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Conserved domains on  [gi|518506211|ref|WP_019676418|]
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cytidylyltransferase domain-containing protein [Arsukibacterium perlucidum]

Protein Classification

similar to acylneuraminate cytidylyltransferase( domain architecture ID 10787207)

protein similar to acylneuraminate cytidylyltransferase

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
NeuA COG1083
CMP-N-acetylneuraminic acid synthetase, NeuA/PseF family [Cell wall/membrane/envelope ...
 1-229 1.28e-87

CMP-N-acetylneuraminic acid synthetase, NeuA/PseF family [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 440700  Cd Length: 228  Bit Score: 258.55  E-value: 1.28e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518506211   1 MSCIAFIFARSGSKGLPGKNIKPLHGKPLLHYAIEVAKQLPQINHIFVSTDCDNIASCAKAAGAGVIIRPTELATDTAPE 80
Cdd:COG1083    1 MKILAIIPARGGSKGIPGKNIRPLAGKPLIAYSIEAALKSGLFDRVVVSTDDEEIAEVAREYGAEVFLRPAELAGDTAST 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518506211  81 WAAWQHAIRYVQQHIGNFTTFVSLPATSPLRSAIDVSNAITQLEHARADLCLAVTPANRNPYFNMVVrDDSNNVQLVSTL 160
Cdd:COG1083   81 IDVILHALEWLEEQGEEFDYVVLLQPTSPLRTAEDIDEAIELLLESGADSVVSVTEAHHPPYWALKL-DEDGRLEPLNPD 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518506211 161 PAGIHRRQDAPAVFDITTVVYAARPEFILQQQKLFDGVITSIEVPKKRAVDIDDIYDFMLAEAILKAEH 229
Cdd:COG1083  160 PHNRPRRQDLPPAYRENGAIYIFKREALLENKSRFGGKTGAYEMPEERSVDIDTEEDFELAEALLKKRK 228
 
Name Accession Description Interval E-value
NeuA COG1083
CMP-N-acetylneuraminic acid synthetase, NeuA/PseF family [Cell wall/membrane/envelope ...
 1-229 1.28e-87

CMP-N-acetylneuraminic acid synthetase, NeuA/PseF family [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440700  Cd Length: 228  Bit Score: 258.55  E-value: 1.28e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518506211   1 MSCIAFIFARSGSKGLPGKNIKPLHGKPLLHYAIEVAKQLPQINHIFVSTDCDNIASCAKAAGAGVIIRPTELATDTAPE 80
Cdd:COG1083    1 MKILAIIPARGGSKGIPGKNIRPLAGKPLIAYSIEAALKSGLFDRVVVSTDDEEIAEVAREYGAEVFLRPAELAGDTAST 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518506211  81 WAAWQHAIRYVQQHIGNFTTFVSLPATSPLRSAIDVSNAITQLEHARADLCLAVTPANRNPYFNMVVrDDSNNVQLVSTL 160
Cdd:COG1083   81 IDVILHALEWLEEQGEEFDYVVLLQPTSPLRTAEDIDEAIELLLESGADSVVSVTEAHHPPYWALKL-DEDGRLEPLNPD 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518506211 161 PAGIHRRQDAPAVFDITTVVYAARPEFILQQQKLFDGVITSIEVPKKRAVDIDDIYDFMLAEAILKAEH 229
Cdd:COG1083  160 PHNRPRRQDLPPAYRENGAIYIFKREALLENKSRFGGKTGAYEMPEERSVDIDTEEDFELAEALLKKRK 228
CMP-NeuAc_Synthase cd02513
CMP-NeuAc_Synthase activates N-acetylneuraminic acid by adding CMP moiety; ...
 4-225 1.53e-84

CMP-NeuAc_Synthase activates N-acetylneuraminic acid by adding CMP moiety; CMP-N-acetylneuraminic acid synthetase (CMP-NeuAc synthetase) or acylneuraminate cytidylyltransferase catalyzes the transfer the CMP moiety of CTP to the anomeric hydroxyl group of NeuAc in the presence of Mg++. It is the second to last step in the sialylation of the oligosaccharide component of glycoconjugates by providing the activated sugar-nucleotide cytidine 5'-monophosphate N-acetylneuraminic acid (CMP-Neu5Ac), the substrate for sialyltransferases. Eukaryotic CMP-NeuAc synthetases are predominantly located in the nucleus. The activated CMP-Neu5Ac diffuses from the nucleus into the cytoplasm.


Pssm-ID: 133006  Cd Length: 223  Bit Score: 250.53  E-value: 1.53e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518506211   4 IAFIFARSGSKGLPGKNIKPLHGKPLLHYAIEVAKQLPQINHIFVSTDCDNIASCAKAAGAGVII-RPTELATDTAPEWA 82
Cdd:cd02513    3 LAIIPARGGSKGIPGKNIRPLGGKPLIAWTIEAALESKLFDRVVVSTDDEEIAEVARKYGAEVPFlRPAELATDTASSID 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518506211  83 AWQHAIRYVQQHIGNFTTFVSLPATSPLRSAIDVSNAITQLEHARADLCLAVTPANRNPYFNMVVRDdsNNVQLVSTLPA 162
Cdd:cd02513   83 VILHALDQLEELGRDFDIVVLLQPTSPLRSAEDIDEAIELLLSEGADSVFSVTEFHRFPWRALGLDD--NGLEPVNYPED 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518506211 163 GIHRRQDAPAVFDITTVVYAARPEFILQQQKLFDGVITSIEVPKKRAVDIDDIYDFMLAEAIL 225
Cdd:cd02513  161 KRTRRQDLPPAYHENGAIYIAKREALLESNSFFGGKTGPYEMPRERSIDIDTEEDFELAEALL 223
PseF TIGR03584
pseudaminic acid cytidylyltransferase; The sequences in this family include the pfam02348 ...
 4-222 3.11e-31

pseudaminic acid cytidylyltransferase; The sequences in this family include the pfam02348 (cytidyltransferase) domain and are homologous to the NeuA protein responsible for the transfer of CMP to neuraminic acid. According to, this gene is responsible for the transfer of CMP to the structurally related sugar, pseudaminic acid which is observed as a component of sugar modifications of flagellin in Campylobacter species. This gene is commonly observed in apparent operons with other genes responsible for the biosynthesis of pseudaminic acid and as a component of flagellar and exopolysaccharide biosynthesis loci.


Pssm-ID: 274660  Cd Length: 222  Bit Score: 114.35  E-value: 3.11e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518506211    4 IAFIFARSGSKGLPGKNIKPLHGKPLLHYAIEVAKQLPQINHIFVSTDCDNIASCAKAAGAGV-IIRPTELATDTAPEWA 82
Cdd:TIGR03584   1 IAIIPARGGSKRIPRKNIKPFCGKPMIAYSIEAALNSGLFDKVVVSTDDEEIAEVAKSYGASVpFLRPKELADDFTGTAP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518506211   83 AWQHAIRYVQQHIGnFTTFVSLPATSPLRSAIDVSNAITQLEHARADLCLAVTPANRNPYFNMVVrddSNNVQLVSTLPA 162
Cdd:TIGR03584  81 VVKHAIEELKLQKQ-YDHACCIYATAPFLQAKILKEAFELLKQPNAHFVFSVTSFAFPIQRAFKL---KENGGVEMFQPE 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518506211  163 GIHRR-QDAPAVFDITTVVYAARPEFILQQQKLFDGVITSIEVPKKRAVDIDDIYDFMLAE 222
Cdd:TIGR03584 157 HFNTRsQDLEEAYHDAGQFYWGKSQAWLESGPIFSPHSIPIVLPRHLVQDIDTLEDWERAE 217
CTP_transf_3 pfam02348
Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) ...
 4-78 2.90e-20

Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) 3-deoxy-manno-octulosonate cytidylyltransferase,, EC:2.7.7.38 catalysing the reaction:- CTP + 3-deoxy-D-manno-octulosonate <=> diphosphate + CMP-3-deoxy-D-manno-octulosonate, 2) acylneuraminate cytidylyltransferase EC:2.7.7.43,, catalysing the reaction:- CTP + N-acylneuraminate <=> diphosphate + CMP-N-acylneuraminate. NeuAc cytydilyltransferase of Mannheimia haemolytica has been characterized describing kinetics and regulation by substrate charge, energetic charge and amino-sugar demand.


Pssm-ID: 396773  Cd Length: 217  Bit Score: 85.47  E-value: 2.90e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518506211    4 IAFIFARSGSKGLPGKNIKPLHGKPLLHYAIEVAKQLPQINHIFVSTDCDNIASCAKAAGAGVIIRPTELATDTA 78
Cdd:pfam02348   1 AAIIPARLGSKRLPGKNLLDLGGKPLIHHVLEAALKSGAFEKVIVATDSEEIADVAKEFGAGVVMTSGSLSSGTD 75
PRK13368 PRK13368
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
 1-67 7.96e-11

3-deoxy-manno-octulosonate cytidylyltransferase; Provisional


Pssm-ID: 184007  Cd Length: 238  Bit Score: 59.98  E-value: 7.96e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518506211   1 MSCIAFIFARSGSKGLPGKNIKPLHGKPLLHYAIEVAKQLPQINHIFVSTDCDNIASCAKAAGAGVI 67
Cdd:PRK13368   1 MKVVVVIPARYGSSRLPGKPLLDILGKPMIQHVYERAAQAAGVEEVYVATDDQRIEDAVEAFGGKVV 67
 
Name Accession Description Interval E-value
NeuA COG1083
CMP-N-acetylneuraminic acid synthetase, NeuA/PseF family [Cell wall/membrane/envelope ...
 1-229 1.28e-87

CMP-N-acetylneuraminic acid synthetase, NeuA/PseF family [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440700  Cd Length: 228  Bit Score: 258.55  E-value: 1.28e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518506211   1 MSCIAFIFARSGSKGLPGKNIKPLHGKPLLHYAIEVAKQLPQINHIFVSTDCDNIASCAKAAGAGVIIRPTELATDTAPE 80
Cdd:COG1083    1 MKILAIIPARGGSKGIPGKNIRPLAGKPLIAYSIEAALKSGLFDRVVVSTDDEEIAEVAREYGAEVFLRPAELAGDTAST 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518506211  81 WAAWQHAIRYVQQHIGNFTTFVSLPATSPLRSAIDVSNAITQLEHARADLCLAVTPANRNPYFNMVVrDDSNNVQLVSTL 160
Cdd:COG1083   81 IDVILHALEWLEEQGEEFDYVVLLQPTSPLRTAEDIDEAIELLLESGADSVVSVTEAHHPPYWALKL-DEDGRLEPLNPD 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518506211 161 PAGIHRRQDAPAVFDITTVVYAARPEFILQQQKLFDGVITSIEVPKKRAVDIDDIYDFMLAEAILKAEH 229
Cdd:COG1083  160 PHNRPRRQDLPPAYRENGAIYIFKREALLENKSRFGGKTGAYEMPEERSVDIDTEEDFELAEALLKKRK 228
CMP-NeuAc_Synthase cd02513
CMP-NeuAc_Synthase activates N-acetylneuraminic acid by adding CMP moiety; ...
 4-225 1.53e-84

CMP-NeuAc_Synthase activates N-acetylneuraminic acid by adding CMP moiety; CMP-N-acetylneuraminic acid synthetase (CMP-NeuAc synthetase) or acylneuraminate cytidylyltransferase catalyzes the transfer the CMP moiety of CTP to the anomeric hydroxyl group of NeuAc in the presence of Mg++. It is the second to last step in the sialylation of the oligosaccharide component of glycoconjugates by providing the activated sugar-nucleotide cytidine 5'-monophosphate N-acetylneuraminic acid (CMP-Neu5Ac), the substrate for sialyltransferases. Eukaryotic CMP-NeuAc synthetases are predominantly located in the nucleus. The activated CMP-Neu5Ac diffuses from the nucleus into the cytoplasm.


Pssm-ID: 133006  Cd Length: 223  Bit Score: 250.53  E-value: 1.53e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518506211   4 IAFIFARSGSKGLPGKNIKPLHGKPLLHYAIEVAKQLPQINHIFVSTDCDNIASCAKAAGAGVII-RPTELATDTAPEWA 82
Cdd:cd02513    3 LAIIPARGGSKGIPGKNIRPLGGKPLIAWTIEAALESKLFDRVVVSTDDEEIAEVARKYGAEVPFlRPAELATDTASSID 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518506211  83 AWQHAIRYVQQHIGNFTTFVSLPATSPLRSAIDVSNAITQLEHARADLCLAVTPANRNPYFNMVVRDdsNNVQLVSTLPA 162
Cdd:cd02513   83 VILHALDQLEELGRDFDIVVLLQPTSPLRSAEDIDEAIELLLSEGADSVFSVTEFHRFPWRALGLDD--NGLEPVNYPED 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518506211 163 GIHRRQDAPAVFDITTVVYAARPEFILQQQKLFDGVITSIEVPKKRAVDIDDIYDFMLAEAIL 225
Cdd:cd02513  161 KRTRRQDLPPAYHENGAIYIAKREALLESNSFFGGKTGPYEMPRERSIDIDTEEDFELAEALL 223
PseF TIGR03584
pseudaminic acid cytidylyltransferase; The sequences in this family include the pfam02348 ...
 4-222 3.11e-31

pseudaminic acid cytidylyltransferase; The sequences in this family include the pfam02348 (cytidyltransferase) domain and are homologous to the NeuA protein responsible for the transfer of CMP to neuraminic acid. According to, this gene is responsible for the transfer of CMP to the structurally related sugar, pseudaminic acid which is observed as a component of sugar modifications of flagellin in Campylobacter species. This gene is commonly observed in apparent operons with other genes responsible for the biosynthesis of pseudaminic acid and as a component of flagellar and exopolysaccharide biosynthesis loci.


Pssm-ID: 274660  Cd Length: 222  Bit Score: 114.35  E-value: 3.11e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518506211    4 IAFIFARSGSKGLPGKNIKPLHGKPLLHYAIEVAKQLPQINHIFVSTDCDNIASCAKAAGAGV-IIRPTELATDTAPEWA 82
Cdd:TIGR03584   1 IAIIPARGGSKRIPRKNIKPFCGKPMIAYSIEAALNSGLFDKVVVSTDDEEIAEVAKSYGASVpFLRPKELADDFTGTAP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518506211   83 AWQHAIRYVQQHIGnFTTFVSLPATSPLRSAIDVSNAITQLEHARADLCLAVTPANRNPYFNMVVrddSNNVQLVSTLPA 162
Cdd:TIGR03584  81 VVKHAIEELKLQKQ-YDHACCIYATAPFLQAKILKEAFELLKQPNAHFVFSVTSFAFPIQRAFKL---KENGGVEMFQPE 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518506211  163 GIHRR-QDAPAVFDITTVVYAARPEFILQQQKLFDGVITSIEVPKKRAVDIDDIYDFMLAE 222
Cdd:TIGR03584 157 HFNTRsQDLEEAYHDAGQFYWGKSQAWLESGPIFSPHSIPIVLPRHLVQDIDTLEDWERAE 217
CTP_transf_3 pfam02348
Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) ...
 4-78 2.90e-20

Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) 3-deoxy-manno-octulosonate cytidylyltransferase,, EC:2.7.7.38 catalysing the reaction:- CTP + 3-deoxy-D-manno-octulosonate <=> diphosphate + CMP-3-deoxy-D-manno-octulosonate, 2) acylneuraminate cytidylyltransferase EC:2.7.7.43,, catalysing the reaction:- CTP + N-acylneuraminate <=> diphosphate + CMP-N-acylneuraminate. NeuAc cytydilyltransferase of Mannheimia haemolytica has been characterized describing kinetics and regulation by substrate charge, energetic charge and amino-sugar demand.


Pssm-ID: 396773  Cd Length: 217  Bit Score: 85.47  E-value: 2.90e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518506211    4 IAFIFARSGSKGLPGKNIKPLHGKPLLHYAIEVAKQLPQINHIFVSTDCDNIASCAKAAGAGVIIRPTELATDTA 78
Cdd:pfam02348   1 AAIIPARLGSKRLPGKNLLDLGGKPLIHHVLEAALKSGAFEKVIVATDSEEIADVAKEFGAGVVMTSGSLSSGTD 75
PRK13368 PRK13368
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
 1-67 7.96e-11

3-deoxy-manno-octulosonate cytidylyltransferase; Provisional


Pssm-ID: 184007  Cd Length: 238  Bit Score: 59.98  E-value: 7.96e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518506211   1 MSCIAFIFARSGSKGLPGKNIKPLHGKPLLHYAIEVAKQLPQINHIFVSTDCDNIASCAKAAGAGVI 67
Cdd:PRK13368   1 MKVVVVIPARYGSSRLPGKPLLDILGKPMIQHVYERAAQAAGVEEVYVATDDQRIEDAVEAFGGKVV 67
SpsF COG1861
Spore coat polysaccharide biosynthesis protein SpsF, cytidylyltransferase family [Cell wall ...
 1-66 6.81e-09

Spore coat polysaccharide biosynthesis protein SpsF, cytidylyltransferase family [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441466  Cd Length: 245  Bit Score: 54.44  E-value: 6.81e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518506211   1 MSCIAFIFARSGSKGLPGKNIKPLHGKPLLHYAIEVAKQLPQINHIFV--STDCDN--IASCAKAAGAGV 66
Cdd:COG1861    2 MKIVAIIQARMGSTRLPGKVLKPLGGKPVLEHVIERLKRSKLIDEVVVatTTDPADdpLVDLAKELGVPV 71
CMP-KDO-Synthetase cd02517
CMP-KDO synthetase catalyzes the activation of KDO which is an essential component of the ...
 2-67 5.25e-08

CMP-KDO synthetase catalyzes the activation of KDO which is an essential component of the lipopolysaccharide; CMP-KDO Synthetase: 3-Deoxy-D-manno-octulosonate cytidylyltransferase (CMP-KDO synthetase) catalyzes the conversion of CTP and 3-deoxy-D-manno-octulosonate into CMP-3-deoxy-D-manno-octulosonate (CMP-KDO) and pyrophosphate. KDO is an essential component of the lipopolysaccharide found in the outer surface of gram-negative eubacteria. It is also a constituent of the capsular polysaccharides of some gram-negative eubacteria. Its presence in the cell wall polysaccharides of green algae and plant were also discovered. However, they have not been found in yeast and animals. The absence of the enzyme in mammalian cells makes it an attractive target molecule for drug design.


Pssm-ID: 133010  Cd Length: 239  Bit Score: 51.71  E-value: 5.25e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518506211   2 SCIAFIFARSGSKGLPGKNIKPLHGKPLLHYAIEVAKQLPQINHIFVSTDCDNIASCAKAAGAGVI 67
Cdd:cd02517    1 KVIVVIPARYASSRLPGKPLADIAGKPMIQHVYERAKKAKGLDEVVVATDDERIADAVESFGGKVV 66
GT2_SpsF cd02518
SpsF is a glycosyltrnasferase implicated in the synthesis of the spore coat; Spore coat ...
 4-63 1.07e-07

SpsF is a glycosyltrnasferase implicated in the synthesis of the spore coat; Spore coat polysaccharide biosynthesis protein F (spsF) is a glycosyltransferase implicated in the synthesis of the spore coat in a variety of bacteria challenged by stress as starvation. The spsF gene is expressed in the late stage of coat development responsible for a terminal step in coat formation that involves the glycosylation of the coat. SpsF gene mutation resulted in spores that appeared normal. But, the spores tended to aggregate and had abnormal adsorption properties, indicating a surface alteration.


Pssm-ID: 133011  Cd Length: 233  Bit Score: 51.03  E-value: 1.07e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518506211   4 IAFIFARSGSKGLPGKNIKPLHGKPLLHYAIEVAKQLPQINHIFVST----DCDNIASCAKAAG 63
Cdd:cd02518    1 VAIIQARMGSTRLPGKVLKPLGGKPLLEHLLDRLKRSKLIDEIVIATstneEDDPLEALAKKLG 64
KdsB COG1212
CMP-2-keto-3-deoxyoctulosonic acid synthetase [Cell wall/membrane/envelope biogenesis]; ...
 1-67 1.21e-07

CMP-2-keto-3-deoxyoctulosonic acid synthetase [Cell wall/membrane/envelope biogenesis]; CMP-2-keto-3-deoxyoctulosonic acid synthetase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440825  Cd Length: 242  Bit Score: 50.83  E-value: 1.21e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518506211   1 MSCIAFIFARSGSKGLPGKNIKPLHGKPLLHYAIEVAKQLPQINHIFVSTDCDNIASCAKAAGAGVI 67
Cdd:COG1212    1 MKFIVVIPARYASTRLPGKPLADIAGKPMIQRVYERALASKGADRVVVATDDERIADAVEAFGGEVV 67
PRK05450 PRK05450
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
 1-67 4.88e-06

3-deoxy-manno-octulosonate cytidylyltransferase; Provisional


Pssm-ID: 235473  Cd Length: 245  Bit Score: 46.26  E-value: 4.88e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518506211   1 MSCIAFIFARSGSKGLPGKNIKPLHGKPLLHYAIEVAKQlPQINHIFVSTDCDNIASCAKAAGAGVI 67
Cdd:PRK05450   1 MKFLIIIPARYASTRLPGKPLADIGGKPMIVRVYERASK-AGADRVVVATDDERIADAVEAFGGEVV 66
PLN02917 PLN02917
CMP-KDO synthetase
 4-68 5.02e-06

CMP-KDO synthetase


Pssm-ID: 215495  Cd Length: 293  Bit Score: 46.37  E-value: 5.02e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518506211   4 IAFIFARSGSKGLPGKNIKPLHGKPLLHYAIEVAKQLPQINHIFVSTDCDNIASCAKAAGAGVII 68
Cdd:PLN02917  49 VGIIPARFASSRFEGKPLVHILGKPMIQRTWERAKLATTLDHIVVATDDERIAECCRGFGADVIM 113
kdsB TIGR00466
3-deoxy-D-manno-octulosonate cytidylyltransferase; [Cell envelope, Biosynthesis and ...
 7-68 2.91e-03

3-deoxy-D-manno-octulosonate cytidylyltransferase; [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 129558  Cd Length: 238  Bit Score: 37.97  E-value: 2.91e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518506211    7 IFARSGSKGLPGKNIKPLHGKPLLHYAIEVAKQlPQINHIFVSTDCDNIASCAKAAGAGVII 68
Cdd:TIGR00466   4 IPARLASSRLPGKPLEDIFGKPMIVHVAENANE-SGADRCIVATDDESVAQTCQKFGIEVCM 64
 
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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