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Conserved domains on  [gi|491113749|ref|WP_004972207|]
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MULTISPECIES: pantetheine-phosphate adenylyltransferase [Acinetobacter]

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 ...
 3-161 1.40e-99

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: 283.05  E-value: 1.40e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113749   3 KTRVIYPGTFDPITNGHIDLVTRAAKMFDEVVVAIAIGHHKNPIFTLEERVELAQASLKHLPNVEFVGFDGLLVNFFREQ 82
Cdd:COG0669    1 MRIAVYPGSFDPITNGHLDIIERAAKLFDEVIVAVAVNPSKKPLFSLEERVELIREALADLPNVEVDSFDGLLVDFAREV 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491113749  83 NATAVLRGLRAVSDFEYEFQLANMNRQLDAKYEAVFLTPSEQYSFISSTLVREIARLKGDVTKFVAPVVVEAFERKLRQ 161
Cdd:COG0669   81 GANVIVRGLRAVSDFEYEFQMALMNRKLAPEIETVFLMTSPEYSFISSSLVKEIARLGGDVSGFVPPAVAEALKEKFAK 159
 
Name Accession Description Interval E-value
CoaD COG0669
Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine ...
 3-161 1.40e-99

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: 283.05  E-value: 1.40e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113749   3 KTRVIYPGTFDPITNGHIDLVTRAAKMFDEVVVAIAIGHHKNPIFTLEERVELAQASLKHLPNVEFVGFDGLLVNFFREQ 82
Cdd:COG0669    1 MRIAVYPGSFDPITNGHLDIIERAAKLFDEVIVAVAVNPSKKPLFSLEERVELIREALADLPNVEVDSFDGLLVDFAREV 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491113749  83 NATAVLRGLRAVSDFEYEFQLANMNRQLDAKYEAVFLTPSEQYSFISSTLVREIARLKGDVTKFVAPVVVEAFERKLRQ 161
Cdd:COG0669   81 GANVIVRGLRAVSDFEYEFQMALMNRKLAPEIETVFLMTSPEYSFISSSLVKEIARLGGDVSGFVPPAVAEALKEKFAK 159
PPAT cd02163
Phosphopantetheine adenylyltransferase; Phosphopantetheine adenylyltransferase (PPAT). PPAT is ...
 5-154 6.16e-90

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: 258.55  E-value: 6.16e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113749   5 RVIYPGTFDPITNGHIDLVTRAAKMFDEVVVAIAIGHHKNPIFTLEERVELAQASLKHLPNVEFVGFDGLLVNFFREQNA 84
Cdd:cd02163    1 IAVYPGSFDPITNGHLDIIERASKLFDEVIVAVAVNPSKKPLFSLEERVELIREATKHLPNVEVDGFDGLLVDFARKHGA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113749  85 TAVLRGLRAVSDFEYEFQLANMNRQLDAKYEAVFLTPSEQYSFISSTLVREIARLKGDVTKFVAPVVVEA 154
Cdd:cd02163   81 NVIVRGLRAVSDFEYEFQMAGMNRKLAPEIETVFLMASPEYSFISSSLVKEIARFGGDVSGFVPPVVAKA 150
coaD_prev_kdtB TIGR01510
pantetheine-phosphate adenylyltransferase, bacterial; This model describes ...
 5-159 1.86e-68

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: 204.43  E-value: 1.86e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113749    5 RVIYPGTFDPITNGHIDLVTRAAKMFDEVVVAIAIGHHKNPIFTLEERVELAQASLKHLPNVEFVGFDGLLVNFFREQNA 84
Cdd:TIGR01510   1 IALYPGSFDPVTNGHLDIIKRAAALFDEVIVAVAKNPSKKPLFSLEERVELIKDATKHLPNVRVDVFDGLLVDYAKELGA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491113749   85 TAVLRGLRAVSDFEYEFQLANMNRQLDAKYEAVFLTPSEQYSFISSTLVREIARLKGDVTKFVAPVVVEAFERKL 159
Cdd:TIGR01510  81 TFIVRGLRAATDFEYELQMALMNKHLAPEIETVFLMASPEYAFVSSSLVKEIASFGGDVSNLVPPAVARRLKAKF 155
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 7-136 2.38e-35

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: 119.73  E-value: 2.38e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113749    7 IYPGTFDPITNGHIDLVTRAAKMFDE-VVVAIAIG----HHKNPIFTLEERVELAQAsLKHLPNVEFVGFDGLLVNFFRE 81
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEdLIVGVPSDepphKLKRPLFSAEERLEMLEL-AKWVDEVIVVAPWELTRELLKE 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 491113749   82 QNATAVLRGLRAVSDFEYEFQLANMNRQLDAKYEAVFLTPSEQYSFISSTLVREI 136
Cdd:pfam01467  80 LNPDVLVIGADSLLDFWYELDEILGNVKLVVVVRPVFFIPLKPTNGISSTDIRER 134
nadD PRK00071
nicotinate-nucleotide adenylyltransferase;
1-153 1.07e-07

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 234611 [Multi-domain]  Cd Length: 203  Bit Score: 49.06  E-value: 1.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113749   1 MSKTRV-IYPGTFDPITNGHIDLVTRAAKMF--DEVV------------------------VAIAIGHhkNPIFTLeERV 53
Cdd:PRK00071   1 EMMKRIgLFGGTFDPPHYGHLAIAEEAAERLglDEVWflpnpgpphkpqkplaplehrlamLELAIAD--NPRFSV-SDI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113749  54 ELAQAS-------LKHL----PNVEFV---GFDgLLVNFFREQNATAVLRGLR-AVSD---FEYEFQLANMNRQLDAKYE 115
Cdd:PRK00071  78 ELERPGpsytidtLRELraryPDVELVfiiGAD-ALAQLPRWKRWEEILDLVHfVVVPrpgYPLEALALPALQQLLEAAG 156

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 491113749 116 AVFLTPSEQySFISSTLVREIARLKGDVTKFVAPVVVE 153
Cdd:PRK00071 157 AITLLDVPL-LAISSTAIRERIKEGRPIRYLLPEAVLD 193
Citrate_ly_lig smart00764
Citrate lyase ligase C-terminal domain; Proteins of this family contain the C-terminal domain ...
 14-69 5.50e-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: 5.50e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 491113749    14 PITNGHIDLVTRAAKMFDEVVVAIAigHHKNPIFTLEERVELAQASLKHLPNVEFV 69
Cdd:smart00764  10 PFTLGHRYLVEQAAAECDWVHLFVV--SEDASLFSFDERFALVKKGTKDLDNVTVH 63
 
Name Accession Description Interval E-value
CoaD COG0669
Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine ...
 3-161 1.40e-99

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: 283.05  E-value: 1.40e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113749   3 KTRVIYPGTFDPITNGHIDLVTRAAKMFDEVVVAIAIGHHKNPIFTLEERVELAQASLKHLPNVEFVGFDGLLVNFFREQ 82
Cdd:COG0669    1 MRIAVYPGSFDPITNGHLDIIERAAKLFDEVIVAVAVNPSKKPLFSLEERVELIREALADLPNVEVDSFDGLLVDFAREV 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491113749  83 NATAVLRGLRAVSDFEYEFQLANMNRQLDAKYEAVFLTPSEQYSFISSTLVREIARLKGDVTKFVAPVVVEAFERKLRQ 161
Cdd:COG0669   81 GANVIVRGLRAVSDFEYEFQMALMNRKLAPEIETVFLMTSPEYSFISSSLVKEIARLGGDVSGFVPPAVAEALKEKFAK 159
PPAT cd02163
Phosphopantetheine adenylyltransferase; Phosphopantetheine adenylyltransferase (PPAT). PPAT is ...
 5-154 6.16e-90

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: 258.55  E-value: 6.16e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113749   5 RVIYPGTFDPITNGHIDLVTRAAKMFDEVVVAIAIGHHKNPIFTLEERVELAQASLKHLPNVEFVGFDGLLVNFFREQNA 84
Cdd:cd02163    1 IAVYPGSFDPITNGHLDIIERASKLFDEVIVAVAVNPSKKPLFSLEERVELIREATKHLPNVEVDGFDGLLVDFARKHGA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113749  85 TAVLRGLRAVSDFEYEFQLANMNRQLDAKYEAVFLTPSEQYSFISSTLVREIARLKGDVTKFVAPVVVEA 154
Cdd:cd02163   81 NVIVRGLRAVSDFEYEFQMAGMNRKLAPEIETVFLMASPEYSFISSSLVKEIARFGGDVSGFVPPVVAKA 150
coaD_prev_kdtB TIGR01510
pantetheine-phosphate adenylyltransferase, bacterial; This model describes ...
 5-159 1.86e-68

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: 204.43  E-value: 1.86e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113749    5 RVIYPGTFDPITNGHIDLVTRAAKMFDEVVVAIAIGHHKNPIFTLEERVELAQASLKHLPNVEFVGFDGLLVNFFREQNA 84
Cdd:TIGR01510   1 IALYPGSFDPVTNGHLDIIKRAAALFDEVIVAVAKNPSKKPLFSLEERVELIKDATKHLPNVRVDVFDGLLVDYAKELGA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491113749   85 TAVLRGLRAVSDFEYEFQLANMNRQLDAKYEAVFLTPSEQYSFISSTLVREIARLKGDVTKFVAPVVVEAFERKL 159
Cdd:TIGR01510  81 TFIVRGLRAATDFEYELQMALMNKHLAPEIETVFLMASPEYAFVSSSLVKEIASFGGDVSNLVPPAVARRLKAKF 155
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 7-136 2.38e-35

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: 119.73  E-value: 2.38e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113749    7 IYPGTFDPITNGHIDLVTRAAKMFDE-VVVAIAIG----HHKNPIFTLEERVELAQAsLKHLPNVEFVGFDGLLVNFFRE 81
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEdLIVGVPSDepphKLKRPLFSAEERLEMLEL-AKWVDEVIVVAPWELTRELLKE 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 491113749   82 QNATAVLRGLRAVSDFEYEFQLANMNRQLDAKYEAVFLTPSEQYSFISSTLVREI 136
Cdd:pfam01467  80 LNPDVLVIGADSLLDFWYELDEILGNVKLVVVVRPVFFIPLKPTNGISSTDIRER 134
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 5-65 6.23e-18

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: 73.11  E-value: 6.23e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491113749    5 RVIYPGTFDPITNGHIDLVTRAAKMFDEVVVAIAI-----GHHKNPIFTLEERVELAQASLKHLPN 65
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELFDELIVGVGSdqfvnPLKGEPVFSLEERLEMLKALKYVDEV 66
cytidylyltransferase_like cd02039
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ...
 5-135 4.09e-13

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: 62.84  E-value: 4.09e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113749   5 RVIYPGTFDPITNGHIDLVTRAAKMFDEVVVaIAIG----HHKNP--IFTLEERVELAQASLKHLPNVEFVGFDG----L 74
Cdd:cd02039    1 VGIIIGRFEPFHLGHLKLIKEALEEALDEVI-IIIVsnppKKKRNkdPFSLHERVEMLKEILKDRLKVVPVDFPEvkilL 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491113749  75 LVNFFREQ----NATAVLRGLRAVSDFEYEFQLANMNRQLDakYEAVFLTPSEQYSFISSTLVRE 135
Cdd:cd02039   80 AVVFILKIllkvGPDKVVVGEDFAFGKNASYNKDLKELFLD--IEIVEVPRVRDGKKISSTLIRE 142
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 4-58 2.75e-10

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: 55.11  E-value: 2.75e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113749   4 TRVIYPGTFDPITNGHIDLVTRAAKMFDEVVVAIA-----IGHHKNPIFTLEERVELAQA 58
Cdd:COG0615    1 KRVITYGTFDLLHPGHINLLKRAKALGDELIVGVAtdefvASKGRKPIIPEEQRKEIVEA 60
nt_trans cd02156
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ...
 6-132 1.38e-09

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: 52.54  E-value: 1.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113749   6 VIYPGTFDPITNGHIDLVTRAAKMFDEVVVAIAIGH---HKNPIFTLEERVELAQASLkhlpnvefvgfdgllvnffreq 82
Cdd:cd02156    2 ARFPGEPGYLHIGHAKLICRAKGIADQCVVRIDDNPpvkVWQDPHELEERKESIEEDI---------------------- 59

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 491113749  83 nataVLRGLRAVSDFEYEFQlANMNRQLDAKYEAVFLTPSE-QYSFISSTL 132
Cdd:cd02156   60 ----SVCGEDFQQNRELYRW-VKDNITLPVDPEQVELPRLNlETTVMSKRK 105
NadR COG1056
Nicotinamide mononucleotide adenylyltransferase [Coenzyme transport and metabolism]; ...
 3-63 1.30e-08

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: 50.96  E-value: 1.30e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491113749   3 KTRVIYPGTFDPITNGHIDLVTRAAKMFDEVVvaIAIGH----H--KNPiFTLEERVELAQASLKHL 63
Cdd:COG1056    2 MKRGLFIGRFQPFHLGHLAVIKWALEEVDELI--IGIGSaqesHtpRNP-FTAGERIEMIRAALKEE 65
NMNAT cd02165
Nicotinamide/nicotinate mononucleotide adenylyltransferase; Nicotinamide/nicotinate ...
 7-153 1.07e-07

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: 49.16  E-value: 1.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113749   7 IYPGTFDPITNGHIDLVTRAAKMF--DEV--VVAIAIGHHKNPIFTLEERVELAQA------------------------ 58
Cdd:cd02165    3 LFGGSFDPPHLGHLAIAEEALEELglDRVllLPSANPPHKPPKPASFEHRLEMLKLaiednpkfevsdieikrdgpsyti 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113749  59 -SLKHL----PNVEF---VGFDgLLVNF-----FRE--QNAT-AVLRglRAVSDFEYEFQLanmnRQLDAKYEAVFLTPS 122
Cdd:cd02165   83 dTLEELreryPNAELyfiIGSD-NLIRLpkwydWEEllSLVHlVVAP--RPGYPIEDASLE----KLLLPGGRIILLDNP 155

                        170       180       190
                 ....*....|....*....|....*....|.
gi 491113749 123 EQYsfISSTLVREIARLKGDVTKFVAPVVVE 153
Cdd:cd02165  156 LLN--ISSTEIRERLKNGKSIRYLLPPAVAD 184
nadD PRK00071
nicotinate-nucleotide adenylyltransferase;
1-153 1.07e-07

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 234611 [Multi-domain]  Cd Length: 203  Bit Score: 49.06  E-value: 1.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113749   1 MSKTRV-IYPGTFDPITNGHIDLVTRAAKMF--DEVV------------------------VAIAIGHhkNPIFTLeERV 53
Cdd:PRK00071   1 EMMKRIgLFGGTFDPPHYGHLAIAEEAAERLglDEVWflpnpgpphkpqkplaplehrlamLELAIAD--NPRFSV-SDI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113749  54 ELAQAS-------LKHL----PNVEFV---GFDgLLVNFFREQNATAVLRGLR-AVSD---FEYEFQLANMNRQLDAKYE 115
Cdd:PRK00071  78 ELERPGpsytidtLRELraryPDVELVfiiGAD-ALAQLPRWKRWEEILDLVHfVVVPrpgYPLEALALPALQQLLEAAG 156

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 491113749 116 AVFLTPSEQySFISSTLVREIARLKGDVTKFVAPVVVE 153
Cdd:PRK00071 157 AITLLDVPL-LAISSTAIRERIKEGRPIRYLLPEAVLD 193
cytidylyltransferase cd02170
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ...
 4-58 1.26e-07

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: 48.06  E-value: 1.26e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113749   4 TRVIYPGTFDPITNGHIDLVTRAAKMFDEVVVAIA----IGHHKN-PIFTLEERVELAQA 58
Cdd:cd02170    2 KRVYAAGTFDIIHPGHIRFLEEAKKLGDYLIVGVArdetVAKIKRrPILPEEQRAEVVEA 61
NadD COG1057
Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; ...
 7-153 3.03e-07

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: 47.81  E-value: 3.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113749   7 IYPGTFDPITNGHIDLVTRAAKMF--DEV--VVAiAIGHHKN--PIFTLEERVELAQASLKHLPNVEFVGFDGLL----- 75
Cdd:COG1057    6 IFGGTFDPIHIGHLALAEEAAEQLglDEVifVPA-GQPPHKKhkPLASAEHRLAMLRLAIADNPRFEVSDIELERpgpsy 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113749  76 ----VNFFREQNATAVLR---GLRAVSDF----EYE--FQLAN---MNR---QLDAKYEAVFLTPSEQYSF-------IS 129
Cdd:COG1057   85 tidtLRELREEYPDAELYfiiGADALLQLpkwkRWEelLELAHlvvVPRpgyELDELEELEALKPGGRIILldvplldIS 164

                        170       180
                 ....*....|....*....|....
gi 491113749 130 STLVREIARLKGDVTKFVAPVVVE 153
Cdd:COG1057  165 STEIRERLAEGKSIRYLVPDAVED 188
PRK01153 PRK01153
nicotinamide-nucleotide adenylyltransferase; Provisional
 4-61 1.17e-06

nicotinamide-nucleotide adenylyltransferase; Provisional


Pssm-ID: 179235  Cd Length: 174  Bit Score: 46.02  E-value: 1.17e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491113749   4 TRVIYPGTFDPITNGHIDLVTRAAKMFDEVVVAIAIGHH----KNPiFTLEERVELAQASLK 61
Cdd:PRK01153   1 MRALFIGRFQPFHKGHLEVIKWILEEVDELIIGIGSAQEshtlKNP-FTAGERILMIRKALE 61
NMNAT_Archaea cd02166
Nicotinamide/nicotinate mononucleotide adenylyltransferase, archaeal; This family of archaeal ...
 5-61 2.55e-05

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: 42.28  E-value: 2.55e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491113749   5 RVIYPGTFDPITNGHIDLVTRAAKMFDEVVVAIAIGH--H--KNPiFTLEERVELAQASLK 61
Cdd:cd02166    1 RALFIGRFQPFHLGHLKVIKWILEEVDELIIGIGSAQesHtlENP-FTAGERVLMIRRALE 60
TIGR00482 TIGR00482
nicotinate (nicotinamide) nucleotide adenylyltransferase; This model represents the ...
 7-64 2.57e-04

nicotinate (nicotinamide) nucleotide adenylyltransferase; This model represents the predominant bacterial/eukaryotic adenylyltransferase for nicotinamide-nucleotide, its deamido form nicotinate nucleotide, or both. The first activity, nicotinamide-nucleotide adenylyltransferase (EC 2.7.7.1), synthesizes NAD by the salvage pathway, while the second, nicotinate-nucleotide adenylyltransferase (EC 2.7.7.18) synthesizes the immediate precursor of NAD by the de novo pathway. In E. coli, NadD activity is biased toward the de novo pathway while salvage activity is channeled through the multifunctional NadR protein, but this division of labor may be exceptional. The given name of this model, nicotinate (nicotinamide) nucleotide adenylyltransferase, reflects the lack of absolute specificity with respect to substrate amidation state in most species. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridine nucleotides]


Pssm-ID: 273101 [Multi-domain]  Cd Length: 193  Bit Score: 39.61  E-value: 2.57e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491113749    7 IYPGTFDPITNGHIDLVTRAAKMF--DEV-VVAIAIGHHKN--PIFTLEERVELAQASLKHLP 64
Cdd:TIGR00482   1 LFGGSFDPIHYGHLLLAEEALDHLdlDKViFVPTANPPHKKtyEAASSHHRLAMLKLAIEDNP 63
PRK08099 PRK08099
multifunctional transcriptional regulator/nicotinamide-nucleotide adenylyltransferase ...
 1-72 9.81e-04

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


Pssm-ID: 236151 [Multi-domain]  Cd Length: 399  Bit Score: 38.48  E-value: 9.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113749   1 MSKTRVIYpGTFDPITNGHIDLVTRAAKMFDEvvVAIAIGHHKNP---IF---------TLEERVELAQASLKHLPNVEF 68
Cdd:PRK08099  51 MKKIGVVF-GKFYPLHTGHIYLIQRACSQVDE--LHIIICYDDERdrkLFedsamsqqpTVSDRLRWLLQTFKYQKNIKI 127


                 ....
gi 491113749  69 VGFD 72
Cdd:PRK08099 128 HAFN 131
nadD PRK07152
nicotinate-nucleotide adenylyltransferase;
6-72 1.34e-03

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 235947 [Multi-domain]  Cd Length: 342  Bit Score: 38.00  E-value: 1.34e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491113749   6 VIYPGTFDPITNGHIDLVTRAAKM--FDEVvvaIAIGHHKNP------IFTLEERVELAQASLKHLPNVEFVGFD 72
Cdd:PRK07152   4 AIFGGSFDPIHKGHINIAKKAIKKlkLDKL---FFVPTYINPfkkkqkASNGEHRLNMLKLALKNLPKMEVSDFE 75
Citrate_lyase_ligase cd02169
Citrate lyase ligase; Citrate lyase ligase, also known as [Citrate (pro-3S)-lyase] ligase, is ...
 14-66 2.47e-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: 37.24  E-value: 2.47e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 491113749  14 PITNGHIDLVTRAAKMFDEV---VVAiaighHKNPIFTLEERVELAQASLKHLPNV 66
Cdd:cd02169  125 PFTLGHRYLVEKAAAENDWVhlfVVS-----EDKSLFSFADRFKLVKKGTKHLKNV 175
PRK00777 PRK00777
pantetheine-phosphate adenylyltransferase;
5-54 2.63e-03

pantetheine-phosphate adenylyltransferase;


Pssm-ID: 234834  Cd Length: 153  Bit Score: 36.35  E-value: 2.63e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 491113749   5 RVIYPGTFDPITNGHIDLVTRAAKMFDEVVVAI-----AIGHHKNPIFTLEERVE 54
Cdd:PRK00777   3 KVAVGGTFDPLHDGHRALLRKAFELGKRVTIGLtsdefAKSYKKHKVRPYEVRLK 57
CCT cd02174
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ...
 5-58 5.42e-03

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: 35.24  E-value: 5.42e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491113749   5 RVIYPGTFDPITNGHIDLVTRAAKMF--DEVVVAI----AIGHHKN-PIFTLEERVELAQA 58
Cdd:cd02174    4 RVYVDGCFDLFHYGHANALRQAKKLGpnDYLIVGVhsdeEIHKHKGpPVMTEEERYEAVRH 64
Citrate_ly_lig smart00764
Citrate lyase ligase C-terminal domain; Proteins of this family contain the C-terminal domain ...
 14-69 5.50e-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: 5.50e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 491113749    14 PITNGHIDLVTRAAKMFDEVVVAIAigHHKNPIFTLEERVELAQASLKHLPNVEFV 69
Cdd:smart00764  10 PFTLGHRYLVEQAAAECDWVHLFVV--SEDASLFSFDERFALVKKGTKDLDNVTVH 63
G3P_Cytidylyltransferase cd02171
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase, ...
 6-58 6.61e-03

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: 34.77  E-value: 6.61e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 491113749   6 VIYPGTFDPITNGHIDLVTRAAKMFDEVVVAIA-----IGHHKNPIFTLEERVELAQA 58
Cdd:cd02171    4 VITYGTFDLLHIGHLNLLERAKALGDKLIVAVStdefnAGKGKKAVIPYEQRAEILES 61
Dsd1 COG3616
D-serine deaminase, pyridoxal phosphate-dependent [Amino acid transport and metabolism];
19-71 8.15e-03

D-serine deaminase, pyridoxal phosphate-dependent [Amino acid transport and metabolism];


Pssm-ID: 442834 [Multi-domain]  Cd Length: 357  Bit Score: 35.49  E-value: 8.15e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 491113749  19 HIDLVTRAAKMFD---EVVVAIAIGHHKNPIFTLEERVELAQAsLKHLPNVEFVGF 71
Cdd:COG3616  113 QAEALAAAAAAAGrplRVLVELDVGGGRTGVRPPEAALALARA-IAASPGLRLAGL 167
NMNAT_Nudix cd02168
Nicotinamide/nicotinate mononucleotide adenylyltransferase of bifunctional proteins, also ...
 7-61 9.12e-03

Nicotinamide/nicotinate mononucleotide adenylyltransferase of bifunctional proteins, also containing a Nudix hydrolase domain; N-terminal NMNAT (Nicotinamide/nicotinate mononucleotide adenylyltransferase) domain of a novel bifunctional enzyme endowed with NMN adenylyltransferase and Nudix hydrolase activities. This domain is highly homologous to the archeal NMN adenyltransferase that catalyzes NAD synthesis from NMN and ATP. NMNAT is an essential 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. The C-terminal domain of this enzyme shares homology with the archaeal ADP-ribose pyrophosphatase, a member of the 'Nudix' hydrolase family.


Pssm-ID: 173919  Cd Length: 181  Bit Score: 35.05  E-value: 9.12e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491113749   7 IYPGTFDPITNGHIDLVTRAAKMFDEVVvaIAIGHH------KNPiFTLEERVELAQASLK 61
Cdd:cd02168    3 VYIGRFQPFHNGHLAVVLIALEKAKKVI--ILIGSArtarniKNP-WTSEEREVMIEAALS 60
 
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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