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Conserved domains on  [gi|739265782|ref|WP_037128704|]
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MULTISPECIES: NTP transferase domain-containing protein [Rhodococcus]

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];
1-188 2.92e-63

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


:

Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 193.84  E-value: 2.92e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739265782   1 MSTCGILLAAGAGSRMGKPKALVTnTEGQSWLHHGVTTLQSAGLSPVIVVLGAQAEDALELLPTTDVIVVI-SDWQHGMS 79
Cdd:COG2068    2 SKVAAIILAAGASSRMGRPKLLLP-LGGKPLLERAVEAALAAGLDPVVVVLGADAEEVAAALAGLGVRVVVnPDWEEGMS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739265782  80 ASLRCGLEAAMriDDADAAAISLVDVPDLNADTVTRIVGHSSPSRNILRRAVFHGRPGHPVLIGRDHWPTLAkSLTGDGG 159
Cdd:COG2068   81 SSLRAGLAALP--ADADAVLVLLGDQPLVTAETLRRLLAAFRESPASIVAPTYDGRRGHPVLFSRRLFPELL-ALTGDQG 157

                        170       180       190
                 ....*....|....*....|....*....|.
gi 739265782 160 ANTYLREHG--VELVECSDLSSGVDVDYPEA 188
Cdd:COG2068  158 ARALLRRHPdrVRLVPVDDPGVLLDIDTPED 188
 
Name Accession Description Interval E-value
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
1-188 2.92e-63

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 193.84  E-value: 2.92e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739265782   1 MSTCGILLAAGAGSRMGKPKALVTnTEGQSWLHHGVTTLQSAGLSPVIVVLGAQAEDALELLPTTDVIVVI-SDWQHGMS 79
Cdd:COG2068    2 SKVAAIILAAGASSRMGRPKLLLP-LGGKPLLERAVEAALAAGLDPVVVVLGADAEEVAAALAGLGVRVVVnPDWEEGMS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739265782  80 ASLRCGLEAAMriDDADAAAISLVDVPDLNADTVTRIVGHSSPSRNILRRAVFHGRPGHPVLIGRDHWPTLAkSLTGDGG 159
Cdd:COG2068   81 SSLRAGLAALP--ADADAVLVLLGDQPLVTAETLRRLLAAFRESPASIVAPTYDGRRGHPVLFSRRLFPELL-ALTGDQG 157

                        170       180       190
                 ....*....|....*....|....*....|.
gi 739265782 160 ANTYLREHG--VELVECSDLSSGVDVDYPEA 188
Cdd:COG2068  158 ARALLRRHPdrVRLVPVDDPGVLLDIDTPED 188
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 3-188 1.12e-54

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: 171.59  E-value: 1.12e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739265782   3 TCGILLAAGAGSRMGKPKALVtNTEGQSWLHHGVTTLQSAGLSPVIVVLGAQAEDALELLPTTDVIVVI-SDWQHGMSAS 81
Cdd:cd04182    1 IAAIILAAGRSSRMGGNKLLL-PLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALAGLPVVVVInPDWEEGMSSS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739265782  82 LRCGLEAAmrIDDADAAAISLVDVPDLNADTVTRIVGHSSPSRNILRRAVFHGRPGHPVLIGRDHWPTLAKsLTGDGGAN 161
Cdd:cd04182   80 LAAGLEAL--PADADAVLILLADQPLVTAETLRALIDAFREDGAGIVAPVYQGRRGHPVLFPRSLFPELLA-LSGDKGAR 156

                        170       180
                 ....*....|....*....|....*...
gi 739265782 162 TYLREHGVEL-VECSDLSSGVDVDYPEA 188
Cdd:cd04182  157 SLLRAHPDRVvVEVDDPGVLIDIDTPED 184
matur_MocA_YgfJ TIGR03310
molybdenum cofactor cytidylyltransferase; Members of this protein include MocA, which ...
 5-187 1.25e-31

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: 112.82  E-value: 1.25e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739265782    5 GILLAAGAGSRMGKPKaLVTNTEGQSWLHHGVTTLQSAGLSPVIVVLGAQAEDALELLPTTDVIVVI--SDWQHGMSASL 82
Cdd:TIGR03310   2 AIILAAGLSSRMGQNK-LLLPYKGKTILEHVVDNALRLFFDEVILVLGHEADELVALLANHSNITLVhnPQYAEGQSSSI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739265782   83 RCGLEAAMRiddADAAAISLVDVPDLNADTVTRIVGHSSPSRNILRRAVFHGRPGHPVLIGRDHWPTLaKSLTGDGGANT 162
Cdd:TIGR03310  81 KLGLELPVQ---SDGYLFLLGDQPFVTPDIIQLLLEAFALKNDEIVVPLYKGKRGHPVLFPRKLFPEL-LALTGDTGGRQ 156

                         170       180
                  ....*....|....*....|....*..
gi 739265782  163 YLREHGVEL--VECSDLSSGVDVDYPE 187
Cdd:TIGR03310 157 ILRELPHEVkyVEVKDPGILFDIDTPE 183
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 5-168 1.43e-28

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: 104.20  E-value: 1.43e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739265782    5 GILLAAGAGSRMGKPKALVTnTEGQSWLHHGVTTLQSAGlSPVIVVLGAqaEDALELLPTTDVIVVI-SDWQHGMSASLR 83
Cdd:pfam12804   1 AVILAGGRSSRMGGDKALLP-LGGKPLLERVLERLRPAG-DEVVVVAND--EEVLAALAGLGVPVVPdPDPGQGPLAGLL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739265782   84 CGLEAAmriDDADAAAISLVDVPDLNADTVTRIVGHSSPSRNILRRAVFHGRPGHPVLIGRDHWPTLAKsLTGDGGANTY 163
Cdd:pfam12804  77 AALRAA---PGADAVLVLACDMPFLTPELLRRLLAAAEESGADIVVPVYDGGRGHPLLYRRRLLPALEA-LLGDRGLRRL 152


                  ....*
gi 739265782  164 LREHG 168
Cdd:pfam12804 153 LRRLD 157
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 6-125 3.14e-08

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 52.25  E-value: 3.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739265782   6 ILLAAGAGSRM--GKPKALVTnTEGQSWLHHGVTTlqSAGLSP--VIVVLGAQAEDALELLPT--TDVIVVISDWQHGMS 79
Cdd:PRK14352   8 IVLAAGAGTRMrsDTPKVLHT-LAGRSMLGHVLHA--AAGLAPqhLVVVVGHDRERVAPAVAElaPEVDIAVQDEQPGTG 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 739265782  80 ASLRCGLEAAmridDADAAAISLV---DVPDLNADTVTRIVGHSSPSRN 125
Cdd:PRK14352  85 HAVQCALEAL----PADFDGTVVVtagDVPLLDGETLADLVATHTAEGN 129
 
Name Accession Description Interval E-value
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
1-188 2.92e-63

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 193.84  E-value: 2.92e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739265782   1 MSTCGILLAAGAGSRMGKPKALVTnTEGQSWLHHGVTTLQSAGLSPVIVVLGAQAEDALELLPTTDVIVVI-SDWQHGMS 79
Cdd:COG2068    2 SKVAAIILAAGASSRMGRPKLLLP-LGGKPLLERAVEAALAAGLDPVVVVLGADAEEVAAALAGLGVRVVVnPDWEEGMS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739265782  80 ASLRCGLEAAMriDDADAAAISLVDVPDLNADTVTRIVGHSSPSRNILRRAVFHGRPGHPVLIGRDHWPTLAkSLTGDGG 159
Cdd:COG2068   81 SSLRAGLAALP--ADADAVLVLLGDQPLVTAETLRRLLAAFRESPASIVAPTYDGRRGHPVLFSRRLFPELL-ALTGDQG 157

                        170       180       190
                 ....*....|....*....|....*....|.
gi 739265782 160 ANTYLREHG--VELVECSDLSSGVDVDYPEA 188
Cdd:COG2068  158 ARALLRRHPdrVRLVPVDDPGVLLDIDTPED 188
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 3-188 1.12e-54

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: 171.59  E-value: 1.12e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739265782   3 TCGILLAAGAGSRMGKPKALVtNTEGQSWLHHGVTTLQSAGLSPVIVVLGAQAEDALELLPTTDVIVVI-SDWQHGMSAS 81
Cdd:cd04182    1 IAAIILAAGRSSRMGGNKLLL-PLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALAGLPVVVVInPDWEEGMSSS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739265782  82 LRCGLEAAmrIDDADAAAISLVDVPDLNADTVTRIVGHSSPSRNILRRAVFHGRPGHPVLIGRDHWPTLAKsLTGDGGAN 161
Cdd:cd04182   80 LAAGLEAL--PADADAVLILLADQPLVTAETLRALIDAFREDGAGIVAPVYQGRRGHPVLFPRSLFPELLA-LSGDKGAR 156

                        170       180
                 ....*....|....*....|....*...
gi 739265782 162 TYLREHGVEL-VECSDLSSGVDVDYPEA 188
Cdd:cd04182  157 SLLRAHPDRVvVEVDDPGVLIDIDTPED 184
matur_MocA_YgfJ TIGR03310
molybdenum cofactor cytidylyltransferase; Members of this protein include MocA, which ...
 5-187 1.25e-31

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: 112.82  E-value: 1.25e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739265782    5 GILLAAGAGSRMGKPKaLVTNTEGQSWLHHGVTTLQSAGLSPVIVVLGAQAEDALELLPTTDVIVVI--SDWQHGMSASL 82
Cdd:TIGR03310   2 AIILAAGLSSRMGQNK-LLLPYKGKTILEHVVDNALRLFFDEVILVLGHEADELVALLANHSNITLVhnPQYAEGQSSSI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739265782   83 RCGLEAAMRiddADAAAISLVDVPDLNADTVTRIVGHSSPSRNILRRAVFHGRPGHPVLIGRDHWPTLaKSLTGDGGANT 162
Cdd:TIGR03310  81 KLGLELPVQ---SDGYLFLLGDQPFVTPDIIQLLLEAFALKNDEIVVPLYKGKRGHPVLFPRKLFPEL-LALTGDTGGRQ 156

                         170       180
                  ....*....|....*....|....*..
gi 739265782  163 YLREHGVEL--VECSDLSSGVDVDYPE 187
Cdd:TIGR03310 157 ILRELPHEVkyVEVKDPGILFDIDTPE 183
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 5-168 1.43e-28

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: 104.20  E-value: 1.43e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739265782    5 GILLAAGAGSRMGKPKALVTnTEGQSWLHHGVTTLQSAGlSPVIVVLGAqaEDALELLPTTDVIVVI-SDWQHGMSASLR 83
Cdd:pfam12804   1 AVILAGGRSSRMGGDKALLP-LGGKPLLERVLERLRPAG-DEVVVVAND--EEVLAALAGLGVPVVPdPDPGQGPLAGLL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739265782   84 CGLEAAmriDDADAAAISLVDVPDLNADTVTRIVGHSSPSRNILRRAVFHGRPGHPVLIGRDHWPTLAKsLTGDGGANTY 163
Cdd:pfam12804  77 AALRAA---PGADAVLVLACDMPFLTPELLRRLLAAAEESGADIVVPVYDGGRGHPLLYRRRLLPALEA-LLGDRGLRRL 152


                  ....*
gi 739265782  164 LREHG 168
Cdd:pfam12804 153 LRRLD 157
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 1-187 7.16e-14

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: 66.37  E-value: 7.16e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739265782   1 MSTCGILLAAGAGSRMGKPKALVTnTEGQSWLHHGVTTLQSAgLSPVIVVlgAQAEDALELLPttdvIVVISDWQHGMS- 79
Cdd:COG0746    3 MPITGVILAGGRSRRMGQDKALLP-LGGRPLLERVLERLRPQ-VDEVVIV--ANRPERYAALG----VPVVPDDPPGAGp 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739265782  80 -AslrcGLEAAMRIDDADAAAISLVDVPDLNADTVTRIVGHSSPSRNIlrrAVFH--GRPgHPV--LIGRDHWPTLAKSL 154
Cdd:COG0746   75 lA----GILAALEAAPAEWVLVLACDMPFLPPDLVRRLLEALEEGADA---VVPRsgGRL-EPLfaLYRRSLLPALEAAL 146

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 739265782 155 -TGDGGANTYLREHGVELVECSDLS-SGVDVDYPE 187
Cdd:COG0746  147 aEGERSLRALLERLDVVYVPFEDLDdAFFNVNTPE 181
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 5-187 1.19e-11

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: 60.28  E-value: 1.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739265782   5 GILLAAGAGSRMGKPKALVTnTEGQSWLHHGVTTLQSAGlSPVIVVLGAQAEDALELlpttdVIVVISDWQHGMS--Asl 82
Cdd:cd02503    3 GVILAGGKSRRMGGDKALLE-LGGKPLLEHVLERLKPLV-DEVVISANRDQERYALL-----GVPVIPDEPPGKGplA-- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739265782  83 rcGLEAAMRIDDADAAAISLVDVPDLNADTVTRIVGHSSPSRNIlrrAVFH--GRPgHPvLIGrdHWPT-LAKSLTGDGG 159
Cdd:cd02503   74 --GILAALRAAPADWVLVLACDMPFLPPELLERLLAAAEEGADA---VVPKsgGRL-QP-LHA--LYHKsLLPALEELLE 144

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 739265782 160 ANTY-----LREHGVELVECSDLSSG--VDVDYPE 187
Cdd:cd02503  145 AGERrlrrlLEKLGVQYVEFEDERLDafFNINTPE 179
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
5-88 9.35e-11

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 58.71  E-value: 9.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739265782   5 GILLAAGAGSRMG-----KPKALVtNTEGQSWLHHGVTTLQSAGLSPVIVVLGAQAEDALELL--PTTDVIVVI-SDWQH 76
Cdd:COG1213    2 AVILAAGRGSRLGpltddIPKCLV-EIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEALarPGPDVTFVYnPDYDE 80

                         90
                 ....*....|...
gi 739265782  77 -GMSASLRCGLEA 88
Cdd:COG1213   81 tNNIYSLWLAREA 93
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 6-88 2.89e-10

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: 57.24  E-value: 2.89e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739265782   6 ILLAAGAGSRMG-----KPKALVtNTEGQSWLHHGVTTLQSAGLSPVIVVLGAQAEDALELLPTTDVIVVI--SDWQH-G 77
Cdd:cd02523    2 IILAAGRGSRLRpltedRPKCLL-EINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKKYPNIKFVynPDYAEtN 80

                         90
                 ....*....|.
gi 739265782  78 MSASLRCGLEA 88
Cdd:cd02523   81 NIYSLYLARDF 91
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 6-119 3.67e-09

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


Pssm-ID: 133020 [Multi-domain]  Cd Length: 229  Bit Score: 54.06  E-value: 3.67e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739265782   6 ILLAAGAGSRM--GKPKALVTnTEGQSWLHHGVTTLQSAGLSPVIVVLGAQAEDALELLPTTDVIVVISDWQHGMSASLR 83
Cdd:cd02540    2 VILAAGKGTRMksDLPKVLHP-LAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVKKALANPNVEFVLQEEQLGTGHAVK 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 739265782  84 CGLEAAmriddADAAAISLV---DVPDLNADTVTRIVGH 119
Cdd:cd02540   81 QALPAL-----KDFEGDVLVlygDVPLITPETLQRLLEA 114
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 6-125 3.14e-08

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 52.25  E-value: 3.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739265782   6 ILLAAGAGSRM--GKPKALVTnTEGQSWLHHGVTTlqSAGLSP--VIVVLGAQAEDALELLPT--TDVIVVISDWQHGMS 79
Cdd:PRK14352   8 IVLAAGAGTRMrsDTPKVLHT-LAGRSMLGHVLHA--AAGLAPqhLVVVVGHDRERVAPAVAElaPEVDIAVQDEQPGTG 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 739265782  80 ASLRCGLEAAmridDADAAAISLV---DVPDLNADTVTRIVGHSSPSRN 125
Cdd:PRK14352  85 HAVQCALEAL----PADFDGTVVVtagDVPLLDGETLADLVATHTAEGN 129
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 1-119 7.67e-07

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: 48.10  E-value: 7.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739265782   1 MSTCGILLAAGAGSRM--GKPKAL--VTnteGQSWLHHGVTTLQSAGLSPVIVVLGAQAEDALELLPTTDVIVVISDWQH 76
Cdd:COG1207    1 SPLAVVILAAGKGTRMksKLPKVLhpLA---GKPMLEHVLDAARALGPDRIVVVVGHGAEQVRAALADLDVEFVLQEEQL 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 739265782  77 GMSASLRCGLEAAmriddADAAAISLV---DVPDLNADTVTRIVGH 119
Cdd:COG1207   78 GTGHAVQQALPAL-----PGDDGTVLVlygDVPLIRAETLKALLAA 118
mobA PRK00317
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
 5-176 1.14e-06

molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed


Pssm-ID: 234725 [Multi-domain]  Cd Length: 193  Bit Score: 46.72  E-value: 1.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739265782   5 GILLAAGAGSRM-GKPKALVTnTEGQSWLHHGVTTL--QSAGLspVIVV---LGAQAEDALEllpttdvivVISDWQHGM 78
Cdd:PRK00317   6 GVILAGGRSRRMgGVDKGLQE-LNGKPLIQHVIERLapQVDEI--VINAnrnLARYAAFGLP---------VIPDSLADF 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739265782  79 SASLrCGLEAAMRIDDADAAAISLVDVPDLNADTVTRIVGHSspSRNILRRAVFH--GRPgHPV--LIGRDHWPTLAKSL 154
Cdd:PRK00317  74 PGPL-AGILAGLKQARTEWVLVVPCDTPFIPPDLVARLAQAA--GKDDADVAWAHdgGRL-HPTfaLYSVALLPDLEAYL 149

                        170       180
                 ....*....|....*....|...
gi 739265782 155 T-GDGGANTYLREHGVELVECSD 176
Cdd:PRK00317 150 AaGERKVMAFYARHGGVAVDFSD 172
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-119 9.76e-06

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 44.85  E-value: 9.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739265782   1 MSTCGILLAAGAGSRM--GKPKALvTNTEGQSWLHHGVTTLQSAGLSPVIVVLGAQAED----ALELLPttDVIVVISDW 74
Cdd:PRK14353   4 RTCLAIILAAGEGTRMksSLPKVL-HPVAGRPMLAHVLAAAASLGPSRVAVVVGPGAEAvaaaAAKIAP--DAEIFVQKE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 739265782  75 QHGMSASLRCGLEAAMRIDdaDAAAISLVDVPDLNADTVTRIVGH 119
Cdd:PRK14353  81 RLGTAHAVLAAREALAGGY--GDVLVLYGDTPLITAETLARLRER 123
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-62 4.32e-05

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 42.90  E-value: 4.32e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 739265782   1 MSTCGILLAAGAGSRM--GKPKAL--VTnteGQSWLHHGVTTLQSAGLSPVIVVLGAQAEDALELL 62
Cdd:PRK14354   1 MNRYAIILAAGKGTRMksKLPKVLhkVC---GKPMVEHVVDSVKKAGIDKIVTVVGHGAEEVKEVL 63
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 3-98 1.52e-04

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


Pssm-ID: 133009 [Multi-domain]  Cd Length: 218  Bit Score: 40.97  E-value: 1.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739265782   3 TCGILLAAGAGSRMG--KPKALVTnTEGQSWLHHGVTTLQSAGL-SPVIVVLGAQ----AEDALELLPTTDVIVVI--SD 73
Cdd:cd02516    1 VAAIILAAGSGSRMGadIPKQFLE-LGGKPVLEHTLEAFLAHPAiDEIVVVVPPDdidlAKELAKYGLSKVVKIVEggAT 79

                         90       100       110
                 ....*....|....*....|....*....|
gi 739265782  74 WQHgmsaSLRCGLEAAMRIDDA-----DAA 98
Cdd:cd02516   80 RQD----SVLNGLKALPDADPDivlihDAA 105
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 6-98 1.67e-04

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


Pssm-ID: 440824  Cd Length: 224  Bit Score: 40.88  E-value: 1.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739265782   6 ILLAAGAGSRMG--KPKALVTnTEGQSWLHHGVTTLQSAGL-SPVIVVLG----AQAEDALELLPTTDVIVVI---SDWQ 75
Cdd:COG1211    1 IIPAAGSGSRMGagIPKQFLP-LGGKPVLEHTLEAFLAHPRiDEIVVVVPpddiEYFEELLAKYGIDKPVRVVaggATRQ 79

                         90       100
                 ....*....|....*....|....*..
gi 739265782  76 HgmsaSLRCGLEAAMRIDDA----DAA 98
Cdd:COG1211   80 D----SVRNGLEALPDDDDWvlvhDAA 102
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-117 3.27e-04

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 40.48  E-value: 3.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739265782   3 TCGILLAAGAGSRM--GKPKALVTnTEGQSWLHHGVTTLQSAGLSPVIVVLGAQAEDALELLPTTDVIVVISDWQHGMSA 80
Cdd:PRK14356   6 TGALILAAGKGTRMhsDKPKVLQT-LLGEPMLRFVYRALRPLFGDNVWTVVGHRADMVRAAFPDEDARFVLQEQQLGTGH 84

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 739265782  81 SLRCGLEaamRIDDADAAAISLV--DVPDLNADTVTRIV 117
Cdd:PRK14356  85 ALQCAWP---SLTAAGLDRVLVVngDTPLVTTDTIDDFL 120
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
1-89 4.27e-04

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 39.73  E-value: 4.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739265782   1 MSTCGILLAAGAGSRMG--KPKALVTnTEGQSWLHHgvtTLQSAGLSP----VIVVLGAQ-AEDALELLPTTDVIVVI-- 71
Cdd:PRK00155   2 MMVYAIIPAAGKGSRMGadRPKQYLP-LGGKPILEH---TLEAFLAHPrideIIVVVPPDdRPDFAELLLAKDPKVTVva 77

                         90       100
                 ....*....|....*....|
gi 739265782  72 --SDWQHgmsaSLRCGLEAA 89
Cdd:PRK00155  78 ggAERQD----SVLNGLQAL 93
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 6-117 5.14e-04

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 39.75  E-value: 5.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739265782   6 ILLAAGAGSRMGKPKALVTNT-EGQSWLHHGVTTLQSAGlSPVIVVLGAQAEDALELLPtTDVIVVISDWQHGMSASLRC 84
Cdd:PRK14357   4 LVLAAGKGTRMKSKIPKVLHKiSGKPMINWVIDTAKKVA-QKVGVVLGHEAELVKKLLP-EWVKIFLQEEQLGTAHAVMC 81

                         90       100       110
                 ....*....|....*....|....*....|...
gi 739265782  85 GLEAamrIDDADAAAISLVDVPDLNADTVTRIV 117
Cdd:PRK14357  82 ARDF---IEPGDDLLILYGDVPLISENTLKRLI 111
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 6-117 1.62e-03

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 38.19  E-value: 1.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739265782   6 ILLAAGAGSRM--GKPKALvTNTEGQSWLHHGVTTLQSAGLSPVIVVLGAQAEDALELLP-TTDVIVVISDWQHGMSASL 82
Cdd:PRK14355   7 IILAAGKGTRMksDLVKVM-HPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHFAgDGDVSFALQEEQLGTGHAV 85

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 739265782  83 RCGLEAAMRIddADAAAISLVDVPDLNADTVTRIV 117
Cdd:PRK14355  86 ACAAPALDGF--SGTVLILCGDVPLLRAETLQGML 118
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 5-56 3.92e-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: 36.79  E-value: 3.92e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 739265782   5 GILLAAGAGSRMG-----KPKALVtNTEGQSWLHHGVTTLQSAGLSPVIVVLGAQAE 56
Cdd:cd04181    1 AVILAAGKGTRLRpltdtRPKPLL-PIAGKPILEYIIERLARAGIDEIILVVGYLGE 56
ispD TIGR00453
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ...
 4-115 3.96e-03

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase, the IspD protein of the deoxyxylulose pathway of IPP biosynthesis. In about twenty percent of bacterial genomes, this protein occurs as IspDF, a bifunctional fusion protein. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 213532  Cd Length: 217  Bit Score: 36.88  E-value: 3.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739265782    4 CGILLAAGAGSRMG--KPKALVTnTEGQSWLHHGVTTLQSA-GLSPVIVVLGAQAEDALELLPTTDVIVVISDWQHGMSA 80
Cdd:TIGR00453   1 SAVIPAAGRGTRFGsgVPKQYLE-LGGRPLLEHALDAFLAHpAIDEVVVVVSPDDTEFFQKYLVARAVPKIVAGGDTRQD 79

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 739265782   81 SLRCGLEAamrIDDADAAAISLVDVPDLNADTVTR 115
Cdd:TIGR00453  80 SVRNGLKA---LKDAEFVLVHDAARPFVPKELLDR 111
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 5-57 6.42e-03

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: 36.01  E-value: 6.42e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 739265782   5 GILLAAGAGSRM-----GKPKALVTNTeGQSWLHHGVTTLQSAGLSPVIVVLGAQAED 57
Cdd:cd04189    3 GLILAGGKGTRLrpltyTRPKQLIPVA-GKPIIQYAIEDLREAGIEDIGIVVGPTGEE 59
 
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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