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Conserved domains on  [gi|1137421795|gb|APZ41876|]
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mannose-1-phosphate guanylyltransferase [Acidihalobacter ferrooxydans]

Protein Classification

nucleotidyltransferase family protein( domain architecture ID 10157586)

nucleotidyltransferase family protein similar to Pseudomonas putida N-acetylmuramic acid alpha-1-phosphate (MurNAc-alpha1-P) uridylyltransferase MurU, which catalyzes the synthesis of uridine diphosphate (UDP)-MurNAc, a crucial precursor of the bacterial peptidoglycan cell wall

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 2-213 1.45e-92

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: 270.21  E-value: 1.45e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795   2 RAMILAAGRGERMRPLTDHTPKPLLPVGGRPLIEHHLLRLAAAGYRDIVINLAWLGDQIRATLGNgAHYGLRIHYSQEPD 81
Cdd:cd06422     1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHLGD-SRFGLRITISDEPD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795  82 GALETAGGIHHALPLLGAGPFLVVNGDIWCDHPLTP------HDPGGDLAHLVLVDNPPQHPHGDFALHG----TRIRPH 151
Cdd:cd06422    80 ELLETGGGIKKALPLLGDEPFLVVNGDILWDGDLAPllllhaWRMDALLLLLPLVRNPGHNGVGDFSLDAdgrlRRGGGG 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1137421795 152 DDNRLTYSGIGYYRPELFADVPDGPQPLAPLLRHAISADRISGEHHHGLWADVGTPDRLHAL 213
Cdd:cd06422   160 AVAPFTFTGIQILSPELFAGIPPGKFSLNPLWDRAIAAGRLFGLVYDGLWFDVGTPERLLAA 221
 
Name Accession Description Interval E-value
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 2-213 1.45e-92

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: 270.21  E-value: 1.45e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795   2 RAMILAAGRGERMRPLTDHTPKPLLPVGGRPLIEHHLLRLAAAGYRDIVINLAWLGDQIRATLGNgAHYGLRIHYSQEPD 81
Cdd:cd06422     1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHLGD-SRFGLRITISDEPD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795  82 GALETAGGIHHALPLLGAGPFLVVNGDIWCDHPLTP------HDPGGDLAHLVLVDNPPQHPHGDFALHG----TRIRPH 151
Cdd:cd06422    80 ELLETGGGIKKALPLLGDEPFLVVNGDILWDGDLAPllllhaWRMDALLLLLPLVRNPGHNGVGDFSLDAdgrlRRGGGG 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1137421795 152 DDNRLTYSGIGYYRPELFADVPDGPQPLAPLLRHAISADRISGEHHHGLWADVGTPDRLHAL 213
Cdd:cd06422   160 AVAPFTFTGIQILSPELFAGIPPGKFSLNPLWDRAIAAGRLFGLVYDGLWFDVGTPERLLAA 221
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 2-215 1.49e-92

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: 270.87  E-value: 1.49e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795   2 RAMILAAGRGERMRPLTDHTPKPLLPVGGRPLIEHHLLRLAAAGYRDIVINLAWLGDQIRATLGNGAHYGLRIHYSQEpD 81
Cdd:COG1208     1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRFGVRITYVDE-G 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795  82 GALETAGGIHHALPLLGAGPFLVVNGDIWCDHPLTP----HDPGGDLAHLVLVDNPPQHPHGDFALHGT-RIR------P 150
Cdd:COG1208    80 EPLGTGGALKRALPLLGDEPFLVLNGDILTDLDLAAllafHREKGADATLALVPVPDPSRYGVVELDGDgRVTrfvekpE 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1137421795 151 HDDNRLTYSGIGYYRPELFADVPDG-PQPLAPLLRHAISADRISGEHHHGLWADVGTPDRLHALNR 215
Cdd:COG1208   160 EPPSNLINAGIYVLEPEIFDYIPEGePFDLEDLLPRLIAEGRVYGYVHDGYWLDIGTPEDLLEANA 225
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 1-207 1.43e-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: 1.43e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795   1 MRAMILAAGRGERMRPLTDHTPKPLLPVGGRPLIEHHLLRLAAAGYRDIVINLAWLGDQIRATLGNGAHYGLRIHYSQ-- 78
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEKVREYFGDGSRGGVPIEYVVqe 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795  79 EPDGaleTAGGIHHALPLLgAGPFLVVNGDIWCDHPLTPH--DPGGDLAHLVLVDNPPQhpHGDFALHGTRIR------P 150
Cdd:TIGR03992  81 EQLG---TADALGSAKEYV-DDEFLVLNGDVLLDSDLLERliRAEAPAIAVVEVDDPSD--YGVVETDGGRVTgivekpE 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1137421795 151 HDDNRLTYSGIGYYRPELFADV------PDGPQPLAPLLRHAISADRISGEHHHGLWADVGTP 207
Cdd:TIGR03992 155 NPPSNLINAGIYLFSPEIFELLektklsPRGEYELTDALQLLIDEGKVKAVELDGFWLDVGRP 217
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-215 7.53e-23

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: 92.32  E-value: 7.53e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795   2 RAMILAAGRGERMRPLTDHTPKPLLPVGGR-PLIEHHLLRLAAAGYRD-IVINLAWLGDQIRATLGNGAHYGLRIHYSQE 79
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREiIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795  80 PDGaLETAGGIHHALPLLG--AGPFLVVNGDIWCDHPLTP----HDPGGDLAhLVLVDNPPQHPHGDFAL----HGTRIR 149
Cdd:pfam00483  81 PEG-KGTAPAVALAADFLGdeKSDVLVLGGDHIYRMDLEQavkfHIEKAADA-TVTFGIVPVEPPTGYGVvefdDNGRVI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795 150 -----PHDDNRLTY--SGIGYYRPELFADVPDGPQPLApllRHA---ISADRISGEHHHGL---------WADVGTPDRL 210
Cdd:pfam00483 159 rfvekPKLPKASNYasMGIYIFNSGVLDFLAKYLEELK---RGEdeiTDILPKALEDGKLAyafifkgyaWLDVGTWDSL 235


                  ....*
gi 1137421795 211 HALNR 215
Cdd:pfam00483 236 WEANL 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 2-80 7.90e-09

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 54.68  E-value: 7.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795   2 RAMILAAGRGERMRPLTDHTPKPLLPVGGRPLIEHHLLRLAAAGYRDI-VINLAWLGDQIRATLGNGAHYGLRIHYSQEP 80
Cdd:PRK15480    5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDIlIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84
 
Name Accession Description Interval E-value
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 2-213 1.45e-92

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: 270.21  E-value: 1.45e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795   2 RAMILAAGRGERMRPLTDHTPKPLLPVGGRPLIEHHLLRLAAAGYRDIVINLAWLGDQIRATLGNgAHYGLRIHYSQEPD 81
Cdd:cd06422     1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHLGD-SRFGLRITISDEPD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795  82 GALETAGGIHHALPLLGAGPFLVVNGDIWCDHPLTP------HDPGGDLAHLVLVDNPPQHPHGDFALHG----TRIRPH 151
Cdd:cd06422    80 ELLETGGGIKKALPLLGDEPFLVVNGDILWDGDLAPllllhaWRMDALLLLLPLVRNPGHNGVGDFSLDAdgrlRRGGGG 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1137421795 152 DDNRLTYSGIGYYRPELFADVPDGPQPLAPLLRHAISADRISGEHHHGLWADVGTPDRLHAL 213
Cdd:cd06422   160 AVAPFTFTGIQILSPELFAGIPPGKFSLNPLWDRAIAAGRLFGLVYDGLWFDVGTPERLLAA 221
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 2-215 1.49e-92

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: 270.87  E-value: 1.49e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795   2 RAMILAAGRGERMRPLTDHTPKPLLPVGGRPLIEHHLLRLAAAGYRDIVINLAWLGDQIRATLGNGAHYGLRIHYSQEpD 81
Cdd:COG1208     1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRFGVRITYVDE-G 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795  82 GALETAGGIHHALPLLGAGPFLVVNGDIWCDHPLTP----HDPGGDLAHLVLVDNPPQHPHGDFALHGT-RIR------P 150
Cdd:COG1208    80 EPLGTGGALKRALPLLGDEPFLVLNGDILTDLDLAAllafHREKGADATLALVPVPDPSRYGVVELDGDgRVTrfvekpE 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1137421795 151 HDDNRLTYSGIGYYRPELFADVPDG-PQPLAPLLRHAISADRISGEHHHGLWADVGTPDRLHALNR 215
Cdd:COG1208   160 EPPSNLINAGIYVLEPEIFDYIPEGePFDLEDLLPRLIAEGRVYGYVHDGYWLDIGTPEDLLEANA 225
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 3-205 1.90e-51

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: 165.83  E-value: 1.90e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795   3 AMILAAGRGERMRPLTDHTPKPLLPVGGRPLIEHHLLRLAAAGYRDIVINLAWLGDQIRATLGNGAHYGLRIHYSQEPDg 82
Cdd:cd04181     1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGSKFGVNIEYVVQEE- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795  83 ALETAGGIHHALPLLGAGPFLVVNGDIWCDHPLTP----HDPGGDLAHLVLVDNPPQHPHGDFALHG----TRIR---PH 151
Cdd:cd04181    80 PLGTAGAVRNAEDFLGDDDFLVVNGDVLTDLDLSEllrfHREKGADATIAVKEVEDPSRYGVVELDDdgrvTRFVekpTL 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1137421795 152 DDNRLTYSGIGYYRPELFADVPDGPQP----LAPLLRHAISADRISGEHHHGLWADVG 205
Cdd:cd04181   160 PESNLANAGIYIFEPEILDYIPEILPRgedeLTDAIPLLIEEGKVYGYPVDGYWLDIG 217
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 3-208 1.94e-35

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: 124.97  E-value: 1.94e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795   3 AMILAAGRGERMRPLTDHTPKPLLPVGGRPLIEHHLLRLAAAGYRDIVINLAWLGDQIRATLGNGAHYGLRIHYSQEPDg 82
Cdd:cd06915     1 AVILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYLAEQIEEYFGDGYRGGIRIYYVIEPE- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795  83 ALETAGGIHHALPLLGAGPFLVVNGDIWCD----HPLTPHDPGGDLAHLVLVDNPPQHPHGDFALH-GTRI------RPH 151
Cdd:cd06915    80 PLGTGGAIKNALPKLPEDQFLVLNGDTYFDvdllALLAALRASGADATMALRRVPDASRYGNVTVDgDGRViafvekGPG 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1137421795 152 DDNRLTYSGIGYYRPELFADVPDGPQPL-APLLRHAISADRISGEHHHGLWADVGTPD 208
Cdd:cd06915   160 AAPGLINGGVYLLRKEILAEIPADAFSLeADVLPALVKRGRLYGFEVDGYFIDIGIPE 217
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 1-207 1.43e-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: 1.43e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795   1 MRAMILAAGRGERMRPLTDHTPKPLLPVGGRPLIEHHLLRLAAAGYRDIVINLAWLGDQIRATLGNGAHYGLRIHYSQ-- 78
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEKVREYFGDGSRGGVPIEYVVqe 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795  79 EPDGaleTAGGIHHALPLLgAGPFLVVNGDIWCDHPLTPH--DPGGDLAHLVLVDNPPQhpHGDFALHGTRIR------P 150
Cdd:TIGR03992  81 EQLG---TADALGSAKEYV-DDEFLVLNGDVLLDSDLLERliRAEAPAIAVVEVDDPSD--YGVVETDGGRVTgivekpE 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1137421795 151 HDDNRLTYSGIGYYRPELFADV------PDGPQPLAPLLRHAISADRISGEHHHGLWADVGTP 207
Cdd:TIGR03992 155 NPPSNLINAGIYLFSPEIFELLektklsPRGEYELTDALQLLIDEGKVKAVELDGFWLDVGRP 217
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 3-109 1.87e-33

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: 119.54  E-value: 1.87e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795   3 AMILAAGRGERMRPLTDHTPKPLLPVGGRPLIEHHLLRLAAAGYRDIVINLAWLGDQIRATLGNGAHYGLRIHYSQEpDG 82
Cdd:cd06426     1 VVIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNYLAEMIEDYFGDGSKFGVNISYVRE-DK 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 1137421795  83 ALETAGgihhALPLLG---AGPFLVVNGDI 109
Cdd:cd06426    80 PLGTAG----ALSLLPekpTDPFLVMNGDI 105
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 1-215 4.08e-33

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: 119.21  E-value: 4.08e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795   1 MRAMILAAGRGERMRPLTDHTPKPLLPVGGRPLIEHHLLRLAAAGYRDIVINLAWLGDQIRATLGNGAHYGLRIHY--SQ 78
Cdd:cd04189     1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEALGDGSRFGVRITYilQE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795  79 EPDGaleTAGGIHHALPLLGAGPFLVVNGDIWCDHPLTPH-----DPGGDlAHLVL--VDNP------------------ 133
Cdd:cd04189    81 EPLG---LAHAVLAARDFLGDEPFVVYLGDNLIQEGISPLvrdflEEDAD-ASILLaeVEDPrrfgvavvddgrivrlve 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795 134 -PQHPHGDFALHGTRI-RP--HDD-NRLTYSgigyYRPELfaDVPDGPQPLapllrhaISADRISGEH-HHGLWADVGTP 207
Cdd:cd04189   157 kPKEPPSNLALVGVYAfTPaiFDAiSRLKPS----WRGEL--EITDAIQWL-------IDRGRRVGYSiVTGWWKDTGTP 223


                  ....*...
gi 1137421795 208 DRLHALNR 215
Cdd:cd04189   224 EDLLEANR 231
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
2-109 5.02e-29

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 108.40  E-value: 5.02e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795   2 RAMILAAGRGERMRPLTDHTPKPLLPVGGRPLIEHHLLRLAAAGYRDIVINLAWLGDQIRATLgngAHYGLRIHYSQEPD 81
Cdd:COG1213     1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEAL---ARPGPDVTFVYNPD 77

                          90       100
                  ....*....|....*....|....*....
gi 1137421795  82 GAL-ETAGGIHHALPLLGaGPFLVVNGDI 109
Cdd:COG1213    78 YDEtNNIYSLWLAREALD-EDFLLLNGDV 105
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 1-116 7.74e-27

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: 102.67  E-value: 7.74e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795   1 MRAMILAAGRGERMRPLTDHTPKPLLPVGGRPLIEHHLLRLAAAGYRDIVINLAWLGDQIRATLGN-GAHYGLRIHYSQE 79
Cdd:cd06425     1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYRPEDMVPFLKEyEKKLGIKITFSIE 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1137421795  80 pDGALETAGGIHHALPLLGAG--PFLVVNGDIWCDHPLT 116
Cdd:cd06425    81 -TEPLGTAGPLALARDLLGDDdePFFVLNSDVICDFPLA 118
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 3-110 2.76e-25

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: 98.46  E-value: 2.76e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795   3 AMILAAGRGERMRPLTDHTPKPLLPVGGRPLIEHHLLRLAAAGYRDIVINLAWLGDQIRATLgnGAHYGLRIHYSQEPDg 82
Cdd:cd02523     1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELL--KKYPNIKFVYNPDYA- 77

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1137421795  83 aleTAGGIH---HALPLLGaGPFLVVNGDIW 110
Cdd:cd02523    78 ---ETNNIYslyLARDFLD-EDFLLLEGDVV 104
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-108 3.08e-24

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 97.08  E-value: 3.08e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795   1 MRAMILAAGRGERMRPLTDHTPKPLLPVGGRPLIEHHLLRLAAAGYRDI-VINLAWLGDQIRATLGNGAHYGLRIHYS-- 77
Cdd:COG1209     1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREIlIISTPEDGPQFERLLGDGSQLGIKISYAvq 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1137421795  78 QEPDGaleTAGGIHHALPLLGAGPFLVVNGD 108
Cdd:COG1209    81 PEPLG---LAHAFIIAEDFIGGDPVALVLGD 108
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-215 7.53e-23

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: 92.32  E-value: 7.53e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795   2 RAMILAAGRGERMRPLTDHTPKPLLPVGGR-PLIEHHLLRLAAAGYRD-IVINLAWLGDQIRATLGNGAHYGLRIHYSQE 79
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREiIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795  80 PDGaLETAGGIHHALPLLG--AGPFLVVNGDIWCDHPLTP----HDPGGDLAhLVLVDNPPQHPHGDFAL----HGTRIR 149
Cdd:pfam00483  81 PEG-KGTAPAVALAADFLGdeKSDVLVLGGDHIYRMDLEQavkfHIEKAADA-TVTFGIVPVEPPTGYGVvefdDNGRVI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795 150 -----PHDDNRLTY--SGIGYYRPELFADVPDGPQPLApllRHA---ISADRISGEHHHGL---------WADVGTPDRL 210
Cdd:pfam00483 159 rfvekPKLPKASNYasMGIYIFNSGVLDFLAKYLEELK---RGEdeiTDILPKALEDGKLAyafifkgyaWLDVGTWDSL 235


                  ....*
gi 1137421795 211 HALNR 215
Cdd:pfam00483 236 WEANL 240
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 3-116 4.61e-19

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: 82.69  E-value: 4.61e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795   3 AMILAAG--RGERMRPLTDHTPKPLLPVGGRPLIEHHLLRLAA-AGYRDIVINLAWLGDQIRATLGNgAH--YGLRIHYS 77
Cdd:cd06428     1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKvPDLKEVLLIGFYPESVFSDFISD-AQqeFNVPIRYL 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1137421795  78 QEPDgALETAGGIHHALPLLGAGP---FLVVNGDIWCDHPLT 116
Cdd:cd06428    80 QEYK-PLGTAGGLYHFRDQILAGNpsaFFVLNADVCCDFPLQ 120
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 1-117 5.88e-18

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: 79.16  E-value: 5.88e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795   1 MRAMILAAGRGERMRPLTDHTPKPLLPVGGRPLIEHHLLRLAAAGYRDIVI-----NLawlgDQIRATLGNGAHYGLRIH 75
Cdd:cd02538     1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIistpeDL----PLFKELLGDGSDLGIRIT 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1137421795  76 YSQEPDgaletAGGIHHALPL----LGAGPFLVVNGD-IWCDHPLTP 117
Cdd:cd02538    77 YAVQPK-----PGGLAQAFIIgeefIGDDPVCLILGDnIFYGQGLSP 118
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 1-118 1.57e-15

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: 72.31  E-value: 1.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795   1 MRAMILAAGRGERMRPLTDHTPKPLLPVGGRPLIEHHLLRLAAAGYRDI-VINLAWLGDQIRATLGNGAHYGLRIHY--- 76
Cdd:cd04198     1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDViVVVPEEEQAEISTYLRSFPLNLKQKLDevt 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1137421795  77 --SQEPDGALETAGGIHHALPllgaGPFLVVNGDIWCDHPLTPH 118
Cdd:cd04198    81 ivLDEDMGTADSLRHIRKKIK----KDFLVLSCDLITDLPLIEL 120
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 3-118 5.38e-15

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: 70.75  E-value: 5.38e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795   3 AMILAAGRGERMRPLTDHTPKPLLPVGGRPLIEHHLLRLAAAGYRDIVINLAWLGDQIRATL----GNGAHYGLRIHY-- 76
Cdd:cd02507     3 AVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQAIIEHLlkskWSSLSSKMIVDVit 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1137421795  77 --SQEPDGaleTAGGIHHALPLLgAGPFLVVNGDIWCDHPLTPH 118
Cdd:cd02507    83 sdLCESAG---DALRLRDIRGLI-RSDFLLLSCDLVSNIPLSEL 122
LicC COG4750
CTP:phosphocholine cytidylyltransferase LicC [Cell wall/membrane/envelope biogenesis, Lipid ...
 1-51 1.19e-14

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


Pssm-ID: 443784 [Multi-domain]  Cd Length: 228  Bit Score: 70.24  E-value: 1.19e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1137421795   1 MRAMILAAGRGERMRPLTDHTPKPLLPVGGRPLIEHHLLRLAAAGYRDIVI 51
Cdd:COG4750     1 MNAIILAAGLGSRFAPITYETPKGLLKVNGEPLIERQIRQLHEAGITDITV 51
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 3-115 7.59e-14

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: 67.93  E-value: 7.59e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795   3 AMILAAGRGERMRpltDHTPKPLLPVGGRPLIEHHLLRLAAAGYRDIVINLAWLGDQIRATLGNgahYGLRIHYSQEPDG 82
Cdd:cd02540     1 AVILAAGKGTRMK---SDLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVKKALAN---PNVEFVLQEEQLG 74

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1137421795  83 aleTAGGIHHALPLLG--AGPFLVVNGdiwcDHPL 115
Cdd:cd02540    75 ---TGHAVKQALPALKdfEGDVLVLYG----DVPL 102
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 3-133 1.36e-12

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: 65.82  E-value: 1.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795   3 AMILAAGRGERMRpltDHTPKPLLPVGGRPLIEHHLLRLAAAGYRDIVINLAWLGDQIRATLgngAHYGLRIHYSQEPDG 82
Cdd:COG1207     5 VVILAAGKGTRMK---SKLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVRAAL---ADLDVEFVLQEEQLG 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1137421795  83 aleTAggihHA----LPLLGA--GPFLVVNGDIwcdhPL-----------TPHDPGGDLAHL-VLVDNP 133
Cdd:COG1207    79 ---TG----HAvqqaLPALPGddGTVLVLYGDV----PLiraetlkallaAHRAAGAAATVLtAELDDP 136
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 3-115 2.55e-11

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: 59.52  E-value: 2.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795   3 AMILAAGRGERMRpltdhTPKPLLPVGGRPLIEHHLLRLAAAGyRDIVINLAWlgDQIRATLgngAHYGLRIHYSQEPDG 82
Cdd:pfam12804   1 AVILAGGRSSRMG-----GDKALLPLGGKPLLERVLERLRPAG-DEVVVVAND--EEVLAAL---AGLGVPVVPDPDPGQ 69

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1137421795  83 AleTAGGIHHALP-LLGAGPFLVVNgdiwCDHPL 115
Cdd:pfam12804  70 G--PLAGLLAALRaAPGADAVLVLA----CDMPF 97
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
3-81 3.10e-10

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 57.48  E-value: 3.10e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1137421795   3 AMILAAGRGERMrpltdHTPKPLLPVGGRPLIEHHLLRLAAAGYRDIVINLAWLGDQIRATLgngAHYGLRIHYSQEPD 81
Cdd:COG2068     6 AIILAAGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADAEEVAAAL---AGLGVRVVVNPDWE 76
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 1-116 3.63e-09

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: 55.23  E-value: 3.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795   1 MRAMILAAGRGERMRPLTDHTPKPLLPVGGRPLIEHHLLRLAAAGYRDIVI---------------------NLAWLGDQ 59
Cdd:cd02541     1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIvtgrgkraiedhfdrsyeleeTLEKKGKT 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1137421795  60 IRATLGNGAHYGLRIHY--SQEPDGaLETAggIHHALPLLGAGPFLVVNGD--IWCDHPLT 116
Cdd:cd02541    81 DLLEEVRIISDLANIHYvrQKEPLG-LGHA--VLCAKPFIGDEPFAVLLGDdlIDSKEPCL 138
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
 3-61 5.95e-09

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: 54.50  E-value: 5.95e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1137421795   3 AMILAAGRGERMRPLTDHTPKPLLPVGGRPLIEHHLLRLAAAGYRDIVINLAWLGDQIR 61
Cdd:cd02524     1 VVILAGGLGTRLSEETELKPKPMVEIGGRPILWHIMKIYSHYGHNDFILCLGYKGHVIK 59
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 2-80 7.90e-09

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 54.68  E-value: 7.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795   2 RAMILAAGRGERMRPLTDHTPKPLLPVGGRPLIEHHLLRLAAAGYRDI-VINLAWLGDQIRATLGNGAHYGLRIHYSQEP 80
Cdd:PRK15480    5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDIlIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 3-79 1.19e-08

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: 52.95  E-value: 1.19e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1137421795   3 AMILAAGRGERMrpltdHTPKPLLPVGGRPLIEHHLLRLAAAGYRDIVINLAWLGDQIRATLGNGAHYGLRIHYSQE 79
Cdd:cd04182     3 AIILAAGRSSRM-----GGNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALAGLPVVVVINPDWEE 74
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
 5-211 5.62e-08

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: 51.49  E-value: 5.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795   5 ILAAGRGERMRPLTDHTPKPLLPVGGRPLIEHHLLRLAAagYRDIVINLAWLGDQIRAT-LGN---GAHYGLRIH-YSQE 79
Cdd:cd04183     3 IPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEWVIESLAK--IFDSRFIFICRDEHNTKFhLDEslkLLAPNATVVeLDGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795  80 PDGALETAGGIHHALPllGAGPFLVVNGDIWCDHPLTPH-----DPGGDLAHLVLvdnPPQHPHGDFAL---HGTRIRPH 151
Cdd:cd04183    81 TLGAACTVLLAADLID--NDDPLLIFNCDQIVESDLLAFlaafrERDLDGGVLTF---FSSHPRWSYVKldeNGRVIETA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795 152 DDNR---LTYSGIGYYRP-ELFADV------PDGPQP----LAPLLRHAIS------ADRISGEHHHGLwadvGTPDRLH 211
Cdd:cd04183   156 EKEPisdLATAGLYYFKSgSLFVEAakkmirKDDSVNgefyISPLYNELILdgkkvgIYLIDKDDYHSF----GTPEDLE 231
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 1-172 9.13e-08

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: 50.27  E-value: 9.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795   1 MRAMILAAGRGERMrpltdHTPKPLLPVGGRPLIEHHLLRLAAAGyRDIVINlawlgdqIRATLGNGAHYGLRIHYSQEP 80
Cdd:cd02503     1 ITGVILAGGKSRRM-----GGDKALLELGGKPLLEHVLERLKPLV-DEVVIS-------ANRDQERYALLGVPVIPDEPP 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795  81 D-GALetaGGIHHALPLLGAGPFLVVNGDiwcdhplTPHDPGGDLAHLVLVDNPPQHPHgdFALHGTRIRPhddnrLtys 159
Cdd:cd02503    68 GkGPL---AGILAALRAAPADWVLVLACD-------MPFLPPELLERLLAAAEEGADAV--VPKSGGRLQP-----L--- 127

                         170
                  ....*....|...
gi 1137421795 160 gIGYYRPELFADV 172
Cdd:cd02503   128 -HALYHKSLLPAL 139
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 3-31 1.56e-07

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 50.84  E-value: 1.56e-07
                          10        20
                  ....*....|....*....|....*....
gi 1137421795   3 AMILAAGRGERMRPLTDHTPKPLLPVGGR 31
Cdd:COG0448     4 AIILAGGRGSRLGPLTKDRAKPAVPFGGK 32
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-108 2.27e-07

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 50.60  E-value: 2.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795   3 AMILAAGRGERMRplTDHtPKPLLPVGGRPLIEHHLLRLAAAGYRDIVINLAWLGDQIRATLGNGAHYGLrihysQEPDg 82
Cdd:PRK14354    5 AIILAAGKGTRMK--SKL-PKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVGHGAEEVKEVLGDRSEFAL-----QEEQ- 75

                          90       100
                  ....*....|....*....|....*...
gi 1137421795  83 aLETAGGIHHALPLLG--AGPFLVVNGD 108
Cdd:PRK14354   76 -LGTGHAVMQAEEFLAdkEGTTLVICGD 102
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 6-109 3.06e-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: 48.73  E-value: 3.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795   6 LAAGRGERMrpltDHTPKPLLPVGGRPLIEHHLLRLAAAGYRDIVInlawlgdqirATLGNgaHYGLRIHYSQEPDGALE 85
Cdd:COG2266     1 MAGGKGTRL----GGGEKPLLEICGKPMIDRVIDALEESCIDKIYV----------AVSPN--TPKTREYLKERGVEVIE 64

                          90       100
                  ....*....|....*....|....*....
gi 1137421795  86 TAGG-----IHHALPLLGaGPFLVVNGDI 109
Cdd:COG2266    65 TPGEgyvedLNEALESIS-GPVLVVPADL 92
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 3-108 3.81e-07

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


Pssm-ID: 440509 [Multi-domain]  Cd Length: 188  Bit Score: 48.65  E-value: 3.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795   3 AMILAAGRGERMrpltdHTPKPLLPVGGRPLIEHHLLRLAAAGyRDIVINlawlgdqiratlGNG----AHYGLRIHYSQ 78
Cdd:COG0746     7 GVILAGGRSRRM-----GQDKALLPLGGRPLLERVLERLRPQV-DEVVIV------------ANRperyAALGVPVVPDD 68

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1137421795  79 EPD-GALetaGGIHHALPLLGAGPFLVVNGD 108
Cdd:COG0746    69 PPGaGPL---AGILAALEAAPAEWVLVLACD 96
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 3-74 4.09e-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: 49.06  E-value: 4.09e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1137421795   3 AMILAAGRGERMRPLTdhtPKPLLPVGGRPLIEHHLLRLAAAGYRD---IVINLAWLgDQIRATLGNGAHYGLRI 74
Cdd:cd02516     3 AIILAAGSGSRMGADI---PKQFLELGGKPVLEHTLEAFLAHPAIDeivVVVPPDDI-DLAKELAKYGLSKVVKI 73
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 5-51 4.64e-07

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: 48.59  E-value: 4.64e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1137421795   5 ILAAGRGERMRpltDHTPKPLLPVGGRPLIEHHLLRLAAAGYRD-IVI 51
Cdd:COG1211     2 IPAAGSGSRMG---AGIPKQFLPLGGKPVLEHTLEAFLAHPRIDeIVV 46
mobA PRK00317
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
 1-180 4.77e-07

molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed


Pssm-ID: 234725 [Multi-domain]  Cd Length: 193  Bit Score: 48.26  E-value: 4.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795   1 MRAMILAAGRGERMrpltDHTPKPLLPVGGRPLIEHHLLRLAAAgYRDIVINLAwlGDQIRAtlgngAHYGLRIHYSQEP 80
Cdd:PRK00317    4 ITGVILAGGRSRRM----GGVDKGLQELNGKPLIQHVIERLAPQ-VDEIVINAN--RNLARY-----AAFGLPVIPDSLA 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795  81 D--GALetaGGIHHALPLLGAGPFLVVNgdiwCDHPLTPHD-------PGGDLAHLVLVDNPPQHPHGDFALHGTRIRPH 151
Cdd:PRK00317   72 DfpGPL---AGILAGLKQARTEWVLVVP----CDTPFIPPDlvarlaqAAGKDDADVAWAHDGGRLHPTFALYSVALLPD 144

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1137421795 152 DDNRLTySGIgyYRPELF--------ADVPDGPQPLA 180
Cdd:PRK00317  145 LEAYLA-AGE--RKVMAFyarhggvaVDFSDPKDAFF 178
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
 3-31 9.18e-07

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: 47.54  E-value: 9.18e-07
                          10        20
                  ....*....|....*....|....*....
gi 1137421795   3 AMILAAGRGERMRPLTDHTPKPLLPVGGR 31
Cdd:cd02508     1 AIILAGGEGTRLSPLTKKRAKPAVPFGGR 29
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-139 1.27e-06

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 48.32  E-value: 1.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795   3 AMILAAGRGERMRpltDHTPKPLLPVGGRPLIEHHLLRLAAAGYRDIVINLAWLGDQIRATLgnGAHYGLRIHYSQEPdg 82
Cdd:PRK14353    8 AIILAAGEGTRMK---SSLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGPGAEAVAAAA--AKIAPDAEIFVQKE-- 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1137421795  83 ALETAGGIHHALPLL--GAGPFLVVNGdiwcDHPLTPH-------DPGGDLAHLVLVDNPPQHPHG 139
Cdd:PRK14353   81 RLGTAHAVLAAREALagGYGDVLVLYG----DTPLITAetlarlrERLADGADVVVLGFRAADPTG 142
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 3-62 1.53e-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: 47.22  E-value: 1.53e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795   3 AMILAAGRGERMRPLTDHTPKPLLPVGGRPLIEHHLLRLAAAGYRDIVINLAWLGDQIRA 62
Cdd:cd04197     3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQIKE 62
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
3-58 3.31e-06

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 46.28  E-value: 3.31e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1137421795   3 AMILAAGRGERMRplTDhTPKPLLPVGGRPLIEHHLLRLAAAGYRD---IVINLAWLGD 58
Cdd:PRK00155    6 AIIPAAGKGSRMG--AD-RPKQYLPLGGKPILEHTLEAFLAHPRIDeiiVVVPPDDRPD 61
ispD TIGR00453
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ...
 3-51 7.33e-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: 45.36  E-value: 7.33e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1137421795   3 AMILAAGRGERMRPltdHTPKPLLPVGGRPLIEHHLLRLAAAGYRDIVI 51
Cdd:TIGR00453   2 AVIPAAGRGTRFGS---GVPKQYLELGGRPLLEHALDAFLAHPAIDEVV 47
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
3-51 8.49e-06

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


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 45.41  E-value: 8.49e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1137421795   3 AMILAAGRGERMRPLTDHTPKPLLPVGGRPLIEHHLLRLAAAGYRDIVI 51
Cdd:COG1210     6 AVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIF 54
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
 3-30 1.49e-05

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 44.83  E-value: 1.49e-05
                          10        20
                  ....*....|....*....|....*...
gi 1137421795   3 AMILAAGRGERMRPLTDHTPKPLLPVGG 30
Cdd:PRK00725   18 ALILAGGRGSRLKELTDKRAKPAVYFGG 45
PRK14489 PRK14489
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; ...
 3-165 1.79e-05

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


Pssm-ID: 237727 [Multi-domain]  Cd Length: 366  Bit Score: 44.74  E-value: 1.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795   3 AMILAAGRGERMrpltDHTPKPLLPVGGRPLIEHHLLRLAAAgYRDIVINLAwlGDQIR-ATLGNGAHYglrihYSQEPD 81
Cdd:PRK14489    8 GVILAGGLSRRM----NGRDKALILLGGKPLIERVVDRLRPQ-FARIHLNIN--RDPARyQDLFPGLPV-----YPDILP 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795  82 GALETAGGIHHALPLLGAGPFLVVNgdiwCDHPLTPHDPGGDLAHLVLVDNPP-------QHPHGDFALHGTRIRP---- 150
Cdd:PRK14489   76 GFQGPLSGILAGLEHADSEYLFVVA----CDTPFLPENLVKRLSKALAIEGADiavphdgERAHPLFALYHRSCLPalrr 151

                         170
                  ....*....|....*..
gi 1137421795 151 --HDDNRLTYSGIGYYR 165
Cdd:PRK14489  152 ylAEGERRLFDFFQRQR 168
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 3-51 3.14e-05

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 44.05  E-value: 3.14e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1137421795   3 AMILAAGRGERMRPLTDHTPKPLLPVGGR-PLIEHHLLRLAAAGYRDIVI 51
Cdd:PRK00844    8 AIVLAGGEGKRLMPLTADRAKPAVPFGGSyRLIDFVLSNLVNSGYLRIYV 57
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
1-51 5.82e-05

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 42.95  E-value: 5.82e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1137421795   1 MRAMILAAGRGERMRPLTDHTPKPLLPVGGRPLIEHHLLRLAAAGYRDIVI 51
Cdd:PRK10122    4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVL 54
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
2-51 1.15e-04

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 42.20  E-value: 1.15e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1137421795   2 RAMILAAGRGERMRPLTDHTPKPLLPVGGRPLIEHHLLRLAAAGYRDIVI 51
Cdd:PRK13389   10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVL 59
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 1-31 1.25e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 42.16  E-value: 1.25e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1137421795   1 MRAMILAAGRGERMRPLTDHTPKPLLPVGGR 31
Cdd:PRK05293    4 MLAMILAGGQGTRLGKLTKNIAKPAVPFGGK 34
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 5-109 1.52e-04

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 41.84  E-value: 1.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795   5 ILAAGRGERMRpltDHTPKPLLPVGGRPLIEH-----HLL----RLAAAGYRdivinlawlGDQIRATLgngAHYGlRIH 75
Cdd:PRK14360    6 ILAAGKGTRMK---SSLPKVLHPLGGKSLVERvldscEELkpdrRLVIVGHQ---------AEEVEQSL---AHLP-GLE 69

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1137421795  76 Y-SQEPDgaLETAGGIHHALPLLGA--GPFLVVNGDI 109
Cdd:PRK14360   70 FvEQQPQ--LGTGHAVQQLLPVLKGfeGDLLVLNGDV 104
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
 1-52 1.59e-04

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: 41.79  E-value: 1.59e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1137421795   1 MRAMILAAGRGERMRPL-TDHTPKPLLPV-GGRPLIEHHLLRLAAAGYRD---IVIN 52
Cdd:cd02509     1 IYPVILAGGSGTRLWPLsRESYPKQFLKLfGDKSLLQQTLDRLKGLVPPDrilVVTN 57
matur_MocA_YgfJ TIGR03310
molybdenum cofactor cytidylyltransferase; Members of this protein include MocA, which ...
 3-103 4.17e-04

molybdenum cofactor cytidylyltransferase; Members of this protein include MocA, which transfers cytosine from CTP to molybdopterin during molybdopterin cytosine dinucleotide (MCD) cofactor biosynthesis. It is distantly related to MobA, the GTP:molybdopterin guanylyltransferase. The MocA family is particularly closely related in phylogenetic distribution to other markers of selenium-dependent molybdenum hydroxylases (SDMH), suggesting most SDMH must use MCD rather than molybdopterin guanine dinucleotide.


Pssm-ID: 274516  Cd Length: 188  Bit Score: 40.02  E-value: 4.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795   3 AMILAAGRGERMRpltdhTPKPLLPVGGRPLIEHHLLR-LAAAGYRDIVInlawLGDQI-RATLGNGAHYGLRI----HY 76
Cdd:TIGR03310   2 AIILAAGLSSRMG-----QNKLLLPYKGKTILEHVVDNaLRLFFDEVILV----LGHEAdELVALLANHSNITLvhnpQY 72

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1137421795  77 ----SQEPDGALETAGGIHHALPLLGAGPFL 103
Cdd:TIGR03310  73 aegqSSSIKLGLELPVQSDGYLFLLGDQPFV 103
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 1-108 5.03e-04

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 40.35  E-value: 5.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795   1 MRAMILAAGRGERMRpltDHTPKPLLPVGGRPLIEHHLLRLAAAGYRDIVINLAWLGDQIRATL-GNGAHYGLRIHYSQE 79
Cdd:PRK14358    8 LDVVILAAGQGTRMK---SALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGAEQVEAALqGSGVAFARQEQQLGT 84

                          90       100
                  ....*....|....*....|....*....
gi 1137421795  80 PDGALETAGGIHHalpllGAGPFLVVNGD 108
Cdd:PRK14358   85 GDAFLSGASALTE-----GDADILVLYGD 108
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-108 6.24e-04

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 40.09  E-value: 6.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795   3 AMILAAGRGERMRpltDHTPKPLLPVGGRPLIEHHLLRLAAAGYRDIVINLAWLGDQIRATLgngAHYGLRIHYSQEpdg 82
Cdd:PRK14356    8 ALILAAGKGTRMH---SDKPKVLQTLLGEPMLRFVYRALRPLFGDNVWTVVGHRADMVRAAF---PDEDARFVLQEQ--- 78

                          90       100
                  ....*....|....*....|....*....
gi 1137421795  83 ALETAGGIHHALPLL---GAGPFLVVNGD 108
Cdd:PRK14356   79 QLGTGHALQCAWPSLtaaGLDRVLVVNGD 107
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-109 7.69e-04

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 39.92  E-value: 7.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795   3 AMILAAGRGERMRpltDHTPKPLLPVGGRPLIEHHLLRLAAAGYRDIVINLAWLGDQIRATLGNGAHyGLRIHYSQEPDG 82
Cdd:PRK14352    7 VIVLAAGAGTRMR---SDTPKVLHTLAGRSMLGHVLHAAAGLAPQHLVVVVGHDRERVAPAVAELAP-EVDIAVQDEQPG 82

                          90       100       110
                  ....*....|....*....|....*....|
gi 1137421795  83 ---ALETAggiHHALPLLGAGPFLVVNGDI 109
Cdd:PRK14352   83 tghAVQCA---LEALPADFDGTVVVTAGDV 109
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-109 1.77e-03

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 38.96  E-value: 1.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137421795   3 AMILAAGRGERMRpltDHTPKPLLPVGGRPLIEHHLLRLAAAGYRDIVINLAWLGDQIRATLGNGAHYGLRIHYSQepdg 82
Cdd:PRK14355    6 AIILAAGKGTRMK---SDLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHFAGDGDVSFALQEEQ---- 78

                          90       100
                  ....*....|....*....|....*....
gi 1137421795  83 aLETAGGIHHALPLL--GAGPFLVVNGDI 109
Cdd:PRK14355   79 -LGTGHAVACAAPALdgFSGTVLILCGDV 106
ispDF PRK09382
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ...
 3-51 2.97e-03

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


Pssm-ID: 236492 [Multi-domain]  Cd Length: 378  Bit Score: 37.90  E-value: 2.97e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1137421795   3 AMILAAGRGERMRPltdHTPKPLLPVGGRPLIEHHLLRLAAAGYRDIVI 51
Cdd:PRK09382    8 LVIVAAGRSTRFSA---EVKKQWLRIGGKPLWLHVLENLSSAPAFKEIV 53
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-66 3.34e-03

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 38.08  E-value: 3.34e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1137421795   1 MRAMILAAGRGERMrpLTDhTPKPLLPVGGRPLIEHHLLRLAAAGYRDIVINLAWLGDQIRATLGN 66
Cdd:PRK09451    6 MSVVILAAGKGTRM--YSD-LPKVLHTLAGKPMVQHVIDAANELGAQHVHLVYGHGGDLLKQTLAD 68
IspD pfam01128
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ...
 3-51 4.03e-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: 37.04  E-value: 4.03e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1137421795   3 AMILAAGRGERMRplTDHtPKPLLPVGGRPLIEHHLLRLAAAGYRDIVI 51
Cdd:pfam01128   1 AVIPAAGSGKRMG--AGV-PKQFLQLLGQPLLEHTVDAFLASPVVDRIV 46
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-68 7.03e-03

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 37.05  E-value: 7.03e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1137421795   1 MRAMILAAGRGERMRpltDHTPKPLLPVGGRPLIEHhllrlaaagyrdiVINLAW-LGDQIRATLGNGA 68
Cdd:PRK14357    1 MRALVLAAGKGTRMK---SKIPKVLHKISGKPMINW-------------VIDTAKkVAQKVGVVLGHEA 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.
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