftDYFPKAMIPVDGKPLIAYTIQhlLSFDFISEITIVCdlkGFGGQ-IKNYFAESKKIkFVQDS 79
Cdd:PRK14357   1 MRALVLAAGKGTRMK---SKIPKVLHKISGKPMINWVID--TAKKVAQKVGVVL---GHEAElVKKLLPEWVKI-FLQEE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739  80 SSGTAGDLMhlkIAKNepfFLWFADNLCAL----------DLRKMLKHYTNKNSLACIATrqFRKEE-TGFAQ-VKDGVV 147
Cdd:PRK14357  72 QLGTAHAVM---CARD---FIEPGDDLLILygdvplisenTLKRLIEEHNRKGADVTILV--ADLEDpTGYGRiIRDGGK 143
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 785769739 148 SQFIEK----PLIKMEDCECTGIYVLSGK-ILDVIRSKAKKNLNLSY---DILQELSKKDLVSSFDI 206
Cdd:PRK14357 144 YRIVEDkdapEEEKKIKEINTGIYVFSGDfLLEVLPKIKNENAKGEYyltDAVNFAEKVRVVKTEDL 210
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
2-178 1.17e-07

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


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 51.19  E-value: 1.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739   2 KAVILAGGKGTRAKPFTDYFPKAMIPVDGKPLIAYTIQHLLSFDfISEITIVCdlkGFG-GQIKNYF----------AES 70
Cdd:COG1210    5 KAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAG-IEEIIFVT---GRGkRAIEDHFdrsyeleatlEAK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739  71 KK---IKFVQDSSSGtaGDLMHL----------------KIAKNEPFFLWFADNLCALD---LRKMLKHYTNKNSlACIA 128
Cdd:COG1210   81 GKeelLEEVRSISPL--ANIHYVrqkeplglghavlcarPFVGDEPFAVLLGDDLIDSEkpcLKQMIEVYEETGG-SVIA 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 785769739 129 TRQFRKEET---GFAQVK---DGV--VSQFIEKPliKMEDCE----CTGIYVLSGKILDVIR 178
Cdd:COG1210  158 VQEVPPEEVskyGIVDGEeieGGVyrVTGLVEKP--APEEAPsnlaIVGRYILTPEIFDILE 217
mobA PRK00317
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
1-54 1.25e-07

molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed


Pssm-ID: 234725 [Multi-domain]  Cd Length: 193  Bit Score: 50.18  E-value: 1.25e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 785769739   1 MKAVILAGGKGTRakpftdyF---PKAMIPVDGKPLIAYTIQHLLSfdFISEITIVC 54
Cdd:PRK00317   4 ITGVILAGGRSRR-------MggvDKGLQELNGKPLIQHVIERLAP--QVDEIVINA 51
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
1-54 1.34e-07

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: 49.88  E-value: 1.34e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 785769739   1 MKAVILAGGKGTRAKpftdyFPKAMIPVDGKPLIAYTIQHLLSfdFISEITIVC 54
Cdd:cd02503    1 ITGVILAGGKSRRMG-----GDKALLELGGKPLLEHVLERLKP--LVDEVVISA 47
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
3-208 2.19e-07

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 50.84  E-value: 2.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739   3 AVILAGGKGTRAKPFTDYFPKAMIPVDGKpliaYTIqhllsFDFI------SEITIVC--------------------DL 56
Cdd:COG0448    4 AIILAGGRGSRLGPLTKDRAKPAVPFGGK----YRI-----IDFPlsncvnSGIRRVGvltqykshslndhigsgkpwDL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739  57 KGFGGQIKNYFAESKKIKfvQDSSSGTAGDL---MHLkIAKNEP-FFLWF-ADNLCALDLRKMLKHYTNKN---SLACIa 128
Cdd:COG0448   75 DRKRGGVFILPPYQQREG--EDWYQGTADAVyqnLDF-IERSDPdYVLILsGDHIYKMDYRQMLDFHIESGadiTVACI- 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739 129 tRQFRKEETGFAQVK---DGVVSQFIEKPLIKMEDCECTGIYVLSGKILdvirskakknlnlsYDILQELSKKdlvSSFD 205
Cdd:COG0448  151 -EVPREEASRFGVMEvdeDGRITEFEEKPKDPKSALASMGIYVFNKDVL--------------IELLEEDAPN---SSHD 212

                 ...
gi 785769739 206 IGK 208
Cdd:COG0448  213 FGK 215
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
1-54 3.36e-07

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: 49.04  E-value: 3.36e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 785769739   1 MKAVILAGGKGTRakpftdyF--PKAMIPVDGKPLIAYTIQHLLSfdFISEITIVC 54
Cdd:COG0746    5 ITGVILAGGRSRR-------MgqDKALLPLGGRPLLERVLERLRP--QVDEVVIVA 51
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
1-174 7.34e-07

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: 49.25  E-value: 7.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739   1 MKAVILAGGKGTRAKPFTdyfPKAMIPVDGKPLIAYTIQHLLSFDfISEITIVCdlkGFGG-QIKNYFAEsKKIKFV-QD 78
Cdd:COG1207    3 LAVVILAAGKGTRMKSKL---PKVLHPLAGKPMLEHVLDAARALG-PDRIVVVV---GHGAeQVRAALAD-LDVEFVlQE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739  79 SSSGTAgdlmH-LKIAknEPFFLWFADN---LCAlD--------LRKMLKHYTNKNSLACIAT----------RQFRKEe 136
Cdd:COG1207   75 EQLGTG----HaVQQA--LPALPGDDGTvlvLYG-DvpliraetLKALLAAHRAAGAAATVLTaelddptgygRIVRDE- 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 785769739 137 tgfaqvkDGVVSQFIE-KplikmeDC--------EC-TGIYVLSGKIL 174
Cdd:COG1207  147 -------DGRVLRIVEeK------DAteeqrairEInTGIYAFDAAAL 181
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
1-54 1.38e-06

GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate guanylyltransferase, also called GDP-mannose pyrophosphorylase (GDP-MP), catalyzes the formation of GDP-Mannose from mannose-1-phosphate and GTP. Mannose is a key monosaccharide for glycosylation of proteins and lipids. GDP-Mannose is the activated donor for mannosylation of various biomolecules. This enzyme is known to be bifunctional, as both mannose-6-phosphate isomerase and mannose-1-phosphate guanylyltransferase. This CD covers the N-terminal GDP-mannose-1-phosphate guanylyltransferase domain, whereas the isomerase function is located at the C-terminal half. GDP-MP is a member of the nucleotidyltransferase family of enzymes.


Pssm-ID: 133003 [Multi-domain]  Cd Length: 274  Bit Score: 47.96  E-value: 1.38e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 785769739   1 MKAVILAGGKGTRAKPF-TDYFPKAMIPV-DGKPLIAYTIQHLLSFDFISEITIVC 54
Cdd:cd02509    1 IYPVILAGGSGTRLWPLsRESYPKQFLKLfGDKSLLQQTLDRLKGLVPPDRILVVT 56
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
3-53 1.90e-06

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 46.69  E-value: 1.90e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 785769739   3 AVILAGGKGTRakpftdyF--PKAMIPVDGKPLIAYTIQHLLSFDFiSEITIV 53
Cdd:COG2068    6 AIILAAGASSR-------MgrPKLLLPLGGKPLLERAVEAALAAGL-DPVVVV 50
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
3-54 2.01e-06

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: 46.78  E-value: 2.01e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 785769739   3 AVILAGGKGTRAKPftdyfPKAMIPVDGKPLIAYTIQHLLSFDFiSEITIVC 54
Cdd:cd04182    3 AIILAAGRSSRMGG-----NKLLLPLDGKPLLRHALDAALAAGL-SRVIVVL 48
CpsB COG0836
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
1-54 3.98e-06

Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440598 [Multi-domain]  Cd Length: 347  Bit Score: 46.98  E-value: 3.98e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 785769739   1 MKAVILAGGKGTRAKPF-TDYFPKAMIPVDG-KPLIAYTIQHLLSFDFISEITIVC 54
Cdd:COG0836    3 IYPVILAGGSGTRLWPLsRESYPKQFLPLLGeKSLLQQTVERLAGLVPPENILVVT 58
ispDF PRK09382
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ...
3-77 1.41e-05

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


Pssm-ID: 236492 [Multi-domain]  Cd Length: 378  Bit Score: 45.22  E-value: 1.41e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 785769739   3 AVILAGGKGTRAKPftdYFPKAMIPVDGKPLIAYTIQHLLSFDFISEITIVCDLKGfGGQIKNYFAESKKIKFVQ 77
Cdd:PRK09382   8 LVIVAAGRSTRFSA---EVKKQWLRIGGKPLWLHVLENLSSAPAFKEIVVVIHPDD-IAYMKKALPEIKFVTLVT 78
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
2-230 1.56e-05

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 45.05  E-value: 1.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739   2 KAVILAGGKGTRAKPFTDYFPKAMIPVDGKPLIAYTIQHLLsFDFISEITIVC---DLKGFGGQIKNYFAESKKIKF-VQ 77
Cdd:PRK15480   5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLM-LAGIRDILIIStpqDTPRFQQLLGDGSQWGLNLQYkVQ 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739  78 DSSSGTA-GDLMHLKIAKNEPFFLWFADNLC-ALDLRKMLKHYTNKNSLACIATRQFRK-EETGFAQV-KDGVVSQFIEK 153
Cdd:PRK15480  84 PSPDGLAqAFIIGEEFIGGDDCALVLGDNIFyGHDLPKLMEAAVNKESGATVFAYHVNDpERYGVVEFdQNGTAISLEEK 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739 154 PLIKMEDCECTGIYVLSGKILDV---IRSKAKKNLNLSyDILQELSKKDLVSSFDIGKT-PWVDVESPAVLERKSDSIKN 229
Cdd:PRK15480 164 PLQPKSNYAVTGLYFYDNDVVEMaknLKPSARGELEIT-DINRIYMEQGRLSVAMMGRGyAWLDTGTHQSLIEASNFIAT 242

                 .
gi 785769739 230 I 230
Cdd:PRK15480 243 I 243
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
2-70 3.01e-05

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 44.13  E-value: 3.01e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 785769739   2 KAVILAGGKGTRAKPFTDYFPKAMIPVDGKPLIAYTIQHLLSFDfISEITIVCdlKGFGGQIKNYFAES 70
Cdd:PRK13389  10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAG-ITEIVLVT--HSSKNSIENHFDTS 75
PLN02728 PLN02728
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
4-55 3.29e-04

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


Pssm-ID: 215387  Cd Length: 252  Bit Score: 40.87  E-value: 3.29e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 785769739   4 VILAGGKGTRAKPftdYFPKAMIPVDGKPLIAYTIQHLLSFDFISEITIVCD 55
Cdd:PLN02728  28 ILLAGGVGKRMGA---NMPKQYLPLLGQPIALYSLYTFARMPEVKEIVVVCD 76
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
1-53 4.71e-04

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 40.64  E-value: 4.71e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 785769739   1 MKAVILAGGKGTRAKPFTDYFPKAMIPVDGKPLIAYTIQHLLSFDfISEITIV 53
Cdd:PRK10122   4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAG-IKEIVLV 55
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
3-31 7.98e-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: 39.06  E-value: 7.98e-04
                         10        20
                 ....*....|....*....|....*....
gi 785769739   3 AVILAGGKGTRAKPFTDYFPKAMIPVDGK 31
Cdd:cd02508    1 AIILAGGEGTRLSPLTKKRAKPAVPFGGR 29
IspD pfam01128
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ...
3-53 9.91e-04

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


Pssm-ID: 460075  Cd Length: 219  Bit Score: 38.97  E-value: 9.91e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 785769739    3 AVILAGGKGTRAKpfTDYfPKAMIPVDGKPLIAYTIQHLLSFDFISEITIV 53
Cdd:pfam01128   1 AVIPAAGSGKRMG--AGV-PKQFLQLLGQPLLEHTVDAFLASPVVDRIVVA 48
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
3-129 1.03e-03

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 39.81  E-value: 1.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739   3 AVILAGGKGTRAKpfTDYfPKAMIPVDGKPLIAYTIQHLLSFDfISEI-TIVcdlkGFGG-QIKNYFAEskKIKFV-QDS 79
Cdd:PRK14354   5 AIILAAGKGTRMK--SKL-PKVLHKVCGKPMVEHVVDSVKKAG-IDKIvTVV----GHGAeEVKEVLGD--RSEFAlQEE 74
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 785769739  80 SSGTAGDLM----HLK--------IAKNEPFFLwfadnlcALDLRKMLKHYTNKNSLACIAT 129
Cdd:PRK14354  75 QLGTGHAVMqaeeFLAdkegttlvICGDTPLIT-------AETLKNLIDFHEEHKAAATILT 129
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
4-175 1.19e-03

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 39.59  E-value: 1.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739   4 VILAGGKGTRAKPFTdyfPKAMIPVDGKPLIAYTIQHLLSfdfIS-EITIVC--DLKGFGGQIKNYFaesKKIKFV-QDS 79
Cdd:PRK14359   6 IILAAGKGTRMKSSL---PKVLHTICGKPMLFYILKEAFA---ISdDVHVVLhhQKERIKEAVLEYF---PGVIFHtQDL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739  80 S--SGTAGDLMHLKIaKNEPFFLWFADN--LCALDLRKMLKHYTNknslacIATRQFRKEE-TGFAQV--KDGVVSQFIE 152
Cdd:PRK14359  77 EnyPGTGGALMGIEP-KHERVLILNGDMplVEKDELEKLLENDAD------IVMSVFHLADpKGYGRVviENGQVKKIVE 149
                        170       180
                 ....*....|....*....|....*..
gi 785769739 153 -KPLIKMEDCECT---GIYVLSGKILD 175
Cdd:PRK14359 150 qKDANEEELKIKSvnaGVYLFDRKLLE 176
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
3-84 1.19e-03

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 39.46  E-value: 1.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739   3 AVILAGGKGTRAKPFTdyfPKAMIPVDGKPLIAYTIQHLLSFDfISEITIVCdlkGFGGQIKNYFAESKKIK---FVQDS 79
Cdd:PRK14353   8 AIILAAGEGTRMKSSL---PKVLHPVAGRPMLAHVLAAAASLG-PSRVAVVV---GPGAEAVAAAAAKIAPDaeiFVQKE 80

                 ....*
gi 785769739  80 SSGTA 84
Cdd:PRK14353  81 RLGTA 85
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
6-53 3.16e-03

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: 37.18  E-value: 3.16e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 785769739   6 LAGGKGTRakpFTDYFpKAMIPVDGKPLIAYTIQHLLSFDfISEITIV 53
Cdd:COG2266    1 MAGGKGTR---LGGGE-KPLLEICGKPMIDRVIDALEESC-IDKIYVA 43
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
1-38 3.60e-03

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 38.08  E-value: 3.60e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 785769739   1 MKAVILAGGKGTRAkpFTDyFPKAMIPVDGKPLIAYTI 38
Cdd:PRK09451   6 MSVVILAAGKGTRM--YSD-LPKVLHTLAGKPMVQHVI 40
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
3-36 3.88e-03

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 37.80  E-value: 3.88e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 785769739   3 AVILAGGKGTRAKpftDYFPKAMIPVDGKPLIAY 36
Cdd:PRK14355   6 AIILAAGKGTRMK---SDLVKVMHPLAGRPMVSW 36
PRK14489 PRK14489
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; ...
3-41 6.62e-03

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


Pssm-ID: 237727 [Multi-domain]  Cd Length: 366  Bit Score: 37.04  E-value: 6.62e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 785769739   3 AVILAGGKGTRakpfTDYFPKAMIPVDGKPLIAYTIQHL 41
Cdd:PRK14489   8 GVILAGGLSRR----MNGRDKALILLGGKPLIERVVDRL 42
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
4-167 6.86e-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: 36.85  E-value: 6.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739   4 VILAGGKGTRAKPFTDYFPKAMIPVDGKPLIAYTIQhLLSFDFISEITIVCDLKgfggQIKNYFAESKKIKFVQDSS--- 80
Cdd:cd04183    2 IIPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEWVIE-SLAKIFDSRFIFICRDE----HNTKFHLDESLKLLAPNATvve 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785769739  81 --SGTAGD-----LMHLKIAKNEPFFLWFADNLCALDLRKMLKHYTNKNSLACIATrqFRKEETGFAQVK---DGVVSQF 150
Cdd:cd04183   77 ldGETLGAactvlLAADLIDNDDPLLIFNCDQIVESDLLAFLAAFRERDLDGGVLT--FFSSHPRWSYVKldeNGRVIET 154
                        170
                 ....*....|....*..
gi 785769739 151 IEKplIKMEDCECTGIY 167
Cdd:cd04183  155 AEK--EPISDLATAGLY 169
 
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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