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Conserved domains on  [gi|831193475|gb|AKL99357|]
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mannose-1-phosphate guanylyltransferase [Burkholderia pyrrocinia]

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 ...
 7-237 6.14e-82

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: 244.68  E-value: 6.14e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831193475   7 TAMIFAAGRGERMRPLTDTRPKPLLEAGGKPLIVWQIEALARAGIETIVINHAWLGERIEAALGDGSRWGVRLAYSAEGE 86
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRFGVRITYVDEGE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831193475  87 ALETAGGIAQALPLLERDgrstVFVAVAGDVFAEFDYGTLAAPAARMSALdapaMHLVMVPNPPFHPSGDFVLGGDGRLS 166
Cdd:COG1208   81 PLGTGGALKRALPLLGDE----PFLVLNGDILTDLDLAALLAFHREKGAD----ATLALVPVPDPSRYGVVELDGDGRVT 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 831193475 167 ------LDGGDRVTFGSIGLYDTRMFRDLAPGTRRALTPYFRATIEAGRASGELYEGIWENVGTPAQLGELDARLRA 237
Cdd:COG1208  153 rfvekpEEPPSNLINAGIYVLEPEIFDYIPEGEPFDLEDLLPRLIAEGRVYGYVHDGYWLDIGTPEDLLEANALLLS 229
 
Name Accession Description Interval E-value
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 7-237 6.14e-82

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: 244.68  E-value: 6.14e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831193475   7 TAMIFAAGRGERMRPLTDTRPKPLLEAGGKPLIVWQIEALARAGIETIVINHAWLGERIEAALGDGSRWGVRLAYSAEGE 86
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRFGVRITYVDEGE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831193475  87 ALETAGGIAQALPLLERDgrstVFVAVAGDVFAEFDYGTLAAPAARMSALdapaMHLVMVPNPPFHPSGDFVLGGDGRLS 166
Cdd:COG1208   81 PLGTGGALKRALPLLGDE----PFLVLNGDILTDLDLAALLAFHREKGAD----ATLALVPVPDPSRYGVVELDGDGRVT 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 831193475 167 ------LDGGDRVTFGSIGLYDTRMFRDLAPGTRRALTPYFRATIEAGRASGELYEGIWENVGTPAQLGELDARLRA 237
Cdd:COG1208  153 rfvekpEEPPSNLINAGIYVLEPEIFDYIPEGEPFDLEDLLPRLIAEGRVYGYVHDGYWLDIGTPEDLLEANALLLS 229
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 7-231 2.65e-78

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: 234.77  E-value: 2.65e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831193475   7 TAMIFAAGRGERMRPLTDTRPKPLLEAGGKPLIVWQIEALARAGIETIVINHAWLGERIEAALGDgSRWGVRLAYSAE-G 85
Cdd:cd06422    1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHLGD-SRFGLRITISDEpD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831193475  86 EALETAGGIAQALPLLerdGRSTVFVaVAGDVFAEFDYG-TLAAPAARMSALDApamHLVMVPNPPFHPSGDFVLGGDGR 164
Cdd:cd06422   80 ELLETGGGIKKALPLL---GDEPFLV-VNGDILWDGDLApLLLLHAWRMDALLL---LLPLVRNPGHNGVGDFSLDADGR 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831193475 165 LSLDGGDRV---TFGSIGLYDTRMFRDLAPGtRRALTPYFRATIEAGRASGELYEGIWENVGTPAQLGEL 231
Cdd:cd06422  153 LRRGGGGAVapfTFTGIQILSPELFAGIPPG-KFSLNPLWDRAIAAGRLFGLVYDGLWFDVGTPERLLAA 221
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 8-233 2.74e-33

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


Pssm-ID: 274908 [Multi-domain]  Cd Length: 393  Bit Score: 123.86  E-value: 2.74e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831193475    8 AMIFAAGRGERMRPLTDTRPKPLLEAGGKPLIVWQIEALARAGIETIVINHAWLGERIEAALGDGSRWGVRLAYSAEGEA 87
Cdd:TIGR03992   3 AVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEKVREYFGDGSRGGVPIEYVVQEEQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831193475   88 LETAGGIAQALPLLerDGRstvFVAVAGDVFaeFDYGTLaapaARMSALDAPAMHLVMVPNPpfhpsGDFvlggdGRLSL 167
Cdd:TIGR03992  83 LGTADALGSAKEYV--DDE---FLVLNGDVL--LDSDLL----ERLIRAEAPAIAVVEVDDP-----SDY-----GVVET 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831193475  168 DGGdRVTF--------------GSIGLYDTRMF---RDLAPGTR--RALTPYFRATIEAGRASGELYEGIWENVGTPAQL 228
Cdd:TIGR03992 142 DGG-RVTGivekpenppsnlinAGIYLFSPEIFellEKTKLSPRgeYELTDALQLLIDEGKVKAVELDGFWLDVGRPWDL 220


                  ....*
gi 831193475  229 geLDA 233
Cdd:TIGR03992 221 --LDA 223
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 8-225 3.71e-26

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: 101.56  E-value: 3.71e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831193475    8 AMIFAAGRGERMRPLTDTRPKPLLEAGGK-PLIVWQIEALARAGI-ETIVINHAWLGERIEAALGDGSRWGVRLAYSAEG 85
Cdd:pfam00483   2 AIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIrEIIVILTQEHRFMLNELLGDGSKFGVQITYALQP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831193475   86 EALETAGGIAQALPLLERDGrSTVFVaVAGDVFAEFDYGTLAAPAArmsALDAPAMHLVMVpnPPFHPSGDFvlggdGRL 165
Cdd:pfam00483  82 EGKGTAPAVALAADFLGDEK-SDVLV-LGGDHIYRMDLEQAVKFHI---EKAADATVTFGI--VPVEPPTGY-----GVV 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831193475  166 SLDGGDRV-------------TFGSIGLY--DTRMF----RDLAPGTRRALTPY--FRATIEAGRASGEL----YEgiWE 220
Cdd:pfam00483 150 EFDDNGRVirfvekpklpkasNYASMGIYifNSGVLdflaKYLEELKRGEDEITdiLPKALEDGKLAYAFifkgYA--WL 227


                  ....*
gi 831193475  221 NVGTP 225
Cdd:pfam00483 228 DVGTW 232
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 7-116 1.97e-08

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 54.07  E-value: 1.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831193475   7 TAMIFAAGRGERMRpltDTRPKPLLEAGGKPLIVWQIEALARAGIETI--VINHAwlGERIEAALGDGSRwgvrlaYSAE 84
Cdd:PRK14354   4 YAIILAAGKGTRMK---SKLPKVLHKVCGKPMVEHVVDSVKKAGIDKIvtVVGHG--AEEVKEVLGDRSE------FALQ 72

                         90       100       110
                 ....*....|....*....|....*....|..
gi 831193475  85 GEALETAGGIAQALPLLErDGRSTVFVaVAGD 116
Cdd:PRK14354  73 EEQLGTGHAVMQAEEFLA-DKEGTTLV-ICGD 102
 
Name Accession Description Interval E-value
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 7-237 6.14e-82

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: 244.68  E-value: 6.14e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831193475   7 TAMIFAAGRGERMRPLTDTRPKPLLEAGGKPLIVWQIEALARAGIETIVINHAWLGERIEAALGDGSRWGVRLAYSAEGE 86
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRFGVRITYVDEGE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831193475  87 ALETAGGIAQALPLLERDgrstVFVAVAGDVFAEFDYGTLAAPAARMSALdapaMHLVMVPNPPFHPSGDFVLGGDGRLS 166
Cdd:COG1208   81 PLGTGGALKRALPLLGDE----PFLVLNGDILTDLDLAALLAFHREKGAD----ATLALVPVPDPSRYGVVELDGDGRVT 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 831193475 167 ------LDGGDRVTFGSIGLYDTRMFRDLAPGTRRALTPYFRATIEAGRASGELYEGIWENVGTPAQLGELDARLRA 237
Cdd:COG1208  153 rfvekpEEPPSNLINAGIYVLEPEIFDYIPEGEPFDLEDLLPRLIAEGRVYGYVHDGYWLDIGTPEDLLEANALLLS 229
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 7-231 2.65e-78

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: 234.77  E-value: 2.65e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831193475   7 TAMIFAAGRGERMRPLTDTRPKPLLEAGGKPLIVWQIEALARAGIETIVINHAWLGERIEAALGDgSRWGVRLAYSAE-G 85
Cdd:cd06422    1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHLGD-SRFGLRITISDEpD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831193475  86 EALETAGGIAQALPLLerdGRSTVFVaVAGDVFAEFDYG-TLAAPAARMSALDApamHLVMVPNPPFHPSGDFVLGGDGR 164
Cdd:cd06422   80 ELLETGGGIKKALPLL---GDEPFLV-VNGDILWDGDLApLLLLHAWRMDALLL---LLPLVRNPGHNGVGDFSLDADGR 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831193475 165 LSLDGGDRV---TFGSIGLYDTRMFRDLAPGtRRALTPYFRATIEAGRASGELYEGIWENVGTPAQLGEL 231
Cdd:cd06422  153 LRRGGGGAVapfTFTGIQILSPELFAGIPPG-KFSLNPLWDRAIAAGRLFGLVYDGLWFDVGTPERLLAA 221
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 8-223 7.82e-46

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: 151.96  E-value: 7.82e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831193475   8 AMIFAAGRGERMRPLTDTRPKPLLEAGGKPLIVWQIEALARAGIETIVINHAWLGERIEAALGDGSRWGVRLAYSAEGEA 87
Cdd:cd04181    1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGSKFGVNIEYVVQEEP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831193475  88 LETAGGIAQALPLLERDgrstVFVAVAGDVFAEFDYGTLAAPAARMSALdaPAMHLVMVPNPpfhpsGDFvlggdGRLSL 167
Cdd:cd04181   81 LGTAGAVRNAEDFLGDD----DFLVVNGDVLTDLDLSELLRFHREKGAD--ATIAVKEVEDP-----SRY-----GVVEL 144

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 831193475 168 DGGDRVT------------FGSIGLY--DTRMFRDLAPGTRRA---LTPYFRATIEAGRASGELYEGIWENVG 223
Cdd:cd04181  145 DDDGRVTrfvekptlpesnLANAGIYifEPEILDYIPEILPRGedeLTDAIPLLIEEGKVYGYPVDGYWLDIG 217
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 8-233 2.74e-33

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


Pssm-ID: 274908 [Multi-domain]  Cd Length: 393  Bit Score: 123.86  E-value: 2.74e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831193475    8 AMIFAAGRGERMRPLTDTRPKPLLEAGGKPLIVWQIEALARAGIETIVINHAWLGERIEAALGDGSRWGVRLAYSAEGEA 87
Cdd:TIGR03992   3 AVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEKVREYFGDGSRGGVPIEYVVQEEQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831193475   88 LETAGGIAQALPLLerDGRstvFVAVAGDVFaeFDYGTLaapaARMSALDAPAMHLVMVPNPpfhpsGDFvlggdGRLSL 167
Cdd:TIGR03992  83 LGTADALGSAKEYV--DDE---FLVLNGDVL--LDSDLL----ERLIRAEAPAIAVVEVDDP-----SDY-----GVVET 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831193475  168 DGGdRVTF--------------GSIGLYDTRMF---RDLAPGTR--RALTPYFRATIEAGRASGELYEGIWENVGTPAQL 228
Cdd:TIGR03992 142 DGG-RVTGivekpenppsnlinAGIYLFSPEIFellEKTKLSPRgeYELTDALQLLIDEGKVKAVELDGFWLDVGRPWDL 220


                  ....*
gi 831193475  229 geLDA 233
Cdd:TIGR03992 221 --LDA 223
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 8-174 2.63e-30

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: 111.88  E-value: 2.63e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831193475   8 AMIFAAGRGERMRPLTDTRPKPLLEAGGKPLIVWQIEALARAGIETIVINHAWLGERIEAALGDGSRWGVRLAYSAEGEA 87
Cdd:cd06915    1 AVILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYLAEQIEEYFGDGYRGGIRIYYVIEPEP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831193475  88 LETAGGIAQALPLLERDgrstVFVAVAGDVFAEFDYGTLAAPAARMSALdapaMHLVMVPNPPFhpsGDFvlggdGRLSL 167
Cdd:cd06915   81 LGTGGAIKNALPKLPED----QFLVLNGDTYFDVDLLALLAALRASGAD----ATMALRRVPDA---SRY-----GNVTV 144


                 ....*..
gi 831193475 168 DGGDRVT 174
Cdd:cd06915  145 DGDGRVI 151
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 8-126 7.94e-29

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: 107.98  E-value: 7.94e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831193475   8 AMIFAAGRGERMRPLTDTRPKPLLEAGGKPLIVWQIEALARAGIETIVINHAWLGERIEAALGDGSRWGVRLAYSAEGEA 87
Cdd:cd06426    1 VVIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNYLAEMIEDYFGDGSKFGVNISYVREDKP 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 831193475  88 LETAGgiaqALPLLERDGRSTVFVAvAGDVFAEFDYGTL 126
Cdd:cd06426   81 LGTAG----ALSLLPEKPTDPFLVM-NGDILTNLNYEHL 114
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 8-233 1.03e-27

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: 105.73  E-value: 1.03e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831193475   8 AMIFAAGRGERMRPLTDTRPKPLLEAGGKPLIVWQIEALARAGIETIVINHAWLGERIEAALGDGSRWGVRLAYSAEGEA 87
Cdd:cd04189    3 GLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEALGDGSRFGVRITYILQEEP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831193475  88 LETAGGIAQALPLLERDGrstvFVAVAGDVFAEFDYGtlaaPAARMSALDAPAMHLVM--VPNP---------------- 149
Cdd:cd04189   83 LGLAHAVLAARDFLGDEP----FVVYLGDNLIQEGIS----PLVRDFLEEDADASILLaeVEDPrrfgvavvddgrivrl 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831193475 150 ---PFHPSGDFVLggdgrlsldggdrvtfgsIGLYdtrMFRDLAPGTRRALTPYFRATIE-----------AGRASGELY 215
Cdd:cd04189  155 vekPKEPPSNLAL------------------VGVY---AFTPAIFDAISRLKPSWRGELEitdaiqwlidrGRRVGYSIV 213

                        250
                 ....*....|....*...
gi 831193475 216 EGIWENVGTPAQLgeLDA 233
Cdd:cd04189  214 TGWWKDTGTPEDL--LEA 229
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 8-225 3.71e-26

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: 101.56  E-value: 3.71e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831193475    8 AMIFAAGRGERMRPLTDTRPKPLLEAGGK-PLIVWQIEALARAGI-ETIVINHAWLGERIEAALGDGSRWGVRLAYSAEG 85
Cdd:pfam00483   2 AIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIrEIIVILTQEHRFMLNELLGDGSKFGVQITYALQP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831193475   86 EALETAGGIAQALPLLERDGrSTVFVaVAGDVFAEFDYGTLAAPAArmsALDAPAMHLVMVpnPPFHPSGDFvlggdGRL 165
Cdd:pfam00483  82 EGKGTAPAVALAADFLGDEK-SDVLV-LGGDHIYRMDLEQAVKFHI---EKAADATVTFGI--VPVEPPTGY-----GVV 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831193475  166 SLDGGDRV-------------TFGSIGLY--DTRMF----RDLAPGTRRALTPY--FRATIEAGRASGEL----YEgiWE 220
Cdd:pfam00483 150 EFDDNGRVirfvekpklpkasNYASMGIYifNSGVLdflaKYLEELKRGEDEITdiLPKALEDGKLAYAFifkgYA--WL 227


                  ....*
gi 831193475  221 NVGTP 225
Cdd:pfam00483 228 DVGTW 232
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
8-165 7.46e-22

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 90.30  E-value: 7.46e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831193475   8 AMIFAAGRGERMRPLTDTRPKPLLEAGGKPLIVWQIEALARAGIETIVINHAWLGERIEAALgDGSRWGVRLAYSAEGEA 87
Cdd:COG1213    2 AVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEAL-ARPGPDVTFVYNPDYDE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831193475  88 LETAGGIAQALPLLERDgrstvFVAVAGDVFaeFDygtlaaPAARMSALDAPAMHLVMVPNPPFHPSGD---FVLGGDGR 164
Cdd:COG1213   81 TNNIYSLWLAREALDED-----FLLLNGDVV--FD------PAILKRLLASDGDIVLLVDRKWEKPLDEevkVRVDEDGR 147


                 .
gi 831193475 165 L 165
Cdd:COG1213  148 I 148
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 8-121 1.09e-21

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: 89.58  E-value: 1.09e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831193475   8 AMIFAAGRGERMRPLTDTRPKPLLEAGGKPLIVWQIEALARAGIETIVINHAWLGERIEAALGDGS-RWGVRLAYSAEGE 86
Cdd:cd06425    3 ALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYRPEDMVPFLKEYEkKLGIKITFSIETE 82

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 831193475  87 ALETAGGIAQALPLLERDGRStvFVAVAGDVFAEF 121
Cdd:cd06425   83 PLGTAGPLALARDLLGDDDEP--FFVLNSDVICDF 115
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
8-98 6.04e-21

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 88.99  E-value: 6.04e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831193475   8 AMIFAAGRGERMRPLTDTRPKPLLEAGGKPLIVWQIEALARAGIETIVI---NHawLGERIEAALGDGSRWGVRLAYSAE 84
Cdd:COG1209    3 GIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIistPE--DGPQFERLLGDGSQLGIKISYAVQ 80

                         90
                 ....*....|....
gi 831193475  85 GEALetagGIAQAL 98
Cdd:COG1209   81 PEPL----GLAHAF 90
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 8-71 1.51e-19

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: 83.82  E-value: 1.51e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 831193475   8 AMIFAAGRGERMRPLTDTRPKPLLEAGGKPLIVWQIEALARAGIETIVINHAWLGERIEAALGD 71
Cdd:cd02523    1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKK 64
LicC COG4750
CTP:phosphocholine cytidylyltransferase LicC [Cell wall/membrane/envelope biogenesis, Lipid ...
 8-56 1.17e-13

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


Pssm-ID: 443784 [Multi-domain]  Cd Length: 228  Bit Score: 67.93  E-value: 1.17e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 831193475   8 AMIFAAGRGERMRPLTDTRPKPLLEAGGKPLIVWQIEALARAGIETIVI 56
Cdd:COG4750    3 AIILAAGLGSRFAPITYETPKGLLKVNGEPLIERQIRQLHEAGITDITV 51
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 8-103 4.79e-13

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: 66.44  E-value: 4.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831193475   8 AMIFAAGRGERMRPLTDTRPKPLLEAGGKPLIVWQIEALARAGIETIVI----NHAWLGERIeaaLGDGSRWGVRLAYSA 83
Cdd:cd02538    3 GIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIistpEDLPLFKEL---LGDGSDLGIRITYAV 79

                         90       100
                 ....*....|....*....|
gi 831193475  84 EgealETAGGIAQALPLLER 103
Cdd:cd02538   80 Q----PKPGGLAQAFIIGEE 95
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 8-56 6.68e-13

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: 65.35  E-value: 6.68e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 831193475   8 AMIFAAGRGERMRPLTDTRPKPLLEAGGKPLIVWQIEALARAGIETIVI 56
Cdd:cd02507    3 AVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFV 51
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 8-117 9.82e-12

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: 62.53  E-value: 9.82e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831193475   8 AMIFAAGRGERMRpltDTRPKPLLEAGGKPLIVWQIEALARAGIETI--VINHAwlGERIEAALGDGsrwGVRLAYSAeg 85
Cdd:cd02540    1 AVILAAGKGTRMK---SDLPKVLHPLAGKPMLEHVLDAARALGPDRIvvVVGHG--AEQVKKALANP---NVEFVLQE-- 70

                         90       100       110
                 ....*....|....*....|....*....|..
gi 831193475  86 EALETAGGIAQALPLLErDGRSTVFVaVAGDV 117
Cdd:cd02540   71 EQLGTGHAVKQALPALK-DFEGDVLV-LYGDV 100
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 6-117 1.41e-11

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: 63.51  E-value: 1.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831193475   6 TTAMIFAAGRGERMRpltDTRPKPLLEAGGKPLIVWQIEALARAGIETI--VINHAwlGERIEAALGDgsrWGVRLAYSA 83
Cdd:COG1207    3 LAVVILAAGKGTRMK---SKLPKVLHPLAGKPMLEHVLDAARALGPDRIvvVVGHG--AEQVRAALAD---LDVEFVLQE 74

                         90       100       110
                 ....*....|....*....|....*....|....
gi 831193475  84 egEALETAGGIAQALPLLERDGrSTVFVaVAGDV 117
Cdd:COG1207   75 --EQLGTGHAVQQALPALPGDD-GTVLV-LYGDV 104
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 8-56 4.87e-11

The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; N-terminal domain of gamma subunit of the eukaryotic translation initiation factor 2B (eIF-2B): eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit gamma shares sequence similarity with epsilon subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.


Pssm-ID: 133041 [Multi-domain]  Cd Length: 214  Bit Score: 60.37  E-value: 4.87e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 831193475   8 AMIFAAGRGERMRPLTDTRPKPLLEAGGKPLIVWQIEALARAGIETIVI 56
Cdd:cd04198    3 AVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIV 51
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 7-116 1.97e-08

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 54.07  E-value: 1.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831193475   7 TAMIFAAGRGERMRpltDTRPKPLLEAGGKPLIVWQIEALARAGIETI--VINHAwlGERIEAALGDGSRwgvrlaYSAE 84
Cdd:PRK14354   4 YAIILAAGKGTRMK---SKLPKVLHKVCGKPMVEHVVDSVKKAGIDKIvtVVGHG--AEEVKEVLGDRSE------FALQ 72

                         90       100       110
                 ....*....|....*....|....*....|..
gi 831193475  85 GEALETAGGIAQALPLLErDGRSTVFVaVAGD 116
Cdd:PRK14354  73 EEQLGTGHAVMQAEEFLA-DKEGTTLV-ICGD 102
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
 9-97 2.49e-08

glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase homotetramer This model describes a tightly conserved but broadly distributed subfamily (here designated as short form) of known and putative bacterial glucose-1-phosphate thymidylyltransferases. It is well characterized in several species as the first of four enzymes involved in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 130274 [Multi-domain]  Cd Length: 286  Bit Score: 53.17  E-value: 2.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831193475    9 MIFAAGRGERMRPLTDTRPKPLLEAGGKPLIVWQIEALARAGIETI-VINHAWLGERIEAALGDGSRWGVRLAYSAEgea 87
Cdd:TIGR01207   3 IILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDIlIISTPEDTPRFQRLLGDGSQWGINLSYAVQ--- 79

                          90
                  ....*....|
gi 831193475   88 lETAGGIAQA 97
Cdd:TIGR01207  80 -PSPDGLAQA 88
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 8-98 3.01e-08

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 53.14  E-value: 3.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831193475   8 AMIFAAGRGERMRPLTDTRPKPLLEAGGKPLIVWQIEALARAGIETI-VINHAWLGERIEAALGDGSRWGVRLAYSAEge 86
Cdd:PRK15480   6 GIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDIlIISTPQDTPRFQQLLGDGSQWGLNLQYKVQ-- 83

                         90
                 ....*....|..
gi 831193475  87 alETAGGIAQAL 98
Cdd:PRK15480  84 --PSPDGLAQAF 93
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
 8-43 1.88e-07

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: 50.26  E-value: 1.88e-07
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 831193475   8 AMIFAAGRGERMRPLTDTRPKPLLEAGGKPlIVWQI 43
Cdd:cd02524    1 VVILAGGLGTRLSEETELKPKPMVEIGGRP-ILWHI 35
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 12-56 2.32e-07

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: 49.50  E-value: 2.32e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 831193475  12 AAGRGERMrpltDTRPKPLLEAGGKPLIVWQIEALARAGIETIVI 56
Cdd:COG2266    2 AGGKGTRL----GGGEKPLLEICGKPMIDRVIDALEESCIDKIYV 42
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
6-71 4.46e-07

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 48.62  E-value: 4.46e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 831193475   6 TTAMIFAAGRGERMRpltdtRPKPLLEAGGKPLIVWQIEALARAGIETI--VINHAwlGERIEAALGD 71
Cdd:COG2068    4 VAAIILAAGASSRMG-----RPKLLLPLGGKPLLERAVEAALAAGLDPVvvVLGAD--AEEVAAALAG 64
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 6-56 5.72e-07

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


Pssm-ID: 133009 [Multi-domain]  Cd Length: 218  Bit Score: 48.67  E-value: 5.72e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 831193475   6 TTAMIFAAGRGERMRPltdTRPKPLLEAGGKPLIVWQIEALARAG-IETIVI 56
Cdd:cd02516    1 VAAIILAAGSGSRMGA---DIPKQFLELGGKPVLEHTLEAFLAHPaIDEIVV 49
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 6-56 1.64e-06

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: 47.91  E-value: 1.64e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 831193475   6 TTAMIFAAGRGERMRPLTDTRPKPLLEAGGKPLIVWQIEALARAGIETIVI 56
Cdd:cd02541    1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIII 51
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
8-56 1.95e-06

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 47.05  E-value: 1.95e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 831193475   8 AMIFAAGRGERMRPltdTRPKPLLEAGGKPLIVWQIEALARAG-IETIVI 56
Cdd:PRK00155   6 AIIPAAGKGSRMGA---DRPKQYLPLGGKPILEHTLEAFLAHPrIDEIIV 52
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
 1-36 2.21e-06

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 47.91  E-value: 2.21e-06
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 831193475   1 MSDTLttAMIFAAGRGERMRPLTDTRPKPLLEAGGK 36
Cdd:PRK00725  13 TRDTL--ALILAGGRGSRLKELTDKRAKPAVYFGGK 46
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 8-126 2.36e-06

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: 47.25  E-value: 2.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831193475   8 AMIFAAG--RGERMRPLTDTRPKPLLEAGGKPLIVWQIEALAR-AGIETIVINHAWLGERIEAALGDGSR-WGVRLAYSA 83
Cdd:cd06428    1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKvPDLKEVLLIGFYPESVFSDFISDAQQeFNVPIRYLQ 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 831193475  84 EGEALETAGGIAQALPLLERDGRSTVFVaVAGDVFAEFDYGTL 126
Cdd:cd06428   81 EYKPLGTAGGLYHFRDQILAGNPSAFFV-LNADVCCDFPLQEL 122
ispD TIGR00453
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ...
 7-56 2.65e-06

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase, the IspD protein of the deoxyxylulose pathway of IPP biosynthesis. In about twenty percent of bacterial genomes, this protein occurs as IspDF, a bifunctional fusion protein. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 213532  Cd Length: 217  Bit Score: 46.90  E-value: 2.65e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 831193475    7 TAMIFAAGRGERMRPltdTRPKPLLEAGGKPLIVWQIEALARA-GIETIVI 56
Cdd:TIGR00453   1 SAVIPAAGRGTRFGS---GVPKQYLELGGRPLLEHALDAFLAHpAIDEVVV 48
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 8-75 2.88e-06

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: 46.83  E-value: 2.88e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 831193475   8 AMIFAAGRGERMRPLTDTRPKPLLEAGGKPLIVWQIEALARAGIETIVINHAWLGERIEAALgDGSRW 75
Cdd:cd04197    3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQIKEYI-EKSKW 69
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 10-56 4.12e-06

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440824  Cd Length: 224  Bit Score: 46.28  E-value: 4.12e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 831193475  10 IFAAGRGERMRpltDTRPKPLLEAGGKPLIVWQIEALARAG-IETIVI 56
Cdd:COG1211    2 IPAAGSGSRMG---AGIPKQFLPLGGKPVLEHTLEAFLAHPrIDEIVV 46
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 6-85 5.50e-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: 45.63  E-value: 5.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831193475   6 TTAMIFAAGRGERMRpltdtRPKPLLEAGGKPLIVWQIEALARAGIETIVINHAWLGERIEAALGDGSRWGVRLAYSAEG 85
Cdd:cd04182    1 IAAIILAAGRSSRMG-----GNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALAGLPVVVVINPDWEEG 75
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 8-117 2.17e-05

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: 43.34  E-value: 2.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831193475    8 AMIFAAGRGERMRpltdtRPKPLLEAGGKPLIVWQIEALARAGiETIVINHAWlgERIEAALgdgSRWGVRLAYSAEgEA 87
Cdd:pfam12804   1 AVILAGGRSSRMG-----GDKALLPLGGKPLLERVLERLRPAG-DEVVVVAND--EEVLAAL---AGLGVPVVPDPD-PG 68

                          90       100       110
                  ....*....|....*....|....*....|
gi 831193475   88 LETAGGIAQAlplLERDGRSTVFVAVAGDV 117
Cdd:pfam12804  69 QGPLAGLLAA---LRAAPGADAVLVLACDM 95
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 8-36 3.01e-05

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 44.30  E-value: 3.01e-05
                         10        20
                 ....*....|....*....|....*....
gi 831193475   8 AMIFAAGRGERMRPLTDTRPKPLLEAGGK 36
Cdd:COG0448    4 AIILAGGRGSRLGPLTKDRAKPAVPFGGK 32
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-170 3.33e-05

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 44.08  E-value: 3.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831193475   1 MSDTLTTAMIFAAGRGERMRpltDTRPKPLLEAGGKPLIVWQIEALARAGIETIVI---NHAwlgERIEAALgdgSRWGV 77
Cdd:PRK14353   1 MTDRTCLAIILAAGEGTRMK---SSLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVvvgPGA---EAVAAAA---AKIAP 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831193475  78 RLAYSAEGEALETAGGIAQALPLLERdGRSTVFVaVAGDV-FAEfdygtlAAPAARMSALDAPAMHLVMVPNPPFHPsgd 156
Cdd:PRK14353  72 DAEIFVQKERLGTAHAVLAAREALAG-GYGDVLV-LYGDTpLIT------AETLARLRERLADGADVVVLGFRAADP--- 140

                        170
                 ....*....|....
gi 831193475 157 fvlGGDGRLSLDGG 170
Cdd:PRK14353 141 ---TGYGRLIVKGG 151
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 8-117 3.39e-05

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 44.35  E-value: 3.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831193475   8 AMIFAAGRGERMRpltDTRPKPLLEAGGKPLIVWQIEALARAGIETIVINHAWLGERIEAALGDgsRWGVRLAYSAegEA 87
Cdd:PRK14355   6 AIILAAGKGTRMK---SDLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHFAG--DGDVSFALQE--EQ 78

                         90       100       110
                 ....*....|....*....|....*....|
gi 831193475  88 LETAGGIAQALPLLerDGRSTVFVAVAGDV 117
Cdd:PRK14355  79 LGTGHAVACAAPAL--DGFSGTVLILCGDV 106
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 1-56 4.62e-05

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: 42.87  E-value: 4.62e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 831193475   1 MSDTLTtAMIFAAGRGERMRpltdtRPKPLLEAGGKPLIVWQIEALARAGIETIVI 56
Cdd:COG0746    1 MTMPIT-GVILAGGRSRRMG-----QDKALLPLGGRPLLERVLERLRPQVDEVVIV 50
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
 10-55 5.57e-05

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: 43.01  E-value: 5.57e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 831193475  10 IFAAGRGERMRPLTDTRPKPLLEAGGKPLIVWQIEALARAGIETIV 55
Cdd:cd04183    3 IPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEWVIESLAKIFDSRFI 48
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
6-56 6.21e-05

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


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 43.10  E-value: 6.21e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 831193475   6 TTAMIFAAGRGERMRPLTDTRPKPLLEAGGKPLIVWQIEALARAGIETIVI 56
Cdd:COG1210    4 RKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIF 54
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 6-56 6.23e-05

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: 42.18  E-value: 6.23e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 831193475   6 TTAMIFAAGRGERMrpltdTRPKPLLEAGGKPLIVWQIEALARAGIETIVI 56
Cdd:cd02503    1 ITGVILAGGKSRRM-----GGDKALLELGGKPLLEHVLERLKPLVDEVVIS 46
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
 8-123 8.36e-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: 42.14  E-value: 8.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831193475   8 AMIFAAGRGERMRPLTDTRPKPLLEAGGK-PLIVWQIEALARAGIETI----------VINHawlgerieaaLGDGSRW- 75
Cdd:cd02508    1 AIILAGGEGTRLSPLTKKRAKPAVPFGGRyRLIDFPLSNMVNSGIRNVgvltqyksrsLNDH----------LGSGKEWd 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 831193475  76 ------GVRLAYSAEGEALE----TAGGIAQALPLLERDGRSTVFVAvAGDVFAEFDY 123
Cdd:cd02508   71 ldrkngGLFILPPQQRKGGDwyrgTADAIYQNLDYIERSDPEYVLIL-SGDHIYNMDY 127
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 2-116 8.46e-05

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 43.17  E-value: 8.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831193475   2 SDTLTTAMIFAAGRGERMRpltDTRPKPLLEAGGKPLIVWQIEALARAGIETI--VINHAwlGERIEAALGDGSRwgvRL 79
Cdd:PRK14356   2 MASTTGALILAAGKGTRMH---SDKPKVLQTLLGEPMLRFVYRALRPLFGDNVwtVVGHR--ADMVRAAFPDEDA---RF 73

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 831193475  80 AYSAegEALETAGGIAQALPLLERDGRSTVFVaVAGD 116
Cdd:PRK14356  74 VLQE--QQLGTGHALQCAWPSLTAAGLDRVLV-VNGD 107
mobA PRK00317
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
 6-57 7.75e-04

molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed


Pssm-ID: 234725 [Multi-domain]  Cd Length: 193  Bit Score: 39.40  E-value: 7.75e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 831193475   6 TTAMIFAAGRGERMrpltDTRPKPLLEAGGKPLIVWQIEALaRAGIETIVIN 57
Cdd:PRK00317   4 ITGVILAGGRSRRM----GGVDKGLQELNGKPLIQHVIERL-APQVDEIVIN 50
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 9-84 8.27e-04

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 39.96  E-value: 8.27e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 831193475   9 MIFAAGRGERMRpltDTRPKPLLEAGGKPLIVWQIEALARAGIETIVINHAWLGERIEAALgDGSrwGVRLAYSAE 84
Cdd:PRK14358  11 VILAAGQGTRMK---SALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGAEQVEAAL-QGS--GVAFARQEQ 80
PRK14489 PRK14489
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; ...
 7-64 1.90e-03

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


Pssm-ID: 237727 [Multi-domain]  Cd Length: 366  Bit Score: 38.97  E-value: 1.90e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 831193475   7 TAMIFAAGRGERMrpltDTRPKPLLEAGGKPLIVWQIEALaRAGIETIVINHAWLGER 64
Cdd:PRK14489   7 AGVILAGGLSRRM----NGRDKALILLGGKPLIERVVDRL-RPQFARIHLNINRDPAR 59
IspD pfam01128
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ...
 8-73 2.54e-03

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: 37.81  E-value: 2.54e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 831193475    8 AMIFAAGRGERMRpltDTRPKPLLEAGGKPLIVWQIEALARAG-IETIVIN-HAWLGERIEAALGDGS 73
Cdd:pfam01128   1 AVIPAAGSGKRMG---AGVPKQFLQLLGQPLLEHTVDAFLASPvVDRIVVAvSPDDTPEFRQLLGDPS 65
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
8-56 3.69e-03

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 37.96  E-value: 3.69e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 831193475   8 AMIFAAGRGERMRPLTDTRPKPLLEAGGKPLIVWQIEALARAGIETIVI 56
Cdd:PRK13389  11 AVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVL 59
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
8-59 4.27e-03

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 37.56  E-value: 4.27e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 831193475   8 AMIFAAGRGERMRPLTDTRPKPLLEAGGKPLIVWQIEALARAGIETIV-INHA 59
Cdd:PRK10122   6 AVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVlVTHA 58
 
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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