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Conserved domains on  [gi|663523550|gb|AIF13800|]
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nucleotidyl transferase [uncultured marine thaumarchaeote KM3_64_C01]

Protein Classification

NDP-sugar synthase( domain architecture ID 11440233)

NDP-sugar synthase such as mannose-1-phosphate guanyltransferase and UTP--glucose-1-phosphate uridylyltransferase, which catalyzes the formation of UDP-glucose from UTP and glucose 1-phosphate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
2-223 3.56e-75

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: 227.34  E-value: 3.56e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550   2 KAMILSGGRGKRLRPVTDTIPKPLIRINNKPLIEWKINYLKKFGIKDIIICSGYKGKKIENYISKKNNFGCNIEYSVETT 81
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRFGVRITYVDEGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550  82 PLGTAGAIKKAIKNIVDDSFIVLNGDIITNINLKKMMA---KPNSIAAI-----ELRTNYGTMKI-KNNKIIQFNEK-TD 151
Cdd:COG1208   81 PLGTGGALKRALPLLGDEPFLVLNGDILTDLDLAALLAfhrEKGADATLalvpvPDPSRYGVVELdGDGRVTRFVEKpEE 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663523550 152 VKNTWMNAGIYHLSTDITKILPTNGSIE-GIVFPKLAKKNSLNTVKFKNvLWRSIDSHKDVETCSKEMIQKKY 223
Cdd:COG1208  161 PPSNLINAGIYVLEPEIFDYIPEGEPFDlEDLLPRLIAEGRVYGYVHDG-YWLDIGTPEDLLEANALLLSGKA 232
 
Name Accession Description Interval E-value
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
2-223 3.56e-75

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: 227.34  E-value: 3.56e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550   2 KAMILSGGRGKRLRPVTDTIPKPLIRINNKPLIEWKINYLKKFGIKDIIICSGYKGKKIENYISKKNNFGCNIEYSVETT 81
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRFGVRITYVDEGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550  82 PLGTAGAIKKAIKNIVDDSFIVLNGDIITNINLKKMMA---KPNSIAAI-----ELRTNYGTMKI-KNNKIIQFNEK-TD 151
Cdd:COG1208   81 PLGTGGALKRALPLLGDEPFLVLNGDILTDLDLAALLAfhrEKGADATLalvpvPDPSRYGVVELdGDGRVTRFVEKpEE 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663523550 152 VKNTWMNAGIYHLSTDITKILPTNGSIE-GIVFPKLAKKNSLNTVKFKNvLWRSIDSHKDVETCSKEMIQKKY 223
Cdd:COG1208  161 PPSNLINAGIYVLEPEIFDYIPEGEPFDlEDLLPRLIAEGRVYGYVHDG-YWLDIGTPEDLLEANALLLSGKA 232
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
3-206 2.26e-69

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: 211.67  E-value: 2.26e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550   3 AMILSGGRGKRLRPVTDTIPKPLIRINNKPLIEWKINYLKKFGIKDIIICSGYKGKKIENYISKKNNFGCNIEYSVETTP 82
Cdd:cd04181    1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGSKFGVNIEYVVQEEP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550  83 LGTAGAIKKAIKNIVDDSFIVLNGDIITNINLKKMMA---KPNSIAAI-----ELRTNYGTMKI-KNNKIIQFNEK-TDV 152
Cdd:cd04181   81 LGTAGAVRNAEDFLGDDDFLVVNGDVLTDLDLSELLRfhrEKGADATIavkevEDPSRYGVVELdDDGRVTRFVEKpTLP 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 663523550 153 KNTWMNAGIYHLSTDITKILPTNG----SIEGIVFPKLAKKNSLNTVKFkNVLWRSID 206
Cdd:cd04181  161 ESNLANAGIYIFEPEILDYIPEILprgeDELTDAIPLLIEEGKVYGYPV-DGYWLDIG 217
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
2-210 1.08e-32

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: 118.51  E-value: 1.08e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550    2 KAMILSGGRGKRLRPVTDTIPKPLIRINNK-PLIEWKINYLKKFGIKDII-ICSGYKGKKIENYISKKNNFGCNIEYSVE 79
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIvILTQEHRFMLNELLGDGSKFGVQITYALQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550   80 TTPLGTAGAIKKAIKNIVDDS--FIVLNGDIITNINLKKMMAKPNSIAAI----------ELRTNYGTMKIKNN-KIIQF 146
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKsdVLVLGGDHIYRMDLEQAVKFHIEKAADatvtfgivpvEPPTGYGVVEFDDNgRVIRF 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663523550  147 NEK--TDVKNTWMNAGIYHLSTDITKILPTNGS--------IEGIVFPKLAKKNSLNTVKFKNVLWRSIDSHKD 210
Cdd:pfam00483 161 VEKpkLPKASNYASMGIYIFNSGVLDFLAKYLEelkrgedeITDILPKALEDGKLAYAFIFKGYAWLDVGTWDS 234
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
2-107 1.21e-24

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: 99.78  E-value: 1.21e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550    2 KAMILSGGRGKRLRPVTDTIPKPLIRINNKPLIEWKINYLKKFGIKDI-IICSGYKGKKIENYISKKNNFGCNIEYSVET 80
Cdd:TIGR01208   1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIgIVVGPVTGEEIKEIVGEGERFGAKITYIVQG 80
                          90       100
                  ....*....|....*....|....*..
gi 663523550   81 TPLGTAGAIKKAIKNIVDDSFIVLNGD 107
Cdd:TIGR01208  81 EPLGLAHAVYTARDFLGDDDFVVYLGD 107
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
2-171 5.75e-13

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 66.62  E-value: 5.75e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550   2 KAMILSGGRGKRLRPVTDTIPKPLIRINNKPLIEWKINYLKKFGIKDIIICSGYKGK-KIENYISKKNNFGCNIEYSVET 80
Cdd:PRK15480   5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTpRFQQLLGDGSQWGLNLQYKVQP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550  81 TPLGTAGAIKKAIKNI-VDDSFIVLNGDIITNINLKKMMA----KPNSIAAIELRTN----YGTMKIKNN-KIIQFNEKT 150
Cdd:PRK15480  85 SPDGLAQAFIIGEEFIgGDDCALVLGDNIFYGHDLPKLMEaavnKESGATVFAYHVNdperYGVVEFDQNgTAISLEEKP 164
                        170       180
                 ....*....|....*....|..
gi 663523550 151 -DVKNTWMNAGIYHLSTDITKI 171
Cdd:PRK15480 165 lQPKSNYAVTGLYFYDNDVVEM 186
 
Name Accession Description Interval E-value
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
2-223 3.56e-75

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: 227.34  E-value: 3.56e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550   2 KAMILSGGRGKRLRPVTDTIPKPLIRINNKPLIEWKINYLKKFGIKDIIICSGYKGKKIENYISKKNNFGCNIEYSVETT 81
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRFGVRITYVDEGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550  82 PLGTAGAIKKAIKNIVDDSFIVLNGDIITNINLKKMMA---KPNSIAAI-----ELRTNYGTMKI-KNNKIIQFNEK-TD 151
Cdd:COG1208   81 PLGTGGALKRALPLLGDEPFLVLNGDILTDLDLAALLAfhrEKGADATLalvpvPDPSRYGVVELdGDGRVTRFVEKpEE 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663523550 152 VKNTWMNAGIYHLSTDITKILPTNGSIE-GIVFPKLAKKNSLNTVKFKNvLWRSIDSHKDVETCSKEMIQKKY 223
Cdd:COG1208  161 PPSNLINAGIYVLEPEIFDYIPEGEPFDlEDLLPRLIAEGRVYGYVHDG-YWLDIGTPEDLLEANALLLSGKA 232
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
3-206 2.26e-69

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: 211.67  E-value: 2.26e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550   3 AMILSGGRGKRLRPVTDTIPKPLIRINNKPLIEWKINYLKKFGIKDIIICSGYKGKKIENYISKKNNFGCNIEYSVETTP 82
Cdd:cd04181    1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGSKFGVNIEYVVQEEP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550  83 LGTAGAIKKAIKNIVDDSFIVLNGDIITNINLKKMMA---KPNSIAAI-----ELRTNYGTMKI-KNNKIIQFNEK-TDV 152
Cdd:cd04181   81 LGTAGAVRNAEDFLGDDDFLVVNGDVLTDLDLSELLRfhrEKGADATIavkevEDPSRYGVVELdDDGRVTRFVEKpTLP 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 663523550 153 KNTWMNAGIYHLSTDITKILPTNG----SIEGIVFPKLAKKNSLNTVKFkNVLWRSID 206
Cdd:cd04181  161 ESNLANAGIYIFEPEILDYIPEILprgeDELTDAIPLLIEEGKVYGYPV-DGYWLDIG 217
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
3-192 1.91e-58

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: 183.91  E-value: 1.91e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550   3 AMILSGGRGKRLRPVTDTIPKPLIRINNKPLIEWKINYLKKFGIKDIIICSGYKGKKIENYISKKNNFGCNIEYSVETTP 82
Cdd:cd06915    1 AVILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYLAEQIEEYFGDGYRGGIRIYYVIEPEP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550  83 LGTAGAIKKAIKNIVDDSFIVLNGDIITNINLKKMMA---KPNSIAAIELRTN-----YGTMKI-KNNKIIQFNEK-TDV 152
Cdd:cd06915   81 LGTGGAIKNALPKLPEDQFLVLNGDTYFDVDLLALLAalrASGADATMALRRVpdasrYGNVTVdGDGRVIAFVEKgPGA 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 663523550 153 KNTWMNAGIYHLSTDITKILPTNG-SIEGIVFPKLAKKNSL 192
Cdd:cd06915  161 APGLINGGVYLLRKEILAEIPADAfSLEADVLPALVKRGRL 201
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
3-175 1.22e-44

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: 148.81  E-value: 1.22e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550   3 AMILSGGRGKRLRPVTDTIPKPLIRINNKPLIEWKINYLKKFGIKDIIICSGYKGKKIENYISKKNNFGCNIEYSVETTP 82
Cdd:cd06426    1 VVIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNYLAEMIEDYFGDGSKFGVNISYVREDKP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550  83 LGTAGAIKKaIKNIVDDSFIVLNGDIITNINLKKMM---AKPNSIAAIELRTN-----YGTMKIKNNKIIQFNEKTdvKN 154
Cdd:cd06426   81 LGTAGALSL-LPEKPTDPFLVMNGDILTNLNYEHLLdfhKENNADATVCVREYevqvpYGVVETEGGRITSIEEKP--TH 157
                        170       180
                 ....*....|....*....|..
gi 663523550 155 TWM-NAGIYHLSTDITKILPTN 175
Cdd:cd06426  158 SFLvNAGIYVLEPEVLDLIPKN 179
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
1-210 1.71e-43

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: 146.20  E-value: 1.71e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550   1 MKAMILSGGRGKRLRPVTDTIPKPLIRINNKPLIEWKINYLKKFGIKDIIICSGYKGKKIENYISK-KNNFGCNIEYSVE 79
Cdd:cd06425    1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYRPEDMVPFLKEyEKKLGIKITFSIE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550  80 TTPLGTAGAIKKAIKNIVDDS--FIVLNGDIITNINLKKMMA--KPNSIAAIELRTN------YGT--MKIKNNKIIQFN 147
Cdd:cd06425   81 TEPLGTAGPLALARDLLGDDDepFFVLNSDVICDFPLAELLDfhKKHGAEGTILVTKvedpskYGVvvHDENTGRIERFV 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663523550 148 EK-TDVKNTWMNAGIYHLSTDI-TKILPTNGSIEGIVFPKLAKKNSLNTVKFKNVlWRSIDSHKD 210
Cdd:cd06425  161 EKpKVFVGNKINAGIYILNPSVlDRIPLRPTSIEKEIFPKMASEGQLYAYELPGF-WMDIGQPKD 224
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
2-120 8.76e-39

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: 133.85  E-value: 8.76e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550   2 KAMILSGGRGKRLRPVTDTIPKPLIRINNKPLIEWKINYLKKFGIKDIIICSGYKGKKIENYISKKnNFGCNIEYSVE-T 80
Cdd:cd06422    1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHLGDS-RFGLRITISDEpD 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 663523550  81 TPLGTAGAIKKAIKNIVDDSFIVLNGDIITNINLKKMMAK 120
Cdd:cd06422   80 ELLETGGGIKKALPLLGDEPFLVVNGDILWDGDLAPLLLL 119
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
1-149 3.72e-36

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: 127.30  E-value: 3.72e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550   1 MKAMILSGGRGKRLRPVTDTIPKPLIRINNKPLIEWKINYLKKFGIKDIIICSGYKGKKIENYISKKNNFGCNIEYSVET 80
Cdd:cd04189    1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEALGDGSRFGVRITYILQE 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 663523550  81 TPLGTAGAIKKAIKNIVDDSFIVLNGDIITNINLKKMM-----AKPNsiAAIELR-----TNYGTMKIKNNKIIQFNEK 149
Cdd:cd04189   81 EPLGLAHAVLAARDFLGDEPFVVYLGDNLIQEGISPLVrdfleEDAD--ASILLAevedpRRFGVAVVDDGRIVRLVEK 157
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
2-210 1.08e-32

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: 118.51  E-value: 1.08e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550    2 KAMILSGGRGKRLRPVTDTIPKPLIRINNK-PLIEWKINYLKKFGIKDII-ICSGYKGKKIENYISKKNNFGCNIEYSVE 79
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIvILTQEHRFMLNELLGDGSKFGVQITYALQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550   80 TTPLGTAGAIKKAIKNIVDDS--FIVLNGDIITNINLKKMMAKPNSIAAI----------ELRTNYGTMKIKNN-KIIQF 146
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKsdVLVLGGDHIYRMDLEQAVKFHIEKAADatvtfgivpvEPPTGYGVVEFDDNgRVIRF 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663523550  147 NEK--TDVKNTWMNAGIYHLSTDITKILPTNGS--------IEGIVFPKLAKKNSLNTVKFKNVLWRSIDSHKD 210
Cdd:pfam00483 161 VEKpkLPKASNYASMGIYIFNSGVLDFLAKYLEelkrgedeITDILPKALEDGKLAYAFIFKGYAWLDVGTWDS 234
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
2-212 1.65e-29

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 109.95  E-value: 1.65e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550   2 KAMILSGGRGKRLRPVTDTIPKPLIRINNKPLIEWKINYLKKFGIKDIIICSGYKGKKIENYISKKN---NFGCNIEYsv 78
Cdd:COG1213    1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEALARPGpdvTFVYNPDY-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550  79 ETTplGTAGAIKKAiKNIVDDSFIVLNGDII--TNInLKKMMAKPNSIA-AIELRTNYGT---MKIK---NNKIIQFNEK 149
Cdd:COG1213   79 DET--NNIYSLWLA-REALDEDFLLLNGDVVfdPAI-LKRLLASDGDIVlLVDRKWEKPLdeeVKVRvdeDGRIVEIGKK 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 663523550 150 TDVKNTWMNA-GIYHLSTDITKILP-----------TNGSIEGiVFPKLAKKN-SLNTVKFKNVLWRSIDSHKDVE 212
Cdd:COG1213  155 LPPEEADGEYiGIFKFSAEGAAALRealealideggPNLYYED-ALQELIDEGgPVKAVDIGGLPWVEIDTPEDLE 229
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-172 1.97e-29

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 111.34  E-value: 1.97e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550   1 MKAMILSGGRGKRLRPVTDTIPKPLIRINNKPLIEWKINYLKKFGIKDIIICSG-YKGKKIENYISKKNNFGCNIEYSVE 79
Cdd:COG1209    1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTpEDGPQFERLLGDGSQLGIKISYAVQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550  80 TTPLGTAGAIKKAIKNIVDDSFIVLNGDiitNI----NLKKMMAKPNSI---AAIELR-----TNYGTMKI-KNNKIIQF 146
Cdd:COG1209   81 PEPLGLAHAFIIAEDFIGGDPVALVLGD---NIfygdGLSELLREAAAResgATIFGYkvedpERYGVVEFdEDGRVVSL 157
                        170       180
                 ....*....|....*....|....*..
gi 663523550 147 NEK-TDVKNTWMNAGIYHLSTDITKIL 172
Cdd:COG1209  158 EEKpKEPKSNLAVTGLYFYDNDVVEIA 184
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
3-214 2.96e-29

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: 109.24  E-value: 2.96e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550   3 AMILSGGRGKRLRPVTDTIPKPLIRINNKPLIEWKINYLKKFGIKDIIICSGYKGKKIENYISKKNNFGC--NIEYsvET 80
Cdd:cd02523    1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKKYPNIKFvyNPDY--AE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550  81 TplGTAGAIKKAiKNIVDDSFIVLNGDII--TNInLKKMMAKPNSIAAIELRTNY----GTMKIKNNKIIQFNEKTDVKN 154
Cdd:cd02523   79 T--NNIYSLYLA-RDFLDEDFLLLEGDVVfdPSI-LERLLSSPADNAILVDKKTKewedEYVKDLDDAGVLLGIISKAKN 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663523550 155 ----TWMNAGIYHLSTDITKIL-----------PTNGSIEGIvFPKLAKKNSLNTVKFKNVLWRSIDSHKDVETC 214
Cdd:cd02523  155 leeiQGEYVGISKFSPEDADRLaealeelieagRVNLYYEDA-LQRLISEEGVKVKDISDGFWYEIDDLEDLERA 228
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
1-120 8.20e-26

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: 100.02  E-value: 8.20e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550   1 MKAMILSGGRGKRLRPVTDTIPKPLIRINNKPLIEWKINYLKKFGIKDIII-CSGYKGKKIENYISKKNNFGC-----NI 74
Cdd:cd02507    1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVvCCEHSQAIIEHLLKSKWSSLSskmivDV 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 663523550  75 EYSVETTPLGTAGAIKKaIKNIVDDSFIVLNGDIITNINLKKMMAK 120
Cdd:cd02507   81 ITSDLCESAGDALRLRD-IRGLIRSDFLLLSCDLVSNIPLSELLEE 125
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
2-107 1.21e-24

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: 99.78  E-value: 1.21e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550    2 KAMILSGGRGKRLRPVTDTIPKPLIRINNKPLIEWKINYLKKFGIKDI-IICSGYKGKKIENYISKKNNFGCNIEYSVET 80
Cdd:TIGR01208   1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIgIVVGPVTGEEIKEIVGEGERFGAKITYIVQG 80
                          90       100
                  ....*....|....*....|....*..
gi 663523550   81 TPLGTAGAIKKAIKNIVDDSFIVLNGD 107
Cdd:TIGR01208  81 EPLGLAHAVYTARDFLGDDDFVVYLGD 107
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
3-210 1.78e-24

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: 97.26  E-value: 1.78e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550   3 AMILSGGRGKRLRPVTDTIPKPLIRINNKPLIeWKI-NYLKKFGIKDIIICSGYKGKKIE----NYISKKNNF-----GC 72
Cdd:cd02524    1 VVILAGGLGTRLSEETELKPKPMVEIGGRPIL-WHImKIYSHYGHNDFILCLGYKGHVIKeyflNYFLHNSDVtidlgTN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550  73 NIEYS-----------VET---TPlgTAGAIKKA---IKNivDDSFIVLNGDIITNINLKKMMA------KPNSIAAIEL 129
Cdd:cd02524   80 RIELHnsdiedwkvtlVDTglnTM--TGGRLKRVrryLGD--DETFMLTYGDGVSDVNINALIEfhrshgKLATVTAVHP 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550 130 RTNYGTMKIK-NNKIIQFNEKTDVKNTWMNAGIYHLSTDITK-ILPTNGSIEGIVFPKLAKKNSLNTVKFKNvLWRSIDS 207
Cdd:cd02524  156 PGRFGELDLDdDGQVTSFTEKPQGDGGWINGGFFVLEPEVFDyIDGDDTVFEREPLERLAKDGELMAYKHTG-FWQCMDT 234

                 ...
gi 663523550 208 HKD 210
Cdd:cd02524  235 LRD 237
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
1-118 3.01e-21

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: 87.71  E-value: 3.01e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550   1 MKAMILSGGRGKRLRPVTDTIPKPLIRINNKPLIEWKINYLKKFGIKDIII-CSGYKGKKIENYI--SKKNNFGCNIEY- 76
Cdd:cd04198    1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVvVPEEEQAEISTYLrsFPLNLKQKLDEVt 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 663523550  77 SVETTPLGTAGAIKKaIKNIVDDSFIVLNGDIITNINLKKMM 118
Cdd:cd04198   81 IVLDEDMGTADSLRH-IRKKIKKDFLVLSCDLITDLPLIELV 121
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
3-168 1.05e-17

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: 79.22  E-value: 1.05e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550   3 AMILSGG--RGKRLRPVTDTIPKPLIRINNKPLIEWKINYLKKF-GIKDIIICSGYKGKKIENYISK-KNNFGCNIEYSV 78
Cdd:cd06428    1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKVpDLKEVLLIGFYPESVFSDFISDaQQEFNVPIRYLQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550  79 ETTPLGTAGAI---KKAIKNIVDDSFIVLNGDIITNINLKKMMA----KPNS--IAAIELR----TNYGTM--KIKNNKI 143
Cdd:cd06428   81 EYKPLGTAGGLyhfRDQILAGNPSAFFVLNADVCCDFPLQELLEfhkkHGASgtILGTEASreqaSNYGCIveDPSTGEV 160
                        170       180
                 ....*....|....*....|....*..
gi 663523550 144 IQFNEK--TDVKNTwMNAGIYHLSTDI 168
Cdd:cd06428  161 LHYVEKpeTFVSDL-INCGVYLFSPEI 186
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
3-162 5.35e-17

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: 76.79  E-value: 5.35e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550   3 AMILSGGRGKRLRpvtDTIPKPLIRINNKPLIEWKINYLKKFGIKDIIICSGYKGKKIENYISKKnnfgcNIEYSVETTP 82
Cdd:cd02540    1 AVILAAGKGTRMK---SDLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVKKALANP-----NVEFVLQEEQ 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550  83 LGTAGAIKKAIKNI--VDDSFIVLNGDI--ITNINLKKMMAKPNSIAA--------IELRTNYGTMKIKNN----KIIQF 146
Cdd:cd02540   73 LGTGHAVKQALPALkdFEGDVLVLYGDVplITPETLQRLLEAHREAGAdvtvltaeLEDPTGYGRIIRDGNgkvlRIVEE 152
                        170
                 ....*....|....*...
gi 663523550 147 NEKTDV--KNTWMNAGIY 162
Cdd:cd02540  153 KDATEEekAIREVNAGIY 170
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
1-171 6.45e-16

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: 74.15  E-value: 6.45e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550   1 MKAMILSGGRGKRLRPVTDTIPKPLIRINNKPLIEWKINYLKKFGIKDIIICSGykGKKIENYIS---KKNNFGCNIEYS 77
Cdd:cd02538    1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIIST--PEDLPLFKEllgDGSDLGIRITYA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550  78 VETTPLGTAGAIKKAIKNIVDDSFIVLNGDiitNI----NLKKMMAKPNS------IAAIELR--TNYGTMKI-KNNKII 144
Cdd:cd02538   79 VQPKPGGLAQAFIIGEEFIGDDPVCLILGD---NIfygqGLSPILQRAAAqkegatVFGYEVNdpERYGVVEFdENGRVL 155
                        170       180
                 ....*....|....*....|....*...
gi 663523550 145 QFNEK-TDVKNTWMNAGIYHLSTDITKI 171
Cdd:cd02538  156 SIEEKpKKPKSNYAVTGLYFYDNDVFEI 183
LicC COG4750
CTP:phosphocholine cytidylyltransferase LicC [Cell wall/membrane/envelope biogenesis, Lipid ...
1-77 4.52e-15

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


Pssm-ID: 443784 [Multi-domain]  Cd Length: 228  Bit Score: 71.40  E-value: 4.52e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 663523550   1 MKAMILSGGRGKRLRPVTDTIPKPLIRINNKPLIEWKINYLKKFGIKDIIICSGYKGKKIENYISKknnFGCNIEYS 77
Cdd:COG4750    1 MNAIILAAGLGSRFAPITYETPKGLLKVNGEPLIERQIRQLHEAGITDITVVVGYLKEQFEYLEDK---YGVKLIYN 74
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
1-172 6.59e-15

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: 71.79  E-value: 6.59e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550   1 MKAMILSGGRGKRLRPVTDTIPKPLIRINNKPLIEWKINYLKKFGIKDIIICSGYKGKKIENY----------ISKKNNF 70
Cdd:cd02541    1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRGKRAIEDHfdrsyeleetLEKKGKT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550  71 -----------GCNIEYSVETTPLGTAGAIKKAIKNIVDDSFIVLNGDII---TNINLKKMMAKPN----SIAAI----- 127
Cdd:cd02541   81 dlleevriisdLANIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLidsKEPCLKQLIEAYEktgaSVIAVeevpp 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 663523550 128 ELRTNYGTMKIKNN-----KIIQFNEKTDVKNTWMN---AGIYHLSTDITKIL 172
Cdd:cd02541  161 EDVSKYGIVKGEKIdgdvfKVKGLVEKPKPEEAPSNlaiVGRYVLTPDIFDIL 213
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
3-117 3.90e-14

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: 68.79  E-value: 3.90e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550   3 AMILSGGRGKRLRPVTDTIPKPLIRINNKPLIEWKINYLKKFGIKDIIICSGYKGKKIENYISKKNNFGCNIEYSVETTP 82
Cdd:cd04197    3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQIKEYIEKSKWSKPKSSLMIVIII 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 663523550  83 LG----TAGAIKKAIKN--IVDDSFIVLNGDIITNINLKKM 117
Cdd:cd04197   83 MSedcrSLGDALRDLDAkgLIRGDFILVSGDVVSNIDLKEI 123
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
2-171 5.75e-13

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 66.62  E-value: 5.75e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550   2 KAMILSGGRGKRLRPVTDTIPKPLIRINNKPLIEWKINYLKKFGIKDIIICSGYKGK-KIENYISKKNNFGCNIEYSVET 80
Cdd:PRK15480   5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTpRFQQLLGDGSQWGLNLQYKVQP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550  81 TPLGTAGAIKKAIKNI-VDDSFIVLNGDIITNINLKKMMA----KPNSIAAIELRTN----YGTMKIKNN-KIIQFNEKT 150
Cdd:PRK15480  85 SPDGLAQAFIIGEEFIgGDDCALVLGDNIFYGHDLPKLMEaavnKESGATVFAYHVNdperYGVVEFDQNgTAISLEEKP 164
                        170       180
                 ....*....|....*....|..
gi 663523550 151 -DVKNTWMNAGIYHLSTDITKI 171
Cdd:PRK15480 165 lQPKSNYAVTGLYFYDNDVVEM 186
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
1-107 1.51e-10

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: 60.04  E-value: 1.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550   1 MKAMILSGGRGKRLRpvtDTIPKPLIRINNKPLIEWKINYLKKFGIKDIIICSGYKGKKIENYISkknnfGCNIEYSVET 80
Cdd:COG1207    3 LAVVILAAGKGTRMK---SKLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVRAALA-----DLDVEFVLQE 74
                         90       100
                 ....*....|....*....|....*....
gi 663523550  81 TPLGTAGAIKKAIKNI--VDDSFIVLNGD 107
Cdd:COG1207   75 EQLGTGHAVQQALPALpgDDGTVLVLYGD 103
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
1-201 3.72e-09

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 55.92  E-value: 3.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550   1 MKAMILSGGRGKRLRpvtDTIPKPLIRINNKPLIEWKINYLKKFGIKdIIICSGYKGKKIENYISKknnfgcNIEYSVET 80
Cdd:PRK14357   1 MRALVLAAGKGTRMK---SKIPKVLHKISGKPMINWVIDTAKKVAQK-VGVVLGHEAELVKKLLPE------WVKIFLQE 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550  81 TPLGTAGAIKKAIKNI-VDDSFIVLNGDI--ITNINLKKMMAKPNS--------IAAIELRTNYGTMkIKNNKIIQFNEK 149
Cdd:PRK14357  71 EQLGTAHAVMCARDFIePGDDLLILYGDVplISENTLKRLIEEHNRkgadvtilVADLEDPTGYGRI-IRDGGKYRIVED 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663523550 150 TDVKN-----TWMNAGIYHLSTD-----ITKILPTNGSIEGIVFPKLAKKNSLNTVKFKNVL 201
Cdd:PRK14357 150 KDAPEeekkiKEINTGIYVFSGDfllevLPKIKNENAKGEYYLTDAVNFAEKVRVVKTEDLL 211
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
5-163 8.40e-09

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: 54.18  E-value: 8.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550   5 ILSGGRGKRLRPVTDTIPKPLIRINNKPLIEWKINYLKKFGIKDII-IC-SGYKGKKIENYISKKNNFGCNIeYSVETTP 82
Cdd:cd04183    3 IPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEWVIESLAKIFDSRFIfICrDEHNTKFHLDESLKLLAPNATV-VELDGET 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550  83 LGTAGAIKKAIKNI-VDDSFIVLNGDIITNINLK---KMMAKPNSIAAI----ELRTNYGTMKI-KNNKIIQFNEKTDVK 153
Cdd:cd04183   82 LGAACTVLLAADLIdNDDPLLIFNCDQIVESDLLaflAAFRERDLDGGVltffSSHPRWSYVKLdENGRVIETAEKEPIS 161
                        170
                 ....*....|
gi 663523550 154 NtWMNAGIYH 163
Cdd:cd04183  162 D-LATAGLYY 170
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
1-168 1.18e-08

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 54.12  E-value: 1.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550   1 MKAMILSGGRGKRLRPVTDTIPKPLIRINNKPLIEWKINYLKKFGIKDIIICSGYKGKKIENYISKKNNFGCNIEYSV-- 78
Cdd:PRK10122   4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAVENHFDTSYELESLLEQRVkr 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550  79 --------------------ETTPLGTAGAIKKAIKNIVDDSFIVLNGDIITN--------INLKKMMAKPNSIAAIEL- 129
Cdd:PRK10122  84 qllaevqsicppgvtimnvrQGQPLGLGHSILCARPAIGDNPFVVVLPDVVIDdasadplrYNLAAMIARFNETGRSQVl 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 663523550 130 -------RTNYGTMKIKN--------NKIIQFNEKTDVKNTW----MNAGIYHLSTDI 168
Cdd:PRK10122 164 akrmpgdLSEYSVIQTKEpldregkvSRIVEFIEKPDQPQTLdsdlMAVGRYVLSADI 221
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
8-108 8.83e-08

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: 50.66  E-value: 8.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550   8 GGRGKRLRPVTdtipKPLIRINNKPLIEWKINYLKKFGIKDIIICSGYKGKKIENYISKKnnfgcNIEYsVETTPLGTAG 87
Cdd:COG2266    3 GGKGTRLGGGE----KPLLEICGKPMIDRVIDALEESCIDKIYVAVSPNTPKTREYLKER-----GVEV-IETPGEGYVE 72
                         90       100
                 ....*....|....*....|.
gi 663523550  88 AIKKAIKNIvDDSFIVLNGDI 108
Cdd:COG2266   73 DLNEALESI-SGPVLVVPADL 92
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
3-167 1.96e-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: 1.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550   3 AMILSGGRGKRLRPVTDTIPKP---------LIR------INNkpliewkinylkkfGIKDIIICSGYKGKKIENYI--- 64
Cdd:COG0448    4 AIILAGGRGSRLGPLTKDRAKPavpfggkyrIIDfplsncVNS--------------GIRRVGVLTQYKSHSLNDHIgsg 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550  65 -----SKKNNFgcnieysVETTP-----------LGTAGAIKKAIkNIVDDS----FIVLNGDIITNINLKKMMAKPN-- 122
Cdd:COG0448   70 kpwdlDRKRGG-------VFILPpyqqregedwyQGTADAVYQNL-DFIERSdpdyVLILSGDHIYKMDYRQMLDFHIes 141
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 663523550 123 ----SIAAIELR----TNYGTMKI-KNNKIIQFNEK-TDVKNTWMNAGIYHLSTD 167
Cdd:COG0448  142 gadiTVACIEVPreeaSRFGVMEVdEDGRITEFEEKpKDPKSALASMGIYVFNKD 196
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
2-134 2.20e-07

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


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 50.42  E-value: 2.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550   2 KAMILSGGRGKRLRPVTDTIPK---PLIrinNKPLIEWKINYLKKFGIKDIIICSGyKGKK-IENY----------ISKK 67
Cdd:COG1210    5 KAVIPVAGLGTRFLPATKAIPKemlPIV---DKPLIQYVVEEAVAAGIEEIIFVTG-RGKRaIEDHfdrsyeleatLEAK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550  68 NNF-----------GCNIEYSVETTPLGTAGAIKKAiKNIV-DDSFIVLNGDIItninlkkMMAKPNSIAA-IELRTNYG 134
Cdd:COG1210   81 GKEelleevrsispLANIHYVRQKEPLGLGHAVLCA-RPFVgDEPFAVLLGDDL-------IDSEKPCLKQmIEVYEETG 152
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
3-120 3.84e-07

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 49.83  E-value: 3.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550   3 AMILSGGRGKRLRpvtDTIPKPLIRINNKPLIEWKINYLKKFGIKDIIICSGYKGKKIENYISKKnnfgcnIEYSVETTP 82
Cdd:PRK14354   5 AIILAAGKGTRMK---SKLPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVGHGAEEVKEVLGDR------SEFALQEEQ 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 663523550  83 LGTAGAIKKAIKNI--VDDSFIVLNGD--IITNINLKKMMAK 120
Cdd:PRK14354  76 LGTGHAVMQAEEFLadKEGTTLVICGDtpLITAETLKNLIDF 117
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
2-63 5.55e-06

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 46.05  E-value: 5.55e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663523550   2 KAMILSGGRGKRLRPVTDTIPKPLIRINNKPLIEWKINYLKKFGIKDIIICSGYKGKKIENY 63
Cdd:PRK13389  10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENH 71
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
1-107 2.34e-05

bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase; Provisional


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 44.58  E-value: 2.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550   1 MKAMILSGGRGKRLRpvtDTIPKPLIRINNKPLIEWKINYLKKFGIKDIIICSGYKGKKIENYISkknnfGCNIEYSVET 80
Cdd:PRK14358   8 LDVVILAAGQGTRMK---SALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGAEQVEAALQ-----GSGVAFARQE 79
                         90       100
                 ....*....|....*....|....*....
gi 663523550  81 TPLGTAGAIKKAIKNIV--DDSFIVLNGD 107
Cdd:PRK14358  80 QQLGTGDAFLSGASALTegDADILVLYGD 108
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
1-162 2.53e-05

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: 44.10  E-value: 2.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550   1 MKAMILSGGRGKRLRPV-TDTIPKPLIRIN-NKPLIEWKINYLKKF-GIKDIIICSGykgkkiENYIS--KKNNFGCNIE 75
Cdd:cd02509    1 IYPVILAGGSGTRLWPLsRESYPKQFLKLFgDKSLLQQTLDRLKGLvPPDRILVVTN------EEYRFlvREQLPEGLPE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550  76 YSVETTPLG--TAGAI----KKAIKNIVDDSFIVLNGD-IITNIN-----LKKMM--AKPNSIAAIELR-----TNYGTM 136
Cdd:cd02509   75 ENIILEPEGrnTAPAIalaaLYLAKRDPDAVLLVLPSDhLIEDVEaflkaVKKAVeaAEEGYLVTFGIKptrpeTGYGYI 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 663523550 137 KIKN------NKIIQFNEKTDVK---------NTWMNAGIY 162
Cdd:cd02509  155 EAGEklgggvYRVKRFVEKPDLEtakeylesgNYLWNSGIF 195
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
3-120 4.07e-05

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: 42.91  E-value: 4.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550   3 AMILSGGRGKRLRPVTDTIPKPLIRINNK-PLIEWKINYLKKFGIKDIIICSGYKGKKIENYISK-KNNFGCNIEYSVET 80
Cdd:cd02508    1 AIILAGGEGTRLSPLTKKRAKPAVPFGGRyRLIDFPLSNMVNSGIRNVGVLTQYKSRSLNDHLGSgKEWDLDRKNGGLFI 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 663523550  81 TP----------LGTAGAIKKAIKNIVD---DSFIVLNGDIITNINLKKMMAK 120
Cdd:cd02508   81 LPpqqrkggdwyRGTADAIYQNLDYIERsdpEYVLILSGDHIYNMDYREMLDF 133
mobA PRK00317
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
1-51 6.44e-05

molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed


Pssm-ID: 234725 [Multi-domain]  Cd Length: 193  Bit Score: 42.48  E-value: 6.44e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 663523550   1 MKAMILSGGRGKRLrpvtDTIPKPLIRINNKPLIEWKINYLKKFgIKDIII 51
Cdd:PRK00317   4 ITGVILAGGRSRRM----GGVDKGLQELNGKPLIQHVIERLAPQ-VDEIVI 49
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
1-52 1.78e-04

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


Pssm-ID: 133000 [Multi-domain]  Cd Length: 181  Bit Score: 41.02  E-value: 1.78e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 663523550   1 MKAMILSGGRGKRLrpvtdTIPKPLIRINNKPLIEWKINYLKKFGIKDIIIC 52
Cdd:cd02503    1 ITGVILAGGKSRRM-----GGDKALLELGGKPLLEHVLERLKPLVDEVVISA 47
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
3-51 1.95e-04

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: 40.97  E-value: 1.95e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 663523550   3 AMILSGGRGKRLRPvtdTIPKPLIRINNKPLIEWKinyLKKF----GIKDIII 51
Cdd:cd02516    3 AIILAAGSGSRMGA---DIPKQFLELGGKPVLEHT---LEAFlahpAIDEIVV 49
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
3-108 3.15e-04

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


Pssm-ID: 463715 [Multi-domain]  Cd Length: 159  Bit Score: 39.87  E-value: 3.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550    3 AMILSGGRGKRLRPvtdtiPKPLIRINNKPLIEWKINYLKKFGiKDIIICSGYkgKKIENYISkknnfGCNIEYSVETTP 82
Cdd:pfam12804   1 AVILAGGRSSRMGG-----DKALLPLGGKPLLERVLERLRPAG-DEVVVVAND--EEVLAALA-----GLGVPVVPDPDP 67
                          90       100
                  ....*....|....*....|....*...
gi 663523550   83 -LGTAGAIKKAIKNIVD-DSFIVLNGDI 108
Cdd:pfam12804  68 gQGPLAGLLAALRAAPGaDAVLVLACDM 95
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
1-151 5.80e-04

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 40.40  E-value: 5.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550   1 MKAMILSGGRGKRLRpvtDTIPKPLIRINNKPLIEWKINYLKKFGIKDIIICSGYKGKKIENYISKKnnfgcNIEYSVET 80
Cdd:PRK09451   6 MSVVILAAGKGTRMY---SDLPKVLHTLAGKPMVQHVIDAANELGAQHVHLVYGHGGDLLKQTLADE-----PLNWVLQA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550  81 TPLGTAGAIKKAIKNIVDDSFI-VLNGDI--ITNINLKKMM-AKP-NSIAAIELR----TNYGTMKIKNNKIIQFNEKTD 151
Cdd:PRK09451  78 EQLGTGHAMQQAAPFFADDEDIlMLYGDVplISVETLQRLRdAKPqGGIGLLTVKldnpTGYGRITRENGKVVGIVEQKD 157
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
3-24 9.86e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 39.44  E-value: 9.86e-04
                         10        20
                 ....*....|....*....|..
gi 663523550   3 AMILSGGRGKRLRPVTDTIPKP 24
Cdd:PRK00725  18 ALILAGGRGSRLKELTDKRAKP 39
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
3-162 1.34e-03

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 39.34  E-value: 1.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550   3 AMILSGGRGKRLRpvtDTIPKPLIRINNKPLIEWKINYLKKFGIKDIIICSGYKGKKIENYISKKNnfgcNIEYSVETTP 82
Cdd:PRK14355   6 AIILAAGKGTRMK---SDLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHFAGDG----DVSFALQEEQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550  83 LGTAGAIKKAIKNI--VDDSFIVLNGDI--ITNINLKKMMAKPNSI-AAIELRT-------NYG-TMKIKNNKIIQFNEK 149
Cdd:PRK14355  79 LGTGHAVACAAPALdgFSGTVLILCGDVplLRAETLQGMLAAHRATgAAVTVLTarlenpfGYGrIVRDADGRVLRIVEE 158
                        170
                 ....*....|....*...
gi 663523550 150 TDVKN-----TWMNAGIY 162
Cdd:PRK14355 159 KDATPeersiREVNSGIY 176
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
1-36 2.51e-03

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


Pssm-ID: 440509 [Multi-domain]  Cd Length: 188  Bit Score: 37.48  E-value: 2.51e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 663523550   1 MKAMILSGGRGKRLRpvtdtIPKPLIRINNKPLIEW 36
Cdd:COG0746    5 ITGVILAGGRSRRMG-----QDKALLPLGGRPLLER 35
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
5-52 4.05e-03

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: 37.42  E-value: 4.05e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 663523550   5 ILSGGRGKRLRpvtDTIPKPLIRINNKPLIEWKINYLKKFG-IKDIIIC 52
Cdd:COG1211    2 IPAAGSGSRMG---AGIPKQFLPLGGKPVLEHTLEAFLAHPrIDEIVVV 47
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
3-51 5.15e-03

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 37.04  E-value: 5.15e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 663523550   3 AMILSGGRGKRLRPvtdTIPKPLIRINNKPLIEWKinyLKKF----GIKDIII 51
Cdd:PRK00155   6 AIIPAAGKGSRMGA---DRPKQYLPLGGKPILEHT---LEAFlahpRIDEIIV 52
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
3-107 6.34e-03

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


Pssm-ID: 133025 [Multi-domain]  Cd Length: 186  Bit Score: 36.38  E-value: 6.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663523550   3 AMILSGGRGKRLRPvtdtiPKPLIRINNKPLIEWKINYLKKFGIKDIIICSGYKGKKIENYISKKN-NFGCNIEYSvett 81
Cdd:cd04182    3 AIILAAGRSSRMGG-----NKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALAGLPvVVVINPDWE---- 73
                         90       100
                 ....*....|....*....|....*...
gi 663523550  82 pLGTAGAIKKAIKNIVDDS--FIVLNGD 107
Cdd:cd04182   74 -EGMSSSLAAGLEALPADAdaVLILLAD 100
 
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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