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Conserved domains on  [gi|557024959|ref|XP_006012644|]
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N-acylneuraminate cytidylyltransferase [Latimeria chalumnae]

Protein Classification

acylneuraminate cytidylyltransferase( domain architecture ID 10118517)

N-acylneuraminate cytidylyltransferase catalyzes the activation of N-acetylneuraminic acid (NeuNAc) to cytidine 5'-monophosphate N-acetylneuraminic acid (CMP-NeuNAc), a substrate required for the addition of sialic acid; contains a HAD (haloacid dehalogenase) domain

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CMP-NeuAc_Synthase cd02513
CMP-NeuAc_Synthase activates N-acetylneuraminic acid by adding CMP moiety; ...
 60-274 3.30e-85

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: 260.16  E-value: 3.30e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557024959  60 VALILARGGSKGIRLKNIKELAGVPLIGWVLRAAKESGVFNSVWISTDHDEIEKVAKIWDA-KVHRRSPEVSKDTSTSVE 138
Cdd:cd02513    3 LAIIPARGGSKGIPGKNIRPLGGKPLIAWTIEAALESKLFDRVVVSTDDEEIAEVARKYGAeVPFLRPAELATDTASSID 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557024959 139 TIQEFLKFHPE----VKIVGHIQATSPCLHPYVLQEVMKKMDQ-GYDSVFSVERRHLFLWKEVENEGEKTEPKNFVPSKR 213
Cdd:cd02513   83 VILHALDQLEElgrdFDIVVLLQPTSPLRSAEDIDEAIELLLSeGADSVFSVTEFHRFPWRALGLDDNGLEPVNYPEDKR 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 557024959 214 PRRQDWKGELCENGSFYFTKREIIMTRGSLQSGKLAYYEMKPEHSVDIDEDIDWPIAEQRI 274
Cdd:cd02513  163 TRRQDLPPAYHENGAIYIAKREALLESNSFFGGKTGPYEMPRERSIDIDTEEDFELAEALL 223
HAD_like super family cl21460
Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes ...
 319-415 2.51e-09

Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes carbon and phosphorus hydrolases such as 2-haloalkonoate dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, among others. These proteins catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All members possess a conserve alpha/beta core domain, and many also possess a small cap domain, with varying folds and functions.


The actual alignment was detected with superfamily member cd01630:

Pssm-ID: 473868 [Multi-domain]  Cd Length: 146  Bit Score: 55.61  E-value: 2.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557024959 319 LQKKGIKVLLILNRH-KIDDILAKNLKCE-IKKKDSDKKAFLEKWLKEKNLSWKQVAYIGCEDSDEEFLKSAAVSCAIEG 396
Cdd:cd01630   40 LQKSGIEVAIITGRQsEAVRRRAKELGIEdLFQGVKDKLEALEELLEKLGLSDEEVAYMGDDLPDLPVMKRVGLSVAPAD 119

                         90
                 ....*....|....*....
gi 557024959 397 VSQKVIKCANFVYRRERGN 415
Cdd:cd01630  120 AHPEVREAADYVTRARGGR 138
 
Name Accession Description Interval E-value
CMP-NeuAc_Synthase cd02513
CMP-NeuAc_Synthase activates N-acetylneuraminic acid by adding CMP moiety; ...
 60-274 3.30e-85

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: 260.16  E-value: 3.30e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557024959  60 VALILARGGSKGIRLKNIKELAGVPLIGWVLRAAKESGVFNSVWISTDHDEIEKVAKIWDA-KVHRRSPEVSKDTSTSVE 138
Cdd:cd02513    3 LAIIPARGGSKGIPGKNIRPLGGKPLIAWTIEAALESKLFDRVVVSTDDEEIAEVARKYGAeVPFLRPAELATDTASSID 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557024959 139 TIQEFLKFHPE----VKIVGHIQATSPCLHPYVLQEVMKKMDQ-GYDSVFSVERRHLFLWKEVENEGEKTEPKNFVPSKR 213
Cdd:cd02513   83 VILHALDQLEElgrdFDIVVLLQPTSPLRSAEDIDEAIELLLSeGADSVFSVTEFHRFPWRALGLDDNGLEPVNYPEDKR 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 557024959 214 PRRQDWKGELCENGSFYFTKREIIMTRGSLQSGKLAYYEMKPEHSVDIDEDIDWPIAEQRI 274
Cdd:cd02513  163 TRRQDLPPAYHENGAIYIAKREALLESNSFFGGKTGPYEMPRERSIDIDTEEDFELAEALL 223
NeuA COG1083
CMP-N-acetylneuraminic acid synthetase, NeuA/PseF family [Cell wall/membrane/envelope ...
 59-272 5.08e-69

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


Pssm-ID: 440700  Cd Length: 228  Bit Score: 218.49  E-value: 5.08e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557024959  59 KVALILARGGSKGIRLKNIKELAGVPLIGWVLRAAKESGVFNSVWISTDHDEIEKVAKIWDAKVHRRSPEVSKDTSTSVE 138
Cdd:COG1083    3 ILAIIPARGGSKGIPGKNIRPLAGKPLIAYSIEAALKSGLFDRVVVSTDDEEIAEVAREYGAEVFLRPAELAGDTASTID 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557024959 139 TIQEFLKF----HPEVKIVGHIQATSPCLHPYVLQEVMKKM-DQGYDSVFSVER-RHLFLWKEVENEGEKTEPKNFVPSK 212
Cdd:COG1083   83 VILHALEWleeqGEEFDYVVLLQPTSPLRTAEDIDEAIELLlESGADSVVSVTEaHHPPYWALKLDEDGRLEPLNPDPHN 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 557024959 213 RPRRQDWKGELCENGSFYFTKREIIMTRGSLQSGKLAYYEMKPEHSVDIDEDIDWPIAEQ 272
Cdd:COG1083  163 RPRRQDLPPAYRENGAIYIFKREALLENKSRFGGKTGAYEMPEERSVDIDTEEDFELAEA 222
CTP_transf_3 pfam02348
Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) ...
 60-270 7.18e-36

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: 131.69  E-value: 7.18e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557024959   60 VALILARGGSKGIRLKNIKELAGVPLIGWVLRAAKESGVFNSVWISTDHDEIEKVAKIWDAKVHRRSPEVSKDTSTSVET 139
Cdd:pfam02348   1 AAIIPARLGSKRLPGKNLLDLGGKPLIHHVLEAALKSGAFEKVIVATDSEEIADVAKEFGAGVVMTSGSLSSGTDRFYEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557024959  140 IQEFLKFHPEvkIVGHIQATSPCLHPYVLQEVMKKM-DQGYDSVFSVerrhlflwkeVENEGEKTEPKNFVPSKRPRRQD 218
Cdd:pfam02348  81 VKAFLNDHDD--IIVNIQGDNPLLQPEVILKAIETLlNNGEPYMSTL----------VVPVGSAEEVLNANALKVVLDDD 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 557024959  219 WKGELCENGSFYFtKREIIMTRGSLQSGKLAYYEMKPEHsVDIDEDIDWPIA 270
Cdd:pfam02348 149 GYALYFSRSVIPY-IREHPAELYYVYLRHIGIYTFRKNM-PLIELVIDTPTA 198
PseF TIGR03584
pseudaminic acid cytidylyltransferase; The sequences in this family include the pfam02348 ...
 60-271 2.32e-30

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: 117.05  E-value: 2.32e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557024959   60 VALILARGGSKGIRLKNIKELAGVPLIGWVLRAAKESGVFNSVWISTDHDEIEKVAKIWDAKV-HRRSPEVSKDTSTSVE 138
Cdd:TIGR03584   1 IAIIPARGGSKRIPRKNIKPFCGKPMIAYSIEAALNSGLFDKVVVSTDDEEIAEVAKSYGASVpFLRPKELADDFTGTAP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557024959  139 TIQ---EFLKFHPEVKIVGHIQATSPCLHPYVLQEVMKKMDQ-GYDSVFSVER------RHLFLwkEVENEGEKTEPKNF 208
Cdd:TIGR03584  81 VVKhaiEELKLQKQYDHACCIYATAPFLQAKILKEAFELLKQpNAHFVFSVTSfafpiqRAFKL--KENGGVEMFQPEHF 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 557024959  209 vpskRPRRQDWKGELCENGSFYFTKREIIMTRGSLQSGKLAYYEMkPEHSV-DIDEDIDWPIAE 271
Cdd:TIGR03584 159 ----NTRSQDLEEAYHDAGQFYWGKSQAWLESGPIFSPHSIPIVL-PRHLVqDIDTLEDWERAE 217
HAD_KDO-like cd01630
haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli ...
 319-415 2.51e-09

haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli 3-deoxy-D-manno-octulosonate 8-phosphate (KDO 8-P) phosphatase KdsC, and rainbow trout N-acylneuraminate cytidylyltransferase; KDO 8-P phosphatase catalyzes the hydrolysis of KDO 8-P to KDO (3-deoxy-D-manno-octulosonate) and inorganic phosphate and is the last enzyme in the KDO biosynthetic pathway. KDO is an 8-carbon sugar that links the lipid A and polysaccharide moieties of the lipopolysaccharide region in Gram-negative bacteria. An interruption in KDO biosynthesis leads to the accumulation of lipid A precursors and subsequent arrest in cell growth. The KDO biosynthesis pathway involves five sequential enzymatic reactions. This family also includes rainbow trout CMP-sialic acid synthetase which effectively converts both deaminoneuraminic acid (KDN, 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid) and N-acetylneuraminic acid (Neu5Ac) to CMP-KDN and CMP-Neu5Ac, respectively. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319769 [Multi-domain]  Cd Length: 146  Bit Score: 55.61  E-value: 2.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557024959 319 LQKKGIKVLLILNRH-KIDDILAKNLKCE-IKKKDSDKKAFLEKWLKEKNLSWKQVAYIGCEDSDEEFLKSAAVSCAIEG 396
Cdd:cd01630   40 LQKSGIEVAIITGRQsEAVRRRAKELGIEdLFQGVKDKLEALEELLEKLGLSDEEVAYMGDDLPDLPVMKRVGLSVAPAD 119

                         90
                 ....*....|....*....
gi 557024959 397 VSQKVIKCANFVYRRERGN 415
Cdd:cd01630  120 AHPEVREAADYVTRARGGR 138
PRK13368 PRK13368
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
 60-175 2.86e-09

3-deoxy-manno-octulosonate cytidylyltransferase; Provisional


Pssm-ID: 184007  Cd Length: 238  Bit Score: 57.28  E-value: 2.86e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557024959  60 VALILARGGSKgiRL--KNIKELAGVPLIGWVLRAAKESGVFNSVWISTDHDEIEKVAKIWDAKVHRRSPEVSKDTSTSV 137
Cdd:PRK13368   4 VVVIPARYGSS--RLpgKPLLDILGKPMIQHVYERAAQAAGVEEVYVATDDQRIEDAVEAFGGKVVMTSDDHLSGTDRLA 81

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 557024959 138 ETIQEFlkfhpEVKIVGHIQATSPCLHPYVLQEVMKKM 175
Cdd:PRK13368  82 EVMLKI-----EADIYINVQGDEPMIRPRDIDTLIQPM 114
 
Name Accession Description Interval E-value
CMP-NeuAc_Synthase cd02513
CMP-NeuAc_Synthase activates N-acetylneuraminic acid by adding CMP moiety; ...
 60-274 3.30e-85

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: 260.16  E-value: 3.30e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557024959  60 VALILARGGSKGIRLKNIKELAGVPLIGWVLRAAKESGVFNSVWISTDHDEIEKVAKIWDA-KVHRRSPEVSKDTSTSVE 138
Cdd:cd02513    3 LAIIPARGGSKGIPGKNIRPLGGKPLIAWTIEAALESKLFDRVVVSTDDEEIAEVARKYGAeVPFLRPAELATDTASSID 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557024959 139 TIQEFLKFHPE----VKIVGHIQATSPCLHPYVLQEVMKKMDQ-GYDSVFSVERRHLFLWKEVENEGEKTEPKNFVPSKR 213
Cdd:cd02513   83 VILHALDQLEElgrdFDIVVLLQPTSPLRSAEDIDEAIELLLSeGADSVFSVTEFHRFPWRALGLDDNGLEPVNYPEDKR 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 557024959 214 PRRQDWKGELCENGSFYFTKREIIMTRGSLQSGKLAYYEMKPEHSVDIDEDIDWPIAEQRI 274
Cdd:cd02513  163 TRRQDLPPAYHENGAIYIAKREALLESNSFFGGKTGPYEMPRERSIDIDTEEDFELAEALL 223
NeuA COG1083
CMP-N-acetylneuraminic acid synthetase, NeuA/PseF family [Cell wall/membrane/envelope ...
 59-272 5.08e-69

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


Pssm-ID: 440700  Cd Length: 228  Bit Score: 218.49  E-value: 5.08e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557024959  59 KVALILARGGSKGIRLKNIKELAGVPLIGWVLRAAKESGVFNSVWISTDHDEIEKVAKIWDAKVHRRSPEVSKDTSTSVE 138
Cdd:COG1083    3 ILAIIPARGGSKGIPGKNIRPLAGKPLIAYSIEAALKSGLFDRVVVSTDDEEIAEVAREYGAEVFLRPAELAGDTASTID 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557024959 139 TIQEFLKF----HPEVKIVGHIQATSPCLHPYVLQEVMKKM-DQGYDSVFSVER-RHLFLWKEVENEGEKTEPKNFVPSK 212
Cdd:COG1083   83 VILHALEWleeqGEEFDYVVLLQPTSPLRTAEDIDEAIELLlESGADSVVSVTEaHHPPYWALKLDEDGRLEPLNPDPHN 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 557024959 213 RPRRQDWKGELCENGSFYFTKREIIMTRGSLQSGKLAYYEMKPEHSVDIDEDIDWPIAEQ 272
Cdd:COG1083  163 RPRRQDLPPAYRENGAIYIFKREALLENKSRFGGKTGAYEMPEERSVDIDTEEDFELAEA 222
CTP_transf_3 pfam02348
Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) ...
 60-270 7.18e-36

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: 131.69  E-value: 7.18e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557024959   60 VALILARGGSKGIRLKNIKELAGVPLIGWVLRAAKESGVFNSVWISTDHDEIEKVAKIWDAKVHRRSPEVSKDTSTSVET 139
Cdd:pfam02348   1 AAIIPARLGSKRLPGKNLLDLGGKPLIHHVLEAALKSGAFEKVIVATDSEEIADVAKEFGAGVVMTSGSLSSGTDRFYEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557024959  140 IQEFLKFHPEvkIVGHIQATSPCLHPYVLQEVMKKM-DQGYDSVFSVerrhlflwkeVENEGEKTEPKNFVPSKRPRRQD 218
Cdd:pfam02348  81 VKAFLNDHDD--IIVNIQGDNPLLQPEVILKAIETLlNNGEPYMSTL----------VVPVGSAEEVLNANALKVVLDDD 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 557024959  219 WKGELCENGSFYFtKREIIMTRGSLQSGKLAYYEMKPEHsVDIDEDIDWPIA 270
Cdd:pfam02348 149 GYALYFSRSVIPY-IREHPAELYYVYLRHIGIYTFRKNM-PLIELVIDTPTA 198
PseF TIGR03584
pseudaminic acid cytidylyltransferase; The sequences in this family include the pfam02348 ...
 60-271 2.32e-30

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: 117.05  E-value: 2.32e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557024959   60 VALILARGGSKGIRLKNIKELAGVPLIGWVLRAAKESGVFNSVWISTDHDEIEKVAKIWDAKV-HRRSPEVSKDTSTSVE 138
Cdd:TIGR03584   1 IAIIPARGGSKRIPRKNIKPFCGKPMIAYSIEAALNSGLFDKVVVSTDDEEIAEVAKSYGASVpFLRPKELADDFTGTAP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557024959  139 TIQ---EFLKFHPEVKIVGHIQATSPCLHPYVLQEVMKKMDQ-GYDSVFSVER------RHLFLwkEVENEGEKTEPKNF 208
Cdd:TIGR03584  81 VVKhaiEELKLQKQYDHACCIYATAPFLQAKILKEAFELLKQpNAHFVFSVTSfafpiqRAFKL--KENGGVEMFQPEHF 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 557024959  209 vpskRPRRQDWKGELCENGSFYFTKREIIMTRGSLQSGKLAYYEMkPEHSV-DIDEDIDWPIAE 271
Cdd:TIGR03584 159 ----NTRSQDLEEAYHDAGQFYWGKSQAWLESGPIFSPHSIPIVL-PRHLVqDIDTLEDWERAE 217
CMP-KDO-Synthetase cd02517
CMP-KDO synthetase catalyzes the activation of KDO which is an essential component of the ...
 60-177 3.54e-10

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: 59.79  E-value: 3.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557024959  60 VALILARGGSKgiRL--KNIKELAGVPLIGWVLRAAKESGVFNSVWISTDHDEIEKVAKIWDAKVhrrspeV--SKDTST 135
Cdd:cd02517    3 IVVIPARYASS--RLpgKPLADIAGKPMIQHVYERAKKAKGLDEVVVATDDERIADAVESFGGKV------VmtSPDHPS 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 557024959 136 SVETIQEFL-KFHPEVKIVGHIQATSPCLHPYVLQEVMKKMDQ 177
Cdd:cd02517   75 GTDRIAEVAeKLDADDDIVVNVQGDEPLIPPEMIDQVVAALKD 117
HAD_KDO-like cd01630
haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli ...
 319-415 2.51e-09

haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli 3-deoxy-D-manno-octulosonate 8-phosphate (KDO 8-P) phosphatase KdsC, and rainbow trout N-acylneuraminate cytidylyltransferase; KDO 8-P phosphatase catalyzes the hydrolysis of KDO 8-P to KDO (3-deoxy-D-manno-octulosonate) and inorganic phosphate and is the last enzyme in the KDO biosynthetic pathway. KDO is an 8-carbon sugar that links the lipid A and polysaccharide moieties of the lipopolysaccharide region in Gram-negative bacteria. An interruption in KDO biosynthesis leads to the accumulation of lipid A precursors and subsequent arrest in cell growth. The KDO biosynthesis pathway involves five sequential enzymatic reactions. This family also includes rainbow trout CMP-sialic acid synthetase which effectively converts both deaminoneuraminic acid (KDN, 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid) and N-acetylneuraminic acid (Neu5Ac) to CMP-KDN and CMP-Neu5Ac, respectively. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319769 [Multi-domain]  Cd Length: 146  Bit Score: 55.61  E-value: 2.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557024959 319 LQKKGIKVLLILNRH-KIDDILAKNLKCE-IKKKDSDKKAFLEKWLKEKNLSWKQVAYIGCEDSDEEFLKSAAVSCAIEG 396
Cdd:cd01630   40 LQKSGIEVAIITGRQsEAVRRRAKELGIEdLFQGVKDKLEALEELLEKLGLSDEEVAYMGDDLPDLPVMKRVGLSVAPAD 119

                         90
                 ....*....|....*....
gi 557024959 397 VSQKVIKCANFVYRRERGN 415
Cdd:cd01630  120 AHPEVREAADYVTRARGGR 138
PRK13368 PRK13368
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
 60-175 2.86e-09

3-deoxy-manno-octulosonate cytidylyltransferase; Provisional


Pssm-ID: 184007  Cd Length: 238  Bit Score: 57.28  E-value: 2.86e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557024959  60 VALILARGGSKgiRL--KNIKELAGVPLIGWVLRAAKESGVFNSVWISTDHDEIEKVAKIWDAKVHRRSPEVSKDTSTSV 137
Cdd:PRK13368   4 VVVIPARYGSS--RLpgKPLLDILGKPMIQHVYERAAQAAGVEEVYVATDDQRIEDAVEAFGGKVVMTSDDHLSGTDRLA 81

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 557024959 138 ETIQEFlkfhpEVKIVGHIQATSPCLHPYVLQEVMKKM 175
Cdd:PRK13368  82 EVMLKI-----EADIYINVQGDEPMIRPRDIDTLIQPM 114
PRK05450 PRK05450
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
 60-177 8.37e-08

3-deoxy-manno-octulosonate cytidylyltransferase; Provisional


Pssm-ID: 235473  Cd Length: 245  Bit Score: 52.81  E-value: 8.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557024959  60 VALILARGGSKgiRLKN--IKELAGVPLIGWVLRAAKESGVfNSVWISTDHDEIEKVAKIWDAKVhrrspeV--SKDTST 135
Cdd:PRK05450   4 LIIIPARYAST--RLPGkpLADIGGKPMIVRVYERASKAGA-DRVVVATDDERIADAVEAFGGEV------VmtSPDHPS 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 557024959 136 SVETIQEFLKFH--PEVKIVGHIQATSPCLHPYVLQEVMKKMDQ 177
Cdd:PRK05450  75 GTDRIAEAAAKLglADDDIVVNVQGDEPLIPPEIIDQVAEPLAN 118
GT2_SpsF cd02518
SpsF is a glycosyltrnasferase implicated in the synthesis of the spore coat; Spore coat ...
 60-180 1.30e-06

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: 49.11  E-value: 1.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557024959  60 VALILARGGSKgiRL--KNIKELAGVPLIGWVLRAAKESGVFNSVWIST----DHDEIEKVAKIWDAKVHRRSPEvskDT 133
Cdd:cd02518    1 VAIIQARMGST--RLpgKVLKPLGGKPLLEHLLDRLKRSKLIDEIVIATstneEDDPLEALAKKLGVKVFRGSEE---DV 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 557024959 134 -STSVETIQEFlkfhpEVKIVGHIQATSPCLHPYVLQEVMKK-MDQGYD 180
Cdd:cd02518   76 lGRYYQAAEEY-----NADVVVRITGDCPLIDPEIIDAVIRLfLKSGAD 119
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 61-122 9.65e-04

MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine dinucleotide biosynthesis protein A). The family also includes a wide range of other NTP transferase domain.


Pssm-ID: 463715 [Multi-domain]  Cd Length: 159  Bit Score: 39.49  E-value: 9.65e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 557024959   61 ALILARGGSKgiRLKNIK---ELAGVPLIGWVLRAAKEsgVFNSVWISTDHDEIEKVAKIWDAKV 122
Cdd:pfam12804   1 AVILAGGRSS--RMGGDKallPLGGKPLLERVLERLRP--AGDEVVVVANDEEVLAALAGLGVPV 61
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 61-102 3.87e-03

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 39.34  E-value: 3.87e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 557024959  61 ALILARGgsKGIRLKN-----IKELAGVPLIGWVLRAAKESGVFNSV 102
Cdd:PRK14355   6 AIILAAG--KGTRMKSdlvkvMHPLAGRPMVSWPVAAAREAGAGRIV 50
 
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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