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Conserved domains on  [gi|477324825|gb|ENF94650|]
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glycerol-3-phosphate cytidylyltransferase [Escherichia coli P0305260.13]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 2-127 8.77e-55

Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane/envelope biogenesis]; Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis


:

Pssm-ID: 440380 [Multi-domain]  Cd Length: 131  Bit Score: 167.59  E-value: 8.77e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 477324825   2 KTVITFGTFDVFHVGHLRLLQRARALGERLLVGVSSDAlNIAKKGRAPVYHQDDRMAIIAGLACVDGVFLEESLEqKAEY 81
Cdd:COG0615    1 KRVITYGTFDLLHPGHINLLKRAKALGDELIVGVATDE-FVASKGRKPIIPEEQRKEIVEALKYVDEVILGEEWD-KFED 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 477324825  82 LRGYSADILVMGDDWAGKFDSF-------AYICEVVYFPRTPSVSTTGIIEVI 127
Cdd:COG0615   79 IEEIKPDVIVLGDDWKGDFDFLkeelekrGIGCEVVYLPRTEGISSTKIKKRI 131
 
Name Accession Description Interval E-value
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 2-127 8.77e-55

Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane/envelope biogenesis]; Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis


Pssm-ID: 440380 [Multi-domain]  Cd Length: 131  Bit Score: 167.59  E-value: 8.77e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 477324825   2 KTVITFGTFDVFHVGHLRLLQRARALGERLLVGVSSDAlNIAKKGRAPVYHQDDRMAIIAGLACVDGVFLEESLEqKAEY 81
Cdd:COG0615    1 KRVITYGTFDLLHPGHINLLKRAKALGDELIVGVATDE-FVASKGRKPIIPEEQRKEIVEALKYVDEVILGEEWD-KFED 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 477324825  82 LRGYSADILVMGDDWAGKFDSF-------AYICEVVYFPRTPSVSTTGIIEVI 127
Cdd:COG0615   79 IEEIKPDVIVLGDDWKGDFDFLkeelekrGIGCEVVYLPRTEGISSTKIKKRI 131
G3P_Cytidylyltransferase cd02171
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase, ...
 1-130 9.42e-49

glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase,(CDP-glycerol pyrophosphorylase). Glycerol-3-phosphate cytidyltransferase acts in pathways of teichoic acid biosynthesis. Teichoic acids are substituted polymers, linked by phosphodiester bonds, of glycerol, ribitol, etc. An example is poly(glycerol phosphate), the major teichoic acid of the Bacillus subtilis cell wall. Most, but not all, species encoding proteins in this family are Gram-positive bacteria. A closely related protein assigned a different function experimentally is a human ethanolamine-phosphate cytidylyltransferase.


Pssm-ID: 173922 [Multi-domain]  Cd Length: 129  Bit Score: 152.25  E-value: 9.42e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 477324825   1 MKTVITFGTFDVFHVGHLRLLQRARALGERLLVGVSSDALNiAKKGRAPVYHQDDRMAIIAGLACVDGVFLEESLEQKAE 80
Cdd:cd02171    1 MKVVITYGTFDLLHIGHLNLLERAKALGDKLIVAVSTDEFN-AGKGKKAVIPYEQRAEILESIRYVDLVIPETNWEQKIE 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 477324825  81 YLRGYSADILVMGDDWAGKFDSFAYICEVVYFPRTPSVSTTGIIEVIRGL 130
Cdd:cd02171   80 DIKKYNVDVFVMGDDWEGKFDFLKEYCEVVYLPRTKGISSTQLKEMLKKL 129
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 5-126 2.41e-20

Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; glycerol-3-phosphate cytidylyltransferase. It also includes putative adenylyltransferases, and FAD synthases.


Pssm-ID: 396172 [Multi-domain]  Cd Length: 134  Bit Score: 80.06  E-value: 2.41e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 477324825    5 ITFGTFDVFHVGHLRLLQRARALG-ERLLVGVSSDalNIAKKGRAPVYHQDDRMAIIAGLACVDGVFLEESLEQKAEYLR 83
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFdEDLIVGVPSD--EPPHKLKRPLFSAEERLEMLELAKWVDEVIVVAPWELTRELLK 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 477324825   84 GYSADILVMGDD-----WAG--------KFDSFAYICEVVYFPRTPSVSTTGIIEV 126
Cdd:pfam01467  79 ELNPDVLVIGADslldfWYEldeilgnvKLVVVVRPVFFIPLKPTNGISSTDIRER 134
PRK11316 PRK11316
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ...
 2-129 4.63e-20

bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase HldE;


Pssm-ID: 183085 [Multi-domain]  Cd Length: 473  Bit Score: 84.11  E-value: 4.63e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 477324825   2 KTVITFGTFDVFHVGHLRLLQRARALGERLLVGVSSDALNIAKKGRA-PVYHQDDRMAIIAGLACVDGV--FLEESLEQK 78
Cdd:PRK11316 341 KIVMTNGCFDILHAGHVSYLANARKLGDRLIVAVNSDASVKRLKGEGrPVNPLEQRMAVLAALEAVDWVvpFEEDTPQRL 420

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 477324825  79 AEYLrgySADILVMGDDW-----AGKFDSFAYICEVVYFPRTPSVSTTGIIEVIRG 129
Cdd:PRK11316 421 IAEI---LPDLLVKGGDYkpeeiAGSKEVWANGGEVKVLNFEDGCSTTNIIKKIRQ 473
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 4-67 1.35e-15

cytidyltransferase-like domain; Protein families that contain at least one copy of this domain include citrate lyase ligase, pantoate-beta-alanine ligase, glycerol-3-phosphate cytidyltransferase, ADP-heptose synthase, phosphocholine cytidylyltransferase, lipopolysaccharide core biosynthesis protein KdtB, the bifunctional protein NadR, and a number whose function is unknown. Many of these proteins are known to use CTP or ATP and release pyrophosphate.


Pssm-ID: 272920 [Multi-domain]  Cd Length: 66  Bit Score: 66.18  E-value: 1.35e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 477324825    4 VITFGTFDVFHVGHLRLLQRARALGERLLVGVSSDALNIAKKGRaPVYHQDDRMAIIAGLACVD 67
Cdd:TIGR00125   2 VIFVGTFDPFHLGHLDLLERAKELFDELIVGVGSDQFVNPLKGE-PVFSLEERLEMLKALKYVD 64
 
Name Accession Description Interval E-value
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 2-127 8.77e-55

Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane/envelope biogenesis]; Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis


Pssm-ID: 440380 [Multi-domain]  Cd Length: 131  Bit Score: 167.59  E-value: 8.77e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 477324825   2 KTVITFGTFDVFHVGHLRLLQRARALGERLLVGVSSDAlNIAKKGRAPVYHQDDRMAIIAGLACVDGVFLEESLEqKAEY 81
Cdd:COG0615    1 KRVITYGTFDLLHPGHINLLKRAKALGDELIVGVATDE-FVASKGRKPIIPEEQRKEIVEALKYVDEVILGEEWD-KFED 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 477324825  82 LRGYSADILVMGDDWAGKFDSF-------AYICEVVYFPRTPSVSTTGIIEVI 127
Cdd:COG0615   79 IEEIKPDVIVLGDDWKGDFDFLkeelekrGIGCEVVYLPRTEGISSTKIKKRI 131
G3P_Cytidylyltransferase cd02171
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase, ...
 1-130 9.42e-49

glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase,(CDP-glycerol pyrophosphorylase). Glycerol-3-phosphate cytidyltransferase acts in pathways of teichoic acid biosynthesis. Teichoic acids are substituted polymers, linked by phosphodiester bonds, of glycerol, ribitol, etc. An example is poly(glycerol phosphate), the major teichoic acid of the Bacillus subtilis cell wall. Most, but not all, species encoding proteins in this family are Gram-positive bacteria. A closely related protein assigned a different function experimentally is a human ethanolamine-phosphate cytidylyltransferase.


Pssm-ID: 173922 [Multi-domain]  Cd Length: 129  Bit Score: 152.25  E-value: 9.42e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 477324825   1 MKTVITFGTFDVFHVGHLRLLQRARALGERLLVGVSSDALNiAKKGRAPVYHQDDRMAIIAGLACVDGVFLEESLEQKAE 80
Cdd:cd02171    1 MKVVITYGTFDLLHIGHLNLLERAKALGDKLIVAVSTDEFN-AGKGKKAVIPYEQRAEILESIRYVDLVIPETNWEQKIE 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 477324825  81 YLRGYSADILVMGDDWAGKFDSFAYICEVVYFPRTPSVSTTGIIEVIRGL 130
Cdd:cd02171   80 DIKKYNVDVFVMGDDWEGKFDFLKEYCEVVYLPRTKGISSTQLKEMLKKL 129
cytidylyltransferase cd02170
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ...
 1-130 3.63e-27

cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate cytidylyltransferase (CCT), glycerol-3-phosphate cytidylyltransferase, RafE and phosphoethanolamine cytidylyltransferase (ECT). All enzymes catalyze the transfer of a cytidylyl group from CTP to various substrates.


Pssm-ID: 173921 [Multi-domain]  Cd Length: 136  Bit Score: 97.75  E-value: 3.63e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 477324825   1 MKTVITFGTFDVFHVGHLRLLQRARALGERLLVGVSSDAlNIAKKGRAPVYHQDDRMAIIAGLACVDGVFLEESLEQKAE 80
Cdd:cd02170    1 MKRVYAAGTFDIIHPGHIRFLEEAKKLGDYLIVGVARDE-TVAKIKRRPILPEEQRAEVVEALKYVDEVILGHPWSYFKP 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 477324825  81 YLRGYSaDILVMGDDWAGKFDSFAYI------CEVVYFPR--TPSVSTTGIIEVIRGL 130
Cdd:cd02170   80 LEELKP-DVIVLGDDQKNGVDEEEVYeelkkrGKVIEVPRkkTEGISSSDIIKRILEL 136
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 5-126 2.41e-20

Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; glycerol-3-phosphate cytidylyltransferase. It also includes putative adenylyltransferases, and FAD synthases.


Pssm-ID: 396172 [Multi-domain]  Cd Length: 134  Bit Score: 80.06  E-value: 2.41e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 477324825    5 ITFGTFDVFHVGHLRLLQRARALG-ERLLVGVSSDalNIAKKGRAPVYHQDDRMAIIAGLACVDGVFLEESLEQKAEYLR 83
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFdEDLIVGVPSD--EPPHKLKRPLFSAEERLEMLELAKWVDEVIVVAPWELTRELLK 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 477324825   84 GYSADILVMGDD-----WAG--------KFDSFAYICEVVYFPRTPSVSTTGIIEV 126
Cdd:pfam01467  79 ELNPDVLVIGADslldfWYEldeilgnvKLVVVVRPVFFIPLKPTNGISSTDIRER 134
PRK11316 PRK11316
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ...
 2-129 4.63e-20

bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase HldE;


Pssm-ID: 183085 [Multi-domain]  Cd Length: 473  Bit Score: 84.11  E-value: 4.63e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 477324825   2 KTVITFGTFDVFHVGHLRLLQRARALGERLLVGVSSDALNIAKKGRA-PVYHQDDRMAIIAGLACVDGV--FLEESLEQK 78
Cdd:PRK11316 341 KIVMTNGCFDILHAGHVSYLANARKLGDRLIVAVNSDASVKRLKGEGrPVNPLEQRMAVLAALEAVDWVvpFEEDTPQRL 420

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 477324825  79 AEYLrgySADILVMGDDW-----AGKFDSFAYICEVVYFPRTPSVSTTGIIEVIRG 129
Cdd:PRK11316 421 IAEI---LPDLLVKGGDYkpeeiAGSKEVWANGGEVKVLNFEDGCSTTNIIKKIRQ 473
RfaE_N cd02172
N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ...
 2-71 1.95e-17

N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ADP-L-glycero-D-manno-heptose, a precursor for LPS inner core biosynthesis. RfaE is a bifunctional protein in Escherichia coli, and separate proteins in other organisms. Domain I is suggested to act in D-glycero-D-manno-heptose 1-phosphate biosynthesis, while domain II (this family) adds ADP to yield ADP-D-glycero-D-manno-heptose .


Pssm-ID: 173923 [Multi-domain]  Cd Length: 144  Bit Score: 72.83  E-value: 1.95e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 477324825   2 KTVITFGTFDVFHVGHLRLLQRARALGERLLVGVSSDALNIAKKGRaPVYHQDDRMAIIAGLACVDGVFL 71
Cdd:cd02172    5 TVVLCHGVFDLLHPGHVRHLQAARSLGDILVVSLTSDRYVNKGPGR-PIFPEDLRAEVLAALGFVDYVVL 73
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 4-67 1.35e-15

cytidyltransferase-like domain; Protein families that contain at least one copy of this domain include citrate lyase ligase, pantoate-beta-alanine ligase, glycerol-3-phosphate cytidyltransferase, ADP-heptose synthase, phosphocholine cytidylyltransferase, lipopolysaccharide core biosynthesis protein KdtB, the bifunctional protein NadR, and a number whose function is unknown. Many of these proteins are known to use CTP or ATP and release pyrophosphate.


Pssm-ID: 272920 [Multi-domain]  Cd Length: 66  Bit Score: 66.18  E-value: 1.35e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 477324825    4 VITFGTFDVFHVGHLRLLQRARALGERLLVGVSSDALNIAKKGRaPVYHQDDRMAIIAGLACVD 67
Cdd:TIGR00125   2 VIFVGTFDPFHLGHLDLLERAKELFDELIVGVGSDQFVNPLKGE-PVFSLEERLEMLKALKYVD 64
PLN02406 PLN02406
ethanolamine-phosphate cytidylyltransferase
 8-124 3.63e-13

ethanolamine-phosphate cytidylyltransferase


Pssm-ID: 215227 [Multi-domain]  Cd Length: 418  Bit Score: 64.70  E-value: 3.63e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 477324825   8 GTFDVFHVGHLRLLQRARALGERLLVGVSSDALNIAKKGrAPVYHQDDRMAIIAGLACVDGVFLEESLEQKAEYLRG--- 84
Cdd:PLN02406  60 GCFDMMHYGHANALRQARALGDELVVGVVSDEEIIANKG-PPVTPMHERMIMVSGVKWVDEVIPDAPYAITEEFMNKlfn 138

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 477324825  85 -YSADILVMGDD---WAGKFDSFAYICEVVYF---PRTPSVSTTGII 124
Cdd:PLN02406 139 eYNIDYIIHGDDpclLPDGTDAYALAKKAGRYkqiKRTEGVSSTDIV 185
CCT cd02174
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ...
 8-124 6.96e-13

CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) catalyzes the condensation of CTP and phosphocholine to form CDP-choline as the rate-limiting and regulatory step in the CDP-choline pathway. CCT is unique in that its enzymatic activity is regulated by the extent of its association with membrane structures. A current model posts that the elastic stress of the bilayer curvature is sensed by CCT and this governs the degree of membrane association, thus providing a mechanism for both positive and negative regulation of activity.


Pssm-ID: 173925  Cd Length: 150  Bit Score: 61.43  E-value: 6.96e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 477324825   8 GTFDVFHVGHLRLLQRARALGE--RLLVGVSSDALNIAKKGRaPVYHQDDRMAIIAGLACVDGV------FLEEsleqka 79
Cdd:cd02174    9 GCFDLFHYGHANALRQAKKLGPndYLIVGVHSDEEIHKHKGP-PVMTEEERYEAVRHCKWVDEVvegapyVTTP------ 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 477324825  80 EYLRGYSADILVMGDDW---------------AGKFdsfayicevVYFPRTPSVSTTGII 124
Cdd:cd02174   82 EFLDKYKCDYVAHGDDIyldadgedcyqevkdAGRF---------KEVKRTEGVSTTDLI 132
cytidylyltransferase_like cd02039
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ...
 4-125 6.27e-12

Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are known to use CTP or ATP and release pyrophosphate. Protein families that contain at least one copy of this domain include citrate lyase ligase, pantoate-beta-alanine ligase, glycerol-3-phosphate cytidyltransferase, ADP-heptose synthase, phosphocholine cytidylyltransferase, lipopolysaccharide core biosynthesis protein KdtB, the bifunctional protein NadR, and a number whose function is unknown.


Pssm-ID: 185678 [Multi-domain]  Cd Length: 143  Bit Score: 58.61  E-value: 6.27e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 477324825   4 VITFGTFDVFHVGHLRLLQRARALG-ERLLVGVSSDALNIAKKGRAPVYHqdDRMAII-AGLACVDGVFLEESLEQK--- 78
Cdd:cd02039    2 GIIIGRFEPFHLGHLKLIKEALEEAlDEVIIIIVSNPPKKKRNKDPFSLH--ERVEMLkEILKDRLKVVPVDFPEVKill 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 477324825  79 -----AEYLRGYSADILVMGDDWAGKFD--------SFAYICEVVYFPR---TPSVSTTGIIE 125
Cdd:cd02039   80 avvfiLKILLKVGPDKVVVGEDFAFGKNasynkdlkELFLDIEIVEVPRvrdGKKISSTLIRE 142
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 8-124 1.32e-11

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 60.18  E-value: 1.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 477324825   8 GTFDVFHVGHLRLLQRARALGERLLVGVSSDALNIAKKGrAPVYHQDDRMAIIAGLACVDGVFLEESLEQKAEYLRGYSA 87
Cdd:PTZ00308  18 GCFDMLHFGHANALRQARALGDELFVGCHSDEEIMRNKG-PPVMHQEERYEALRACKWVDEVVEGYPYTTRLEDLERLEC 96

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 477324825  88 DILVMGDDWA----GKfDSFAYICEVVYFP---RTPSVSTTGII 124
Cdd:PTZ00308  97 DFVVHGDDISvdlnGR-NSYQEIIDAGKFKvvkRTEGISTTDLV 139
ECT cd02173
CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine ...
 8-127 1.62e-11

CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine cytidylyltransferase (ECT) catalyzes the conversion of phosphoethanolamine to CDP-ethanolamine as part of the CDP-ethanolamine biosynthesis pathway. ECT expression in hepatocytes is localized predominantly to areas of the cytoplasm that are rich in rough endoplasmic reticulum. Several ECTs, including yeast and human ECT, have large repetitive sequences located within their N- and C-termini.


Pssm-ID: 173924  Cd Length: 152  Bit Score: 57.65  E-value: 1.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 477324825   8 GTFDVFHVGHLRLLQRARALGERLLVGVSSDALNIAKKGRA-PVYHQDDRmaIIAGLAC--VDGVFLEESLEQKAEYLRG 84
Cdd:cd02173    9 GAFDLFHIGHIEFLEKARELGDYLIVGVHDDQTVNEYKGSNyPIMNLHER--VLSVLACryVDEVVIGAPYVITKELIEH 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 477324825  85 YSADILVMG-----DDWAGKFDSFAYICEVVYFPRTPS---VSTTGIIEVI 127
Cdd:cd02173   87 FKIDVVVHGkteetPDSLDGEDPYAVPKEMGIFKEIDSgsdLTTRDIVNRI 137
PRK00777 PRK00777
pantetheine-phosphate adenylyltransferase;
1-58 7.61e-11

pantetheine-phosphate adenylyltransferase;


Pssm-ID: 234834  Cd Length: 153  Bit Score: 55.99  E-value: 7.61e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 477324825   1 MKTVITFGTFDVFHVGHLRLLQRARALGERLLVGVSSDALNIAKKGRaPVYHQDDRMA 58
Cdd:PRK00777   1 MMKVAVGGTFDPLHDGHRALLRKAFELGKRVTIGLTSDEFAKSYKKH-KVRPYEVRLK 57
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 8-95 2.48e-10

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 56.33  E-value: 2.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 477324825   8 GTFDVFHVGHLRLLQRARALGERLLVGVSSD-ALNIAKKGRAPVYHQDDRmaIIAGLAC--VDGVFLEESLEQKAEYLRG 84
Cdd:PTZ00308 199 GSFDLFHIGHIRVLQKARELGDYLIVGVHEDqVVNEQKGSNYPIMNLNER--VLGVLSCryVDEVVIGAPFDVTKEVIDS 276

                         90
                 ....*....|.
gi 477324825  85 YSADILVMGDD 95
Cdd:PTZ00308 277 LHINVVVGGKF 287
PLN02406 PLN02406
ethanolamine-phosphate cytidylyltransferase
 8-127 1.57e-09

ethanolamine-phosphate cytidylyltransferase


Pssm-ID: 215227 [Multi-domain]  Cd Length: 418  Bit Score: 54.30  E-value: 1.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 477324825   8 GTFDVFHVGHLRLLQRARALGERLLVGVSSDALNIAKKGRA-PVYHQDDRMaiIAGLAC--VDGVFLEESLEQKAEYLRG 84
Cdd:PLN02406 258 GAFDLFHAGHVEILRLARALGDFLLVGIHTDQTVSAHRGAHrPIMNLHERS--LSVLACryVDEVIIGAPWEVSKDMITT 335

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 477324825  85 YSADILVMG------DDWAGKFDSFAYICEVVYFPRTPS---VSTTGIIEVI 127
Cdd:PLN02406 336 FNISLVVHGtvaennDFLKGEDDPYAVPKSMGIFQVLESpldITTSTIIRRI 387
PPAT_CoAS cd02164
phosphopantetheine adenylyltransferase domain of eukaryotic and archaeal bifunctional enzymes; ...
 8-58 9.76e-08

phosphopantetheine adenylyltransferase domain of eukaryotic and archaeal bifunctional enzymes; The PPAT domain of the bifunctional enzyme with PPAT and DPCK functions. The final two steps of the CoA biosynthesis pathway are catalyzed by phosphopantetheine adenylyltransferase (PPAT) and dephospho-CoA (dPCoA) kinase (DPCK). The PPAT reaction involves the reversible adenylation of 4'-phosphopantetheine to form 3'-dPCoA and PPi, and DPCK catalyses phosphorylation of the 3'-hydroxy group of the ribose moiety of dPCoA. In eukaryotes the two enzymes are part of a large multienzyme complex . Studies in Corynebacterium ammoniagenes suggested that separate enzymes were present, and this was confirmed through identification of the bacterial PPAT/CoAD.


Pssm-ID: 173915  Cd Length: 143  Bit Score: 47.66  E-value: 9.76e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 477324825   8 GTFDVFHVGHLRLLQRARALG-ERLLVGVSSDALNIAKKGRAPVYHQDDRMA 58
Cdd:cd02164    6 GTFDRLHDGHKILLSVAFLLAgEKLIIGVTSDELLKNKSLKELIEPYEERIA 57
nt_trans cd02156
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ...
 3-114 3.02e-07

nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily includes the class I amino-acyl tRNA synthetases, pantothenate synthetase (PanC), ATP sulfurylase, and the cytidylyltransferases, all of which have a conserved dinucleotide-binding domain.


Pssm-ID: 173912 [Multi-domain]  Cd Length: 105  Bit Score: 45.61  E-value: 3.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 477324825   3 TVITFGTFDVFHVGHLRLLQRARALGERLLVGVSSDALNIAKkgraPVYHQDDrmaiiaglacvdgvfleesleqkaEYL 82
Cdd:cd02156    1 KARFPGEPGYLHIGHAKLICRAKGIADQCVVRIDDNPPVKVW----QDPHELE------------------------ERK 52

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 477324825  83 RGYSADILVMGDDWAGKFD---------SFAYICEVVYFPR 114
Cdd:cd02156   53 ESIEEDISVCGEDFQQNRElyrwvkdniTLPVDPEQVELPR 93
CoaD COG0669
Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine ...
 1-60 1.67e-05

Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine adenylyltransferase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 440433  Cd Length: 159  Bit Score: 41.91  E-value: 1.67e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 477324825   1 MKTVITFGTFDVFHVGHLRLLQRARALGERLLVGVssdALNIAKKGRAPVyhqDDRMAII 60
Cdd:COG0669    1 MRIAVYPGSFDPITNGHLDIIERAAKLFDEVIVAV---AVNPSKKPLFSL---EERVELI 54
PLN02413 PLN02413
choline-phosphate cytidylyltransferase
 8-124 2.34e-05

choline-phosphate cytidylyltransferase


Pssm-ID: 215229  Cd Length: 294  Bit Score: 42.24  E-value: 2.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 477324825   8 GTFDVFHVGHLRLLQRARAL--GERLLVGVSSDALNIAKKGRApVYHQDDRMAIIAGLACVDGVFLEESLEQKAEYLR-- 83
Cdd:PLN02413  34 GIYDLFHFGHARSLEQAKKLfpNTYLLVGCCNDELTHKYKGKT-VMTEDERYESLRHCKWVDEVIPDAPWVITQEFLDkh 112

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 477324825  84 --GYSA-DILVMGDDWAGKFDSFAYICEVVYF---PRTPSVSTTGII 124
Cdd:PLN02413 113 riDYVAhDALPYADASGAGKDVYEFVKKIGKFketKRTDGISTSDII 159
PRK05627 PRK05627
bifunctional riboflavin kinase/FAD synthetase;
3-95 1.66e-04

bifunctional riboflavin kinase/FAD synthetase;


Pssm-ID: 235536 [Multi-domain]  Cd Length: 305  Bit Score: 39.75  E-value: 1.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 477324825   3 TVITFGTFDVFHVGHLRLLQRARALGERLlvGVSSDALNIAK-------KGRAPVY--HQDDRMAIIAGLAcVDGV---- 69
Cdd:PRK05627  15 CVLTIGNFDGVHRGHQALLARAREIARER--GLPSVVMTFEPhprevfaPDKAPARltPLRDKAELLAELG-VDYVlvlp 91

                         90       100       110
                 ....*....|....*....|....*....|..
gi 477324825  70 FLEESLEQKAE------YLRGYSADILVMGDD 95
Cdd:PRK05627  92 FDEEFAKLSAEefiedlLVKGLNAKHVVVGFD 123
PRK01170 PRK01170
bifunctional pantetheine-phosphate adenylyltransferase/NTP phosphatase;
1-38 1.97e-04

bifunctional pantetheine-phosphate adenylyltransferase/NTP phosphatase;


Pssm-ID: 234912 [Multi-domain]  Cd Length: 322  Bit Score: 39.42  E-value: 1.97e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 477324825   1 MKTVITfGTFDVFHVGHLRLLQRARALGERLLVGVSSD 38
Cdd:PRK01170   1 MITVVG-GTFSKLHKGHKALLKKAIETGDEVVIGLTSD 37
NMNAT_NadR cd02167
Nicotinamide/nicotinate mononucleotide adenylyltransferase of bifunctional NadR-like proteins; ...
 5-39 2.74e-04

Nicotinamide/nicotinate mononucleotide adenylyltransferase of bifunctional NadR-like proteins; NMNAT domain of NadR protein. The NadR protein (NadR) is a bifunctional enzyme possessing both NMN adenylytransferase (NMNAT) and ribosylnicotinamide kinase (RNK) activities. Its function is essential for the growth and survival of H. influenzae and thus may present a new highly specific anti-infectious drug target. The N-terminal domain that hosts the NMNAT activity is closely related to archaeal NMNAT. The bound NAD at the active site of the NMNAT domain reveals several critical interactions between NAD and the protein.The NMNAT domain of hiNadR defines yet another member of the pyridine nucleotide adenylyltransferase


Pssm-ID: 173918  Cd Length: 158  Bit Score: 38.62  E-value: 2.74e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 477324825   5 ITFGTFDVFHVGHLRLLQRARALGERLLVGVSSDA 39
Cdd:cd02167    3 IVFGKFAPLHTGHVYLIYKALSQVDELLIIVGSDD 37
coaD_prev_kdtB TIGR01510
pantetheine-phosphate adenylyltransferase, bacterial; This model describes ...
 8-60 6.89e-04

pantetheine-phosphate adenylyltransferase, bacterial; This model describes pantetheine-phosphate adenylyltransferase, the penultimate enzyme of coenzyme A (CoA) biosynthesis in bacteria. It does not show any strong homology to eukaryotic enzymes of coenzyme A biosynthesis. This protein was previously designated KdtB and postulated (because of cytidyltransferase homology and proximity to kdtA) to be an enzyme of LPS biosynthesis, a cytidyltransferase for 3-deoxy-D-manno-2-octulosonic acid. However, no activity toward that compound was found with either CTP or ATP. The phylogenetic distribution of this enzyme is more consistent with coenzyme A biosynthesis than with LPS biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]


Pssm-ID: 273663 [Multi-domain]  Cd Length: 155  Bit Score: 37.25  E-value: 6.89e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 477324825    8 GTFDVFHVGHLRLLQRARALGERLLVGVssdALNIAKKgraPVYHQDDRMAII 60
Cdd:TIGR01510   6 GSFDPVTNGHLDIIKRAAALFDEVIVAV---AKNPSKK---PLFSLEERVELI 52
FAD_synthetase_N cd02064
FAD synthetase, N-terminal domain of the bifunctional enzyme; FAD synthetase_N. N-terminal ...
 3-92 7.88e-04

FAD synthetase, N-terminal domain of the bifunctional enzyme; FAD synthetase_N. N-terminal domain of the bifunctional riboflavin biosynthesis protein riboflavin kinase/FAD synthetase. These enzymes have both ATP:riboflavin 5'-phosphotransferase and ATP:FMN-adenylyltransferase activities. The N-terminal domain is believed to play a role in the adenylylation reaction of FAD synthetases. The C-terminal domain is thought to have kinase activity. FAD synthetase is present among all kingdoms of life. However, the bifunctional enzyme is not found in mammals, which use separate enzymes for FMN and FAD formation.


Pssm-ID: 185679 [Multi-domain]  Cd Length: 180  Bit Score: 37.52  E-value: 7.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 477324825   3 TVITFGTFDVFHVGHLRLLQRARALGERLlvGVSSDALNIAKKGRApVYHQDDRMAIIAglacvdgvfleeSLEQKAEYL 82
Cdd:cd02064    1 TVVAIGNFDGVHLGHQALIKTLKKIARER--GLPSAVLTFDPHPRE-VFLPDKAPPRLT------------TLEEKLELL 65

                         90
                 ....*....|
gi 477324825  83 RGYSADILVM 92
Cdd:cd02064   66 ESLGVDYLLV 75
PRK07143 PRK07143
hypothetical protein; Provisional
 2-44 1.15e-03

hypothetical protein; Provisional


Pssm-ID: 235946 [Multi-domain]  Cd Length: 279  Bit Score: 37.29  E-value: 1.15e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 477324825   2 KTVITFGTFDVFHVGHLRLLQRARALGERLLVGVSSDALNIAK 44
Cdd:PRK07143  16 KPTFVLGGFESFHLGHLELFKKAKESNDEIVIVIFKNPENLPK 58
PPAT cd02163
Phosphopantetheine adenylyltransferase; Phosphopantetheine adenylyltransferase (PPAT). PPAT is ...
 8-60 1.40e-03

Phosphopantetheine adenylyltransferase; Phosphopantetheine adenylyltransferase (PPAT). PPAT is an essential enzyme in bacteria, responsible for catalyzing the rate-limiting step in coenzyme A (CoA) biosynthesis. The dinucleotide-binding fold of PPAT is homologous to class I aminoacyl-tRNA synthetases. CoA has been shown to inhibit PPAT and competes with ATP, PhP, and dPCoA. PPAT is a homohexamer in E. coli.


Pssm-ID: 173914 [Multi-domain]  Cd Length: 153  Bit Score: 36.29  E-value: 1.40e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 477324825   8 GTFDVFHVGHLRLLQRARALGERLLVGVssdALNIAKKgraPVYHQDDRMAII 60
Cdd:cd02163    6 GSFDPITNGHLDIIERASKLFDEVIVAV---AVNPSKK---PLFSLEERVELI 52
NadR COG1056
Nicotinamide mononucleotide adenylyltransferase [Coenzyme transport and metabolism]; ...
 1-38 2.81e-03

Nicotinamide mononucleotide adenylyltransferase [Coenzyme transport and metabolism]; Nicotinamide mononucleotide adenylyltransferase is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 440676 [Multi-domain]  Cd Length: 162  Bit Score: 35.56  E-value: 2.81e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 477324825   1 MKTVITFGTFDVFHVGHLRLLQRARALGERLLVGVSSD 38
Cdd:COG1056    2 MKRGLFIGRFQPFHLGHLAVIKWALEEVDELIIGIGSA 39
PRK08099 PRK08099
multifunctional transcriptional regulator/nicotinamide-nucleotide adenylyltransferase ...
 1-38 5.21e-03

multifunctional transcriptional regulator/nicotinamide-nucleotide adenylyltransferase/ribosylnicotinamide kinase NadR;


Pssm-ID: 236151 [Multi-domain]  Cd Length: 399  Bit Score: 35.40  E-value: 5.21e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 477324825   1 MKTV-ITFGTFDVFHVGHLRLLQRARALGERLLVGVSSD 38
Cdd:PRK08099  51 MKKIgVVFGKFYPLHTGHIYLIQRACSQVDELHIIICYD 89
 
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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