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Conserved domains on  [gi|502612495|ref|WP_012849468|]
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nicotinate-nucleotide adenylyltransferase [Edwardsiella piscicida]

Protein Classification

nicotinate-nucleotide adenylyltransferase( domain architecture ID 10011203)

nicotinate-nucleotide adenylyltransferase catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide

EC:  2.7.7.18
Gene Ontology:  GO:0004515|GO:0005524|GO:0009435
PubMed:  19273075
SCOP:  4003834

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
nadD PRK00071
nicotinate-nucleotide adenylyltransferase;
10-221 1.45e-90

nicotinate-nucleotide adenylyltransferase;


:

Pssm-ID: 234611 [Multi-domain]  Cd Length: 203  Bit Score: 264.77  E-value: 1.45e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612495  10 PSLLALFGGTFDPIHYGHLKPVTALAQEVGLGHITLLPNHVPPHRPQ-PEACAAQRLEMVRLAIADDPLFSVDDRELRRD 88
Cdd:PRK00071   3 MKRIGLFGGTFDPPHYGHLAIAEEAAERLGLDEVWFLPNPGPPHKPQkPLAPLEHRLAMLELAIADNPRFSVSDIELERP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612495  89 SPSYTIDTLEALRAeLGPQRPLAFIIGQDSLLTLHKWQRWQDILRCCHLLVCARPGYP-DRLDTPALQAWLEQhrtrdvq 167
Cdd:PRK00071  83 GPSYTIDTLRELRA-RYPDVELVFIIGADALAQLPRWKRWEEILDLVHFVVVPRPGYPlEALALPALQQLLEA------- 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 502612495 168 rlhrqpHGFIYLADTPLLSVSATDIRQRRHLGISCDDLLPRAVQRYIELQGLYR 221
Cdd:PRK00071 155 ------AGAITLLDVPLLAISSTAIRERIKEGRPIRYLLPEAVLDYIEKHGLYR 202
 
Name Accession Description Interval E-value
nadD PRK00071
nicotinate-nucleotide adenylyltransferase;
10-221 1.45e-90

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 234611 [Multi-domain]  Cd Length: 203  Bit Score: 264.77  E-value: 1.45e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612495  10 PSLLALFGGTFDPIHYGHLKPVTALAQEVGLGHITLLPNHVPPHRPQ-PEACAAQRLEMVRLAIADDPLFSVDDRELRRD 88
Cdd:PRK00071   3 MKRIGLFGGTFDPPHYGHLAIAEEAAERLGLDEVWFLPNPGPPHKPQkPLAPLEHRLAMLELAIADNPRFSVSDIELERP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612495  89 SPSYTIDTLEALRAeLGPQRPLAFIIGQDSLLTLHKWQRWQDILRCCHLLVCARPGYP-DRLDTPALQAWLEQhrtrdvq 167
Cdd:PRK00071  83 GPSYTIDTLRELRA-RYPDVELVFIIGADALAQLPRWKRWEEILDLVHFVVVPRPGYPlEALALPALQQLLEA------- 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 502612495 168 rlhrqpHGFIYLADTPLLSVSATDIRQRRHLGISCDDLLPRAVQRYIELQGLYR 221
Cdd:PRK00071 155 ------AGAITLLDVPLLAISSTAIRERIKEGRPIRYLLPEAVLDYIEKHGLYR 202
NadD COG1057
Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; ...
 13-221 9.48e-90

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: 262.36  E-value: 9.48e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612495  13 LALFGGTFDPIHYGHLKPVTALAQEVGLGHITLLPNHVPPHRPQ-PEACAAQRLEMVRLAIADDPLFSVDDRELRRDSPS 91
Cdd:COG1057    4 IGIFGGTFDPIHIGHLALAEEAAEQLGLDEVIFVPAGQPPHKKHkPLASAEHRLAMLRLAIADNPRFEVSDIELERPGPS 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612495  92 YTIDTLEALRAELgPQRPLAFIIGQDSLLTLHKWQRWQDILRCCHLLVCARPGYPdrldtpalqawleQHRTRDVQRLhr 171
Cdd:COG1057   84 YTIDTLRELREEY-PDAELYFIIGADALLQLPKWKRWEELLELAHLVVVPRPGYE-------------LDELEELEAL-- 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 502612495 172 QPHGFIYLADTPLLSVSATDIRQRRHLGISCDDLLPRAVQRYIELQGLYR 221
Cdd:COG1057  148 KPGGRIILLDVPLLDISSTEIRERLAEGKSIRYLVPDAVEDYIREHGLYR 197
NMNAT cd02165
Nicotinamide/nicotinate mononucleotide adenylyltransferase; Nicotinamide/nicotinate ...
 13-220 9.66e-77

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: 229.05  E-value: 9.66e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612495  13 LALFGGTFDPIHYGHLKPVTALAQEVGLGHITLLPNHVPPHRPQPEACAAQRLEMVRLAIADDPLFSVDDRELRRDSPSY 92
Cdd:cd02165    1 IALFGGSFDPPHLGHLAIAEEALEELGLDRVLLLPSANPPHKPPKPASFEHRLEMLKLAIEDNPKFEVSDIEIKRDGPSY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612495  93 TIDTLEALRaELGPQRPLAFIIGQDSLLTLHKWQRWQDILRCCHLLVCARPGYPDRLDTPALQAWleqhrtrdvqrlhrq 172
Cdd:cd02165   81 TIDTLEELR-ERYPNAELYFIIGSDNLIRLPKWYDWEELLSLVHLVVAPRPGYPIEDASLEKLLL--------------- 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 502612495 173 PHGFIYLADTPLLSVSATDIRQRRHLGISCDDLLPRAVQRYIELQGLY 220
Cdd:cd02165  145 PGGRIILLDNPLLNISSTEIRERLKNGKSIRYLLPPAVADYIKEHGLY 192
TIGR00482 TIGR00482
nicotinate (nicotinamide) nucleotide adenylyltransferase; This model represents the ...
 15-220 1.75e-67

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: 205.63  E-value: 1.75e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612495   15 LFGGTFDPIHYGHLKPVTALAQEVGLGHITLLPNHVPPHRP-QPEACAAQRLEMVRLAIADDPLFSVDDRELRRDSPSYT 93
Cdd:TIGR00482   1 LFGGSFDPIHYGHLLLAEEALDHLDLDKVIFVPTANPPHKKtYEAASSHHRLAMLKLAIEDNPKFEVDDFEIKRGGPSYT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612495   94 IDTLEALRAELgPQRPLAFIIGQDSLLTLHKWQRWQDILRCCHLLVCARPGYPDRLDTPALQAWleqhrtrdvqrlhRQP 173
Cdd:TIGR00482  81 IDTLKHLKKKY-PDVELYFIIGADALRSFPLWKDWQELLELVHLVIVPRPGYTLDKALLEKAIL-------------RMH 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 502612495  174 HGFIYLADTPLLSVSATDIRQRRHLGISCDDLLPRAVQRYIELQGLY 220
Cdd:TIGR00482 147 HGNLTLLHNPRVPISSTEIRQRIRQGKSIEYLLPDPVIKYIKQHGLY 193
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 15-195 6.70e-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: 95.08  E-value: 6.70e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612495   15 LFGGTFDPIHYGHLKPVTALAQEVGLGHITLLPNHVPPHR-PQPEACAAQRLEMVRLAIADDPLFSVDDRELRRDspsyt 93
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEDLIVGVPSDEPPHKlKRPLFSAEERLEMLELAKWVDEVIVVAPWELTRE----- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612495   94 idtleaLRAELGPQrplAFIIGQDSLLTLhkWQRWQDILRCCHLLVCARPGYpdrldtpalqawleqhrtrdvqrlhrqp 173
Cdd:pfam01467  76 ------LLKELNPD---VLVIGADSLLDF--WYELDEILGNVKLVVVVRPVF---------------------------- 116

                         170       180
                  ....*....|....*....|..
gi 502612495  174 hgFIYLADTPLlsVSATDIRQR 195
Cdd:pfam01467 117 --FIPLKPTNG--ISSTDIRER 134
 
Name Accession Description Interval E-value
nadD PRK00071
nicotinate-nucleotide adenylyltransferase;
10-221 1.45e-90

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 234611 [Multi-domain]  Cd Length: 203  Bit Score: 264.77  E-value: 1.45e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612495  10 PSLLALFGGTFDPIHYGHLKPVTALAQEVGLGHITLLPNHVPPHRPQ-PEACAAQRLEMVRLAIADDPLFSVDDRELRRD 88
Cdd:PRK00071   3 MKRIGLFGGTFDPPHYGHLAIAEEAAERLGLDEVWFLPNPGPPHKPQkPLAPLEHRLAMLELAIADNPRFSVSDIELERP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612495  89 SPSYTIDTLEALRAeLGPQRPLAFIIGQDSLLTLHKWQRWQDILRCCHLLVCARPGYP-DRLDTPALQAWLEQhrtrdvq 167
Cdd:PRK00071  83 GPSYTIDTLRELRA-RYPDVELVFIIGADALAQLPRWKRWEEILDLVHFVVVPRPGYPlEALALPALQQLLEA------- 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 502612495 168 rlhrqpHGFIYLADTPLLSVSATDIRQRRHLGISCDDLLPRAVQRYIELQGLYR 221
Cdd:PRK00071 155 ------AGAITLLDVPLLAISSTAIRERIKEGRPIRYLLPEAVLDYIEKHGLYR 202
NadD COG1057
Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; ...
 13-221 9.48e-90

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: 262.36  E-value: 9.48e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612495  13 LALFGGTFDPIHYGHLKPVTALAQEVGLGHITLLPNHVPPHRPQ-PEACAAQRLEMVRLAIADDPLFSVDDRELRRDSPS 91
Cdd:COG1057    4 IGIFGGTFDPIHIGHLALAEEAAEQLGLDEVIFVPAGQPPHKKHkPLASAEHRLAMLRLAIADNPRFEVSDIELERPGPS 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612495  92 YTIDTLEALRAELgPQRPLAFIIGQDSLLTLHKWQRWQDILRCCHLLVCARPGYPdrldtpalqawleQHRTRDVQRLhr 171
Cdd:COG1057   84 YTIDTLRELREEY-PDAELYFIIGADALLQLPKWKRWEELLELAHLVVVPRPGYE-------------LDELEELEAL-- 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 502612495 172 QPHGFIYLADTPLLSVSATDIRQRRHLGISCDDLLPRAVQRYIELQGLYR 221
Cdd:COG1057  148 KPGGRIILLDVPLLDISSTEIRERLAEGKSIRYLVPDAVEDYIREHGLYR 197
NMNAT cd02165
Nicotinamide/nicotinate mononucleotide adenylyltransferase; Nicotinamide/nicotinate ...
 13-220 9.66e-77

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: 229.05  E-value: 9.66e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612495  13 LALFGGTFDPIHYGHLKPVTALAQEVGLGHITLLPNHVPPHRPQPEACAAQRLEMVRLAIADDPLFSVDDRELRRDSPSY 92
Cdd:cd02165    1 IALFGGSFDPPHLGHLAIAEEALEELGLDRVLLLPSANPPHKPPKPASFEHRLEMLKLAIEDNPKFEVSDIEIKRDGPSY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612495  93 TIDTLEALRaELGPQRPLAFIIGQDSLLTLHKWQRWQDILRCCHLLVCARPGYPDRLDTPALQAWleqhrtrdvqrlhrq 172
Cdd:cd02165   81 TIDTLEELR-ERYPNAELYFIIGSDNLIRLPKWYDWEELLSLVHLVVAPRPGYPIEDASLEKLLL--------------- 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 502612495 173 PHGFIYLADTPLLSVSATDIRQRRHLGISCDDLLPRAVQRYIELQGLY 220
Cdd:cd02165  145 PGGRIILLDNPLLNISSTEIRERLKNGKSIRYLLPPAVADYIKEHGLY 192
TIGR00482 TIGR00482
nicotinate (nicotinamide) nucleotide adenylyltransferase; This model represents the ...
 15-220 1.75e-67

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: 205.63  E-value: 1.75e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612495   15 LFGGTFDPIHYGHLKPVTALAQEVGLGHITLLPNHVPPHRP-QPEACAAQRLEMVRLAIADDPLFSVDDRELRRDSPSYT 93
Cdd:TIGR00482   1 LFGGSFDPIHYGHLLLAEEALDHLDLDKVIFVPTANPPHKKtYEAASSHHRLAMLKLAIEDNPKFEVDDFEIKRGGPSYT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612495   94 IDTLEALRAELgPQRPLAFIIGQDSLLTLHKWQRWQDILRCCHLLVCARPGYPDRLDTPALQAWleqhrtrdvqrlhRQP 173
Cdd:TIGR00482  81 IDTLKHLKKKY-PDVELYFIIGADALRSFPLWKDWQELLELVHLVIVPRPGYTLDKALLEKAIL-------------RMH 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 502612495  174 HGFIYLADTPLLSVSATDIRQRRHLGISCDDLLPRAVQRYIELQGLY 220
Cdd:TIGR00482 147 HGNLTLLHNPRVPISSTEIRQRIRQGKSIEYLLPDPVIKYIKQHGLY 193
PRK06973 PRK06973
nicotinate-nucleotide adenylyltransferase;
2-221 1.81e-34

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 180781 [Multi-domain]  Cd Length: 243  Bit Score: 122.97  E-value: 1.81e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612495   2 PSESQPAAPSLLALFGGTFDPIHYGHLKPVTALAQEVGLGHITLLPNHVPPHRPQPEAcAAQRLEMVRLAIA--DDP--L 77
Cdd:PRK06973  13 EPAPPLARPRRIGILGGTFDPIHDGHLALARRFADVLDLTELVLIPAGQPWQKADVSA-AEHRLAMTRAAAAslVLPgvT 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612495  78 FSVDDRELRRDSPSYTIDTLEALRAELGPQRPLAFIIGQDSLLTLHKWQRWQDILRCCHLLVCARPGYPDRLDTPALQAW 157
Cdd:PRK06973  92 VRVATDEIEHAGPTYTVDTLARWRERIGPDASLALLIGADQLVRLDTWRDWRRLFDYAHLCAATRPGFDLGAASPAVAAE 171

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502612495 158 LEQhRTRDVQRLHRQPHGFIYLADTPLLSVSATDIRQRRHLGIS--------CDDLLPRAVQRYIELQGLYR 221
Cdd:PRK06973 172 IAA-RQADADVLQATPAGHLLIDTTLAFDLSATDIRAHLRACIArraqvpdaSAEHVPAAVWAYILQHRLYH 242
nadD PRK07152
nicotinate-nucleotide adenylyltransferase;
13-220 2.27e-29

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 235947 [Multi-domain]  Cd Length: 342  Bit Score: 111.96  E-value: 2.27e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612495  13 LALFGGTFDPIHYGHLKPVTALAQEVGLGHITLLPNHVPPHRPQPEACAAQ-RLEMVRLAIADDPLFSVDDRELRRDSPS 91
Cdd:PRK07152   3 IAIFGGSFDPIHKGHINIAKKAIKKLKLDKLFFVPTYINPFKKKQKASNGEhRLNMLKLALKNLPKMEVSDFEIKRQNVS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612495  92 YTIDTLEALRaELGPQRPLAFIIGQDSLLTLHKWQRWQDILRCCHLLVCARPGYPDRLDTPAlqawleqhrtrdvqrlhr 171
Cdd:PRK07152  83 YTIDTIKYFK-KKYPNDEIYFIIGSDNLEKFKKWKNIEEILKKVQIVVFKRKKNINKKNLKK------------------ 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 502612495 172 qpHGFIYLaDTPLLSVSATDIRQRRHLGiscddLLPRAVQRYIELQGLY 220
Cdd:PRK07152 144 --YNVLLL-KNKNLNISSTKIRKGNLLG-----KLDPKVNDYINENFLY 184
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 15-195 6.70e-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: 95.08  E-value: 6.70e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612495   15 LFGGTFDPIHYGHLKPVTALAQEVGLGHITLLPNHVPPHR-PQPEACAAQRLEMVRLAIADDPLFSVDDRELRRDspsyt 93
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEDLIVGVPSDEPPHKlKRPLFSAEERLEMLELAKWVDEVIVVAPWELTRE----- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612495   94 idtleaLRAELGPQrplAFIIGQDSLLTLhkWQRWQDILRCCHLLVCARPGYpdrldtpalqawleqhrtrdvqrlhrqp 173
Cdd:pfam01467  76 ------LLKELNPD---VLVIGADSLLDF--WYELDEILGNVKLVVVVRPVF---------------------------- 116

                         170       180
                  ....*....|....*....|..
gi 502612495  174 hgFIYLADTPLlsVSATDIRQR 195
Cdd:pfam01467 117 --FIPLKPTNG--ISSTDIRER 134
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 14-76 1.41e-09

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: 52.69  E-value: 1.41e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502612495   14 ALFGGTFDPIHYGHLKPVTALAQEVGLGHITLLP-NHVPPHRPQPEACAAQRLEMVRLAIADDP 76
Cdd:TIGR00125   2 VIFVGTFDPFHLGHLDLLERAKELFDELIVGVGSdQFVNPLKGEPVFSLEERLEMLKALKYVDE 65
cytidylyltransferase_like cd02039
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ...
 14-125 3.33e-04

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: 39.73  E-value: 3.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612495  14 ALFGGTFDPIHYGHLKpVTALAQEVGLGHITLLPNHVPPHRPQPE--ACAAQRLEMVRLAIADdpLFSVDDRELRRDSPS 91
Cdd:cd02039    2 GIIIGRFEPFHLGHLK-LIKEALEEALDEVIIIIVSNPPKKKRNKdpFSLHERVEMLKEILKD--RLKVVPVDFPEVKIL 78

                         90       100       110
                 ....*....|....*....|....*....|....
gi 502612495  92 YTIDTLEALRAELGpqrPLAFIIGQDSLLTLHKW 125
Cdd:cd02039   79 LAVVFILKILLKVG---PDKVVVGEDFAFGKNAS 109
PRK08887 PRK08887
nicotinate-nicotinamide nucleotide adenylyltransferase;
13-140 5.86e-04

nicotinate-nicotinamide nucleotide adenylyltransferase;


Pssm-ID: 181576 [Multi-domain]  Cd Length: 174  Bit Score: 39.32  E-value: 5.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612495  13 LALFGGTFDPIHYGHLKPVTALAQ------EVGLGHI---TLLPNHVpphrpqpeacaaqRLEMVRLAIADDPLFSVDDR 83
Cdd:PRK08887   4 IAVFGSAFNPPSLGHKSVIESLSHfdlvllVPSIAHAwgkTMLDYET-------------RCQLVDAFIQDLGLSNVQRS 70

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502612495  84 ELRR-----DSPSYTIDTLEALRaELGPQRPLAFIIGQDSLLTLHKWQRWQDILRCCHLLVC 140
Cdd:PRK08887  71 DIEQelyapDESVTTYALLTRLQ-ELYPEADLTFVIGPDNFLKFAKFYKADEITQRWTVMAC 131
coaD_prev_kdtB TIGR01510
pantetheine-phosphate adenylyltransferase, bacterial; This model describes ...
 14-76 6.48e-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: 38.79  E-value: 6.48e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502612495   14 ALFGGTFDPIHYGHL---KPVTALAQEVglgHITLLPNhvPPHRPQPEACaaQRLEMVRLAIADDP 76
Cdd:TIGR01510   2 ALYPGSFDPVTNGHLdiiKRAAALFDEV---IVAVAKN--PSKKPLFSLE--ERVELIKDATKHLP 60
NadR COG1056
Nicotinamide mononucleotide adenylyltransferase [Coenzyme transport and metabolism]; ...
 14-215 5.92e-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: 36.33  E-value: 5.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612495  14 ALFGGTFDPIHYGHLKPVTALAQE-----VGLGHitllPNhvPPHRPQPEACAAQRLEMVRlaiaddplfsvddrelrrd 88
Cdd:COG1056    5 GLFIGRFQPFHLGHLAVIKWALEEvdeliIGIGS----AQ--ESHTPRNPFTAGERIEMIR------------------- 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612495  89 spsytidtlEALRaELGPQRplAFIIgqdSLLTLHKWQRW-QDILRCCHllvcarpgYPDRLDTpalqawleqhRTRDVQ 167
Cdd:COG1056   60 ---------AALK-EEGLSR--VYIV---PIPDINNNSLWvSHVKSLVP--------PFDVVYS----------NNPLVG 106

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 502612495 168 RLHRQPHgfIYLADTPLLS---VSATDIRQRRHLGISCDDLLPRAVQRYIE 215
Cdd:COG1056  107 RLFKEAG--YEVLLPPLFEreeYSGTEIRRLMLEGEDWESLVPPAVAEVIE 155
CoaD COG0669
Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine ...
 14-28 6.52e-03

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: 36.13  E-value: 6.52e-03
                         10
                 ....*....|....*
gi 502612495  14 ALFGGTFDPIHYGHL 28
Cdd:COG0669    4 AVYPGSFDPITNGHL 18
 
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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