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Conserved domains on  [gi|516731103|ref|WP_018071331|]
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NTP transferase domain-containing protein [Rhizobium ruizarguesonis]

Protein Classification

MocA family protein( domain architecture ID 10005267)

MocA family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
3-194 6.48e-65

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


:

Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 198.46  E-value: 6.48e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516731103   3 KASVAIVILAAGKASRMGAggkHKLLAEFGGVPLVRRSALTALGADAASVIVVTGHRRSEIEAALDELALTLVDNPDYAS 82
Cdd:COG2068    1 MSKVAAIILAAGASSRMGR---PKLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADAEEVAAALAGLGVRVVVNPDWEE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516731103  83 GMASSLMAGLSSkRADGADGILVMLADMPGISTAHLNALIFTFRNAGGeAVVRAVSQGKPGNPVILPRSLNHAVLRLEGD 162
Cdd:COG2068   78 GMSSSLRAGLAA-LPADADAVLVLLGDQPLVTAETLRRLLAAFRESPA-SIVAPTYDGRRGHPVLFSRRLFPELLALTGD 155

                        170       180       190
                 ....*....|....*....|....*....|...
gi 516731103 163 VGARDVIGTSGLPVLDVDVGDAACL-DVDTPDD 194
Cdd:COG2068  156 QGARALLRRHPDRVRLVPVDDPGVLlDIDTPED 188
 
Name Accession Description Interval E-value
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
3-194 6.48e-65

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 198.46  E-value: 6.48e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516731103   3 KASVAIVILAAGKASRMGAggkHKLLAEFGGVPLVRRSALTALGADAASVIVVTGHRRSEIEAALDELALTLVDNPDYAS 82
Cdd:COG2068    1 MSKVAAIILAAGASSRMGR---PKLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADAEEVAAALAGLGVRVVVNPDWEE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516731103  83 GMASSLMAGLSSkRADGADGILVMLADMPGISTAHLNALIFTFRNAGGeAVVRAVSQGKPGNPVILPRSLNHAVLRLEGD 162
Cdd:COG2068   78 GMSSSLRAGLAA-LPADADAVLVLLGDQPLVTAETLRRLLAAFRESPA-SIVAPTYDGRRGHPVLFSRRLFPELLALTGD 155

                        170       180       190
                 ....*....|....*....|....*....|...
gi 516731103 163 VGARDVIGTSGLPVLDVDVGDAACL-DVDTPDD 194
Cdd:COG2068  156 QGARALLRRHPDRVRLVPVDDPGVLlDIDTPED 188
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 6-194 9.96e-59

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: 182.37  E-value: 9.96e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516731103   6 VAIVILAAGKASRMGAggkHKLLAEFGGVPLVRRSALTALGADAASVIVVTGHRRSEIEAALDELALTLVDNPDYASGMA 85
Cdd:cd04182    1 IAAIILAAGRSSRMGG---NKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALAGLPVVVVINPDWEEGMS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516731103  86 SSLMAGLSSKRADgADGILVMLADMPGISTAHLNALIFTFRNAgGEAVVRAVSQGKPGNPVILPRSLNHAVLRLEGDVGA 165
Cdd:cd04182   78 SSLAAGLEALPAD-ADAVLILLADQPLVTAETLRALIDAFRED-GAGIVAPVYQGRRGHPVLFPRSLFPELLALSGDKGA 155

                        170       180
                 ....*....|....*....|....*....
gi 516731103 166 RDVIGTSGLPVLDVDVGDAACLDVDTPDD 194
Cdd:cd04182  156 RSLLRAHPDRVVVEVDDPGVLIDIDTPED 184
matur_MocA_YgfJ TIGR03310
molybdenum cofactor cytidylyltransferase; Members of this protein include MocA, which ...
 9-194 1.16e-46

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


Pssm-ID: 274516  Cd Length: 188  Bit Score: 151.72  E-value: 1.16e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516731103    9 VILAAGKASRMGAGgkhKLLAEFGGVPLVRRSALTALGADAASVIVVTGHRRSEIEAAL-DELALTLVDNPDYASGMASS 87
Cdd:TIGR03310   3 IILAAGLSSRMGQN---KLLLPYKGKTILEHVVDNALRLFFDEVILVLGHEADELVALLaNHSNITLVHNPQYAEGQSSS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516731103   88 LMAGLSSkrADGADGILVMLADMPGISTAHLNALIFTFRnAGGEAVVRAVSQGKPGNPVILPRSLNHAVLRLEGDVGARD 167
Cdd:TIGR03310  80 IKLGLEL--PVQSDGYLFLLGDQPFVTPDIIQLLLEAFA-LKNDEIVVPLYKGKRGHPVLFPRKLFPELLALTGDTGGRQ 156

                         170       180
                  ....*....|....*....|....*...
gi 516731103  168 VIGTSGLPVLDVDVGDAACL-DVDTPDD 194
Cdd:TIGR03310 157 ILRELPHEVKYVEVKDPGILfDIDTPED 184
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 9-169 2.10e-33

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: 116.91  E-value: 2.10e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516731103    9 VILAAGKASRMGaggKHKLLAEFGGVPLVRRsALTALGADAASVIVVTGHRrsEIEAALDELALTLVDNPDYASGMASSL 88
Cdd:pfam12804   2 VILAGGRSSRMG---GDKALLPLGGKPLLER-VLERLRPAGDEVVVVANDE--EVLAALAGLGVPVVPDPDPGQGPLAGL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516731103   89 MAGLSskRADGADGILVMLADMPGISTAHLNALIFTFRNAGGEAVVrAVSQGKPGNPVILPRSLNHAVLRLEGDVGARDV 168
Cdd:pfam12804  76 LAALR--AAPGADAVLVLACDMPFLTPELLRRLLAAAEESGADIVV-PVYDGGRGHPLLYRRRLLPALEALLGDRGLRRL 152


                  .
gi 516731103  169 I 169
Cdd:pfam12804 153 L 153
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-134 1.90e-09

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 56.10  E-value: 1.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516731103   4 ASVAIVILAAGKASRMGAGgKHKLLAEFGGVPLVRRSALTALGADAASVIVVTGHRRSEIEAALDELALT-LVDNPDYAS 82
Cdd:PRK14352   3 RPTAVIVLAAGAGTRMRSD-TPKVLHTLAGRSMLGHVLHAAAGLAPQHLVVVVGHDRERVAPAVAELAPEvDIAVQDEQP 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 516731103  83 GMASSLMAGLSSKRADGADGILVMLADMPGISTAHLNALIFTFRNAGGEAVV 134
Cdd:PRK14352  82 GTGHAVQCALEALPADFDGTVVVTAGDVPLLDGETLADLVATHTAEGNAVTV 133
 
Name Accession Description Interval E-value
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
3-194 6.48e-65

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 198.46  E-value: 6.48e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516731103   3 KASVAIVILAAGKASRMGAggkHKLLAEFGGVPLVRRSALTALGADAASVIVVTGHRRSEIEAALDELALTLVDNPDYAS 82
Cdd:COG2068    1 MSKVAAIILAAGASSRMGR---PKLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADAEEVAAALAGLGVRVVVNPDWEE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516731103  83 GMASSLMAGLSSkRADGADGILVMLADMPGISTAHLNALIFTFRNAGGeAVVRAVSQGKPGNPVILPRSLNHAVLRLEGD 162
Cdd:COG2068   78 GMSSSLRAGLAA-LPADADAVLVLLGDQPLVTAETLRRLLAAFRESPA-SIVAPTYDGRRGHPVLFSRRLFPELLALTGD 155

                        170       180       190
                 ....*....|....*....|....*....|...
gi 516731103 163 VGARDVIGTSGLPVLDVDVGDAACL-DVDTPDD 194
Cdd:COG2068  156 QGARALLRRHPDRVRLVPVDDPGVLlDIDTPED 188
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 6-194 9.96e-59

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: 182.37  E-value: 9.96e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516731103   6 VAIVILAAGKASRMGAggkHKLLAEFGGVPLVRRSALTALGADAASVIVVTGHRRSEIEAALDELALTLVDNPDYASGMA 85
Cdd:cd04182    1 IAAIILAAGRSSRMGG---NKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALAGLPVVVVINPDWEEGMS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516731103  86 SSLMAGLSSKRADgADGILVMLADMPGISTAHLNALIFTFRNAgGEAVVRAVSQGKPGNPVILPRSLNHAVLRLEGDVGA 165
Cdd:cd04182   78 SSLAAGLEALPAD-ADAVLILLADQPLVTAETLRALIDAFRED-GAGIVAPVYQGRRGHPVLFPRSLFPELLALSGDKGA 155

                        170       180
                 ....*....|....*....|....*....
gi 516731103 166 RDVIGTSGLPVLDVDVGDAACLDVDTPDD 194
Cdd:cd04182  156 RSLLRAHPDRVVVEVDDPGVLIDIDTPED 184
matur_MocA_YgfJ TIGR03310
molybdenum cofactor cytidylyltransferase; Members of this protein include MocA, which ...
 9-194 1.16e-46

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


Pssm-ID: 274516  Cd Length: 188  Bit Score: 151.72  E-value: 1.16e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516731103    9 VILAAGKASRMGAGgkhKLLAEFGGVPLVRRSALTALGADAASVIVVTGHRRSEIEAAL-DELALTLVDNPDYASGMASS 87
Cdd:TIGR03310   3 IILAAGLSSRMGQN---KLLLPYKGKTILEHVVDNALRLFFDEVILVLGHEADELVALLaNHSNITLVHNPQYAEGQSSS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516731103   88 LMAGLSSkrADGADGILVMLADMPGISTAHLNALIFTFRnAGGEAVVRAVSQGKPGNPVILPRSLNHAVLRLEGDVGARD 167
Cdd:TIGR03310  80 IKLGLEL--PVQSDGYLFLLGDQPFVTPDIIQLLLEAFA-LKNDEIVVPLYKGKRGHPVLFPRKLFPELLALTGDTGGRQ 156

                         170       180
                  ....*....|....*....|....*...
gi 516731103  168 VIGTSGLPVLDVDVGDAACL-DVDTPDD 194
Cdd:TIGR03310 157 ILRELPHEVKYVEVKDPGILfDIDTPED 184
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 9-169 2.10e-33

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: 116.91  E-value: 2.10e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516731103    9 VILAAGKASRMGaggKHKLLAEFGGVPLVRRsALTALGADAASVIVVTGHRrsEIEAALDELALTLVDNPDYASGMASSL 88
Cdd:pfam12804   2 VILAGGRSSRMG---GDKALLPLGGKPLLER-VLERLRPAGDEVVVVANDE--EVLAALAGLGVPVVPDPDPGQGPLAGL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516731103   89 MAGLSskRADGADGILVMLADMPGISTAHLNALIFTFRNAGGEAVVrAVSQGKPGNPVILPRSLNHAVLRLEGDVGARDV 168
Cdd:pfam12804  76 LAALR--AAPGADAVLVLACDMPFLTPELLRRLLAAAEESGADIVV-PVYDGGRGHPLLYRRRLLPALEALLGDRGLRRL 152


                  .
gi 516731103  169 I 169
Cdd:pfam12804 153 L 153
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 8-198 7.35e-17

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: 75.73  E-value: 7.35e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516731103   8 IVILAAGKASRMGA--GGKHKLLAEFGGVPLVRRSALTALGADAASVIVVTGHRRSEIEAALDEL-ALTLVDNPDYAS-G 83
Cdd:cd02523    1 AIILAAGRGSRLRPltEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKKYpNIKFVYNPDYAEtN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516731103  84 MASSLMAGLSSKRAD----GAD-----GILVMLADMPG----ISTAHLNALIFTFRNAGGEAVVRAVSQGKPGNPV-ILP 149
Cdd:cd02523   81 NIYSLYLARDFLDEDflllEGDvvfdpSILERLLSSPAdnaiLVDKKTKEWEDEYVKDLDDAGVLLGIISKAKNLEeIQG 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516731103 150 RSLNHAVLRLEG---------------------DVGARDVIGTSGLPVLDVDVGDaaCLDVDTPDDIVAA 198
Cdd:cd02523  161 EYVGISKFSPEDadrlaealeelieagrvnlyyEDALQRLISEEGVKVKDISDGF--WYEIDDLEDLERA 228
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
9-198 1.44e-16

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 74.89  E-value: 1.44e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516731103   9 VILAAGKASRMGAG--GKHKLLAEFGGVPLVRRS--ALTALGADaaSVIVVTGHRRSEIEAALDE--LALTLVDNPDYAS 82
Cdd:COG1213    3 VILAAGRGSRLGPLtdDIPKCLVEIGGKTLLERQleALAAAGIK--DIVVVTGYKAELIEEALARpgPDVTFVYNPDYDE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516731103  83 -GMASSLMAGlsskRADGADGILVMLADM---PGI-----STAHLNALI--FTFRNAGGEAV---------VRAVSQGKP 142
Cdd:COG1213   81 tNNIYSLWLA----REALDEDFLLLNGDVvfdPAIlkrllASDGDIVLLvdRKWEKPLDEEVkvrvdedgrIVEIGKKLP 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516731103 143 GNPVI----------------LPRSLNHAVLRLEGDVGARDVIGT---SGLPVLDVDVGDAACLDVDTPDDIVAA 198
Cdd:COG1213  157 PEEADgeyigifkfsaegaaaLREALEALIDEGGPNLYYEDALQElidEGGPVKAVDIGGLPWVEIDTPEDLERA 231
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 3-198 4.47e-16

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: 72.53  E-value: 4.47e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516731103   3 KASVAIVILAAGKASRMGAggkHKLLAEFGGVPLVRRsALTALGADAASVIVVTghRRSEIEAALDelALTLVDNPDYA- 81
Cdd:COG0746    2 TMPITGVILAGGRSRRMGQ---DKALLPLGGRPLLER-VLERLRPQVDEVVIVA--NRPERYAALG--VPVVPDDPPGAg 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516731103  82 --SGMASSLmaglsskRADGADGILVMLADMPGISTAHLNALIfTFRNAGGEAVVrAVSQGKPgNPV--ILPRSLNHAVL 157
Cdd:COG0746   74 plAGILAAL-------EAAPAEWVLVLACDMPFLPPDLVRRLL-EALEEGADAVV-PRSGGRL-EPLfaLYRRSLLPALE 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 516731103 158 RL--EGDVGARDVIGTSGLPVLDVDVGDAACLDVDTPDDIVAA 198
Cdd:COG0746  144 AAlaEGERSLRALLERLDVVYVPFEDLDDAFFNVNTPEDLARA 186
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 8-134 2.78e-14

N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate uridyltransferase (GlmU). GlmU is an essential bacterial enzyme with both an acetyltransferase and an uridyltransferase activity which have been mapped to the C-terminal and N-terminal domains, respectively. This family represents the N-terminal uridyltransferase. GlmU performs the last two steps in the synthesis of UDP-N-acetylglucosamine (UDP-GlcNAc), which is an essential precursor in both the peptidoglycan and the lipopolysaccharide metabolic pathways in Gram-positive and Gram-negative bacteria, respectively.


Pssm-ID: 133020 [Multi-domain]  Cd Length: 229  Bit Score: 68.70  E-value: 2.78e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516731103   8 IVILAAGKASRMGAGgKHKLLAEFGGVPLVRRSALTALGADAASVIVVTGHRRSEIEAALDELALTLV--DNPDyasGMA 85
Cdd:cd02540    1 AVILAAGKGTRMKSD-LPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVKKALANPNVEFVlqEEQL---GTG 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 516731103  86 SSLMAGLSSKRADGADgILVMLADMPGISTAHLNALIFTFRNAGGEAVV 134
Cdd:cd02540   77 HAVKQALPALKDFEGD-VLVLYGDVPLITPETLQRLLEAHREAGADVTV 124
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 9-194 3.95e-14

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: 67.22  E-value: 3.95e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516731103   9 VILAAGKASRMGAggkHKLLAEFGGVPLVRRsALTALGADAASVIVVTgHRRSEIEAALDelALTLVDNPDYA---SGMA 85
Cdd:cd02503    4 VILAGGKSRRMGG---DKALLELGGKPLLEH-VLERLKPLVDEVVISA-NRDQERYALLG--VPVIPDEPPGKgplAGIL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516731103  86 SSLmaglsskRADGADGILVMLADMPGISTAHLNALIfTFRNAGGEAVVrAVSQGKPgNPV--ILPRSLNHAVLRL--EG 161
Cdd:cd02503   77 AAL-------RAAPADWVLVLACDMPFLPPELLERLL-AAAEEGADAVV-PKSGGRL-QPLhaLYHKSLLPALEELleAG 146

                        170       180       190
                 ....*....|....*....|....*....|....
gi 516731103 162 DVGARDVIGTSGLPVLDV-DVGDAACLDVDTPDD 194
Cdd:cd02503  147 ERRLRRLLEKLGVQYVEFeDERLDAFFNINTPED 180
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 4-134 3.08e-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: 67.36  E-value: 3.08e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516731103   4 ASVAIVILAAGKASRMGAGgKHKLLAEFGGVPLVRRSALTALGADAASVIVVTGHRRSEIEAALDELALTLVD-NPDYAS 82
Cdd:COG1207    1 SPLAVVILAAGKGTRMKSK-LPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVRAALADLDVEFVLqEEQLGT 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 516731103  83 GMAssLMAGLSSKRADGADgILVMLADMPGISTAHLNALIFTFRNAGGEAVV 134
Cdd:COG1207   80 GHA--VQQALPALPGDDGT-VLVLYGDVPLIRAETLKALLAAHRAAGAAATV 128
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-134 1.90e-09

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 56.10  E-value: 1.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516731103   4 ASVAIVILAAGKASRMGAGgKHKLLAEFGGVPLVRRSALTALGADAASVIVVTGHRRSEIEAALDELALT-LVDNPDYAS 82
Cdd:PRK14352   3 RPTAVIVLAAGAGTRMRSD-TPKVLHTLAGRSMLGHVLHAAAGLAPQHLVVVVGHDRERVAPAVAELAPEvDIAVQDEQP 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 516731103  83 GMASSLMAGLSSKRADGADGILVMLADMPGISTAHLNALIFTFRNAGGEAVV 134
Cdd:PRK14352  82 GTGHAVQCALEALPADFDGTVVVTAGDVPLLDGETLADLVATHTAEGNAVTV 133
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 8-134 4.94e-09

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 54.99  E-value: 4.94e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516731103   8 IVILAAGKASRMGAGgKHKLLAEFGGVPLVRRSALTALGADAASVIVVTGHRRSEIEAALDELALTLVDNpDYASGMASS 87
Cdd:PRK14358  10 VVILAAGQGTRMKSA-LPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGAEQVEAALQGSGVAFARQ-EQQLGTGDA 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 516731103  88 LMAGLSSKRADGADgILVMLADMPGISTAHLNALIFTFRNAGGEAVV 134
Cdd:PRK14358  88 FLSGASALTEGDAD-ILVLYGDTPLLRPDTLRALVADHRAQGSAMTI 133
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 7-122 7.05e-09

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 54.73  E-value: 7.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516731103   7 AIVILAAGKASRMGAgGKHKLLAEFGGVPLVRR--SALTALGADAasVIVVTGHRRSEIEAALDELALTLVDNPDYAsGM 84
Cdd:PRK14356   7 GALILAAGKGTRMHS-DKPKVLQTLLGEPMLRFvyRALRPLFGDN--VWTVVGHRADMVRAAFPDEDARFVLQEQQL-GT 82

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 516731103  85 ASSLMAGLSSKRADGADGILVMLADMPGISTAHLNALI 122
Cdd:PRK14356  83 GHALQCAWPSLTAAGLDRVLVVNGDTPLVTTDTIDDFL 120
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-134 1.30e-07

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 51.02  E-value: 1.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516731103   1 MLKASVAIVILAAGKASRMGAGgKHKLLAEFGGVPLVRRSALTALGADAASVIVVTGHRRSEIEAA---LDELALTLVDN 77
Cdd:PRK14353   1 MTDRTCLAIILAAGEGTRMKSS-LPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGPGAEAVAAAaakIAPDAEIFVQK 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 516731103  78 PDYASGMASslmagLSSKRA--DGADGILVMLADMPGISTAHLNALIftFRNAGGEAVV 134
Cdd:PRK14353  80 ERLGTAHAV-----LAAREAlaGGYGDVLVLYGDTPLITAETLARLR--ERLADGADVV 131
ispD TIGR00453
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ...
 9-198 5.89e-07

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: 48.05  E-value: 5.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516731103    9 VILAAGKASRMGAgGKHKLLAEFGGVPLVRRS--ALTALGAdAASVIVVTghrrSEIEAALDELALTLVDNPDYASGMAS 86
Cdd:TIGR00453   3 VIPAAGRGTRFGS-GVPKQYLELGGRPLLEHAldAFLAHPA-IDEVVVVV----SPDDTEFFQKYLVARAVPKIVAGGDT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516731103   87 ---SLMAGLssKRADGADGILVMLADMPGISTAHLNALIFTFRNAGGEAVVRAVS----QGKPGNPVI--LPRSL----- 152
Cdd:TIGR00453  77 rqdSVRNGL--KALKDAEFVLVHDAARPFVPKELLDRLLEALRKAGAAILALPVAdtlkRVEADGFVVetVDREGlwaaq 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 516731103  153 ------------NHAVLRLEGDVGARD--VIGTSGLPVLDVDvGDAACLDVDTPDDIVAA 198
Cdd:TIGR00453 155 tpqafrtellkkALARAKLEGFEITDDasAVEKLGGKVQLVE-GDALNFKITTPEDLALA 213
PRK02726 PRK02726
molybdenum cofactor guanylyltransferase;
2-56 6.76e-07

molybdenum cofactor guanylyltransferase;


Pssm-ID: 235063  Cd Length: 200  Bit Score: 47.72  E-value: 6.76e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 516731103   2 LKASVAIVILAAGKASRMgagGKHKLLAEFGGVPLVRRSALTALGAdAASVIVVT 56
Cdd:PRK02726   4 VKNNLVALILAGGKSSRM---GQDKALLPWQGVPLLQRVARIAAAC-ADEVYIIT 54
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 9-75 3.66e-06

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


Pssm-ID: 440824  Cd Length: 224  Bit Score: 45.89  E-value: 3.66e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516731103   9 VILAAGKASRMGAGGKhKLLAEFGGVPLVRRSALTALGADAASVIVVTGH--RRSEIEAALDELALTLV 75
Cdd:COG1211    1 IIPAAGSGSRMGAGIP-KQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPpdDIEYFEELLAKYGIDKP 68
mobA PRK00317
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
 8-152 9.08e-06

molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed


Pssm-ID: 234725 [Multi-domain]  Cd Length: 193  Bit Score: 44.41  E-value: 9.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516731103   8 IVILAAGKASRMgaGGKHKLLAEFGGVPLVRRsALTALGADAASVIVVT-GHRrseieAALDELALTLV--DNPDYA--- 81
Cdd:PRK00317   6 GVILAGGRSRRM--GGVDKGLQELNGKPLIQH-VIERLAPQVDEIVINAnRNL-----ARYAAFGLPVIpdSLADFPgpl 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516731103  82 SGMAsslmAGLSSKRadgADGILVMLADMPGISTAHLNALIFTFRNAggEAVVRAVSQGKPGNPVI--LPRSL 152
Cdd:PRK00317  78 AGIL----AGLKQAR---TEWVLVVPCDTPFIPPDLVARLAQAAGKD--DADVAWAHDGGRLHPTFalYSVAL 141
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-142 9.79e-06

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 45.12  E-value: 9.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516731103   4 ASVAIVILAAGKASRMGAGgKHKLLAEFGGVPLVRRSALTALGADAASVIVVTGHR----------RSEIEAALDELALt 73
Cdd:PRK14355   2 NNLAAIILAAGKGTRMKSD-LVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQaekvrehfagDGDVSFALQEEQL- 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516731103  74 lvdNPDYASGMASSLMAGLSSKradgadgILVMLADMPGISTAHLNALIFTFRNAGGEAVVRAVSQGKP 142
Cdd:PRK14355  80 ---GTGHAVACAAPALDGFSGT-------VLILCGDVPLLRAETLQGMLAAHRATGAAVTVLTARLENP 138
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 6-138 1.19e-05

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: 44.44  E-value: 1.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516731103   6 VAIVILAAGKASRMGAGGKhKLLAEFGGVPLVRRSALTALGADAASVIVVTGHrRSEIEAALDELALTLVDNPDYASGMA 85
Cdd:cd02516    1 VAAIILAAGSGSRMGADIP-KQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVP-PDDIDLAKELAKYGLSKVVKIVEGGA 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 516731103  86 S---SLMAGLSSKRADGADGILVMLADMPGISTAHLNALIFTFRNAGGEAVVRAVS 138
Cdd:cd02516   79 TrqdSVLNGLKALPDADPDIVLIHDAARPFVSPELIDRLIDALKEYGAAIPAVPVT 134
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 11-133 8.35e-05

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: 41.41  E-value: 8.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516731103  11 LAAGKASRMGagGKHKLLAEFGGVPLVRR--SALTALGADaaSVIVVTGHRRSEIEAALDELALTLVDNPDyaSGMASSL 88
Cdd:COG2266    1 MAGGKGTRLG--GGEKPLLEICGKPMIDRviDALEESCID--KIYVAVSPNTPKTREYLKERGVEVIETPG--EGYVEDL 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 516731103  89 MAGLSSKRadgaDGILVMLADMPGISTAHLNALIFTFRNAGGEAV 133
Cdd:COG2266   75 NEALESIS----GPVLVVPADLPLLTPEIIDDIIDAYLESGKPSL 115
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 9-134 9.32e-05

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 42.51  E-value: 9.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516731103   9 VILAAGKASRMGAgGKHKLLAEFGGVPLVRRSALTALGADAASVIVVTGHRRSEIEAALDELALTLVDNPDYASG----M 84
Cdd:PRK14354   6 IILAAGKGTRMKS-KLPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVGHGAEEVKEVLGDRSEFALQEEQLGTGhavmQ 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 516731103  85 ASSLMAGLsskraDGAdgILVMLADMPGISTAHLNALIFTFRNAGGEAVV 134
Cdd:PRK14354  85 AEEFLADK-----EGT--TLVICGDTPLITAETLKNLIDFHEEHKAAATI 127
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 9-134 1.31e-04

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: 41.29  E-value: 1.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516731103   9 VILAAGKASRMGAGGKH--KLLAEFGGVPLVRRS--ALTALGADaaSVIVVTGHRRSEIEAALDE-----LALTLVDNPD 79
Cdd:COG1208    3 VILAGGLGTRLRPLTDTrpKPLLPVGGKPLLEHIleRLAAAGIT--EIVINVGYLAEQIEEYFGDgsrfgVRITYVDEGE 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 516731103  80 yASGMASSLmaglssKRAD---GADGILVMLADmpGISTAHLNALIFTFRNAGGEAVV 134
Cdd:COG1208   81 -PLGTGGAL------KRALpllGDEPFLVLNGD--ILTDLDLAALLAFHREKGADATL 129
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-122 1.57e-04

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 41.55  E-value: 1.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516731103   1 MLKASVAIVILAAGKASRMGAgGKHKLLAEFGGVPLVRRSALTALGADAASVIVVTGHRRSEIEAALDELALTLVDNPD- 79
Cdd:PRK09451   1 MLNSAMSVVILAAGKGTRMYS-DLPKVLHTLAGKPMVQHVIDAANELGAQHVHLVYGHGGDLLKQTLADEPLNWVLQAEq 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 516731103  80 YASGMAsslMAGLSSKRADGADgILVMLADMPGISTAHLNALI 122
Cdd:PRK09451  80 LGTGHA---MQQAAPFFADDED-ILMLYGDVPLISVETLQRLR 118
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 6-70 8.31e-04

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 39.53  E-value: 8.31e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516731103   6 VAIVILAAGKASRMgAGGKHKLLAEFGGVPLVRRSALTALGADAASVIVVTGHRRSEIEAALDEL 70
Cdd:PRK14360   2 LAVAILAAGKGTRM-KSSLPKVLHPLGGKSLVERVLDSCEELKPDRRLVIVGHQAEEVEQSLAHL 65
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 9-122 1.22e-03

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 38.98  E-value: 1.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516731103   9 VILAAGKASRMGAggKH-KLLAEFGGVPLVRRSALTAlGADAASVIVVTGHRRSEIEAALDELALTLVDNPDYASGMAss 87
Cdd:PRK14357   4 LVLAAGKGTRMKS--KIpKVLHKISGKPMINWVIDTA-KKVAQKVGVVLGHEAELVKKLLPEWVKIFLQEEQLGTAHA-- 78

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 516731103  88 LMAGLSSkrADGADGILVMLADMPGISTAHLNALI 122
Cdd:PRK14357  79 VMCARDF--IEPGDDLLILYGDVPLISENTLKRLI 111
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
3-56 2.19e-03

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 37.81  E-value: 2.19e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 516731103   3 KASVAIVILAAGKASRMGAgGKHKLLAEFGGVPLVRRSALTALGADA-ASVIVVT 56
Cdd:PRK00155   1 MMMVYAIIPAAGKGSRMGA-DRPKQYLPLGGKPILEHTLEAFLAHPRiDEIIVVV 54
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 5-122 2.86e-03

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 37.66  E-value: 2.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516731103   5 SVAIVILAAGKASRMGAgGKHKLLAEFGGVPLVRRSALTALgADAASVIVVTGHRRSEIEAALDE----LALTLVDNPDY 80
Cdd:PRK14359   2 KLSIIILAAGKGTRMKS-SLPKVLHTICGKPMLFYILKEAF-AISDDVHVVLHHQKERIKEAVLEyfpgVIFHTQDLENY 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 516731103  81 aSGMASSLMaGLSSKradgADGILVMLADMPGISTAHLNALI 122
Cdd:PRK14359  80 -PGTGGALM-GIEPK----HERVLILNGDMPLVEKDELEKLL 115
molyb_mobA TIGR02665
molybdenum cofactor guanylyltransferase, proteobacterial; In many molybdopterin-containing ...
 6-39 4.14e-03

molybdenum cofactor guanylyltransferase, proteobacterial; In many molybdopterin-containing enzymes, including nitrate reductase and dimethylsulfoxide reductase, the cofactor is molybdopterin-guanine dinucleotide. The family described here contains MobA, molybdenum cofactor guanylyltransferase, from the Proteobacteria only. MobA can reconstitute molybdopterin-guanine dinucleotide biosynthesis without the product of the neighboring gene MobB. The probable MobA proteins of other lineages differ sufficiently that they are not included in scope of this family. [Biosynthesis of cofactors, prosthetic groups, and carriers, Molybdopterin]


Pssm-ID: 274249  Cd Length: 186  Bit Score: 36.49  E-value: 4.14e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 516731103    6 VAIVILAAGKASRMgaGGKHKLLAEFGGVPLVRR 39
Cdd:TIGR02665   1 ISGVILAGGRARRM--GGRDKGLVELGGKPLIEH 32
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 9-134 5.95e-03

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: 36.40  E-value: 5.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516731103   9 VILAAGKASRMG--AGGKHKLLAEFGGVPLVRR--SALTALGADaaSVIVVTGHRRSEIEAALDELALTLVdNPDYAS-- 82
Cdd:cd04181    2 VILAAGKGTRLRplTDTRPKPLLPIAGKPILEYiiERLARAGID--EIILVVGYLGEQIEEYFGDGSKFGV-NIEYVVqe 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 516731103  83 ---GMASSLMAGlssKRADGADGILVMLADMpgISTAHLNALIFTFRNAGGEAVV 134
Cdd:cd04181   79 eplGTAGAVRNA---EDFLGDDDFLVVNGDV--LTDLDLSELLRFHREKGADATI 128
IspD pfam01128
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ...
 8-122 7.64e-03

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes which catalyze the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from cytidine triphosphate and 2-C-methyl-D-erythritol 4-phosphate (MEP).


Pssm-ID: 460075  Cd Length: 219  Bit Score: 36.27  E-value: 7.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516731103    8 IVILAAGKASRMGAgGKHKLLAEFGGVPLVRRSALTALGADAASVIVVTGH--RRSEIEAALDELALTLVDNpdyASGMA 85
Cdd:pfam01128   1 AVIPAAGSGKRMGA-GVPKQFLQLLGQPLLEHTVDAFLASPVVDRIVVAVSpdDTPEFRQLLGDPSIQLVAG---GDTRQ 76

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 516731103   86 SSLMAGLSSkRADGADGILVMLADMPGISTAHLNALI 122
Cdd:pfam01128  77 DSVLNGLKA-LAGTAKFVLVHDGARPCLPHADLARLL 112
ispDF PRK09382
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ...
 1-72 7.93e-03

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


Pssm-ID: 236492 [Multi-domain]  Cd Length: 378  Bit Score: 36.36  E-value: 7.93e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516731103   1 MLKASVAIVILAAGKASRMGAGGKhKLLAEFGGVPLVRRS--ALTALGADAASVIVVTGHRRSEIEAALDELAL 72
Cdd:PRK09382   1 TLMSDISLVIVAAGRSTRFSAEVK-KQWLRIGGKPLWLHVleNLSSAPAFKEIVVVIHPDDIAYMKKALPEIKF 73
 
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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