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Conserved domains on  [gi|757599179|ref|WP_042846826|]
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MULTISPECIES: pantetheine-phosphate adenylyltransferase [Providencia]

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 ...
 1-160 4.49e-84

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: 243.76  E-value: 4.49e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599179   1 MKhKAIYPGTFDPVTSGHVDIVTRAAAMFDHVLLAIANSQRKNPMFSLDERVALAKEVTSHLNNVEVVGFSELMANFAQK 80
Cdd:COG0669    1 MR-IAVYPGSFDPITNGHLDIIERAAKLFDEVIVAVAVNPSKKPLFSLEERVELIREALADLPNVEVDSFDGLLVDFARE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599179  81 NGANILIRGVRSVADFEYEWQLANMNRHFVPDLETVFLLPSQSLSFVSSSLIKDVALHDGDISSFLPPVVAEAMLKKLNK 160
Cdd:COG0669   80 VGANVIVRGLRAVSDFEYEFQMALMNRKLAPEIETVFLMTSPEYSFISSSLVKEIARLGGDVSGFVPPAVAEALKEKFAK 159
 
Name Accession Description Interval E-value
CoaD COG0669
Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine ...
 1-160 4.49e-84

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: 243.76  E-value: 4.49e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599179   1 MKhKAIYPGTFDPVTSGHVDIVTRAAAMFDHVLLAIANSQRKNPMFSLDERVALAKEVTSHLNNVEVVGFSELMANFAQK 80
Cdd:COG0669    1 MR-IAVYPGSFDPITNGHLDIIERAAKLFDEVIVAVAVNPSKKPLFSLEERVELIREALADLPNVEVDSFDGLLVDFARE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599179  81 NGANILIRGVRSVADFEYEWQLANMNRHFVPDLETVFLLPSQSLSFVSSSLIKDVALHDGDISSFLPPVVAEAMLKKLNK 160
Cdd:COG0669   80 VGANVIVRGLRAVSDFEYEFQMALMNRKLAPEIETVFLMTSPEYSFISSSLVKEIARLGGDVSGFVPPAVAEALKEKFAK 159
PPAT cd02163
Phosphopantetheine adenylyltransferase; Phosphopantetheine adenylyltransferase (PPAT). PPAT is ...
 4-156 2.03e-80

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: 234.67  E-value: 2.03e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599179   4 KAIYPGTFDPVTSGHVDIVTRAAAMFDHVLLAIANSQRKNPMFSLDERVALAKEVTSHLNNVEVVGFSELMANFAQKNGA 83
Cdd:cd02163    1 IAVYPGSFDPITNGHLDIIERASKLFDEVIVAVAVNPSKKPLFSLEERVELIREATKHLPNVEVDGFDGLLVDFARKHGA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 757599179  84 NILIRGVRSVADFEYEWQLANMNRHFVPDLETVFLLPSQSLSFVSSSLIKDVALHDGDISSFLPPVVAEAMLK 156
Cdd:cd02163   81 NVIVRGLRAVSDFEYEFQMAGMNRKLAPEIETVFLMASPEYSFISSSLVKEIARFGGDVSGFVPPVVAKALKE 153
coaD_prev_kdtB TIGR01510
pantetheine-phosphate adenylyltransferase, bacterial; This model describes ...
 4-158 6.11e-60

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: 182.86  E-value: 6.11e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599179    4 KAIYPGTFDPVTSGHVDIVTRAAAMFDHVLLAIANSQRKNPMFSLDERVALAKEVTSHLNNVEVVGFSELMANFAQKNGA 83
Cdd:TIGR01510   1 IALYPGSFDPVTNGHLDIIKRAAALFDEVIVAVAKNPSKKPLFSLEERVELIKDATKHLPNVRVDVFDGLLVDYAKELGA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 757599179   84 NILIRGVRSVADFEYEWQLANMNRHFVPDLETVFLLPSQSLSFVSSSLIKDVALHDGDISSFLPPVVAEAMLKKL 158
Cdd:TIGR01510  81 TFIVRGLRAATDFEYELQMALMNKHLAPEIETVFLMASPEYAFVSSSLVKEIASFGGDVSNLVPPAVARRLKAKF 155
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 6-120 8.08e-25

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: 92.77  E-value: 8.08e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599179    6 IYPGTFDPVTSGHVDIVTRAAAMFDHVLL-AIANSQ----RKNPMFSLDERVALAKEVTsHLNNVEVVGFSELMANFAQK 80
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEDLIvGVPSDEpphkLKRPLFSAEERLEMLELAK-WVDEVIVVAPWELTRELLKE 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 757599179   81 NGANILIRGVRSVADFEYEWQLANMNRHFVPDLETVFLLP 120
Cdd:pfam01467  80 LNPDVLVIGADSLLDFWYELDEILGNVKLVVVVRPVFFIP 119
nadD PRK00071
nicotinate-nucleotide adenylyltransferase;
1-67 1.94e-06

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 234611 [Multi-domain]  Cd Length: 203  Bit Score: 45.60  E-value: 1.94e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 757599179   1 MKHKAIYPGTFDPVTSGHVDIVTRAAAMF--DHVLLAIA--NSQRKN-PMFSLDERVALAKEVTSHLNNVEV 67
Cdd:PRK00071   3 MKRIGLFGGTFDPPHYGHLAIAEEAAERLglDEVWFLPNpgPPHKPQkPLAPLEHRLAMLELAIADNPRFSV 74
Citrate_ly_lig smart00764
Citrate lyase ligase C-terminal domain; Proteins of this family contain the C-terminal domain ...
 13-78 1.03e-04

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: 40.69  E-value: 1.03e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 757599179    13 PVTSGHVDIVTRAAAMFDHVLLAIANSQRKnpMFSLDERVALAKEVTSHLNNVEVVGFSELMANFA 78
Cdd:smart00764  10 PFTLGHRYLVEQAAAECDWVHLFVVSEDAS--LFSFDERFALVKKGTKDLDNVTVHSGSDYIISRA 73
 
Name Accession Description Interval E-value
CoaD COG0669
Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine ...
 1-160 4.49e-84

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: 243.76  E-value: 4.49e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599179   1 MKhKAIYPGTFDPVTSGHVDIVTRAAAMFDHVLLAIANSQRKNPMFSLDERVALAKEVTSHLNNVEVVGFSELMANFAQK 80
Cdd:COG0669    1 MR-IAVYPGSFDPITNGHLDIIERAAKLFDEVIVAVAVNPSKKPLFSLEERVELIREALADLPNVEVDSFDGLLVDFARE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599179  81 NGANILIRGVRSVADFEYEWQLANMNRHFVPDLETVFLLPSQSLSFVSSSLIKDVALHDGDISSFLPPVVAEAMLKKLNK 160
Cdd:COG0669   80 VGANVIVRGLRAVSDFEYEFQMALMNRKLAPEIETVFLMTSPEYSFISSSLVKEIARLGGDVSGFVPPAVAEALKEKFAK 159
PPAT cd02163
Phosphopantetheine adenylyltransferase; Phosphopantetheine adenylyltransferase (PPAT). PPAT is ...
 4-156 2.03e-80

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: 234.67  E-value: 2.03e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599179   4 KAIYPGTFDPVTSGHVDIVTRAAAMFDHVLLAIANSQRKNPMFSLDERVALAKEVTSHLNNVEVVGFSELMANFAQKNGA 83
Cdd:cd02163    1 IAVYPGSFDPITNGHLDIIERASKLFDEVIVAVAVNPSKKPLFSLEERVELIREATKHLPNVEVDGFDGLLVDFARKHGA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 757599179  84 NILIRGVRSVADFEYEWQLANMNRHFVPDLETVFLLPSQSLSFVSSSLIKDVALHDGDISSFLPPVVAEAMLK 156
Cdd:cd02163   81 NVIVRGLRAVSDFEYEFQMAGMNRKLAPEIETVFLMASPEYSFISSSLVKEIARFGGDVSGFVPPVVAKALKE 153
coaD_prev_kdtB TIGR01510
pantetheine-phosphate adenylyltransferase, bacterial; This model describes ...
 4-158 6.11e-60

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: 182.86  E-value: 6.11e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599179    4 KAIYPGTFDPVTSGHVDIVTRAAAMFDHVLLAIANSQRKNPMFSLDERVALAKEVTSHLNNVEVVGFSELMANFAQKNGA 83
Cdd:TIGR01510   1 IALYPGSFDPVTNGHLDIIKRAAALFDEVIVAVAKNPSKKPLFSLEERVELIKDATKHLPNVRVDVFDGLLVDYAKELGA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 757599179   84 NILIRGVRSVADFEYEWQLANMNRHFVPDLETVFLLPSQSLSFVSSSLIKDVALHDGDISSFLPPVVAEAMLKKL 158
Cdd:TIGR01510  81 TFIVRGLRAATDFEYELQMALMNKHLAPEIETVFLMASPEYAFVSSSLVKEIASFGGDVSNLVPPAVARRLKAKF 155
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 6-120 8.08e-25

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: 92.77  E-value: 8.08e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599179    6 IYPGTFDPVTSGHVDIVTRAAAMFDHVLL-AIANSQ----RKNPMFSLDERVALAKEVTsHLNNVEVVGFSELMANFAQK 80
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEDLIvGVPSDEpphkLKRPLFSAEERLEMLELAK-WVDEVIVVAPWELTRELLKE 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 757599179   81 NGANILIRGVRSVADFEYEWQLANMNRHFVPDLETVFLLP 120
Cdd:pfam01467  80 LNPDVLVIGADSLLDFWYELDEILGNVKLVVVVRPVFFIP 119
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 4-64 7.54e-14

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: 62.71  E-value: 7.54e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 757599179    4 KAIYPGTFDPVTSGHVDIVTRAAAMFDHVLLAI-----ANSQRKNPMFSLDERVALAKEVTSHLNN 64
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELFDELIVGVgsdqfVNPLKGEPVFSLEERLEMLKALKYVDEV 66
NMNAT cd02165
Nicotinamide/nicotinate mononucleotide adenylyltransferase; Nicotinamide/nicotinate ...
 5-67 4.77e-09

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: 52.63  E-value: 4.77e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 757599179   5 AIYPGTFDPVTSGHVDIVTRAAAMF--DHVLL--AIANSQRKNPMFSLDERVALAKEVTSHLNNVEV 67
Cdd:cd02165    2 ALFGGSFDPPHLGHLAIAEEALEELglDRVLLlpSANPPHKPPKPASFEHRLEMLKLAIEDNPKFEV 68
nt_trans cd02156
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ...
 4-118 3.39e-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: 45.99  E-value: 3.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599179   4 KAIYPGTFDPVTSGHVDIVTRAAAMFDHVLLAIANSQR---KNPMFSLDERVALAKEVtshlnnvevvgfselmanfaqk 80
Cdd:cd02156    1 KARFPGEPGYLHIGHAKLICRAKGIADQCVVRIDDNPPvkvWQDPHELEERKESIEED---------------------- 58

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 757599179  81 nganILIRGVRSVADFEYEWQlANMNRHFVPDLETVFL 118
Cdd:cd02156   59 ----ISVCGEDFQQNRELYRW-VKDNITLPVDPEQVEL 91
cytidylyltransferase_like cd02039
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ...
 4-120 3.40e-07

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: 47.05  E-value: 3.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599179   4 KAIYPGTFDPVTSGHVDIVTRAAAMFDHVLLAIANSQRKNP-----MFSLDERVALAKEVTSHLNNVEVVGFSELMANFA 78
Cdd:cd02039    1 VGIIIGRFEPFHLGHLKLIKEALEEALDEVIIIIVSNPPKKkrnkdPFSLHERVEMLKEILKDRLKVVPVDFPEVKILLA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 757599179  79 Q--------KNGANILIRGVRSVADFEYEWQLANMNrhFVPDLETVFLLP 120
Cdd:cd02039   81 VvfilkillKVGPDKVVVGEDFAFGKNASYNKDLKE--LFLDIEIVEVPR 128
nadD PRK00071
nicotinate-nucleotide adenylyltransferase;
1-67 1.94e-06

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 234611 [Multi-domain]  Cd Length: 203  Bit Score: 45.60  E-value: 1.94e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 757599179   1 MKHKAIYPGTFDPVTSGHVDIVTRAAAMF--DHVLLAIA--NSQRKN-PMFSLDERVALAKEVTSHLNNVEV 67
Cdd:PRK00071   3 MKRIGLFGGTFDPPHYGHLAIAEEAAERLglDEVWFLPNpgPPHKPQkPLAPLEHRLAMLELAIADNPRFSV 74
NadD COG1057
Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; ...
 1-67 2.82e-05

Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; Nicotinate-nucleotide adenylyltransferase NadD is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 440677 [Multi-domain]  Cd Length: 197  Bit Score: 42.42  E-value: 2.82e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 757599179   1 MKHKAIYPGTFDPVTSGHVDIVTRAAAMF--DHVLL--AIANSQRKN-PMFSLDERVALAKEVTSHLNNVEV 67
Cdd:COG1057    1 MMRIGIFGGTFDPIHIGHLALAEEAAEQLglDEVIFvpAGQPPHKKHkPLASAEHRLAMLRLAIADNPRFEV 72
Citrate_lyase_ligase cd02169
Citrate lyase ligase; Citrate lyase ligase, also known as [Citrate (pro-3S)-lyase] ligase, is ...
 13-78 9.39e-05

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: 41.10  E-value: 9.39e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 757599179  13 PVTSGHVDIVTRAAAMFDHVLLAIANSQRKnpMFSLDERVALAKEVTSHLNNVEVVGFSELMANFA 78
Cdd:cd02169  125 PFTLGHRYLVEKAAAENDWVHLFVVSEDKS--LFSFADRFKLVKKGTKHLKNVTVHSGGDYIISSA 188
Citrate_ly_lig smart00764
Citrate lyase ligase C-terminal domain; Proteins of this family contain the C-terminal domain ...
 13-78 1.03e-04

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: 40.69  E-value: 1.03e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 757599179    13 PVTSGHVDIVTRAAAMFDHVLLAIANSQRKnpMFSLDERVALAKEVTSHLNNVEVVGFSELMANFA 78
Cdd:smart00764  10 PFTLGHRYLVEQAAAECDWVHLFVVSEDAS--LFSFDERFALVKKGTKDLDNVTVHSGSDYIISRA 73
PRK00777 PRK00777
pantetheine-phosphate adenylyltransferase;
9-67 7.12e-04

pantetheine-phosphate adenylyltransferase;


Pssm-ID: 234834  Cd Length: 153  Bit Score: 37.89  E-value: 7.12e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 757599179   9 GTFDPVTSGHVDIVTRAAAMFDHVLLAI-----ANSQRKNPMFSLDERVA-LAKEVTSHLNNVEV 67
Cdd:PRK00777   8 GTFDPLHDGHRALLRKAFELGKRVTIGLtsdefAKSYKKHKVRPYEVRLKnLKKFLKAVEYDREY 72
PRK01153 PRK01153
nicotinamide-nucleotide adenylyltransferase; Provisional
 3-52 7.60e-04

nicotinamide-nucleotide adenylyltransferase; Provisional


Pssm-ID: 179235  Cd Length: 174  Bit Score: 37.93  E-value: 7.60e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 757599179   3 HKAIYPGTFDPVTSGHVDIVTRAAAMFDHVLLAIANSQR----KNPmFSLDERV 52
Cdd:PRK01153   1 MRALFIGRFQPFHKGHLEVIKWILEEVDELIIGIGSAQEshtlKNP-FTAGERI 53
NMNAT_Archaea cd02166
Nicotinamide/nicotinate mononucleotide adenylyltransferase, archaeal; This family of archaeal ...
 4-57 1.61e-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: 36.89  E-value: 1.61e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 757599179   4 KAIYPGTFDPVTSGHVDIVTRAAAMFDHVLLAIANSQR----KNPmFSLDERVALAKE 57
Cdd:cd02166    1 RALFIGRFQPFHLGHLKVIKWILEEVDELIIGIGSAQEshtlENP-FTAGERVLMIRR 57
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 8-68 2.88e-03

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: 35.85  E-value: 2.88e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 757599179   8 PGTFDPVTSGHVDIVTRAAAMFDHVLLAIANSQ-----RKNPMFSLDERvalaKEVTSHLNNV-EVV 68
Cdd:COG0615    6 YGTFDLLHPGHINLLKRAKALGDELIVGVATDEfvaskGRKPIIPEEQR----KEIVEALKYVdEVI 68
PRK08887 PRK08887
nicotinate-nicotinamide nucleotide adenylyltransferase;
1-66 6.90e-03

nicotinate-nicotinamide nucleotide adenylyltransferase;


Pssm-ID: 181576 [Multi-domain]  Cd Length: 174  Bit Score: 35.47  E-value: 6.90e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599179   1 MKHKAIYPGTFDPVTSGHVDIVTRaAAMFDHVLL--AIANSQRKNpMFSLDERVALAKEVTSHL--NNVE 66
Cdd:PRK08887   1 MKKIAVFGSAFNPPSLGHKSVIES-LSHFDLVLLvpSIAHAWGKT-MLDYETRCQLVDAFIQDLglSNVQ 68
 
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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