NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1442778102|gb|AXK38654|]
View 

nucleotidyltransferase family protein [Crenobacter cavernae]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 2-221 2.74e-91

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: 267.79  E-value: 2.74e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102   2 KAMILAAGRGERMRPLTDATPKPLLMAGSQPLIGWHLKRLAEAGVKDVVINHAWLGKEIEARLADGAEWGVHIAYSPEPE 81
Cdd:COG1208     1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRFGVRITYVDEGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102  82 ALETAGGIATALPLLGDAPFAVVNGDVLTDFPFAHLIDAaprLDGAERLAHLVLIDNPAHHAAGDFSLDKNGVVHD---- 157
Cdd:COG1208    81 PLGTGGALKRALPLLGDEPFLVLNGDILTDLDLAALLAF---HREKGADATLALVPVPDPSRYGVVELDGDGRVTRfvek 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1442778102 158 ----EPGLTFAGIGVYHPALFEGLEAHRPAKLAPLLRAAMARGQVTGEHYRGLWHDVGTTQRLAEADA 221
Cdd:COG1208   158 peepPSNLINAGIYVLEPEIFDYIPEGEPFDLEDLLPRLIAEGRVYGYVHDGYWLDIGTPEDLLEANA 225
 
Name Accession Description Interval E-value
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 2-221 2.74e-91

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: 267.79  E-value: 2.74e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102   2 KAMILAAGRGERMRPLTDATPKPLLMAGSQPLIGWHLKRLAEAGVKDVVINHAWLGKEIEARLADGAEWGVHIAYSPEPE 81
Cdd:COG1208     1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRFGVRITYVDEGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102  82 ALETAGGIATALPLLGDAPFAVVNGDVLTDFPFAHLIDAaprLDGAERLAHLVLIDNPAHHAAGDFSLDKNGVVHD---- 157
Cdd:COG1208    81 PLGTGGALKRALPLLGDEPFLVLNGDILTDLDLAALLAF---HREKGADATLALVPVPDPSRYGVVELDGDGRVTRfvek 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1442778102 158 ----EPGLTFAGIGVYHPALFEGLEAHRPAKLAPLLRAAMARGQVTGEHYRGLWHDVGTTQRLAEADA 221
Cdd:COG1208   158 peepPSNLINAGIYVLEPEIFDYIPEGEPFDLEDLLPRLIAEGRVYGYVHDGYWLDIGTPEDLLEANA 225
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 2-219 7.52e-84

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: 248.64  E-value: 7.52e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102   2 KAMILAAGRGERMRPLTDATPKPLLMAGSQPLIGWHLKRLAEAGVKDVVINHAWLGKEIEARLADGAeWGVHIAYSPEP- 80
Cdd:cd06422     1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHLGDSR-FGLRITISDEPd 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102  81 EALETAGGIATALPLLGDAPFAVVNGDVLTDFPFAHLIDAAPRLDGAeRLAHLVLIDNPAHHAAGDFSLDKNGVVHDEPG 160
Cdd:cd06422    80 ELLETGGGIKKALPLLGDEPFLVVNGDILWDGDLAPLLLLHAWRMDA-LLLLLPLVRNPGHNGVGDFSLDADGRLRRGGG 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1442778102 161 -----LTFAGIGVYHPALFEGLEAhRPAKLAPLLRAAMARGQVTGEHYRGLWHDVGTTQRLAEA 219
Cdd:cd06422   159 gavapFTFTGIQILSPELFAGIPP-GKFSLNPLWDRAIAAGRLFGLVYDGLWFDVGTPERLLAA 221
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 1-211 1.68e-34

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: 126.55  E-value: 1.68e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102   1 MKAMILAAGRGERMRPLTDATPKPLLMAGSQPLIGWHLKRLAEAGVKDVVINHAWLGKEIEARLADGAEWGVHIAYSPEP 80
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEKVREYFGDGSRGGVPIEYVVQE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102  81 EALETAGGIATALPLLGDaPFAVVNGDVLTDFPfahLIDAAPRLDGAERLAHLVliDNPAhhAAGDFSLDKNGVVH---- 156
Cdd:TIGR03992  81 EQLGTADALGSAKEYVDD-EFLVLNGDVLLDSD---LLERLIRAEAPAIAVVEV--DDPS--DYGVVETDGGRVTGivek 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1442778102 157 --DEPG-LTFAGIGVYHPALFEGLEAHRPAK-----LAPLLRAAMARGQVTGEHYRGLWHDVG 211
Cdd:TIGR03992 153 peNPPSnLINAGIYLFSPEIFELLEKTKLSPrgeyeLTDALQLLIDEGKVKAVELDGFWLDVG 215
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-219 3.17e-24

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


Pssm-ID: 425709 [Multi-domain]  Cd Length: 243  Bit Score: 96.17  E-value: 3.17e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102   2 KAMILAAGRGERMRPLTDATPKPL-LMAGSQPLIGWHLKRLAEAGVKD-VVINHAWLGKEIEARLADGAEWGVHIAYSPE 79
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLvPVGGKYPLIDYPLSRLANAGIREiIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102  80 PEALETAGGIATALPLLGD--APFAVVNGDVLTDFPFAHLIDAApRLDGAERLAHLVLIDNPAHHAAGDFSLDKNGVVHD 157
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDekSDVLVLGGDHIYRMDLEQAVKFH-IEKAADATVTFGIVPVEPPTGYGVVEFDDNGRVIR 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1442778102 158 -------EPGLTFAGIGVY--HPALFEGLEAH--RPAKLAP----LLRAAMARGQVTGEH-YRG-LWHDVGTTQRLAEA 219
Cdd:pfam00483 160 fvekpklPKASNYASMGIYifNSGVLDFLAKYleELKRGEDeitdILPKALEDGKLAYAFiFKGyAWLDVGTWDSLWEA 238
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 2-219 2.01e-12

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 65.08  E-value: 2.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102   2 KAMILAAGRGERMRPLTDATPKPLLMAGSQPLIGWHLKRLAEAGVKDV-VINHAWLGKEIEARLADGAEWGVHIAYSPEP 80
Cdd:PRK15480    5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDIlIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102  81 EALETAGGIATALPLLGDAPFAVVNGD-VLTDFPFAHLIDAA-PRLDGAERLAHLVliDNPAHHAAGDFslDKNGVVHD- 157
Cdd:PRK15480   85 SPDGLAQAFIIGEEFIGGDDCALVLGDnIFYGHDLPKLMEAAvNKESGATVFAYHV--NDPERYGVVEF--DQNGTAISl 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1442778102 158 -----EPGLTFA--GIGVYHPALFEGLEAHRPA-----KLAPLLRAAMARGQVT----GEHYRglWHDVGTTQRLAEA 219
Cdd:PRK15480  161 eekplQPKSNYAvtGLYFYDNDVVEMAKNLKPSargelEITDINRIYMEQGRLSvammGRGYA--WLDTGTHQSLIEA 236
 
Name Accession Description Interval E-value
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 2-221 2.74e-91

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: 267.79  E-value: 2.74e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102   2 KAMILAAGRGERMRPLTDATPKPLLMAGSQPLIGWHLKRLAEAGVKDVVINHAWLGKEIEARLADGAEWGVHIAYSPEPE 81
Cdd:COG1208     1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRFGVRITYVDEGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102  82 ALETAGGIATALPLLGDAPFAVVNGDVLTDFPFAHLIDAaprLDGAERLAHLVLIDNPAHHAAGDFSLDKNGVVHD---- 157
Cdd:COG1208    81 PLGTGGALKRALPLLGDEPFLVLNGDILTDLDLAALLAF---HREKGADATLALVPVPDPSRYGVVELDGDGRVTRfvek 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1442778102 158 ----EPGLTFAGIGVYHPALFEGLEAHRPAKLAPLLRAAMARGQVTGEHYRGLWHDVGTTQRLAEADA 221
Cdd:COG1208   158 peepPSNLINAGIYVLEPEIFDYIPEGEPFDLEDLLPRLIAEGRVYGYVHDGYWLDIGTPEDLLEANA 225
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 2-219 7.52e-84

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: 248.64  E-value: 7.52e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102   2 KAMILAAGRGERMRPLTDATPKPLLMAGSQPLIGWHLKRLAEAGVKDVVINHAWLGKEIEARLADGAeWGVHIAYSPEP- 80
Cdd:cd06422     1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHLGDSR-FGLRITISDEPd 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102  81 EALETAGGIATALPLLGDAPFAVVNGDVLTDFPFAHLIDAAPRLDGAeRLAHLVLIDNPAHHAAGDFSLDKNGVVHDEPG 160
Cdd:cd06422    80 ELLETGGGIKKALPLLGDEPFLVVNGDILWDGDLAPLLLLHAWRMDA-LLLLLPLVRNPGHNGVGDFSLDADGRLRRGGG 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1442778102 161 -----LTFAGIGVYHPALFEGLEAhRPAKLAPLLRAAMARGQVTGEHYRGLWHDVGTTQRLAEA 219
Cdd:cd06422   159 gavapFTFTGIQILSPELFAGIPP-GKFSLNPLWDRAIAAGRLFGLVYDGLWFDVGTPERLLAA 221
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 3-211 1.02e-49

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: 161.59  E-value: 1.02e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102   3 AMILAAGRGERMRPLTDATPKPLLMAGSQPLIGWHLKRLAEAGVKDVVINHAWLGKEIEARLADGAEWGVHIAYSPEPEA 82
Cdd:cd04181     1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGSKFGVNIEYVVQEEP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102  83 LETAGGIATALPLLGDAPFAVVNGDVLTDFPFAHLIDAApRLDGAERLAHLVLIDNPAHHaaGDFSLDKNGVVHD----- 157
Cdd:cd04181    81 LGTAGAVRNAEDFLGDDDFLVVNGDVLTDLDLSELLRFH-REKGADATIAVKEVEDPSRY--GVVELDDDGRVTRfvekp 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102 158 -EPGLTFAGIGVYH--PALFEGLEAHRPAK---LAPLLRAAMARGQVTGEHYRGLWHDVG 211
Cdd:cd04181   158 tLPESNLANAGIYIfePEILDYIPEILPRGedeLTDAIPLLIEEGKVYGYPVDGYWLDIG 217
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 3-220 1.49e-37

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: 130.37  E-value: 1.49e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102   3 AMILAAGRGERMRPLTDATPKPLLMAGSQPLIGWHLKRLAEAGVKDVVINHAWLGKEIEARLADGAEWGVHIAYSPEPEA 82
Cdd:cd06915     1 AVILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYLAEQIEEYFGDGYRGGIRIYYVIEPEP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102  83 LETAGGIATALPLLGDAPFAVVNGDVLTDFPFAHLIDAAPRLDGaerLAHLVLIDNPAHHAAGDFSLDKNGVV------- 155
Cdd:cd06915    81 LGTGGAIKNALPKLPEDQFLVLNGDTYFDVDLLALLAALRASGA---DATMALRRVPDASRYGNVTVDGDGRViafvekg 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1442778102 156 -HDEPGLTFAGIGVYHPALFEGLEAHRPAKLAPLLRAAMARGQVTGEHYRGLWHDVGTTQRLAEAD 220
Cdd:cd06915   158 pGAAPGLINGGVYLLRKEILAEIPADAFSLEADVLPALVKRGRLYGFEVDGYFIDIGIPEDYARAQ 223
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 1-211 1.68e-34

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: 126.55  E-value: 1.68e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102   1 MKAMILAAGRGERMRPLTDATPKPLLMAGSQPLIGWHLKRLAEAGVKDVVINHAWLGKEIEARLADGAEWGVHIAYSPEP 80
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEKVREYFGDGSRGGVPIEYVVQE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102  81 EALETAGGIATALPLLGDaPFAVVNGDVLTDFPfahLIDAAPRLDGAERLAHLVliDNPAhhAAGDFSLDKNGVVH---- 156
Cdd:TIGR03992  81 EQLGTADALGSAKEYVDD-EFLVLNGDVLLDSD---LLERLIRAEAPAIAVVEV--DDPS--DYGVVETDGGRVTGivek 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1442778102 157 --DEPG-LTFAGIGVYHPALFEGLEAHRPAK-----LAPLLRAAMARGQVTGEHYRGLWHDVG 211
Cdd:TIGR03992 153 peNPPSnLINAGIYLFSPEIFELLEKTKLSPrgeyeLTDALQLLIDEGKVKAVELDGFWLDVG 215
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 1-221 2.99e-31

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: 114.59  E-value: 2.99e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102   1 MKAMILAAGRGERMRPLTDATPKPLLMAGSQPLIGWHLKRLAEAGVKDVVINHAWLGKEIEARLADGAEWGVHIAYSPEP 80
Cdd:cd04189     1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEALGDGSRFGVRITYILQE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102  81 EALETAGGIATALPLLGDAPFAVVNGDVLTDFPFAHLIDaapRLDGAERLAHLVL--IDNPahHAAGDFSLDKNGVVH-- 156
Cdd:cd04189    81 EPLGLAHAVLAARDFLGDEPFVVYLGDNLIQEGISPLVR---DFLEEDADASILLaeVEDP--RRFGVAVVDDGRIVRlv 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1442778102 157 ---DEPGLTFAGIGVY--HPALFEGLEAHRPAK-----LAPLLRAAMARG-QVTGEHYRGLWHDVGTTQRLAEADA 221
Cdd:cd04189   156 ekpKEPPSNLALVGVYafTPAIFDAISRLKPSWrgeleITDAIQWLIDRGrRVGYSIVTGWWKDTGTPEDLLEANR 231
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 3-119 9.32e-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: 107.60  E-value: 9.32e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102   3 AMILAAGRGERMRPLTDATPKPLLMAGSQPLIGWHLKRLAEAGVKDVVINHAWLGKEIEARLADGAEWGVHIAYSPEPEA 82
Cdd:cd06426     1 VVIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNYLAEMIEDYFGDGSKFGVNISYVREDKP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1442778102  83 LETAGgiatALPLLG---DAPFAVVNGDVLTDFPFAHLID 119
Cdd:cd06426    81 LGTAG----ALSLLPekpTDPFLVMNGDILTNLNYEHLLD 116
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 1-119 2.15e-26

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: 101.90  E-value: 2.15e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102   1 MKAMILAAGRGERMRPLTDATPKPLLMAGSQPLIGWHLKRLAEAGVKDVVINHAWLGKEIEARLAD-GAEWGVHIAYSPE 79
Cdd:cd06425     1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYRPEDMVPFLKEyEKKLGIKITFSIE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1442778102  80 PEALETAGGIATALPLLG--DAPFAVVNGDVLTDFPFAHLID 119
Cdd:cd06425    81 TEPLGTAGPLALARDLLGddDEPFFVLNSDVICDFPLAELLD 122
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-219 3.17e-24

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


Pssm-ID: 425709 [Multi-domain]  Cd Length: 243  Bit Score: 96.17  E-value: 3.17e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102   2 KAMILAAGRGERMRPLTDATPKPL-LMAGSQPLIGWHLKRLAEAGVKD-VVINHAWLGKEIEARLADGAEWGVHIAYSPE 79
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLvPVGGKYPLIDYPLSRLANAGIREiIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102  80 PEALETAGGIATALPLLGD--APFAVVNGDVLTDFPFAHLIDAApRLDGAERLAHLVLIDNPAHHAAGDFSLDKNGVVHD 157
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDekSDVLVLGGDHIYRMDLEQAVKFH-IEKAADATVTFGIVPVEPPTGYGVVEFDDNGRVIR 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1442778102 158 -------EPGLTFAGIGVY--HPALFEGLEAH--RPAKLAP----LLRAAMARGQVTGEH-YRG-LWHDVGTTQRLAEA 219
Cdd:pfam00483 160 fvekpklPKASNYASMGIYifNSGVLDFLAKYleELKRGEDeitdILPKALEDGKLAYAFiFKGyAWLDVGTWDSLWEA 238
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-219 1.00e-23

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 95.93  E-value: 1.00e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102   1 MKAMILAAGRGERMRPLTDATPKPLL-MAGsQPLIGWHLKRLAEAGVKDVVI---NHawLGKEIEARLADGAEWGVHIAY 76
Cdd:COG1209     1 MKGIILAGGSGTRLRPLTLTVSKQLLpVYD-KPMIYYPLSTLMLAGIREILIistPE--DGPQFERLLGDGSQLGIKISY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102  77 SPEPEALETAGGIATALPLLGDAPFAVV------NGDVLTDFpfahLIDAAPRLDGAERLAHLVliDNPahHAAGDFSLD 150
Cdd:COG1209    78 AVQPEPLGLAHAFIIAEDFIGGDPVALVlgdnifYGDGLSEL----LREAAARESGATIFGYKV--EDP--ERYGVVEFD 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102 151 KNG-VVH-----DEPGLTFAGIGVYH--PALFEGLEAHRPAK-----LAPLLRAAMARGQVTGEH-YRGL-WHDVGTTQR 215
Cdd:COG1209   150 EDGrVVSleekpKEPKSNLAVTGLYFydNDVVEIAKNLKPSArgeleITDANQAYLERGKLVVELlGRGFaWLDTGTHES 229


                  ....
gi 1442778102 216 LAEA 219
Cdd:COG1209   230 LLEA 233
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
2-224 1.23e-23

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 94.54  E-value: 1.23e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102   2 KAMILAAGRGERMRPLTDATPKPLLMAGSQPLIGWHLKRLAEAGVKDVVINHAWLGKEIEARLADGAeWGVHIAYSPEPE 81
Cdd:COG1213     1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEALARPG-PDVTFVYNPDYD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102  82 ALETAGGIATALPLLGDaPFAVVNGDVLtdFP---FAHLIDAAPRLdgaerlahLVLIDNPAHHAAGD---FSLDKNGVV 155
Cdd:COG1213    80 ETNNIYSLWLAREALDE-DFLLLNGDVV--FDpaiLKRLLASDGDI--------VLLVDRKWEKPLDEevkVRVDEDGRI 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102 156 ----HDEPGLTFAG--IGVYH------PALFEGLEAHRPAKLAPL-----LRAAMARGQ------VTGehyrGLWHDVGT 212
Cdd:COG1213   149 veigKKLPPEEADGeyIGIFKfsaegaAALREALEALIDEGGPNLyyedaLQELIDEGGpvkavdIGG----LPWVEIDT 224

                         250
                  ....*....|..
gi 1442778102 213 TQRLAEADAIAR 224
Cdd:COG1213   225 PEDLERAEELFA 236
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 1-225 8.68e-21

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: 86.86  E-value: 8.68e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102   1 MKAMILAAGRGERMRPLTDATPKPLLMAGSQPLIGWHLKRLAEAGVKDVVI----NHAWLGKEIearLADGAEWGVHIAY 76
Cdd:cd02538     1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIistpEDLPLFKEL---LGDGSDLGIRITY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102  77 SPEPEaletAGGIATALPL----LGDAPFAVVNGD-VLTDFPFAHLID-AAPRLDGAERLAHLVliDNPahHAAGDFSLD 150
Cdd:cd02538    78 AVQPK----PGGLAQAFIIgeefIGDDPVCLILGDnIFYGQGLSPILQrAAAQKEGATVFGYEV--NDP--ERYGVVEFD 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102 151 KNGVV------HDEPGLTFA--GIGVYHPALFEGLEAHRPAKLAPL-----LRAAMARGQVTGEHY-RGL-WHDVGTTQR 215
Cdd:cd02538   150 ENGRVlsieekPKKPKSNYAvtGLYFYDNDVFEIAKQLKPSARGELeitdvNNEYLEKGKLSVELLgRGFaWLDTGTHES 229

                         250
                  ....*....|
gi 1442778102 216 LAEADAIART 225
Cdd:cd02538   230 LLEASNFVQT 239
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 3-109 4.40e-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: 82.28  E-value: 4.40e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102   3 AMILAAGRGERMRPLTDATPKPLLMAGSQPLIGWHLKRLAEAGVKDVVINHAWLGKEIEARLADgaEWGVHIAYSPEPEA 82
Cdd:cd02523     1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKK--YPNIKFVYNPDYAE 78

                          90       100
                  ....*....|....*....|....*..
gi 1442778102  83 LETAGGIATALPLLGDaPFAVVNGDVL 109
Cdd:cd02523    79 TNNIYSLYLARDFLDE-DFLLLEGDVV 104
LicC COG4750
CTP:phosphocholine cytidylyltransferase LicC [Cell wall/membrane/envelope biogenesis, Lipid ...
 1-79 1.50e-13

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


Pssm-ID: 443784 [Multi-domain]  Cd Length: 228  Bit Score: 67.16  E-value: 1.50e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1442778102   1 MKAMILAAGRGERMRPLTDATPKPLLMAGSQPLIGWHLKRLAEAGVKDVVINHAWLgKEIEARLADgaEWGVHIAYSPE 79
Cdd:COG4750     1 MNAIILAAGLGSRFAPITYETPKGLLKVNGEPLIERQIRQLHEAGITDITVVVGYL-KEQFEYLED--KYGVKLIYNPD 76
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 1-212 3.40e-13

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: 66.79  E-value: 3.40e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102   1 MKAMILAAGRGERMRPLTDATPKPLLMAGSQPLIGWHLKRLAEAGVKDVVI----------NHAWLGKEIEARL------ 64
Cdd:cd02541     1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIvtgrgkraieDHFDRSYELEETLekkgkt 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102  65 --ADGAEW---GVHIAYSPEPEALETAGGIATALPLLGDAPFAVVNGDVLTD---FPFAHLIDAAPRLDG--------AE 128
Cdd:cd02541    81 dlLEEVRIisdLANIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLIDskePCLKQLIEAYEKTGAsviaveevPP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102 129 RLAHLVLIDNPAHHAAGDFSLdkNGVVH----DEPGLTFAGIG--VYHPALFEGLEAHRPAK-----LAPLLRAAMARGQ 197
Cdd:cd02541   161 EDVSKYGIVKGEKIDGDVFKV--KGLVEkpkpEEAPSNLAIVGryVLTPDIFDILENTKPGKggeiqLTDAIAKLLEEEP 238

                         250
                  ....*....|....*
gi 1442778102 198 VTGEHYRGLWHDVGT 212
Cdd:cd02541   239 VYAYVFEGKRYDCGN 253
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 2-219 2.01e-12

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 65.08  E-value: 2.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102   2 KAMILAAGRGERMRPLTDATPKPLLMAGSQPLIGWHLKRLAEAGVKDV-VINHAWLGKEIEARLADGAEWGVHIAYSPEP 80
Cdd:PRK15480    5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDIlIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102  81 EALETAGGIATALPLLGDAPFAVVNGD-VLTDFPFAHLIDAA-PRLDGAERLAHLVliDNPAHHAAGDFslDKNGVVHD- 157
Cdd:PRK15480   85 SPDGLAQAFIIGEEFIGGDDCALVLGDnIFYGHDLPKLMEAAvNKESGATVFAYHV--NDPERYGVVEF--DQNGTAISl 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1442778102 158 -----EPGLTFA--GIGVYHPALFEGLEAHRPA-----KLAPLLRAAMARGQVT----GEHYRglWHDVGTTQRLAEA 219
Cdd:PRK15480  161 eekplQPKSNYAvtGLYFYDNDVVEMAKNLKPSargelEITDINRIYMEQGRLSvammGRGYA--WLDTGTHQSLIEA 236
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 3-120 2.85e-12

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: 64.20  E-value: 2.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102   3 AMILAAG--RGERMRPLTDATPKPLLMAGSQPLIGWHLKRLAE-AGVKDVVInhawLGKEIEARLAD-----GAEWGVHI 74
Cdd:cd06428     1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKvPDLKEVLL----IGFYPESVFSDfisdaQQEFNVPI 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1442778102  75 AYSPEPEALETAGGIATALP-LLGDAP--FAVVNGDVLTDFPFAHLIDA 120
Cdd:cd06428    77 RYLQEYKPLGTAGGLYHFRDqILAGNPsaFFVLNADVCCDFPLQELLEF 125
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 1-125 1.20e-10

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: 58.80  E-value: 1.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102   1 MKAMILAAGRGERMRPLTDATPKPLLMAGSQPLIGWHLKRLAEAGVKDVVI---NHAwlGKEIEARLA-DGAEWG----V 72
Cdd:cd02507     1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVvccEHS--QAIIEHLLKsKWSSLSskmiV 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1442778102  73 HIAYSPEPEALETAG-GIATALPLLGDapFAVVNGDVLTDFPFAHLIDAAPRLD 125
Cdd:cd02507    79 DVITSDLCESAGDALrLRDIRGLIRSD--FLLLSCDLVSNIPLSELLEERRKKD 130
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 1-119 7.37e-10

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: 56.90  E-value: 7.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102   1 MKAMILAAGRGERMRPLTDATPKPLLMAGSQPLIGWHLKRLAEAGVKDVVI----NHAwlgKEIEARLADGAEWGVHIAY 76
Cdd:cd04198     1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVvvpeEEQ---AEISTYLRSFPLNLKQKLD 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1442778102  77 SpEPEALETAGGIATAL-----PLLGDapFAVVNGDVLTDFPFAHLID 119
Cdd:cd04198    78 E-VTIVLDEDMGTADSLrhirkKIKKD--FLVLSCDLITDLPLIELVD 122
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
1-111 1.74e-09

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 56.44  E-value: 1.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102   1 MKAMILAAGRGERMRPLTDATPKPLLMAGSQPLIGWHLKRLAEAGVKDVVI----------NHAWLGKEIEARLADGAEW 70
Cdd:PRK10122    4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLvthasknaveNHFDTSYELESLLEQRVKR 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1442778102  71 ------------GVHIAYSPEPEALETAGGIATALPLLGDAPFAVVNGDVLTD 111
Cdd:PRK10122   84 qllaevqsicppGVTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPDVVID 136
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 3-108 2.54e-09

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: 55.21  E-value: 2.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102   3 AMILAAGRGERMRpltDATPKPLLMAGSQPLIGWHLKRLAEAGVKD--VVINHAwlGKEIEARLADGaewGVHIAYSPEP 80
Cdd:cd02540     1 AVILAAGKGTRMK---SDLPKVLHPLAGKPMLEHVLDAARALGPDRivVVVGHG--AEQVKKALANP---NVEFVLQEEQ 72

                          90       100       110
                  ....*....|....*....|....*....|
gi 1442778102  81 eaLETAGGIATALPLLGD--APFAVVNGDV 108
Cdd:cd02540    73 --LGTGHAVKQALPALKDfeGDVLVLYGDV 100
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 1-149 5.08e-09

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: 55.42  E-value: 5.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102   1 MKAMILAAGRGERMRpltDATPKPLLMAGSQPLIGWHLKRLAEAGVKD--VVINHAwlGKEIEARLADgaeWGVHIAYSP 78
Cdd:COG1207     3 LAVVILAAGKGTRMK---SKLPKVLHPLAGKPMLEHVLDAARALGPDRivVVVGHG--AEQVRAALAD---LDVEFVLQE 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1442778102  79 EPeaLETAGGIATALPLLG--DAPFAVVNGDVltdfPfahLIDaaprldgAERLAHLVlidnpAHHAAGDFSL 149
Cdd:COG1207    75 EQ--LGTGHAVQQALPALPgdDGTVLVLYGDV----P---LIR-------AETLKALL-----AAHRAAGAAA 126
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 3-127 2.27e-07

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: 48.73  E-value: 2.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102   3 AMILAAGRGERMRpltdaTPKPLLMAGSQPLIGWHLKRLAEAGvKDVVINHAWlgkeiEARLADGAEWGVHIAYSPEPEA 82
Cdd:pfam12804   1 AVILAGGRSSRMG-----GDKALLPLGGKPLLERVLERLRPAG-DEVVVVAND-----EEVLAALAGLGVPVVPDPDPGQ 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1442778102  83 lETAGGIATALPLLGDAPFAVVngdVLTDFPF------AHLIDAAPRLDGA 127
Cdd:pfam12804  70 -GPLAGLLAALRAAPGADAVLV---LACDMPFltpellRRLLAAAEESGAD 116
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
2-111 2.80e-07

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


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 50.03  E-value: 2.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102   2 KAMILAAGRGERMRPLTDATPKPLLMAGSQPLIGWHLKRLAEAGVKDVVI----------NH--------AWL---GKEI 60
Cdd:COG1210     5 KAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFvtgrgkraieDHfdrsyeleATLeakGKEE 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1442778102  61 EARLADGAEWGVHIAYSPEPEALETAGGIATALPLLGDAPFAVVNGDVLTD 111
Cdd:COG1210    85 LLEEVRSISPLANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLID 135
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
 3-51 3.93e-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: 49.49  E-value: 3.93e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1442778102   3 AMILAAGRGERMRPLTDATPKPLLMAGSQPLIgWHLKRL-AEAGVKDVVI 51
Cdd:cd02524     1 VVILAGGLGTRLSEETELKPKPMVEIGGRPIL-WHIMKIySHYGHNDFIL 49
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
3-101 5.25e-07

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 48.23  E-value: 5.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102   3 AMILAAGRGERMrpltdATPKPLLMAGSQPLIGWHLKRLAEAGVKDVVINhawLGKEIEARLADGAEWGVHIAYSPEPE- 81
Cdd:COG2068     6 AIILAAGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPVVVV---LGADAEEVAAALAGLGVRVVVNPDWEe 77

                          90       100
                  ....*....|....*....|....*....
gi 1442778102  82 --------ALETAGGIATA-LPLLGDAPF 101
Cdd:COG2068    78 gmssslraGLAALPADADAvLVLLGDQPL 106
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
2-111 4.71e-06

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 46.44  E-value: 4.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102   2 KAMILAAGRGERMRPLTDATPKPLLMAGSQPLIGWHLKRLAEAGVKDVVI----------NHAWLGKEIEARLADGAEWG 71
Cdd:PRK13389   10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLvthssknsieNHFDTSFELEAMLEKRVKRQ 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1442778102  72 ----VHIAYSPEPEALETAGGIATAL--------PLLGDAPFAVVNGDVLTD 111
Cdd:PRK13389   90 lldeVQSICPPHVTIMQVRQGLAKGLghavlcahPVVGDEPVAVILPDVILD 141
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
 1-118 1.41e-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: 44.87  E-value: 1.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102   1 MKAMILAAGRGERMRPL-TDATPKPLL-MAGSQPLIGWHLKRLAEAGVKD---VVIN--HAWLGKEiearlaDGAEWGVH 73
Cdd:cd02509     1 IYPVILAGGSGTRLWPLsRESYPKQFLkLFGDKSLLQQTLDRLKGLVPPDrilVVTNeeYRFLVRE------QLPEGLPE 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1442778102  74 IAYSPEPEALETAGGIATALPLL----GDAPFAVvngdvltdFPFAHLI 118
Cdd:cd02509    75 ENIILEPEGRNTAPAIALAALYLakrdPDAVLLV--------LPSDHLI 115
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 3-123 6.81e-05

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


Pssm-ID: 133025 [Multi-domain]  Cd Length: 186  Bit Score: 42.16  E-value: 6.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102   3 AMILAAGRGERMRpltdaTPKPLLMAGSQPLIGWHLKRLAEAGVKDVVINHAWLGKEIEARLADGaewGVHIAYSPEPE- 81
Cdd:cd04182     3 AIILAAGRSSRMG-----GNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALAGL---PVVVVINPDWEe 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1442778102  82 --------ALETAGGIATA-LPLLGDAPFavVNGDVLtdfpfAHLIDAAPR 123
Cdd:cd04182    75 gmssslaaGLEALPADADAvLILLADQPL--VTAETL-----RALIDAFRE 118
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 1-107 1.26e-04

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 42.27  E-value: 1.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102   1 MKAMILAAGRGERMRpltDATPKPLLMAGSQPLIGWHLKRLAEAGVKDVVINHAWLGKEIEARLAdgaewGVHIAYSPEP 80
Cdd:PRK14358    8 LDVVILAAGQGTRMK---SALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGAEQVEAALQ-----GSGVAFARQE 79

                          90       100
                  ....*....|....*....|....*....
gi 1442778102  81 EALETAGGIATALPLL--GDAPFAVVNGD 107
Cdd:PRK14358   80 QQLGTGDAFLSGASALteGDADILVLYGD 108
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 1-127 1.38e-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: 1.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102   1 MKAMILAAGRGERMrpltdATPKPLLMAGSQPLIGWHLKRLAEAgVKDVVINhawlgkeIEARLADGAEWGVHIAyspeP 80
Cdd:cd02503     1 ITGVILAGGKSRRM-----GGDKALLELGGKPLLEHVLERLKPL-VDEVVIS-------ANRDQERYALLGVPVI----P 63

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1442778102  81 EALETAG---GIATALPLL---------GDAPFavVNGDVLtdfpfAHLIDAAPRLDGA 127
Cdd:cd02503    64 DEPPGKGplaGILAALRAApadwvlvlaCDMPF--LPPELL-----ERLLAAAEEGADA 115
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 3-120 2.02e-04

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


Pssm-ID: 133040 [Multi-domain]  Cd Length: 217  Bit Score: 41.05  E-value: 2.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102   3 AMILAAGRGERMRPLTDATPKPLLMAGSQPLIGWHLKRLAEAGVKDVVI---NHAWLGKE-IEARLADGAEWG---VHIA 75
Cdd:cd04197     3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVfccSHSDQIKEyIEKSKWSKPKSSlmiVIII 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1442778102  76 YSPEPEAletaggiatalplLGDA------------PFAVVNGDVLTDFPFAHLIDA 120
Cdd:cd04197    83 MSEDCRS-------------LGDAlrdldakglirgDFILVSGDVVSNIDLKEILEE 126
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-107 3.16e-04

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 40.97  E-value: 3.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102   3 AMILAAGRGERMRpltDATPKPLLMAGSQPLIGWHLKRLAEAGVKD--VVINHAwlGKEIEARLADGAEwgvhiaYSPEP 80
Cdd:PRK14354    5 AIILAAGKGTRMK---SKLPKVLHKVCGKPMVEHVVDSVKKAGIDKivTVVGHG--AEEVKEVLGDRSE------FALQE 73

                          90       100
                  ....*....|....*....|....*....
gi 1442778102  81 EALETAGGIATALPLLGDAP--FAVVNGD 107
Cdd:PRK14354   74 EQLGTGHAVMQAEEFLADKEgtTLVICGD 102
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-116 4.74e-04

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 40.50  E-value: 4.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102   3 AMILAAGRGERMRpltDATPKPLLMAGSQPLIGWHLKRLAEAGVKDVVINHAWLGKEIEARLADGAEwgvhIAYSPEPEA 82
Cdd:PRK14355    6 AIILAAGKGTRMK---SDLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHFAGDGD----VSFALQEEQ 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1442778102  83 LETAGGIATALP-----------LLGDAPfaVVNGDVLTDFPFAH 116
Cdd:PRK14355   79 LGTGHAVACAAPaldgfsgtvliLCGDVP--LLRAETLQGMLAAH 121
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 3-24 5.69e-04

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 40.06  E-value: 5.69e-04
                          10        20
                  ....*....|....*....|..
gi 1442778102   3 AMILAAGRGERMRPLTDATPKP 24
Cdd:COG0448     4 AIILAGGRGSRLGPLTKDRAKP 25
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 1-123 1.17e-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: 38.63  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102   1 MKAMILAAGRGERMrpltdATPKPLLMAGSQPLIGWHLKRLAEAgVKDVVINhawlGKEIEARladgAEWGVHIAyspeP 80
Cdd:COG0746     5 ITGVILAGGRSRRM-----GQDKALLPLGGRPLLERVLERLRPQ-VDEVVIV----ANRPERY----AALGVPVV----P 66

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1442778102  81 EALETAG---GIATALPLLGDAPFAVVNGDV--LTDFPFAHLIDAAPR 123
Cdd:COG0746    67 DDPPGAGplaGILAALEAAPAEWVLVLACDMpfLPPDLVRRLLEALEE 114
ispD TIGR00453
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ...
 3-51 1.90e-03

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: 38.04  E-value: 1.90e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1442778102   3 AMILAAGRGERMRPltdATPKPLLMAGSQPLIGWHLKRLAEA-GVKDVVI 51
Cdd:TIGR00453   2 AVIPAAGRGTRFGS---GVPKQYLELGGRPLLEHALDAFLAHpAIDEVVV 48
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
 3-24 2.03e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 38.67  E-value: 2.03e-03
                          10        20
                  ....*....|....*....|..
gi 1442778102   3 AMILAAGRGERMRPLTDATPKP 24
Cdd:PRK00725   18 ALILAGGRGSRLKELTDKRAKP 39
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-132 2.03e-03

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 38.69  E-value: 2.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102   3 AMILAAGRGERMRpltDATPKPLLMAGSQPLIGWHLKRLAEAGVKD--VVINHawlGKEIEARLADGAEWGVHIAYSPEP 80
Cdd:PRK14353    8 AIILAAGEGTRMK---SSLPKVLHPVAGRPMLAHVLAAAASLGPSRvaVVVGP---GAEAVAAAAAKIAPDAEIFVQKER 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1442778102  81 eaLETAGGIATALPLLGDAPfavvnGDVLTDFPFAHLIDAAPRLDGAERLAH 132
Cdd:PRK14353   82 --LGTAHAVLAAREALAGGY-----GDVLVLYGDTPLITAETLARLRERLAD 126
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 3-51 2.43e-03

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: 37.89  E-value: 2.43e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1442778102   3 AMILAAGRGERMRPltdATPKPLLMAGSQPLIGWHLKRLAEAG-VKDVVI 51
Cdd:cd02516     3 AIILAAGSGSRMGA---DIPKQFLELGGKPVLEHTLEAFLAHPaIDEIVV 49
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
3-66 2.97e-03

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 37.81  E-value: 2.97e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1442778102   3 AMILAAGRGERMRPltdATPKPLLMAGSQPLIGWHLKRLAEAGVKD---VVINHAWLGKEIEARLAD 66
Cdd:PRK00155    6 AIIPAAGKGSRMGA---DRPKQYLPLGGKPILEHTLEAFLAHPRIDeiiVVVPPDDRPDFAELLLAK 69
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
 5-127 4.33e-03

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


Pssm-ID: 133026 [Multi-domain]  Cd Length: 231  Bit Score: 37.23  E-value: 4.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1442778102   5 ILAAGRGERMRPLTDATPKPLLMAGSQPLIGWHLKRLAEAG-------VKDVVINHAWLGKEIEARLADgaewgVHIAYS 77
Cdd:cd04183     3 IPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEWVIESLAKIFdsrfifiCRDEHNTKFHLDESLKLLAPN-----ATVVEL 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1442778102  78 PEpealETAGGIATALPLL----GDAPFAVVNGDVLTDFP-FAHLIDAAPR-LDGA 127
Cdd:cd04183    78 DG----ETLGAACTVLLAAdlidNDDPLLIFNCDQIVESDlLAFLAAFRERdLDGG 129
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 5-56 5.56e-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: 36.65  E-value: 5.56e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1442778102   5 ILAAGRGERMRpltDATPKPLLMAGSQPLIGWHLKRLAEAGVKD---VVINHAWL 56
Cdd:COG1211     2 IPAAGSGSRMG---AGIPKQFLPLGGKPVLEHTLEAFLAHPRIDeivVVVPPDDI 53
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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