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Conserved domains on  [gi|1403366218|emb|SQG00725|]
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nucleotidyl transferase [Paucimonas lemoignei]

Protein Classification

NDP-sugar synthase( domain architecture ID 11440233)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
2-223 1.57e-96

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: 281.27  E-value: 1.57e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403366218   2 KAMILAAGKGERMRPLTLHTPKPLVRAGGVPLIEYHLRALHEAGFHEVVINHAWLGQQIEDHLGDGERFGLRIAYSPEGE 81
Cdd:COG1208     1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRFGVRITYVDEGE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403366218  82 PLETGGGIHRALPLLGDEPFLVVNGDVWTDYPFKALR---MPLAGLAHLVLINNPAHHPEGDFSLI-DGQVRD----SRD 153
Cdd:COG1208    81 PLGTGGALKRALPLLGDEPFLVLNGDILTDLDLAALLafhREKGADATLALVPVPDPSRYGVVELDgDGRVTRfvekPEE 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1403366218 154 AGTRLTYSGIAVLHPKLFAGCQEG-AFKLAPLLRTAMEQGQVTGEHFTGRWVDVGTHERLAEVERLLVAGR 223
Cdd:COG1208   161 PPSNLINAGIYVLEPEIFDYIPEGePFDLEDLLPRLIAEGRVYGYVHDGYWLDIGTPEDLLEANALLLSGK 231
 
Name Accession Description Interval E-value
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
2-223 1.57e-96

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: 281.27  E-value: 1.57e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403366218   2 KAMILAAGKGERMRPLTLHTPKPLVRAGGVPLIEYHLRALHEAGFHEVVINHAWLGQQIEDHLGDGERFGLRIAYSPEGE 81
Cdd:COG1208     1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRFGVRITYVDEGE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403366218  82 PLETGGGIHRALPLLGDEPFLVVNGDVWTDYPFKALR---MPLAGLAHLVLINNPAHHPEGDFSLI-DGQVRD----SRD 153
Cdd:COG1208    81 PLGTGGALKRALPLLGDEPFLVLNGDILTDLDLAALLafhREKGADATLALVPVPDPSRYGVVELDgDGRVTRfvekPEE 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1403366218 154 AGTRLTYSGIAVLHPKLFAGCQEG-AFKLAPLLRTAMEQGQVTGEHFTGRWVDVGTHERLAEVERLLVAGR 223
Cdd:COG1208   161 PPSNLINAGIYVLEPEIFDYIPEGePFDLEDLLPRLIAEGRVYGYVHDGYWLDIGTPEDLLEANALLLSGK 231
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
2-214 5.19e-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: 269.06  E-value: 5.19e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403366218   2 KAMILAAGKGERMRPLTLHTPKPLVRAGGVPLIEYHLRALHEAGFHEVVINHAWLGQQIEDHLGDgERFGLRIAYSPE-G 80
Cdd:cd06422     1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHLGD-SRFGLRITISDEpD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403366218  81 EPLETGGGIHRALPLLGDEPFLVVNGDVWTDYPF------KALRMPlAGLAHLVLINNPAHHPEGDFSLI-DGQVRDSRD 153
Cdd:cd06422    80 ELLETGGGIKKALPLLGDEPFLVVNGDILWDGDLapllllHAWRMD-ALLLLLPLVRNPGHNGVGDFSLDaDGRLRRGGG 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1403366218 154 AGT-RLTYSGIAVLHPKLFAGCQEGAFKLAPLLRTAMEQGQVTGEHFTGRWVDVGTHERLAE 214
Cdd:cd06422   159 GAVaPFTFTGIQILSPELFAGIPPGKFSLNPLWDRAIAAGRLFGLVYDGLWFDVGTPERLLA 220
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
1-207 2.98e-36

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: 131.18  E-value: 2.98e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403366218   1 MKAMILAAGKGERMRPLTLHTPKPLVRAGGVPLIEYHLRALHEAGFHEVVINHAWLGQQIEDHLGDGERFGLRIAYSPEG 80
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEKVREYFGDGSRGGVPIEYVVQE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403366218  81 EPLETGGGIHRALPLLgDEPFLVVNGDVWTDYPF--KALRMPLAGLAhLVLINNPAHHpeGDFSLIDGQVRD----SRDA 154
Cdd:TIGR03992  81 EQLGTADALGSAKEYV-DDEFLVLNGDVLLDSDLleRLIRAEAPAIA-VVEVDDPSDY--GVVETDGGRVTGivekPENP 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1403366218 155 GTRLTYSGIAVLHPKLFAGCQE------GAFKLAPLLRTAMEQGQVTGEHFTGRWVDVG 207
Cdd:TIGR03992 157 PSNLINAGIYLFSPEIFELLEKtklsprGEYELTDALQLLIDEGKVKAVELDGFWLDVG 215
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
2-215 5.14e-26

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


Pssm-ID: 425709 [Multi-domain]  Cd Length: 243  Bit Score: 100.79  E-value: 5.14e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403366218   2 KAMILAAGKGERMRPLTLHTPKPLV-RAGGVPLIEYHLRALHEAGFHE-VVINHAWLGQQIEDHLGDGERFGLRIAYSPE 79
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVpVGGKYPLIDYPLSRLANAGIREiIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403366218  80 GEPLETGGGIHRALPLLGDE--PFLVVNGDVWTDYPFK-ALR--MPLAGLAhLVLINNPAHHPEGDFSLI----DGQVRD 150
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEksDVLVLGGDHIYRMDLEqAVKfhIEKAADA-TVTFGIVPVEPPTGYGVVefddNGRVIR 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1403366218 151 -----SRDAGTRLTYSGIAVLHPKLF---AGCQEGAFKLAP----LLRTAMEQGQVTGEH-FTG-RWVDVGTHERLAEV 215
Cdd:pfam00483 160 fvekpKLPKASNYASMGIYIFNSGVLdflAKYLEELKRGEDeitdILPKALEDGKLAYAFiFKGyAWLDVGTWDSLWEA 238
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
3-107 1.36e-07

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 51.37  E-value: 1.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403366218   3 AMILAAGKGERMRPltlHTPKPLVRAGGVPLIEYHLRALHEAGFHE--VVINHAwlGQQIEDHLGDgerfglRIAYSPEG 80
Cdd:PRK14354    5 AIILAAGKGTRMKS---KLPKVLHKVCGKPMVEHVVDSVKKAGIDKivTVVGHG--AEEVKEVLGD------RSEFALQE 73
                          90       100
                  ....*....|....*....|....*....
gi 1403366218  81 EPLETGGGIHRALPLLGDEP--FLVVNGD 107
Cdd:PRK14354   74 EQLGTGHAVMQAEEFLADKEgtTLVICGD 102
 
Name Accession Description Interval E-value
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
2-223 1.57e-96

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: 281.27  E-value: 1.57e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403366218   2 KAMILAAGKGERMRPLTLHTPKPLVRAGGVPLIEYHLRALHEAGFHEVVINHAWLGQQIEDHLGDGERFGLRIAYSPEGE 81
Cdd:COG1208     1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRFGVRITYVDEGE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403366218  82 PLETGGGIHRALPLLGDEPFLVVNGDVWTDYPFKALR---MPLAGLAHLVLINNPAHHPEGDFSLI-DGQVRD----SRD 153
Cdd:COG1208    81 PLGTGGALKRALPLLGDEPFLVLNGDILTDLDLAALLafhREKGADATLALVPVPDPSRYGVVELDgDGRVTRfvekPEE 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1403366218 154 AGTRLTYSGIAVLHPKLFAGCQEG-AFKLAPLLRTAMEQGQVTGEHFTGRWVDVGTHERLAEVERLLVAGR 223
Cdd:COG1208   161 PPSNLINAGIYVLEPEIFDYIPEGePFDLEDLLPRLIAEGRVYGYVHDGYWLDIGTPEDLLEANALLLSGK 231
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
2-214 5.19e-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: 269.06  E-value: 5.19e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403366218   2 KAMILAAGKGERMRPLTLHTPKPLVRAGGVPLIEYHLRALHEAGFHEVVINHAWLGQQIEDHLGDgERFGLRIAYSPE-G 80
Cdd:cd06422     1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHLGD-SRFGLRITISDEpD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403366218  81 EPLETGGGIHRALPLLGDEPFLVVNGDVWTDYPF------KALRMPlAGLAHLVLINNPAHHPEGDFSLI-DGQVRDSRD 153
Cdd:cd06422    80 ELLETGGGIKKALPLLGDEPFLVVNGDILWDGDLapllllHAWRMD-ALLLLLPLVRNPGHNGVGDFSLDaDGRLRRGGG 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1403366218 154 AGT-RLTYSGIAVLHPKLFAGCQEGAFKLAPLLRTAMEQGQVTGEHFTGRWVDVGTHERLAE 214
Cdd:cd06422   159 GAVaPFTFTGIQILSPELFAGIPPGKFSLNPLWDRAIAAGRLFGLVYDGLWFDVGTPERLLA 220
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
3-207 1.54e-55

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: 176.23  E-value: 1.54e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403366218   3 AMILAAGKGERMRPLTLHTPKPLVRAGGVPLIEYHLRALHEAGFHEVVINHAWLGQQIEDHLGDGERFGLRIAYSPEGEP 82
Cdd:cd04181     1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGSKFGVNIEYVVQEEP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403366218  83 LETGGGIHRALPLLGDEPFLVVNGDVWTDYPFKA-LRMPLAGLAHLVLINNPAHHPEgDFSLI----DGQVRD----SRD 153
Cdd:cd04181    81 LGTAGAVRNAEDFLGDDDFLVVNGDVLTDLDLSElLRFHREKGADATIAVKEVEDPS-RYGVVelddDGRVTRfvekPTL 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1403366218 154 AGTRLTYSGIAVLHPKLFAGCQEGAFK----LAPLLRTAMEQGQVTGEHFTGRWVDVG 207
Cdd:cd04181   160 PESNLANAGIYIFEPEILDYIPEILPRgedeLTDAIPLLIEEGKVYGYPVDGYWLDIG 217
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
3-214 5.33e-39

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: 134.22  E-value: 5.33e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403366218   3 AMILAAGKGERMRPLTLHTPKPLVRAGGVPLIEYHLRALHEAGFHEVVINHAWLGQQIEDHLGDGERFGLRIAYSPEGEP 82
Cdd:cd06915     1 AVILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYLAEQIEEYFGDGYRGGIRIYYVIEPEP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403366218  83 LETGGGIHRALPLLGDEPFLVVNGDVWTDYPFKALRMPLA---GLAHLVLINNPahhpegDFS-----LIDGQVR----D 150
Cdd:cd06915    81 LGTGGAIKNALPKLPEDQFLVLNGDTYFDVDLLALLAALRasgADATMALRRVP------DASrygnvTVDGDGRviafV 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1403366218 151 SRDAGTRLTY--SGIAVLHPKLFAGCQEGAFKL-APLLRTAMEQGQVTGEHFTGRWVDVGTHERLAE 214
Cdd:cd06915   155 EKGPGAAPGLinGGVYLLRKEILAEIPADAFSLeADVLPALVKRGRLYGFEVDGYFIDIGIPEDYAR 221
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
1-220 1.48e-36

G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family is the long form of Glucose-1-phosphate thymidylyltransferase. Glucose-1-phosphate thymidylyltransferase catalyses the formation of dTDP-glucose, from dTTP and glucose 1-phosphate. It is the first enzyme in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme.There are two forms of Glucose-1-phosphate thymidylyltransferase in bacteria and archeae; short form and long form. The long form, which has an extra 50 amino acids c-terminal, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced.The long from enzymes also have a left-handed parallel helix domain at the c-terminus, whereas, th eshort form enzymes do not have this domain. The homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose.


Pssm-ID: 133032 [Multi-domain]  Cd Length: 236  Bit Score: 128.07  E-value: 1.48e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403366218   1 MKAMILAAGKGERMRPLTLHTPKPLVRAGGVPLIEYHLRALHEAGFHEVVINHAWLGQQIEDHLGDGERFGLRIAYSPEG 80
Cdd:cd04189     1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEALGDGSRFGVRITYILQE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403366218  81 EPLETGGGIHRALPLLGDEPFLVVNGDVWTDYPFKALRMPLA---GLAHLVL--INNPAHH--PEGDFSLIDGQVRDSRD 153
Cdd:cd04189    81 EPLGLAHAVLAARDFLGDEPFVVYLGDNLIQEGISPLVRDFLeedADASILLaeVEDPRRFgvAVVDDGRIVRLVEKPKE 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1403366218 154 AGTRLTYSGIAVLHPKLFAGCQE------GAFKLAPLLRTAMEQG-QVTGEHFTGRWVDVGTHERLAEVERLLV 220
Cdd:cd04189   161 PPSNLALVGVYAFTPAIFDAISRlkpswrGELEITDAIQWLIDRGrRVGYSIVTGWWKDTGTPEDLLEANRLLL 234
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
1-207 2.98e-36

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: 131.18  E-value: 2.98e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403366218   1 MKAMILAAGKGERMRPLTLHTPKPLVRAGGVPLIEYHLRALHEAGFHEVVINHAWLGQQIEDHLGDGERFGLRIAYSPEG 80
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEKVREYFGDGSRGGVPIEYVVQE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403366218  81 EPLETGGGIHRALPLLgDEPFLVVNGDVWTDYPF--KALRMPLAGLAhLVLINNPAHHpeGDFSLIDGQVRD----SRDA 154
Cdd:TIGR03992  81 EQLGTADALGSAKEYV-DDEFLVLNGDVLLDSDLleRLIRAEAPAIA-VVEVDDPSDY--GVVETDGGRVTGivekPENP 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1403366218 155 GTRLTYSGIAVLHPKLFAGCQE------GAFKLAPLLRTAMEQGQVTGEHFTGRWVDVG 207
Cdd:TIGR03992 157 PSNLINAGIYLFSPEIFELLEKtklsprGEYELTDALQLLIDEGKVKAVELDGFWLDVG 215
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
3-210 4.44e-35

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: 123.78  E-value: 4.44e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403366218   3 AMILAAGKGERMRPLTLHTPKPLVRAGGVPLIEYHLRALHEAGFHEVVINHAWLGQQIEDHLGDGERFGLRIAYSPEGEP 82
Cdd:cd06426     1 VVIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNYLAEMIEDYFGDGSKFGVNISYVREDKP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403366218  83 LETGGgihrALPLLG---DEPFLVVNGDVWTDYPFKALR---------MPLAGLAHLVLInnpahhPEGDFSLIDGQVRD 150
Cdd:cd06426    81 LGTAG----ALSLLPekpTDPFLVMNGDILTNLNYEHLLdfhkennadATVCVREYEVQV------PYGVVETEGGRITS 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1403366218 151 SRDAGTrLTY---SGIAVLHPKLFAGCQEGAFKLAP-LLRTAMEQGQVTGEH-FTGRWVDVGTHE 210
Cdd:cd06426   151 IEEKPT-HSFlvnAGIYVLEPEVLDLIPKNEFFDMPdLIEKLIKEGKKVGVFpIHEYWLDIGRPE 214
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
1-117 9.41e-31

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: 113.07  E-value: 9.41e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403366218   1 MKAMILAAGKGERMRPLTLHTPKPLVRAGGVPLIEYHLRALHEAGFHEVVINHAWLGQQIEDHLGDGE-RFGLRIAYSPE 79
Cdd:cd06425     1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYRPEDMVPFLKEYEkKLGIKITFSIE 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1403366218  80 GEPLETGGGIHRALPLLG--DEPFLVVNGDVWTDYPFKAL 117
Cdd:cd06425    81 TEPLGTAGPLALARDLLGddDEPFFVLNSDVICDFPLAEL 120
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
2-215 5.14e-26

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


Pssm-ID: 425709 [Multi-domain]  Cd Length: 243  Bit Score: 100.79  E-value: 5.14e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403366218   2 KAMILAAGKGERMRPLTLHTPKPLV-RAGGVPLIEYHLRALHEAGFHE-VVINHAWLGQQIEDHLGDGERFGLRIAYSPE 79
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVpVGGKYPLIDYPLSRLANAGIREiIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403366218  80 GEPLETGGGIHRALPLLGDE--PFLVVNGDVWTDYPFK-ALR--MPLAGLAhLVLINNPAHHPEGDFSLI----DGQVRD 150
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEksDVLVLGGDHIYRMDLEqAVKfhIEKAADA-TVTFGIVPVEPPTGYGVVefddNGRVIR 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1403366218 151 -----SRDAGTRLTYSGIAVLHPKLF---AGCQEGAFKLAP----LLRTAMEQGQVTGEH-FTG-RWVDVGTHERLAEV 215
Cdd:pfam00483 160 fvekpKLPKASNYASMGIYIFNSGVLdflAKYLEELKRGEDeitdILPKALEDGKLAYAFiFKGyAWLDVGTWDSLWEA 238
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
2-108 5.63e-26

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 100.70  E-value: 5.63e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403366218   2 KAMILAAGKGERMRPLTLHTPKPLVRAGGVPLIEYHLRALHEAGFHEVVINHAWLGQQIEDHLgDGERFGLRIAYSPEGE 81
Cdd:COG1213     1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEAL-ARPGPDVTFVYNPDYD 79
                          90       100
                  ....*....|....*....|....*..
gi 1403366218  82 PLETGGGIHRALPLLgDEPFLVVNGDV 108
Cdd:COG1213    80 ETNNIYSLWLAREAL-DEDFLLLNGDV 105
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-107 1.96e-25

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 100.55  E-value: 1.96e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403366218   1 MKAMILAAGKGERMRPLTLHTPKPLVRAGGVPLIEYHLRALHEAGFHEVVI---NHawLGQQIEDHLGDGERFGLRIAYS 77
Cdd:COG1209     1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIistPE--DGPQFERLLGDGSQLGIKISYA 78
                          90       100       110
                  ....*....|....*....|....*....|
gi 1403366218  78 PEGEPLETGGGIHRALPLLGDEPFLVVNGD 107
Cdd:COG1209    79 VQPEPLGLAHAFIIAEDFIGGDPVALVLGD 108
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
3-109 5.21e-21

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: 87.29  E-value: 5.21e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403366218   3 AMILAAGKGERMRPLTLHTPKPLVRAGGVPLIEYHLRALHEAGFHEVVINHAWLGQQIEDHLgdGERFGLRIAYSPegEP 82
Cdd:cd02523     1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELL--KKYPNIKFVYNP--DY 76
                          90       100
                  ....*....|....*....|....*....
gi 1403366218  83 LETGGGI--HRALPLLgDEPFLVVNGDVW 109
Cdd:cd02523    77 AETNNIYslYLARDFL-DEDFLLLEGDVV 104
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
3-117 2.11e-18

N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose pyrophosphorylase; N-terminal domain of the M1P-guanylyltransferase A-isoform like proteins: The proteins of this family are likely to be a isoform of GDP-mannose pyrophosphorylase. Their sequences are highly conserved with mannose-1-phosphate guanyltransferase, but generally about 40-60 bases longer. GDP-mannose pyrophosphorylase (GTP: alpha-d-mannose-1-phosphate guanyltransferase) catalyzes the formation of GDP-d-mannose from GTP and alpha-d-mannose-1-Phosphate. It contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain. GDP-d-mannose is the activated form of mannose for formation of cell wall lipoarabinomannan and various mannose-containing glycolipids and polysaccharides. The function of GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability. Repression of GDP-mannose pyrophosphorylase in yeast leads to phenotypes including cell lysis, defective cell wall, and failure of polarized growth and cell separation.


Pssm-ID: 133050 [Multi-domain]  Cd Length: 257  Bit Score: 80.76  E-value: 2.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403366218   3 AMILAAG--KGERMRPLTLHTPKPLVRAGGVPLIEYHLRALHE-AGFHEVVINHAWLGQQIEDHLGDGER-FGLRIAYSP 78
Cdd:cd06428     1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKvPDLKEVLLIGFYPESVFSDFISDAQQeFNVPIRYLQ 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1403366218  79 EGEPLETGGGIH--RALPLLGD-EPFLVVNGDVWTDYPFKAL 117
Cdd:cd06428    81 EYKPLGTAGGLYhfRDQILAGNpSAFFVLNADVCCDFPLQEL 122
LicC COG4750
CTP:phosphocholine cytidylyltransferase LicC [Cell wall/membrane/envelope biogenesis, Lipid ...
1-114 1.86e-17

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


Pssm-ID: 443784 [Multi-domain]  Cd Length: 228  Bit Score: 77.56  E-value: 1.86e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403366218   1 MKAMILAAGKGERMRPLTLHTPKPLVRAGGVPLIEYHLRALHEAGFHEVVINHAWLGQQIEDHLgdgERFGLRIAYSPEG 80
Cdd:COG4750     1 MNAIILAAGLGSRFAPITYETPKGLLKVNGEPLIERQIRQLHEAGITDITVVVGYLKEQFEYLE---DKYGVKLIYNPDY 77
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1403366218  81 EPLETGGGIHRALPLLGDEpfLVVNGDVW-TDYPF 114
Cdd:COG4750    78 AEYNNISSLYLVRDKLGNT--YICSSDNYlTENPF 110
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
1-107 1.12e-15

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: 72.99  E-value: 1.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403366218   1 MKAMILAAGKGERMRPLTLHTPKPLVRAGGVPLIEYHLRALHEAGFHEVVI--NHAWLGqQIEDHLGDGERFGLRIAYSP 78
Cdd:cd02538     1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIisTPEDLP-LFKELLGDGSDLGIRITYAV 79
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1403366218  79 EGEPletgGGIHRALPL----LGDEPFLVVNGD 107
Cdd:cd02538    80 QPKP----GGLAQAFIIgeefIGDDPVCLILGD 108
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
1-108 1.62e-13

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: 68.51  E-value: 1.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403366218   1 MKAMILAAGKGERMRPltlHTPKPLVRAGGVPLIEYHLRALHEAGFHE--VVINHAwlGQQIEDHLGDgerFGLRIAYsp 78
Cdd:COG1207     3 LAVVILAAGKGTRMKS---KLPKVLHPLAGKPMLEHVLDAARALGPDRivVVVGHG--AEQVRAALAD---LDVEFVL-- 72
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1403366218  79 EGEPLETGGGIHRALPLLG--DEPFLVVNGDV 108
Cdd:COG1207    73 QEEQLGTGHAVQQALPALPgdDGTVLVLYGDV 104
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
1-117 3.45e-13

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


Pssm-ID: 133001 [Multi-domain]  Cd Length: 216  Bit Score: 66.12  E-value: 3.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403366218   1 MKAMILAAGKGERMRPLTLHTPKPLVRAGGVPLIEYHLRALHEAGFHEVVI---NHAwlgQQIEDHLGDGERFGLR---- 73
Cdd:cd02507     1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVvccEHS---QAIIEHLLKSKWSSLSskmi 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1403366218  74 --IAYSPEGEPLETGG-GIHRALPLLGDepFLVVNGDVWTDYPFKAL 117
Cdd:cd02507    78 vdVITSDLCESAGDALrLRDIRGLIRSD--FLLLSCDLVSNIPLSEL 122
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
3-108 4.99e-13

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: 65.61  E-value: 4.99e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403366218   3 AMILAAGKGERMRPltlHTPKPLVRAGGVPLIEYHLRALHEAGFHE--VVINHAwlGQQIEDHLGDgerFGLRIAYSPeg 80
Cdd:cd02540     1 AVILAAGKGTRMKS---DLPKVLHPLAGKPMLEHVLDAARALGPDRivVVVGHG--AEQVKKALAN---PNVEFVLQE-- 70
                          90       100       110
                  ....*....|....*....|....*....|
gi 1403366218  81 EPLETGGGIHRALPLLGD--EPFLVVNGDV 108
Cdd:cd02540    71 EQLGTGHAVKQALPALKDfeGDVLVLYGDV 100
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
1-114 1.10e-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: 58.82  E-value: 1.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403366218   1 MKAMILAAGKGERMRPLTLHTPKPLVRAGGVPLIEYHLRALHEAGFHEVVI----NHAwlgQQIEDHLGDGERFGLRIAY 76
Cdd:cd04198     1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVvvpeEEQ---AEISTYLRSFPLNLKQKLD 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1403366218  77 SPEG---EPLETGGGI-HRALPLLGDepFLVVNGDVWTDYPF 114
Cdd:cd04198    78 EVTIvldEDMGTADSLrHIRKKIKKD--FLVLSCDLITDLPL 117
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
1-108 2.71e-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: 55.62  E-value: 2.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403366218   1 MKAMILAAGKGERMRPLTLHTPK---PLVRAggvPLIEYHLRALHEAGFHEVVI-----NHAwlgqqIEDH--------- 63
Cdd:cd02541     1 RKAVIPAAGLGTRFLPATKAIPKemlPIVDK---PVIQYIVEEAVAAGIEDIIIvtgrgKRA-----IEDHfdrsyelee 72
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1403366218  64 ---------LGDGER---FGLRIAYSPEGEPLETGGGIHRALPLLGDEPFLVVNGDV 108
Cdd:cd02541    73 tlekkgktdLLEEVRiisDLANIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDD 129
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
3-108 1.11e-08

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: 52.58  E-value: 1.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403366218   3 AMILAAGKGERMRpltlhTPKPLVRAGGVPLIEYHLRALHEAgFHEVVINHAWlgqqiEDHLGDGERFGLRIAYSPEGE- 81
Cdd:pfam12804   1 AVILAGGRSSRMG-----GDKALLPLGGKPLLERVLERLRPA-GDEVVVVAND-----EEVLAALAGLGVPVVPDPDPGq 69
                          90       100
                  ....*....|....*....|....*....
gi 1403366218  82 -PLetgGGIHRALPLLGD-EPFLVVNGDV 108
Cdd:pfam12804  70 gPL---AGLLAALRAAPGaDAVLVLACDM 95
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
3-79 4.66e-08

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 51.31  E-value: 4.66e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1403366218   3 AMILAAGKGERMrpltlHTPKPLVRAGGVPLIEYHLRALHEAGFHE--VVINHAwlGQQIEDHLgdgERFGLRIAYSPE 79
Cdd:COG2068     6 AIILAAGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPvvVVLGAD--AEEVAAAL---AGLGVRVVVNPD 74
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
3-107 1.36e-07

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 51.37  E-value: 1.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403366218   3 AMILAAGKGERMRPltlHTPKPLVRAGGVPLIEYHLRALHEAGFHE--VVINHAwlGQQIEDHLGDgerfglRIAYSPEG 80
Cdd:PRK14354    5 AIILAAGKGTRMKS---KLPKVLHKVCGKPMVEHVVDSVKKAGIDKivTVVGHG--AEEVKEVLGD------RSEFALQE 73
                          90       100
                  ....*....|....*....|....*....
gi 1403366218  81 EPLETGGGIHRALPLLGDEP--FLVVNGD 107
Cdd:PRK14354   74 EQLGTGHAVMQAEEFLADKEgtTLVICGD 102
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
2-219 2.02e-07

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 50.44  E-value: 2.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403366218   2 KAMILAAGKGERMRPLTLHTPKPLVRAGGVPLIEYHLRALHEAGFHEV-VINHAWLGQQIEDHLGDGERFGLRIAYSPEG 80
Cdd:PRK15480    5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDIlIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403366218  81 EPletgGGIHRALP-----LLGDEPFLVVNGDVWTDYPF-----KALRMPLAGLAHLVLINNPAHHPEGDF-------SL 143
Cdd:PRK15480   85 SP----DGLAQAFIigeefIGGDDCALVLGDNIFYGHDLpklmeAAVNKESGATVFAYHVNDPERYGVVEFdqngtaiSL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403366218 144 IDGQVR-DSRDAGTRLT-YSGIAVLHPKLFAGCQEGAFKLAPLLRTAMEQGQVTGEhFTGR---WVDVGTHERLAEVERL 218
Cdd:PRK15480  161 EEKPLQpKSNYAVTGLYfYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVA-MMGRgyaWLDTGTHQSLIEASNF 239

                  .
gi 1403366218 219 L 219
Cdd:PRK15480  240 I 240
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
3-130 3.09e-07

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 50.25  E-value: 3.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403366218   3 AMILAAGKGERMRPltlHTPKPLVRAGGVPLIEYHLRALHEAGFHEVVI---NHAwlgQQIEDHLgdgERFGLRIAYSPE 79
Cdd:PRK14353    8 AIILAAGEGTRMKS---SLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVvvgPGA---EAVAAAA---AKIAPDAEIFVQ 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1403366218  80 GEPLETGGGIHRALPLL--GDEPFLVVNGDV--WTDYPFKALRMPLAGLAHLVLI 130
Cdd:PRK14353   79 KERLGTAHAVLAAREALagGYGDVLVLYGDTplITAETLARLRERLADGADVVVL 133
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
1-107 5.02e-07

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


Pssm-ID: 133000 [Multi-domain]  Cd Length: 181  Bit Score: 48.34  E-value: 5.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403366218   1 MKAMILAAGKGERMrpltlHTPKPLVRAGGVPLIEYHLRALHEAgFHEVVINhawlgqqIEDHLGDGERFGLRIAY-SPE 79
Cdd:cd02503     1 ITGVILAGGKSRRM-----GGDKALLELGGKPLLEHVLERLKPL-VDEVVIS-------ANRDQERYALLGVPVIPdEPP 67
                          90       100
                  ....*....|....*....|....*....
gi 1403366218  80 GE-PLetgGGIHRALPLLGDEPFLVVNGD 107
Cdd:cd02503    68 GKgPL---AGILAALRAAPADWVLVLACD 93
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
1-111 8.54e-07

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 48.35  E-value: 8.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403366218   1 MKAMILAAGKGERMRPLTLHTPKPLVRAGGVPLIEYHLRALHEAGFHEVVI----------NH--------AWLGQQIED 62
Cdd:PRK10122    4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLvthasknaveNHfdtsyeleSLLEQRVKR 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1403366218  63 HLGDGERF----GLRIAYSPEGEPLETGGGIHRALPLLGDEPFLVVNGDVWTD 111
Cdd:PRK10122   84 QLLAEVQSicppGVTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPDVVID 136
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
3-64 1.09e-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: 47.60  E-value: 1.09e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1403366218   3 AMILAAGKGERMRPLTLHTPK---PLVragGVPLIEYHLRALHEAGFHEVVINHAWLGQQIEDHL 64
Cdd:cd04197     3 AVVLADSFNRRFRPLTKEKPRcllPLA---NVPLIDYTLEFLALNGVEEVFVFCCSHSDQIKEYI 64
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
1-107 5.36e-06

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: 45.18  E-value: 5.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403366218   1 MKAMILAAGKGERMrpltlHTPKPLVRAGGVPLIEYHLRALHEAgFHEVVINHAWlGQQIedhlgdgERFGLRIAY-SPE 79
Cdd:COG0746     5 ITGVILAGGRSRRM-----GQDKALLPLGGRPLLERVLERLRPQ-VDEVVIVANR-PERY-------AALGVPVVPdDPP 70
                          90       100
                  ....*....|....*....|....*....
gi 1403366218  80 GE-PLetgGGIHRALPLLGDEPFLVVNGD 107
Cdd:COG0746    71 GAgPL---AGILAALEAAPAEWVLVLACD 96
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
6-108 8.92e-06

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: 44.49  E-value: 8.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403366218   6 LAAGKGERMRPltlhTPKPLVRAGGVPLIEYHLRALHEAGFHEVVI----NH----AWLgqqiedhlgdgERFGLRIays 77
Cdd:COG2266     1 MAGGKGTRLGG----GEKPLLEICGKPMIDRVIDALEESCIDKIYVavspNTpktrEYL-----------KERGVEV--- 62
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1403366218  78 pegepLETGGG-----IHRALPLLgDEPFLVVNGDV 108
Cdd:COG2266    63 -----IETPGEgyvedLNEALESI-SGPVLVVPADL 92
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
3-51 1.39e-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: 44.09  E-value: 1.39e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1403366218   3 AMILAAGKGERMrpltlHTPKPLVRAGGVPLIEYHLRALHEAGFHEVVI 51
Cdd:cd04182     3 AIILAAGRSSRM-----GGNKLLLPLDGKPLLRHALDAALAAGLSRVIV 46
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
3-203 2.36e-05

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: 44.10  E-value: 2.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403366218   3 AMILAAGKGERMRPLTLHTPKPLVRAGGVPLIeYHLRALHEA-GFHEVVI--------------NHAWL---------GQ 58
Cdd:cd02524     1 VVILAGGLGTRLSEETELKPKPMVEIGGRPIL-WHIMKIYSHyGHNDFILclgykghvikeyflNYFLHnsdvtidlgTN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403366218  59 QIEDHLGDGERFglRIAYSPEGEPLETGGGIHRALPLLGD-EPFLVVNGDVWTDYPFKALRMPLAglAHLVLINNPAHHP 137
Cdd:cd02524    80 RIELHNSDIEDW--KVTLVDTGLNTMTGGRLKRVRRYLGDdETFMLTYGDGVSDVNINALIEFHR--SHGKLATVTAVHP 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1403366218 138 EGDFSLI----DGQVR---DSRDAGTRLTYSGIAVLHPKLFAGCQEGA--FKLAPlLRTAMEQGQVTGEHFTGRW 203
Cdd:cd02524   156 PGRFGELdlddDGQVTsftEKPQGDGGWINGGFFVLEPEVFDYIDGDDtvFEREP-LERLAKDGELMAYKHTGFW 229
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
3-107 3.80e-05

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 43.94  E-value: 3.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403366218   3 AMILAAGKGERMrpltlHTPKPLVRAG--GVPLIEYHLRALhEAGFHE---VVINH-AWLGQQIEDHLGDgeRFGLriay 76
Cdd:PRK14356    8 ALILAAGKGTRM-----HSDKPKVLQTllGEPMLRFVYRAL-RPLFGDnvwTVVGHrADMVRAAFPDEDA--RFVL---- 75
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1403366218  77 spEGEPLETGGGIHRALPLL---GDEPFLVVNGD 107
Cdd:PRK14356   76 --QEQQLGTGHALQCAWPSLtaaGLDRVLVVNGD 107
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
3-51 1.10e-04

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


Pssm-ID: 133009 [Multi-domain]  Cd Length: 218  Bit Score: 41.74  E-value: 1.10e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1403366218   3 AMILAAGKGERMRPLtlhTPKPLVRAGGVPLIEYHLRALHEAG-FHEVVI 51
Cdd:cd02516     3 AIILAAGSGSRMGAD---IPKQFLELGGKPVLEHTLEAFLAHPaIDEIVV 49
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
3-108 1.38e-04

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 42.04  E-value: 1.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403366218   3 AMILAAGKGERMRPLTLHTPKPLvraGGVPLIEYHLRALHEAGFHEVVINHAWLGQQIEDHL-GDGErfglrIAYSPEGE 81
Cdd:PRK14355    6 AIILAAGKGTRMKSDLVKVMHPL---AGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHFaGDGD-----VSFALQEE 77
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1403366218  82 PLETGGGIHRALPLLgdEPF----LVVNGDV 108
Cdd:PRK14355   78 QLGTGHAVACAAPAL--DGFsgtvLILCGDV 106
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
5-108 1.74e-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: 1.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403366218   5 ILAAGKGERMRPlTLhtPKPLVRAGGVPLIEYHLRALHEAGFHE--VVINHAwlGQQIEDHLGDGErfglRIAYSPEGEP 82
Cdd:PRK14360    6 ILAAGKGTRMKS-SL--PKVLHPLGGKSLVERVLDSCEELKPDRrlVIVGHQ--AEEVEQSLAHLP----GLEFVEQQPQ 76
                          90       100
                  ....*....|....*....|....*...
gi 1403366218  83 LETGGGIHRALPLLGD--EPFLVVNGDV 108
Cdd:PRK14360   77 LGTGHAVQQLLPVLKGfeGDLLVLNGDV 104
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
5-51 2.17e-04

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: 40.88  E-value: 2.17e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1403366218   5 ILAAGKGERMRpltLHTPKPLVRAGGVPLIEYHLRALHEAG-FHEVVI 51
Cdd:COG1211     2 IPAAGSGSRMG---AGIPKQFLPLGGKPVLEHTLEAFLAHPrIDEIVV 46
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
1-108 2.63e-04

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 41.17  E-value: 2.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403366218   1 MKAMILAAGKGERMRPltlHTPKPLVRAGGVPLIEYHLRALHEAGFHEV--VINHAwlGQQIEDHLGDGerfglRIAYSP 78
Cdd:PRK09451    6 MSVVILAAGKGTRMYS---DLPKVLHTLAGKPMVQHVIDAANELGAQHVhlVYGHG--GDLLKQTLADE-----PLNWVL 75
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1403366218  79 EGEPLETGGGIHRALPLLGD-EPFLVVNGDV 108
Cdd:PRK09451   76 QAEQLGTGHAMQQAAPFFADdEDILMLYGDV 106
mobA PRK00317
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
1-108 2.91e-04

molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed


Pssm-ID: 234725 [Multi-domain]  Cd Length: 193  Bit Score: 40.17  E-value: 2.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403366218   1 MKAMILAAGKGERMRpltlHTPKPLVRAGGVPLIEYHLRALhEAGFHEVVINHAwlgqqieDHLGDGERFGLRIAysPEG 80
Cdd:PRK00317    4 ITGVILAGGRSRRMG----GVDKGLQELNGKPLIQHVIERL-APQVDEIVINAN-------RNLARYAAFGLPVI--PDS 69
                          90       100       110
                  ....*....|....*....|....*....|
gi 1403366218  81 EPLETG--GGIHRALPLLGDEPFLVVNGDV 108
Cdd:PRK00317   70 LADFPGplAGILAGLKQARTEWVLVVPCDT 99
ispD TIGR00453
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ...
3-51 2.92e-04

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: 40.73  E-value: 2.92e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1403366218   3 AMILAAGKGERMRPltlHTPKPLVRAGGVPLIEYHLRALHEA-GFHEVVI 51
Cdd:TIGR00453   2 AVIPAAGRGTRFGS---GVPKQYLELGGRPLLEHALDAFLAHpAIDEVVV 48
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
3-30 3.38e-04

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 40.83  E-value: 3.38e-04
                          10        20
                  ....*....|....*....|....*...
gi 1403366218   3 AMILAAGKGERMRPLTLHTPKPLVRAGG 30
Cdd:COG0448     4 AIILAGGRGSRLGPLTKDRAKPAVPFGG 31
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
5-116 5.87e-04

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: 39.54  E-value: 5.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403366218   5 ILAAGKGERMRPLTLHTPKPLVRAGGVPLIEYHLRALHEAGFHEV--VINhawlgqqiEDHLgdgERFGLR---IAYSPE 79
Cdd:cd04183     3 IPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEWVIESLAKIFDSRFifICR--------DEHN---TKFHLDeslKLLAPN 71
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1403366218  80 GE----PLETGGGIHRALPLL----GDEPFLVVNGDVWTDYPFKA 116
Cdd:cd04183    72 ATvvelDGETLGAACTVLLAAdlidNDDPLLIFNCDQIVESDLLA 116
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
3-72 7.03e-04

ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ADP-glucose pyrophosphorylase (glucose-1-phosphate adenylyltransferase) catalyzes a very important step in the biosynthesis of alpha 1,4-glucans (glycogen or starch) in bacteria and plants: synthesis of the activated glucosyl donor, ADP-glucose, from glucose-1-phosphate and ATP. ADP-glucose pyrophosphorylase is a tetrameric allosterically regulated enzyme. While a homotetramer in bacteria, in plant chloroplasts and amyloplasts, it is a heterotetramer of two different, yet evolutionary related, subunits. There are a number of conserved regions in the sequence of bacterial and plant ADP-glucose pyrophosphorylase subunits. It is a subfamily of a very diverse glycosy transferase family 2.


Pssm-ID: 133002 [Multi-domain]  Cd Length: 200  Bit Score: 39.45  E-value: 7.03e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1403366218   3 AMILAAGKGERMRPLTLHTPKPLVRAGG-VPLIEYHLRALHEAGFHEVVINHAWLGQQIEDHLGDGERFGL 72
Cdd:cd02508     1 AIILAGGEGTRLSPLTKKRAKPAVPFGGrYRLIDFPLSNMVNSGIRNVGVLTQYKSRSLNDHLGSGKEWDL 71
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
1-30 9.41e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 39.47  E-value: 9.41e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1403366218   1 MKAMILAAGKGERMRPLTLHTPKPLVRAGG 30
Cdd:PRK05293    4 MLAMILAGGQGTRLGKLTKNIAKPAVPFGG 33
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
3-51 9.42e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 39.42  E-value: 9.42e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1403366218   3 AMILAAGKGERMRPLTLHTPKPLVRAGGV-PLIEYHLRALHEAGFHEVVI 51
Cdd:PRK00844    8 AIVLAGGEGKRLMPLTADRAKPAVPFGGSyRLIDFVLSNLVNSGYLRIYV 57
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
3-51 1.06e-03

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 38.96  E-value: 1.06e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1403366218   3 AMILAAGKGERMRPLtlhTPKPLVRAGGVPLIEYHLRALHEAG-FHEVVI 51
Cdd:PRK00155    6 AIIPAAGKGSRMGAD---RPKQYLPLGGKPILEHTLEAFLAHPrIDEIIV 52
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
2-111 1.97e-03

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 38.35  E-value: 1.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403366218   2 KAMILAAGKGERMRPLTLHTPKPLVRAGGVPLIEYHLRALHEAGFHEVVINHAWLGQQIEDHLGDGERF----------- 70
Cdd:PRK13389   10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFDTSFELeamlekrvkrq 89
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1403366218  71 -----------GLRIAYSPEGEPLETGGGIHRALPLLGDEPFLVVNGDVWTD 111
Cdd:PRK13389   90 lldevqsicppHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILD 141
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
3-30 2.73e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 38.28  E-value: 2.73e-03
                          10        20
                  ....*....|....*....|....*...
gi 1403366218   3 AMILAAGKGERMRPLTLHTPKPLVRAGG 30
Cdd:PRK00725   18 ALILAGGRGSRLKELTDKRAKPAVYFGG 45
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
1-102 5.81e-03

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 37.27  E-value: 5.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403366218   1 MKAMILAAGKGERMRPLTlhtPKPLVRAGGVPLIEYHLRALHEAGFHEVVINHAWLGQQIEDHL-GDGERF-------GL 72
Cdd:PRK14358    8 LDVVILAAGQGTRMKSAL---PKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGAEQVEAALqGSGVAFarqeqqlGT 84
                          90       100       110
                  ....*....|....*....|....*....|
gi 1403366218  73 RIAYSPEGEPLETGGGihRALPLLGDEPFL 102
Cdd:PRK14358   85 GDAFLSGASALTEGDA--DILVLYGDTPLL 112
 
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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