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Conserved domains on  [gi|657873790|ref|WP_029578348|]
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pantetheine-phosphate adenylyltransferase [Bordetella hinzii]

Protein Classification

pantetheine-phosphate adenylyltransferase( domain architecture ID 10786277)

pantetheine-phosphate adenylyltransferase catalyzes the reversible transfer of an adenylyl group from ATP to 4'-phosphopantetheine (Ppant) to form dephospho-CoA (dPCoA) and pyrophosphate in the Coenzyme A (CoA) biosynthetic pathway

CATH:  3.40.50.620
EC:  2.7.7.3
Gene Ontology:  GO:0005524|GO:0015937|GO:0004595
PubMed:  33271445

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CoaD COG0669
Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine ...
 1-159 1.47e-105

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: 298.45  E-value: 1.47e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657873790   1 MITAVYPGTFDPLTRGHEDLVRRAAALFDKVVVGVAYSRNKKPFFSIDERVEIAREVLGHYPNVEVQSFGGLLKDFVREQ 80
Cdd:COG0669    1 MRIAVYPGSFDPITNGHLDIIERAAKLFDEVIVAVAVNPSKKPLFSLEERVELIREALADLPNVEVDSFDGLLVDFAREV 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 657873790  81 NGRVIVRGLRAVSDFEYEFQMAGMNRHLLPDVETLFMTPSDQYQFISGTIVREIAQLGGDVSKFVFPSVERWLQAKAKE 159
Cdd:COG0669   81 GANVIVRGLRAVSDFEYEFQMALMNRKLAPEIETVFLMTSPEYSFISSSLVKEIARLGGDVSGFVPPAVAEALKEKFAK 159
 
Name Accession Description Interval E-value
CoaD COG0669
Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine ...
 1-159 1.47e-105

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: 298.45  E-value: 1.47e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657873790   1 MITAVYPGTFDPLTRGHEDLVRRAAALFDKVVVGVAYSRNKKPFFSIDERVEIAREVLGHYPNVEVQSFGGLLKDFVREQ 80
Cdd:COG0669    1 MRIAVYPGSFDPITNGHLDIIERAAKLFDEVIVAVAVNPSKKPLFSLEERVELIREALADLPNVEVDSFDGLLVDFAREV 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 657873790  81 NGRVIVRGLRAVSDFEYEFQMAGMNRHLLPDVETLFMTPSDQYQFISGTIVREIAQLGGDVSKFVFPSVERWLQAKAKE 159
Cdd:COG0669   81 GANVIVRGLRAVSDFEYEFQMALMNRKLAPEIETVFLMTSPEYSFISSSLVKEIARLGGDVSGFVPPAVAEALKEKFAK 159
PPAT cd02163
Phosphopantetheine adenylyltransferase; Phosphopantetheine adenylyltransferase (PPAT). PPAT is ...
 3-155 1.83e-94

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: 270.49  E-value: 1.83e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657873790   3 TAVYPGTFDPLTRGHEDLVRRAAALFDKVVVGVAYSRNKKPFFSIDERVEIAREVLGHYPNVEVQSFGGLLKDFVREQNG 82
Cdd:cd02163    1 IAVYPGSFDPITNGHLDIIERASKLFDEVIVAVAVNPSKKPLFSLEERVELIREATKHLPNVEVDGFDGLLVDFARKHGA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 657873790  83 RVIVRGLRAVSDFEYEFQMAGMNRHLLPDVETLFMTPSDQYQFISGTIVREIAQLGGDVSKFVFPSVERWLQA 155
Cdd:cd02163   81 NVIVRGLRAVSDFEYEFQMAGMNRKLAPEIETVFLMASPEYSFISSSLVKEIARFGGDVSGFVPPVVAKALKE 153
coaD_prev_kdtB TIGR01510
pantetheine-phosphate adenylyltransferase, bacterial; This model describes ...
 3-156 1.72e-72

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: 214.83  E-value: 1.72e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657873790    3 TAVYPGTFDPLTRGHEDLVRRAAALFDKVVVGVAYSRNKKPFFSIDERVEIAREVLGHYPNVEVQSFGGLLKDFVREQNG 82
Cdd:TIGR01510   1 IALYPGSFDPVTNGHLDIIKRAAALFDEVIVAVAKNPSKKPLFSLEERVELIKDATKHLPNVRVDVFDGLLVDYAKELGA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 657873790   83 RVIVRGLRAVSDFEYEFQMAGMNRHLLPDVETLFMTPSDQYQFISGTIVREIAQLGGDVSKFVFPSVERWLQAK 156
Cdd:TIGR01510  81 TFIVRGLRAATDFEYELQMALMNKHLAPEIETVFLMASPEYAFVSSSLVKEIASFGGDVSNLVPPAVARRLKAK 154
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 5-134 3.23e-31

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: 109.33  E-value: 3.23e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657873790    5 VYPGTFDPLTRGHEDLVRRAAALFDK-VVVGVAYS----RNKKPFFSIDERVEIAREvLGHYPNVEVQSFGGLLKDFVRE 79
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEdLIVGVPSDepphKLKRPLFSAEERLEMLEL-AKWVDEVIVVAPWELTRELLKE 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 657873790   80 QNGRVIVRGLRAVSDFEYEFQMAGMNRHLLPDVETLFMTPSDQYQFISGTIVREI 134
Cdd:pfam01467  80 LNPDVLVIGADSLLDFWYELDEILGNVKLVVVVRPVFFIPLKPTNGISSTDIRER 134
PRK00777 PRK00777
pantetheine-phosphate adenylyltransferase;
8-52 6.30e-05

pantetheine-phosphate adenylyltransferase;


Pssm-ID: 234834  Cd Length: 153  Bit Score: 40.97  E-value: 6.30e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 657873790   8 GTFDPLTRGHEDLVRRAAALFDKVVVGV-----AYSRNKKPFFSIDERVE 52
Cdd:PRK00777   8 GTFDPLHDGHRALLRKAFELGKRVTIGLtsdefAKSYKKHKVRPYEVRLK 57
Citrate_ly_lig smart00764
Citrate lyase ligase C-terminal domain; Proteins of this family contain the C-terminal domain ...
 12-68 5.88e-03

Citrate lyase ligase C-terminal domain; Proteins of this family contain the C-terminal domain of citrate lyase ligase EC:6.2.1.22.


Pssm-ID: 129003  Cd Length: 182  Bit Score: 35.68  E-value: 5.88e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 657873790    12 PLTRGHEDLVRRAAALFDKVVVGVAysRNKKPFFSIDERVEIAREVLGHYPNVEVQS 68
Cdd:smart00764  10 PFTLGHRYLVEQAAAECDWVHLFVV--SEDASLFSFDERFALVKKGTKDLDNVTVHS 64
 
Name Accession Description Interval E-value
CoaD COG0669
Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine ...
 1-159 1.47e-105

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: 298.45  E-value: 1.47e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657873790   1 MITAVYPGTFDPLTRGHEDLVRRAAALFDKVVVGVAYSRNKKPFFSIDERVEIAREVLGHYPNVEVQSFGGLLKDFVREQ 80
Cdd:COG0669    1 MRIAVYPGSFDPITNGHLDIIERAAKLFDEVIVAVAVNPSKKPLFSLEERVELIREALADLPNVEVDSFDGLLVDFAREV 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 657873790  81 NGRVIVRGLRAVSDFEYEFQMAGMNRHLLPDVETLFMTPSDQYQFISGTIVREIAQLGGDVSKFVFPSVERWLQAKAKE 159
Cdd:COG0669   81 GANVIVRGLRAVSDFEYEFQMALMNRKLAPEIETVFLMTSPEYSFISSSLVKEIARLGGDVSGFVPPAVAEALKEKFAK 159
PPAT cd02163
Phosphopantetheine adenylyltransferase; Phosphopantetheine adenylyltransferase (PPAT). PPAT is ...
 3-155 1.83e-94

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: 270.49  E-value: 1.83e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657873790   3 TAVYPGTFDPLTRGHEDLVRRAAALFDKVVVGVAYSRNKKPFFSIDERVEIAREVLGHYPNVEVQSFGGLLKDFVREQNG 82
Cdd:cd02163    1 IAVYPGSFDPITNGHLDIIERASKLFDEVIVAVAVNPSKKPLFSLEERVELIREATKHLPNVEVDGFDGLLVDFARKHGA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 657873790  83 RVIVRGLRAVSDFEYEFQMAGMNRHLLPDVETLFMTPSDQYQFISGTIVREIAQLGGDVSKFVFPSVERWLQA 155
Cdd:cd02163   81 NVIVRGLRAVSDFEYEFQMAGMNRKLAPEIETVFLMASPEYSFISSSLVKEIARFGGDVSGFVPPVVAKALKE 153
coaD_prev_kdtB TIGR01510
pantetheine-phosphate adenylyltransferase, bacterial; This model describes ...
 3-156 1.72e-72

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: 214.83  E-value: 1.72e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657873790    3 TAVYPGTFDPLTRGHEDLVRRAAALFDKVVVGVAYSRNKKPFFSIDERVEIAREVLGHYPNVEVQSFGGLLKDFVREQNG 82
Cdd:TIGR01510   1 IALYPGSFDPVTNGHLDIIKRAAALFDEVIVAVAKNPSKKPLFSLEERVELIKDATKHLPNVRVDVFDGLLVDYAKELGA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 657873790   83 RVIVRGLRAVSDFEYEFQMAGMNRHLLPDVETLFMTPSDQYQFISGTIVREIAQLGGDVSKFVFPSVERWLQAK 156
Cdd:TIGR01510  81 TFIVRGLRAATDFEYELQMALMNKHLAPEIETVFLMASPEYAFVSSSLVKEIASFGGDVSNLVPPAVARRLKAK 154
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 5-134 3.23e-31

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: 109.33  E-value: 3.23e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657873790    5 VYPGTFDPLTRGHEDLVRRAAALFDK-VVVGVAYS----RNKKPFFSIDERVEIAREvLGHYPNVEVQSFGGLLKDFVRE 79
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEdLIVGVPSDepphKLKRPLFSAEERLEMLEL-AKWVDEVIVVAPWELTRELLKE 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 657873790   80 QNGRVIVRGLRAVSDFEYEFQMAGMNRHLLPDVETLFMTPSDQYQFISGTIVREI 134
Cdd:pfam01467  80 LNPDVLVIGADSLLDFWYELDEILGNVKLVVVVRPVFFIPLKPTNGISSTDIRER 134
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 4-63 1.23e-13

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: 62.32  E-value: 1.23e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 657873790    4 AVYPGTFDPLTRGHEDLVRRAAALFDKVVVGVAYSRN-----KKPFFSIDERVEIAREVLGHYPN 63
Cdd:TIGR00125   2 VIFVGTFDPFHLGHLDLLERAKELFDELIVGVGSDQFvnplkGEPVFSLEERLEMLKALKYVDEV 66
cytidylyltransferase_like cd02039
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ...
 4-133 5.83e-10

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: 54.75  E-value: 5.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657873790   4 AVYPGTFDPLTRGHEDLVRRAAA-LFDKVVVGV-----AYSRNKKpFFSIDERVEIAREVLGHYPNVEVQSF-------G 70
Cdd:cd02039    2 GIIIGRFEPFHLGHLKLIKEALEeALDEVIIIIvsnppKKKRNKD-PFSLHERVEMLKEILKDRLKVVPVDFpevkillA 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 657873790  71 GLLKDFVREQNG-RVIVRGLRAVSDFEYEFQMagMNRHLLPDVETLFMTPSDQYQFISGTIVRE 133
Cdd:cd02039   81 VVFILKILLKVGpDKVVVGEDFAFGKNASYNK--DLKELFLDIEIVEVPRVRDGKKISSTLIRE 142
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 5-53 2.83e-08

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: 49.72  E-value: 2.83e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 657873790   5 VY-PGTFDPLTRGHEDLVRRAAALFDKVVVGVA-----YSRNKKPFFSIDERVEI 53
Cdd:COG0615    3 VItYGTFDLLHPGHINLLKRAKALGDELIVGVAtdefvASKGRKPIIPEEQRKEI 57
nt_trans cd02156
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ...
 3-129 1.81e-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: 47.15  E-value: 1.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657873790   3 TAVYPGTFDPLTRGHEDLVRRAAALFDKVVVGVA---YSRNKKPFFSIDERVEIAREVlghypnvevqsfggllkdfvre 79
Cdd:cd02156    1 KARFPGEPGYLHIGHAKLICRAKGIADQCVVRIDdnpPVKVWQDPHELEERKESIEED---------------------- 58

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 657873790  80 qngrVIVRGLRAVSDFEYEFQmAGMNRHLLPDVETLFMTPS-DQYQFISGT 129
Cdd:cd02156   59 ----ISVCGEDFQQNRELYRW-VKDNITLPVDPEQVELPRLnLETTVMSKR 104
NMNAT cd02165
Nicotinamide/nicotinate mononucleotide adenylyltransferase; Nicotinamide/nicotinate ...
 3-66 1.82e-05

Nicotinamide/nicotinate mononucleotide adenylyltransferase; Nicotinamide/nicotinate mononucleotide (NMN/ NaMN)adenylyltransferase (NMNAT). NMNAT represents the primary bacterial and eukaryotic adenylyltransferases for nicotinamide-nucleotide and for the deamido form, nicotinate nucleotide. It is an indispensable enzyme in the biosynthesis of NAD(+) and NADP(+). Nicotinamide-nucleotide adenylyltransferase synthesizes NAD via the salvage pathway, while nicotinate-nucleotide adenylyltransferase synthesizes the immediate precursor of NAD via the de novo pathway. Human NMNAT displays unique dual substrate specificity toward both NMN and NaMN, and can participate in both de novo and salvage pathways of NAD synthesis.


Pssm-ID: 185680 [Multi-domain]  Cd Length: 192  Bit Score: 43.00  E-value: 1.82e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 657873790   3 TAVYPGTFDPLTRGHEDLVRRAAALF--DKVVVGVAYSRNKKP--FFSIDERVEIAREVLGHYPNVEV 66
Cdd:cd02165    1 IALFGGSFDPPHLGHLAIAEEALEELglDRVLLLPSANPPHKPpkPASFEHRLEMLKLAIEDNPKFEV 68
G3P_Cytidylyltransferase cd02171
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase, ...
 8-57 4.54e-05

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: 40.93  E-value: 4.54e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 657873790   8 GTFDPLTRGHEDLVRRAAALFDKVVVGVAYS-----RNKKPFFSIDERVEIAREV 57
Cdd:cd02171    8 GTFDLLHIGHLNLLERAKALGDKLIVAVSTDefnagKGKKAVIPYEQRAEILESI 62
cytidylyltransferase cd02170
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ...
 8-85 5.36e-05

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: 41.12  E-value: 5.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657873790   8 GTFDPLTRGHEDLVRRAAALFDKVVVGVAYSRN-----KKPFFSIDERVEIARE-------VLGH-----------YPNV 64
Cdd:cd02170    8 GTFDIIHPGHIRFLEEAKKLGDYLIVGVARDETvakikRRPILPEEQRAEVVEAlkyvdevILGHpwsyfkpleelKPDV 87

                         90       100
                 ....*....|....*....|....*..
gi 657873790  65 EVQSF---GGLLKDFVRE---QNGRVI 85
Cdd:cd02170   88 IVLGDdqkNGVDEEEVYEelkKRGKVI 114
PRK00777 PRK00777
pantetheine-phosphate adenylyltransferase;
8-52 6.30e-05

pantetheine-phosphate adenylyltransferase;


Pssm-ID: 234834  Cd Length: 153  Bit Score: 40.97  E-value: 6.30e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 657873790   8 GTFDPLTRGHEDLVRRAAALFDKVVVGV-----AYSRNKKPFFSIDERVE 52
Cdd:PRK00777   8 GTFDPLHDGHRALLRKAFELGKRVTIGLtsdefAKSYKKHKVRPYEVRLK 57
Citrate_lyase_ligase cd02169
Citrate lyase ligase; Citrate lyase ligase, also known as [Citrate (pro-3S)-lyase] ligase, is ...
 12-68 1.46e-03

Citrate lyase ligase; Citrate lyase ligase, also known as [Citrate (pro-3S)-lyase] ligase, is responsible for acetylation of the (2-(5''-phosphoribosyl)-3'-dephosphocoenzyme-A) prosthetic group of the gamma subunit of citrate lyase, converting the inactive thiol form of this enzyme to the active form. The acetylation of 1 molecule of deacetyl-citrate lyase to enzymatically active citrate lyase requires 6 molecules of ATP. The Adenylylyltranferase activity of the enzyme involves the formation of AMP and and pyrophosphate in the acetylation reaction.


Pssm-ID: 173920 [Multi-domain]  Cd Length: 297  Bit Score: 38.01  E-value: 1.46e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 657873790  12 PLTRGHEDLVRRAAALFDKVVVGVAysRNKKPFFSIDERVEIAREVLGHYPNVEVQS 68
Cdd:cd02169  125 PFTLGHRYLVEKAAAENDWVHLFVV--SEDKSLFSFADRFKLVKKGTKHLKNVTVHS 179
nadD PRK00071
nicotinate-nucleotide adenylyltransferase;
1-66 1.94e-03

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 234611 [Multi-domain]  Cd Length: 203  Bit Score: 37.12  E-value: 1.94e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 657873790   1 MITAVYPGTFDPLTRGHEDLVRRAAALF--DKVVVGVAYS---RNKKPFFSIDERVEIAREVLGHYPNVEV 66
Cdd:PRK00071   4 KRIGLFGGTFDPPHYGHLAIAEEAAERLglDEVWFLPNPGpphKPQKPLAPLEHRLAMLELAIADNPRFSV 74
NMNAT_Archaea cd02166
Nicotinamide/nicotinate mononucleotide adenylyltransferase, archaeal; This family of archaeal ...
 4-59 3.85e-03

Nicotinamide/nicotinate mononucleotide adenylyltransferase, archaeal; This family of archaeal proteins exhibits nicotinamide-nucleotide adenylyltransferase (NMNAT) activity utilizing the salvage pathway to synthesize NAD. In some cases, the enzyme was tested and found also to have the activity of nicotinate-nucleotide adenylyltransferase an enzyme of NAD de novo biosynthesis, although with a higher Km. In some archaeal species, a number of proteins which are uncharacterized with respect to activity, are also present.


Pssm-ID: 173917  Cd Length: 163  Bit Score: 36.12  E-value: 3.85e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 657873790   4 AVYPGTFDPLTRGHEDLVRRAAALFDKVVVGVA---YSRNKKPFFSIDERVEIAREVLG 59
Cdd:cd02166    2 ALFIGRFQPFHLGHLKVIKWILEEVDELIIGIGsaqESHTLENPFTAGERVLMIRRALE 60
Citrate_ly_lig smart00764
Citrate lyase ligase C-terminal domain; Proteins of this family contain the C-terminal domain ...
 12-68 5.88e-03

Citrate lyase ligase C-terminal domain; Proteins of this family contain the C-terminal domain of citrate lyase ligase EC:6.2.1.22.


Pssm-ID: 129003  Cd Length: 182  Bit Score: 35.68  E-value: 5.88e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 657873790    12 PLTRGHEDLVRRAAALFDKVVVGVAysRNKKPFFSIDERVEIAREVLGHYPNVEVQS 68
Cdd:smart00764  10 PFTLGHRYLVEQAAAECDWVHLFVV--SEDASLFSFDERFALVKKGTKDLDNVTVHS 64
PRK01153 PRK01153
nicotinamide-nucleotide adenylyltransferase; Provisional
 4-61 9.28e-03

nicotinamide-nucleotide adenylyltransferase; Provisional


Pssm-ID: 179235  Cd Length: 174  Bit Score: 35.23  E-value: 9.28e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 657873790   4 AVYPGTFDPLTRGHEDLVRRAAALFDKVVVGVA---YSRNKKPFFSIDERVEIAREVLGHY 61
Cdd:PRK01153   3 ALFIGRFQPFHKGHLEVIKWILEEVDELIIGIGsaqESHTLKNPFTAGERILMIRKALEEE 63
 
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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