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Conserved domains on  [gi|339265237|ref|XP_003366256|]
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mannose-1-phosphate guanyltransferase alpha-A, partial [Trichinella spiralis]

Protein Classification

glycosyltransferase family protein( domain architecture ID 27718)

glycosyltransferase family protein may synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Glyco_tranf_GTA_type super family cl11394
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 11-228 1.45e-108

Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold; Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases 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. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.


The actual alignment was detected with superfamily member cd06428:

Pssm-ID: 472172 [Multi-domain]  Cd Length: 257  Bit Score: 313.04  E-value: 1.45e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339265237  11 AVILIGGPQKGTRFRPLSLDCPKPLFPIAGVPSVQHHIEALTKIPGLKEILFIGFYqPNDHWATFISDIQgQYSTVNIRY 90
Cdd:cd06428    1 AVILVGGPQKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKVPDLKEVLLIGFY-PESVFSDFISDAQ-QEFNVPIRY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339265237  91 LQEFAPLGTAGGIYHFRDQILLGGTDACFVLNADVCGDLPLMEMvdqlntlIDKHSATENILLMLTTEAAREQSMNFGCA 170
Cdd:cd06428   79 LQEYKPLGTAGGLYHFRDQILAGNPSAFFVLNADVCCDFPLQEL-------LEFHKKHGASGTILGTEASREQASNYGCI 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 339265237 171 AIN-DSSEIIHYVEKPTTFLSKWINCGVYLMQMGIIDTLADVFKNKT---LLSNSNNGFHIP 228
Cdd:cd06428  152 VEDpSTGEVLHYVEKPETFVSDLINCGVYLFSPEIFDTIKKAFQSRQqeaQLGDDNNREGRA 213
 
Name Accession Description Interval E-value
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 11-228 1.45e-108

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: 313.04  E-value: 1.45e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339265237  11 AVILIGGPQKGTRFRPLSLDCPKPLFPIAGVPSVQHHIEALTKIPGLKEILFIGFYqPNDHWATFISDIQgQYSTVNIRY 90
Cdd:cd06428    1 AVILVGGPQKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKVPDLKEVLLIGFY-PESVFSDFISDAQ-QEFNVPIRY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339265237  91 LQEFAPLGTAGGIYHFRDQILLGGTDACFVLNADVCGDLPLMEMvdqlntlIDKHSATENILLMLTTEAAREQSMNFGCA 170
Cdd:cd06428   79 LQEYKPLGTAGGLYHFRDQILAGNPSAFFVLNADVCCDFPLQEL-------LEFHKKHGASGTILGTEASREQASNYGCI 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 339265237 171 AIN-DSSEIIHYVEKPTTFLSKWINCGVYLMQMGIIDTLADVFKNKT---LLSNSNNGFHIP 228
Cdd:cd06428  152 VEDpSTGEVLHYVEKPETFVSDLINCGVYLFSPEIFDTIKKAFQSRQqeaQLGDDNNREGRA 213
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 10-210 1.64e-37

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: 131.04  E-value: 1.64e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339265237  10 KAVILIGGpqKGTRFRPLSLDCPKPLFPIAGVPSVQHHIEALTKIpGLKEILFIGFYQPnDHWATFISDiqGQYSTVNIR 89
Cdd:COG1208    1 KAVILAGG--LGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAA-GITEIVINVGYLA-EQIEEYFGD--GSRFGVRIT 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339265237  90 YLQEFAPLGTAGGIYHFRDQIllgGTDACFVLNADVCGDLPlmemvdqLNTLIDKHSATENILLMLTTEaaREQSMNFGC 169
Cdd:COG1208   75 YVDEGEPLGTGGALKRALPLL---GDEPFLVLNGDILTDLD-------LAALLAFHREKGADATLALVP--VPDPSRYGV 142

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 339265237 170 AAINDSSEIIHYVEKPTTFLSKWINCGVYLMQMGIIDTLAD 210
Cdd:COG1208  143 VELDGDGRVTRFVEKPEEPPSNLINAGIYVLEPEIFDYIPE 183
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 10-213 3.47e-26

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


Pssm-ID: 425709 [Multi-domain]  Cd Length: 243  Bit Score: 101.95  E-value: 3.47e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339265237   10 KAVILIGGpqKGTRFRPLSLDCPKPLFPIAG-VPSVQHHIEALTKIpGLKEILFIGFYQP----NDHWAtfisdiQGQYS 84
Cdd:pfam00483   1 KAIILAGG--SGTRLWPLTRTLAKPLVPVGGkYPLIDYPLSRLANA-GIREIIVILTQEHrfmlNELLG------DGSKF 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339265237   85 TVNIRYLQEFAPLGTAGGIYHFRDqILLGGTDACFVLNADVCGDLPLMEMVDQLntliDKHSATENILLMLT-TEAAREq 163
Cdd:pfam00483  72 GVQITYALQPEGKGTAPAVALAAD-FLGDEKSDVLVLGGDHIYRMDLEQAVKFH----IEKAADATVTFGIVpVEPPTG- 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 339265237  164 smnFGCAAINDSSEIIHYVEKPTTF-LSKWINCGVYLMQMGIIDTLADVFK 213
Cdd:pfam00483 146 ---YGVVEFDDNGRVIRFVEKPKLPkASNYASMGIYIFNSGVLDFLAKYLE 193
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 10-211 2.44e-23

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: 96.89  E-value: 2.44e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339265237   10 KAVILIGGpqKGTRFRPLSLDCPKPLFPIAGVPSVQHHIEALTKIpGLKEILFIGFYQPnDHWATFISDiqGQYSTVNIR 89
Cdd:TIGR03992   2 KAVILAAG--KGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDA-GIDDFVFVVGYGK-EKVREYFGD--GSRGGVPIE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339265237   90 YLQEFAPLGTAGGIYHFRDQIllggTDACFVLNADVCGDLPLMEmvdqlnTLIDKHSATenillMLTTEAAREQSmnFGC 169
Cdd:TIGR03992  76 YVVQEEQLGTADALGSAKEYV----DDEFLVLNGDVLLDSDLLE------RLIRAEAPA-----IAVVEVDDPSD--YGV 138

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 339265237  170 AAINDsSEIIHYVEKPTTFLSKWINCGVYLMQMGIIDTLADV 211
Cdd:TIGR03992 139 VETDG-GRVTGIVEKPENPPSNLINAGIYLFSPEIFELLEKT 179
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 11-222 1.16e-07

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 51.67  E-value: 1.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339265237  11 AVILIGGpqKGTRFRPlslDCPKPLFPIAGVPSVQHHIEALTKIPGLKEILFIGfyqpndHWATFISDIQGQYSTVNIRy 90
Cdd:PRK14355   6 AIILAAG--KGTRMKS---DLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVG------HQAEKVREHFAGDGDVSFA- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339265237  91 LQEfAPLGTAGGIYHFRDQiLLGGTDACFVLnadvCGDLPLMEmVDQLNTLIDKHSATENILLMLTTEAarEQSMNFGCA 170
Cdd:PRK14355  74 LQE-EQLGTGHAVACAAPA-LDGFSGTVLIL----CGDVPLLR-AETLQGMLAAHRATGAAVTVLTARL--ENPFGYGRI 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 339265237 171 AINDSSEIIHYVEK----PTTFLSKWINCGVYLMQMGIidtladVFKNKTLLSNSN 222
Cdd:PRK14355 145 VRDADGRVLRIVEEkdatPEERSIREVNSGIYCVEAAF------LFDAIGRLGNDN 194
 
Name Accession Description Interval E-value
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 11-228 1.45e-108

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: 313.04  E-value: 1.45e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339265237  11 AVILIGGPQKGTRFRPLSLDCPKPLFPIAGVPSVQHHIEALTKIPGLKEILFIGFYqPNDHWATFISDIQgQYSTVNIRY 90
Cdd:cd06428    1 AVILVGGPQKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKVPDLKEVLLIGFY-PESVFSDFISDAQ-QEFNVPIRY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339265237  91 LQEFAPLGTAGGIYHFRDQILLGGTDACFVLNADVCGDLPLMEMvdqlntlIDKHSATENILLMLTTEAAREQSMNFGCA 170
Cdd:cd06428   79 LQEYKPLGTAGGLYHFRDQILAGNPSAFFVLNADVCCDFPLQEL-------LEFHKKHGASGTILGTEASREQASNYGCI 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 339265237 171 AIN-DSSEIIHYVEKPTTFLSKWINCGVYLMQMGIIDTLADVFKNKT---LLSNSNNGFHIP 228
Cdd:cd06428  152 VEDpSTGEVLHYVEKPETFVSDLINCGVYLFSPEIFDTIKKAFQSRQqeaQLGDDNNREGRA 213
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 11-200 1.94e-42

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: 143.10  E-value: 1.94e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339265237  11 AVILIGGpqKGTRFRPLSLDCPKPLFPIAGVPSVQHHIEALTKIpGLKEILFIGFYQPNDhwatfISDIQGQYST--VNI 88
Cdd:cd04181    1 AVILAAG--KGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARA-GIDEIILVVGYLGEQ-----IEEYFGDGSKfgVNI 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339265237  89 RYLQEFAPLGTAGGIYHFRDQIllgGTDACFVLNADVCGDLPLMEMvdqlntlIDKHSATENILLMLTTEaaREQSMNFG 168
Cdd:cd04181   73 EYVVQEEPLGTAGAVRNAEDFL---GDDDFLVVNGDVLTDLDLSEL-------LRFHREKGADATIAVKE--VEDPSRYG 140

                        170       180       190
                 ....*....|....*....|....*....|..
gi 339265237 169 CAAINDSSEIIHYVEKPTTFLSKWINCGVYLM 200
Cdd:cd04181  141 VVELDDDGRVTRFVEKPTLPESNLANAGIYIF 172
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 10-210 1.64e-37

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: 131.04  E-value: 1.64e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339265237  10 KAVILIGGpqKGTRFRPLSLDCPKPLFPIAGVPSVQHHIEALTKIpGLKEILFIGFYQPnDHWATFISDiqGQYSTVNIR 89
Cdd:COG1208    1 KAVILAGG--LGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAA-GITEIVINVGYLA-EQIEEYFGD--GSRFGVRIT 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339265237  90 YLQEFAPLGTAGGIYHFRDQIllgGTDACFVLNADVCGDLPlmemvdqLNTLIDKHSATENILLMLTTEaaREQSMNFGC 169
Cdd:COG1208   75 YVDEGEPLGTGGALKRALPLL---GDEPFLVLNGDILTDLD-------LAALLAFHREKGADATLALVP--VPDPSRYGV 142

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 339265237 170 AAINDSSEIIHYVEKPTTFLSKWINCGVYLMQMGIIDTLAD 210
Cdd:COG1208  143 VELDGDGRVTRFVEKPEEPPSNLINAGIYVLEPEIFDYIPE 183
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 10-206 3.71e-32

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: 117.31  E-value: 3.71e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339265237  10 KAVILIGGpqKGTRFRPLSLDCPKPLFPIAGVPSVQHHIEALTKIpGLKEILFIGFYQPNDhWATFISDIQGQYStVNIR 89
Cdd:cd06425    2 KALILVGG--YGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKA-GVKEIILAVNYRPED-MVPFLKEYEKKLG-IKIT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339265237  90 YLQEFAPLGTAGGIYHFRDqILLGGTDACFVLNADVCGDLPLMEMVDQLNtlidKHSATENILLMLTTEAAReqsmnFGC 169
Cdd:cd06425   77 FSIETEPLGTAGPLALARD-LLGDDDEPFFVLNSDVICDFPLAELLDFHK----KHGAEGTILVTKVEDPSK-----YGV 146

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 339265237 170 AAINDSSEIIH-YVEKPTTFLSKWINCGVYLMQMGIID 206
Cdd:cd06425  147 VVHDENTGRIErFVEKPKVFVGNKINAGIYILNPSVLD 184
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 10-213 3.47e-26

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


Pssm-ID: 425709 [Multi-domain]  Cd Length: 243  Bit Score: 101.95  E-value: 3.47e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339265237   10 KAVILIGGpqKGTRFRPLSLDCPKPLFPIAG-VPSVQHHIEALTKIpGLKEILFIGFYQP----NDHWAtfisdiQGQYS 84
Cdd:pfam00483   1 KAIILAGG--SGTRLWPLTRTLAKPLVPVGGkYPLIDYPLSRLANA-GIREIIVILTQEHrfmlNELLG------DGSKF 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339265237   85 TVNIRYLQEFAPLGTAGGIYHFRDqILLGGTDACFVLNADVCGDLPLMEMVDQLntliDKHSATENILLMLT-TEAAREq 163
Cdd:pfam00483  72 GVQITYALQPEGKGTAPAVALAAD-FLGDEKSDVLVLGGDHIYRMDLEQAVKFH----IEKAADATVTFGIVpVEPPTG- 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 339265237  164 smnFGCAAINDSSEIIHYVEKPTTF-LSKWINCGVYLMQMGIIDTLADVFK 213
Cdd:pfam00483 146 ---YGVVEFDDNGRVIRFVEKPKLPkASNYASMGIYIFNSGVLDFLAKYLE 193
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 11-213 2.41e-24

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: 96.47  E-value: 2.41e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339265237  11 AVILIGGpqKGTRFRPLSLDCPKPLFPIAGVPSVQHHIEALTKiPGLKEILF-IGfyqpndHWATFISDI--QGQYSTVN 87
Cdd:cd06915    1 AVILAGG--LGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLAR-QGISRIVLsVG------YLAEQIEEYfgDGYRGGIR 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339265237  88 IRYLQEFAPLGTAGGIYHFRDQILlggTDACFVLNADVcgdlplMEMVDqLNTLIDKHSATENILLMLTTE---AAReqs 164
Cdd:cd06915   72 IYYVIEPEPLGTGGAIKNALPKLP---EDQFLVLNGDT------YFDVD-LLALLAALRASGADATMALRRvpdASR--- 138

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 339265237 165 mnFGCAAINDSSEIIHYVEKPTTFLSKWINCGVYLMQMGIIDTL--------ADVFK 213
Cdd:cd06915  139 --YGNVTVDGDGRVIAFVEKGPGAAPGLINGGVYLLRKEILAEIpadafsleADVLP 193
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 11-210 1.98e-23

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: 93.73  E-value: 1.98e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339265237  11 AVILIGGpqKGTRFRPLSLDCPKPLFPIAGVPSVQHHIEALTKIpGLKEILFIGFYQPN---DHWAtfisdiQGQYSTVN 87
Cdd:cd06426    1 VVIMAGG--KGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQ-GFRNFYISVNYLAEmieDYFG------DGSKFGVN 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339265237  88 IRYLQEFAPLGTAGGIYHFRDQIllggTDACFVLNADVCGDLPLMEMVDQlntlidkHSATENILLMltteAAREQSMN- 166
Cdd:cd06426   72 ISYVREDKPLGTAGALSLLPEKP----TDPFLVMNGDILTNLNYEHLLDF-------HKENNADATV----CVREYEVQv 136

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 339265237 167 -FGCAAINDsSEIIHYVEKPT-TFLskwINCGVYLMQMGIIDTLAD 210
Cdd:cd06426  137 pYGVVETEG-GRITSIEEKPThSFL---VNAGIYVLEPEVLDLIPK 178
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 10-211 2.44e-23

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: 96.89  E-value: 2.44e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339265237   10 KAVILIGGpqKGTRFRPLSLDCPKPLFPIAGVPSVQHHIEALTKIpGLKEILFIGFYQPnDHWATFISDiqGQYSTVNIR 89
Cdd:TIGR03992   2 KAVILAAG--KGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDA-GIDDFVFVVGYGK-EKVREYFGD--GSRGGVPIE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339265237   90 YLQEFAPLGTAGGIYHFRDQIllggTDACFVLNADVCGDLPLMEmvdqlnTLIDKHSATenillMLTTEAAREQSmnFGC 169
Cdd:TIGR03992  76 YVVQEEQLGTADALGSAKEYV----DDEFLVLNGDVLLDSDLLE------RLIRAEAPA-----IAVVEVDDPSD--YGV 138

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 339265237  170 AAINDsSEIIHYVEKPTTFLSKWINCGVYLMQMGIIDTLADV 211
Cdd:TIGR03992 139 VETDG-GRVTGIVEKPENPPSNLINAGIYLFSPEIFELLEKT 179
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
 10-214 9.37e-19

glucose-1-phosphate thymidylylransferase, long form; The family of known and putative glucose-1-phosphate thymidyltransferase (also called dTDP-glucose synthase) shows a deep split into a short form (see TIGR01207) and a long form described by this model. The homotetrameric short form is found in numerous bacterial species that incorporate dTDP-L-rhamnose, which it helps synthesize, into the cell wall. It is subject to feedback inhibition. This form, in contrast, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced. Alternate name: dTDP-D-glucose synthase


Pssm-ID: 273500 [Multi-domain]  Cd Length: 353  Bit Score: 83.61  E-value: 9.37e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339265237   10 KAVILIGGpqKGTRFRPLSLDCPKPLFPIAGVPSVQHHIEALTKIpGLKEILFIGFYQPNDHWATFISDiqGQYSTVNIR 89
Cdd:TIGR01208   1 KALILAAG--KGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEA-GITDIGIVVGPVTGEEIKEIVGE--GERFGAKIT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339265237   90 YLQEFAPLGTAGGIYHFRDQilLGGTDACFVLnadvcGDLPLMEMVDQLNTLIDKHSATENILLMLTTEAAReqsmnFGC 169
Cdd:TIGR01208  76 YIVQGEPLGLAHAVYTARDF--LGDDDFVVYL-----GDNLIQDGISRFVKSFEEKDYDALILLTKVRDPTA-----FGV 143

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 339265237  170 AAINDSSEIIHYVEKPTTFLSKWINCGVYLMQmgiiDTLADVFKN 214
Cdd:TIGR01208 144 AVLEDGKRILKLVEKPKEPPSNLAVVGLYMFR----PLIFEAIKN 184
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 10-159 3.66e-17

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: 77.23  E-value: 3.66e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339265237  10 KAVILIGGpqKGTRFRPLSLDCPKPLFPIAGVPSVQHHIEALTKIpGLKEILFigfyqpNDHW--ATFISDIQGQYSTVN 87
Cdd:cd06422    1 KAMILAAG--LGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAA-GIRRIVV------NTHHlaDQIEAHLGDSRFGLR 71

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 339265237  88 IRYLQE-FAPLGTAGGIYHFRDqilLGGTDACFVLNADVCGDLPLmemVDQLNTLIDKHSAteNILLMLTTEA 159
Cdd:cd06422   72 ITISDEpDELLETGGGIKKALP---LLGDEPFLVVNGDILWDGDL---APLLLLHAWRMDA--LLLLLPLVRN 136
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 10-199 2.36e-16

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: 75.30  E-value: 2.36e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339265237  10 KAVILIGGpqKGTRFRPLSLDCPKPLFPIAGVPSVQHHIEALTKIpGLKEILFIGFYQPNDhwatfISDIQGQYST--VN 87
Cdd:cd04189    2 KGLILAGG--KGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREA-GIEDIGIVVGPTGEE-----IKEALGDGSRfgVR 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339265237  88 IRYLQEFAPLGTAGGIYHFRDQilLGGTDACFVLNADVCGDlPLMEMVDQLntliDKHSATENILLmltteAAREQSMNF 167
Cdd:cd04189   74 ITYILQEEPLGLAHAVLAARDF--LGDEPFVVYLGDNLIQE-GISPLVRDF----LEEDADASILL-----AEVEDPRRF 141

                        170       180       190
                 ....*....|....*....|....*....|..
gi 339265237 168 GCAAINDSSeIIHYVEKPTTFLSKWINCGVYL 199
Cdd:cd04189  142 GVAVVDDGR-IVRLVEKPKEPPSNLALVGVYA 172
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
10-234 5.95e-12

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 63.96  E-value: 5.95e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339265237  10 KAVILIGGpqKGTRFRPLSLDCPKPLFPIAGVPSVQHHIEALTKIpGLKEILFI-GFY-QPNdhwatFISDI-QGQYSTV 86
Cdd:COG1209    2 KGIILAGG--SGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLA-GIREILIIsTPEdGPQ-----FERLLgDGSQLGI 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339265237  87 NIRY-LQEfAPLGTAGGIYHFRDQIllGGTDACFVLnadvcGDlplmemvdqlnTLIDKHSATEnillMLTTEAAREQSM 165
Cdd:COG1209   74 KISYaVQP-EPLGLAHAFIIAEDFI--GGDPVALVL-----GD-----------NIFYGDGLSE----LLREAAARESGA 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339265237 166 -----------NFGCAAINDSSEIIHYVEKPTTFLSKWINCGVYLmqmgIIDTLADVFKNktlLSNSNNG-FHIPKALEA 233
Cdd:COG1209  131 tifgykvedpeRYGVVEFDEDGRVVSLEEKPKEPKSNLAVTGLYF----YDNDVVEIAKN---LKPSARGeLEITDANQA 203


                 .
gi 339265237 234 M 234
Cdd:COG1209  204 Y 204
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 9-155 8.35e-11

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


Pssm-ID: 133041 [Multi-domain]  Cd Length: 214  Bit Score: 59.59  E-value: 8.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339265237   9 YKAVILIGGpqKGTRFRPLSLDCPKPLFPIAGVPSVQHHIEALTKIpGLKEILFI--GFYQP--NDHWATFISDIQGQYS 84
Cdd:cd04198    1 FQAVILAGG--GGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKA-GFEDVIVVvpEEEQAeiSTYLRSFPLNLKQKLD 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 339265237  85 TVNIrylQEFAPLGTAGGIYHFRDQILlggTDAcFVLNADVCGDLPLMEmvdqlntLIDKHSATENILLML 155
Cdd:cd04198   78 EVTI---VLDEDMGTADSLRHIRKKIK---KDF-LVLSCDLITDLPLIE-------LVDLHRSHDASLTVL 134
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 9-217 1.04e-10

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


Pssm-ID: 133001 [Multi-domain]  Cd Length: 216  Bit Score: 59.19  E-value: 1.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339265237   9 YKAVILIGGpqKGTRFRPLSLDCPKPLFPIAGVPSVQHHIEALTKIpGLKEIlFIgFY-----QPNDHWATFISDIQGQY 83
Cdd:cd02507    1 FQAVVLADG--FGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKA-GVEEV-FV-VCcehsqAIIEHLLKSKWSSLSSK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339265237  84 STVNIRYLQEFAPLGTAGGIYHFRDQILlggTDAcFVLNADVCGDLPLMEMVDQLNtliDKHSATENILLML------TT 157
Cdd:cd02507   76 MIVDVITSDLCESAGDALRLRDIRGLIR---SDF-LLLSCDLVSNIPLSELLEERR---KKDKNAIATLTVLlasppvST 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 339265237 158 EAAR--EQSMNFGCAAINDSSEIIHY-------VEKPTTFLSKWINCGVYLMqMGIIDTLADVFKNKTL 217
Cdd:cd02507  149 EQSKktEEEDVIAVDSKTQRLLLLHYeedldedLELIIRKSLLSKHPNVTIR-TDLLDCHIYICSPDVL 216
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
10-125 1.93e-10

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 58.71  E-value: 1.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339265237  10 KAVILIGGpqKGTRFRPLSLDCPKPLFPIAGVPSVQHHIEALTKIpGLKEILFIGFYQpNDHWATFISDIQGQYSTV-NI 88
Cdd:COG1213    1 KAVILAAG--RGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAA-GIKDIVVVTGYK-AELIEEALARPGPDVTFVyNP 76

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 339265237  89 RYLQEfaplGTAGGIYHFRDQIllggTDACFVLNADV 125
Cdd:COG1213   77 DYDET----NNIYSLWLAREAL----DEDFLLLNGDV 105
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 11-125 7.73e-09

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: 54.16  E-value: 7.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339265237  11 AVILIGGpqKGTRFRPLSLDCPKPLFPIAGVPSVQHHIEALTKIpGLKEILFIGFYQpndhwATFISDIQGQYSTVNIRY 90
Cdd:cd02523    1 AIILAAG--RGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEA-GIDDIVIVTGYK-----KEQIEELLKKYPNIKFVY 72

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 339265237  91 LQEFAPLGTAGGIYHFRDQIllggTDACFVLNADV 125
Cdd:cd02523   73 NPDYAETNNIYSLYLARDFL----DEDFLLLEGDV 103
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 11-160 1.49e-08

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: 53.29  E-value: 1.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339265237  11 AVILIGGpqKGTRFRplSlDCPKPLFPIAGVPSVQHHIEALTKIpGLKEILFIGFYQpndhwatfISDIQGQYSTVNIRY 90
Cdd:cd02540    1 AVILAAG--KGTRMK--S-DLPKVLHPLAGKPMLEHVLDAARAL-GPDRIVVVVGHG--------AEQVKKALANPNVEF 66

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 339265237  91 -LQEfAPLGTAGGIyhfrdqilLGGTDACFVLNADV---CGDLPLMEmVDQLNTLIDKHSATENILLMLTTEAA 160
Cdd:cd02540   67 vLQE-EQLGTGHAV--------KQALPALKDFEGDVlvlYGDVPLIT-PETLQRLLEAHREAGADVTVLTAELE 130
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 11-222 1.16e-07

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 51.67  E-value: 1.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339265237  11 AVILIGGpqKGTRFRPlslDCPKPLFPIAGVPSVQHHIEALTKIPGLKEILFIGfyqpndHWATFISDIQGQYSTVNIRy 90
Cdd:PRK14355   6 AIILAAG--KGTRMKS---DLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVG------HQAEKVREHFAGDGDVSFA- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339265237  91 LQEfAPLGTAGGIYHFRDQiLLGGTDACFVLnadvCGDLPLMEmVDQLNTLIDKHSATENILLMLTTEAarEQSMNFGCA 170
Cdd:PRK14355  74 LQE-EQLGTGHAVACAAPA-LDGFSGTVLIL----CGDVPLLR-AETLQGMLAAHRATGAAVTVLTARL--ENPFGYGRI 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 339265237 171 AINDSSEIIHYVEK----PTTFLSKWINCGVYLMQMGIidtladVFKNKTLLSNSN 222
Cdd:PRK14355 145 VRDADGRVLRIVEEkdatPEERSIREVNSGIYCVEAAF------LFDAIGRLGNDN 194
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 7-206 4.54e-06

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 46.59  E-value: 4.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339265237   7 KSYKAVILIGGpqKGTRFRPLSLDCPKPLFPIAGVPSVQHHIEALTkIPGLKEILFIGFYQPNDHWATFISDiqGQYSTV 86
Cdd:PRK15480   2 KTRKGIILAGG--SGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLM-LAGIRDILIISTPQDTPRFQQLLGD--GSQWGL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339265237  87 NIRYLQEFAPLGTAGGIYHFRDqiLLGGTDACFVLNADVC--GDLP-LMEMVdqlntlIDKHSATeNILLMLTTEAAReq 163
Cdd:PRK15480  77 NLQYKVQPSPDGLAQAFIIGEE--FIGGDDCALVLGDNIFygHDLPkLMEAA------VNKESGA-TVFAYHVNDPER-- 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 339265237 164 smnFGCAAINDSSEIIHYVEKPTTFLSKWINCGVYLMQMGIID 206
Cdd:PRK15480 146 ---YGVVEFDQNGTAISLEEKPLQPKSNYAVTGLYFYDNDVVE 185
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 21-185 6.61e-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: 45.68  E-value: 6.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339265237  21 GTRFRPLSLDCPKPLFPIAGVPSVQHHIEALTKiPGLKEI-LFIGFY--QPNDHWATFISDIQG-QYSTVNIRYLQEFAP 96
Cdd:cd04197   11 NRRFRPLTKEKPRCLLPLANVPLIDYTLEFLAL-NGVEEVfVFCCSHsdQIKEYIEKSKWSKPKsSLMIVIIIMSEDCRS 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339265237  97 LGTA-------GGIY-HFrdqILLGGtdacfvlnaDVCGDLPLMEMVDQ--LNTLIDKhsatENILLMLTTEA-----AR 161
Cdd:cd04197   90 LGDAlrdldakGLIRgDF---ILVSG---------DVVSNIDLKEILEEhkERRKKDK----NAIMTMVLKEAspphrTR 153

                        170       180
                 ....*....|....*....|....
gi 339265237 162 EQSMNFGCAAINDSSEIIHYVEKP 185
Cdd:cd04197  154 RTGEEFVIAVDPKTSRLLHYEELP 177
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 11-160 7.15e-06

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: 46.17  E-value: 7.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339265237  11 AVILIGGpqKGTRFRplSlDCPKPLFPIAGVPSVQHHIEALTKIPGLKEILFIGfyqpndHWAtfiSDIQGQYSTVNIRY 90
Cdd:COG1207    5 VVILAAG--KGTRMK--S-KLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVG------HGA---EQVRAALADLDVEF 70

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 339265237  91 -LQEfAPLGTAGGIYHFRDQiLLGGTDACFVLnadvCGDLPLMEmVDQLNTLIDKHSATENILLMLTTEAA 160
Cdd:COG1207   71 vLQE-EQLGTGHAVQQALPA-LPGDDGTVLVL----YGDVPLIR-AETLKALLAAHRAAGAAATVLTAELD 134
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 11-222 3.62e-05

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 44.33  E-value: 3.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339265237  11 AVILIGGpqKGTRFRPlslDCPKPLFPIAGVPSVQHHIEALTKIPGLKEILFIGfyqpndHWAtfiSDIQGQYSTVNIRY 90
Cdd:PRK14356   8 ALILAAG--KGTRMHS---DKPKVLQTLLGEPMLRFVYRALRPLFGDNVWTVVG------HRA---DMVRAAFPDEDARF 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339265237  91 LQEFAPLGTAGGIYHFRDQILLGGTDACFVLNadvcGDLPLMEmVDQLNTLIDKHSATENILLMLTTEA----AREQSMN 166
Cdd:PRK14356  74 VLQEQQLGTGHALQCAWPSLTAAGLDRVLVVN----GDTPLVT-TDTIDDFLKEAAGADLAFMTLTLPDpgayGRVVRRN 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 339265237 167 FGCAAINDSSEIIHYVEKPTTflsKWINCGVYLMQMGIIDTLADvfknktLLSNSN 222
Cdd:PRK14356 149 GHVAAIVEAKDYDEALHGPET---GEVNAGIYYLRLDAVESLLP------RLTNAN 195
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 10-199 8.06e-05

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: 42.56  E-value: 8.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339265237  10 KAVILIGGpqKGTRFRPLSLDCPKPLFPIAGVPSVQHHIEALtKIPGLKEILFIGFYQPNDHWATFISDiqGQYSTVNIR 89
Cdd:cd02538    2 KGIILAGG--SGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTL-MLAGIREILIISTPEDLPLFKELLGD--GSDLGIRIT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339265237  90 YLQEFAPLGTAGGIY---HFrdqilLGGTDACFVLNADVCGDLPLMEMVDQLNTLidKHSATenILLMLTTEAAReqsmn 166
Cdd:cd02538   77 YAVQPKPGGLAQAFIigeEF-----IGDDPVCLILGDNIFYGQGLSPILQRAAAQ--KEGAT--VFGYEVNDPER----- 142

                        170       180       190
                 ....*....|....*....|....*....|...
gi 339265237 167 FGCAAINDSSEIIHYVEKPTTFLSKWINCGVYL 199
Cdd:cd02538  143 YGVVEFDENGRVLSIEEKPKKPKSNYAVTGLYF 175
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 11-138 8.67e-05

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


Pssm-ID: 463715 [Multi-domain]  Cd Length: 159  Bit Score: 41.80  E-value: 8.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339265237   11 AVILIGGpqKGTRFRPlsldcPKPLFPIAGVPSVQHHIEALTKIPGlkEILFIGfyqpNDHwatfisDIQGQYSTVNIRY 90
Cdd:pfam12804   1 AVILAGG--RSSRMGG-----DKALLPLGGKPLLERVLERLRPAGD--EVVVVA----NDE------EVLAALAGLGVPV 61

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 339265237   91 L-QEFAPLGTAGGIYHFRDQilLGGTDACFVLNAdvcgDLPLM--EMVDQL 138
Cdd:pfam12804  62 VpDPDPGQGPLAGLLAALRA--APGADAVLVLAC----DMPFLtpELLRRL 106
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 3-200 1.05e-04

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 42.66  E-value: 1.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339265237   3 TSAEKSYKAVILIGGpqKGTRFRPLsldCPKPLFPIAGVPSVQHHIEALTKIPGLKEILFIGfyqpndHWAtfiSDIQGQ 82
Cdd:PRK14358   2 TEQTRPLDVVILAAG--QGTRMKSA---LPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTG------HGA---EQVEAA 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339265237  83 YSTVNIRYLQEFAPLGTAGGiyhfrdqiLLGGTDACFVLNADVC---GDLPLMEmVDQLNTLIDKHSATENILLMLTTEA 159
Cdd:PRK14358  68 LQGSGVAFARQEQQLGTGDA--------FLSGASALTEGDADILvlyGDTPLLR-PDTLRALVADHRAQGSAMTILTGEL 138

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 339265237 160 AreQSMNFGCAAINDSSEIIHYVE-KPTTFLSKWI---NCGVYLM 200
Cdd:PRK14358 139 P--DATGYGRIVRGADGAVERIVEqKDATDAEKAIgefNSGVYVF 181
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
 11-210 8.42e-04

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: 39.48  E-value: 8.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339265237  11 AVILIGGpqKGTRFRPLSLDCPKPLFPIAGVPSVQHhieaLTKI---PGLKE-ILFIGF-------YQPNDHWATfiSDI 79
Cdd:cd02524    1 VVILAGG--LGTRLSEETELKPKPMVEIGGRPILWH----IMKIyshYGHNDfILCLGYkghvikeYFLNYFLHN--SDV 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339265237  80 QGQYSTVNIRYLQE--------FAPLG----TAGGIYHFRDQIllgGTDACFVLN-ADVCGDLPlmemvdqLNTLIDKHS 146
Cdd:cd02524   73 TIDLGTNRIELHNSdiedwkvtLVDTGlntmTGGRLKRVRRYL---GDDETFMLTyGDGVSDVN-------INALIEFHR 142

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 339265237 147 AtENILLMLTteAAREQSMnFGCAAINDSSEIIHYVEKPTTFLSkWINCGVYLMQMGIIDTLAD 210
Cdd:cd02524  143 S-HGKLATVT--AVHPPGR-FGELDLDDDGQVTSFTEKPQGDGG-WINGGFFVLEPEVFDYIDG 201
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-54 8.72e-04

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 40.01  E-value: 8.72e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 339265237   1 MKTSAeksYKAVILIGGpqKGTRfrpLSLDCPKPLFPIAGVPSVQHHIEALTKI 54
Cdd:PRK09451   1 MLNSA---MSVVILAAG--KGTR---MYSDLPKVLHTLAGKPMVQHVIDAANEL 46
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-125 2.46e-03

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 38.69  E-value: 2.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339265237   4 SAEKSYKAVILIGGpqKGTRFRPlslDCPKPLFPIAGVPSVQHHIEALTKIPGLKEILFIGFYQPNdhWATFISDIQGQY 83
Cdd:PRK14353   1 MTDRTCLAIILAAG--EGTRMKS---SLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGPGAEA--VAAAAAKIAPDA 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 339265237  84 STVniryLQEfAPLGTAGGIYHFRDQiLLGGTDACFVLNADV 125
Cdd:PRK14353  74 EIF----VQK-ERLGTAHAVLAAREA-LAGGYGDVLVLYGDT 109
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
 10-63 8.87e-03

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: 36.40  E-value: 8.87e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 339265237  10 KAVILIGGpqKGTRFRPLS-LDCPKPLFPIAGVPS-VQHHIEALTKIPGLKEILFI 63
Cdd:cd02509    2 YPVILAGG--SGTRLWPLSrESYPKQFLKLFGDKSlLQQTLDRLKGLVPPDRILVV 55
 
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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