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Conserved domains on  [gi|1834199467|ref|NP_730474|]
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CMP-sialic acid synthase [Drosophila melanogaster]

Protein Classification

acylneuraminate cytidylyltransferase family protein( domain architecture ID 10118501)

acylneuraminate cytidylyltransferase family protein, similar to N-acylneuraminate cytidylyltransferase that 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

EC:  2.7.7.-
Gene Ontology:  GO:0016779
PubMed:  9445404|12691742
SCOP:  4002789

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; ...
 32-240 2.09e-62

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: 195.06  E-value: 2.09e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199467  32 ALILARGGSKGIKLKNLAEIGGSSLLARTIMTIKNSTCFRHIWVSTDDKRIAIEAQKYGAI-IHHRPEKFARDDTPSLHA 110
Cdd:cd02513     4 AIIPARGGSKGIPGKNIRPLGGKPLIAWTIEAALESKLFDRVVVSTDDEEIAEVARKYGAEvPFLRPAELATDTASSIDV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199467 111 ISEFLDVHRSIHD----FALFQCTSVFLKTKYIQEAVRKFESH--DCVFAAKRSHYLRWK---VVDGELMPAEFDLSARP 181
Cdd:cd02513    84 ILHALDQLEELGRdfdiVVLLQPTSPLRSAEDIDEAIELLLSEgaDSVFSVTEFHRFPWRalgLDDNGLEPVNYPEDKRT 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199467 182 RRQDWQGDIVETGMFYFSRRK-LVDSGLLQNNRCSVVEIDAKDSLEIDSSHDLTLAKYIL 240
Cdd:cd02513   164 RRQDLPPAYHENGAIYIAKREaLLESNSFFGGKTGPYEMPRERSIDIDTEEDFELAEALL 223
 
Name Accession Description Interval E-value
CMP-NeuAc_Synthase cd02513
CMP-NeuAc_Synthase activates N-acetylneuraminic acid by adding CMP moiety; ...
 32-240 2.09e-62

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: 195.06  E-value: 2.09e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199467  32 ALILARGGSKGIKLKNLAEIGGSSLLARTIMTIKNSTCFRHIWVSTDDKRIAIEAQKYGAI-IHHRPEKFARDDTPSLHA 110
Cdd:cd02513     4 AIIPARGGSKGIPGKNIRPLGGKPLIAWTIEAALESKLFDRVVVSTDDEEIAEVARKYGAEvPFLRPAELATDTASSIDV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199467 111 ISEFLDVHRSIHD----FALFQCTSVFLKTKYIQEAVRKFESH--DCVFAAKRSHYLRWK---VVDGELMPAEFDLSARP 181
Cdd:cd02513    84 ILHALDQLEELGRdfdiVVLLQPTSPLRSAEDIDEAIELLLSEgaDSVFSVTEFHRFPWRalgLDDNGLEPVNYPEDKRT 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199467 182 RRQDWQGDIVETGMFYFSRRK-LVDSGLLQNNRCSVVEIDAKDSLEIDSSHDLTLAKYIL 240
Cdd:cd02513   164 RRQDLPPAYHENGAIYIAKREaLLESNSFFGGKTGPYEMPRERSIDIDTEEDFELAEALL 223
NeuA COG1083
CMP-N-acetylneuraminic acid synthetase, NeuA/PseF family [Cell wall/membrane/envelope ...
 30-240 5.24e-57

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


Pssm-ID: 440700  Cd Length: 228  Bit Score: 181.13  E-value: 5.24e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199467  30 IHALILARGGSKGIKLKNLAEIGGSSLLARTIMTIKNSTCFRHIWVSTDDKRIAIEAQKYGAIIHHRPEKFARDDTPS-- 107
Cdd:COG1083     3 ILAIIPARGGSKGIPGKNIRPLAGKPLIAYSIEAALKSGLFDRVVVSTDDEEIAEVAREYGAEVFLRPAELAGDTASTid 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199467 108 --LHAISEFLDVHRSIHDFALFQCTSVFLKTKYIQEAVRKFESH--DCVFAAKRSHYLRWKVV----DGELMPAEFDLSA 179
Cdd:COG1083    83 viLHALEWLEEQGEEFDYVVLLQPTSPLRTAEDIDEAIELLLESgaDSVVSVTEAHHPPYWALkldeDGRLEPLNPDPHN 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1834199467 180 RPRRQDWQGDIVETGMFYFSRRKLvdsgLLQNN-----RCSVVEIDAKDSLEIDSSHDLTLAKYIL 240
Cdd:COG1083   163 RPRRQDLPPAYRENGAIYIFKREA----LLENKsrfggKTGAYEMPEERSVDIDTEEDFELAEALL 224
CTP_transf_3 pfam02348
Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) ...
 32-144 1.36e-14

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: 70.44  E-value: 1.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199467  32 ALILARGGSKGIKLKNLAEIGGSSLLARTIMTIKNSTCFRHIWVSTDDKRIAIEAQKYGAIIHHRPEKFARDDTPSLHAI 111
Cdd:pfam02348   2 AIIPARLGSKRLPGKNLLDLGGKPLIHHVLEAALKSGAFEKVIVATDSEEIADVAKEFGAGVVMTSGSLSSGTDRFYEVV 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1834199467 112 SEFldvHRSIHDFAL-FQCTSVFLKTKYIQEAVR 144
Cdd:pfam02348  82 KAF---LNDHDDIIVnIQGDNPLLQPEVILKAIE 112
PRK05450 PRK05450
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
 30-91 5.17e-03

3-deoxy-manno-octulosonate cytidylyltransferase; Provisional


Pssm-ID: 235473  Cd Length: 245  Bit Score: 37.40  E-value: 5.17e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1834199467  30 IHALILARGGSKGIKLKNLAEIGGSSLLARTIMTIKNSTcFRHIWVSTDDKRIAIEAQKYGA 91
Cdd:PRK05450    3 FLIIIPARYASTRLPGKPLADIGGKPMIVRVYERASKAG-ADRVVVATDDERIADAVEAFGG 63
 
Name Accession Description Interval E-value
CMP-NeuAc_Synthase cd02513
CMP-NeuAc_Synthase activates N-acetylneuraminic acid by adding CMP moiety; ...
 32-240 2.09e-62

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: 195.06  E-value: 2.09e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199467  32 ALILARGGSKGIKLKNLAEIGGSSLLARTIMTIKNSTCFRHIWVSTDDKRIAIEAQKYGAI-IHHRPEKFARDDTPSLHA 110
Cdd:cd02513     4 AIIPARGGSKGIPGKNIRPLGGKPLIAWTIEAALESKLFDRVVVSTDDEEIAEVARKYGAEvPFLRPAELATDTASSIDV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199467 111 ISEFLDVHRSIHD----FALFQCTSVFLKTKYIQEAVRKFESH--DCVFAAKRSHYLRWK---VVDGELMPAEFDLSARP 181
Cdd:cd02513    84 ILHALDQLEELGRdfdiVVLLQPTSPLRSAEDIDEAIELLLSEgaDSVFSVTEFHRFPWRalgLDDNGLEPVNYPEDKRT 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199467 182 RRQDWQGDIVETGMFYFSRRK-LVDSGLLQNNRCSVVEIDAKDSLEIDSSHDLTLAKYIL 240
Cdd:cd02513   164 RRQDLPPAYHENGAIYIAKREaLLESNSFFGGKTGPYEMPRERSIDIDTEEDFELAEALL 223
NeuA COG1083
CMP-N-acetylneuraminic acid synthetase, NeuA/PseF family [Cell wall/membrane/envelope ...
 30-240 5.24e-57

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


Pssm-ID: 440700  Cd Length: 228  Bit Score: 181.13  E-value: 5.24e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199467  30 IHALILARGGSKGIKLKNLAEIGGSSLLARTIMTIKNSTCFRHIWVSTDDKRIAIEAQKYGAIIHHRPEKFARDDTPS-- 107
Cdd:COG1083     3 ILAIIPARGGSKGIPGKNIRPLAGKPLIAYSIEAALKSGLFDRVVVSTDDEEIAEVAREYGAEVFLRPAELAGDTASTid 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199467 108 --LHAISEFLDVHRSIHDFALFQCTSVFLKTKYIQEAVRKFESH--DCVFAAKRSHYLRWKVV----DGELMPAEFDLSA 179
Cdd:COG1083    83 viLHALEWLEEQGEEFDYVVLLQPTSPLRTAEDIDEAIELLLESgaDSVVSVTEAHHPPYWALkldeDGRLEPLNPDPHN 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1834199467 180 RPRRQDWQGDIVETGMFYFSRRKLvdsgLLQNN-----RCSVVEIDAKDSLEIDSSHDLTLAKYIL 240
Cdd:COG1083   163 RPRRQDLPPAYRENGAIYIFKREA----LLENKsrfggKTGAYEMPEERSVDIDTEEDFELAEALL 224
CTP_transf_3 pfam02348
Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) ...
 32-144 1.36e-14

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: 70.44  E-value: 1.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199467  32 ALILARGGSKGIKLKNLAEIGGSSLLARTIMTIKNSTCFRHIWVSTDDKRIAIEAQKYGAIIHHRPEKFARDDTPSLHAI 111
Cdd:pfam02348   2 AIIPARLGSKRLPGKNLLDLGGKPLIHHVLEAALKSGAFEKVIVATDSEEIADVAKEFGAGVVMTSGSLSSGTDRFYEVV 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1834199467 112 SEFldvHRSIHDFAL-FQCTSVFLKTKYIQEAVR 144
Cdd:pfam02348  82 KAF---LNDHDDIIVnIQGDNPLLQPEVILKAIE 112
CMP-KDO-Synthetase cd02517
CMP-KDO synthetase catalyzes the activation of KDO which is an essential component of the ...
 29-91 6.45e-06

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: 45.93  E-value: 6.45e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1834199467  29 DIHALILARGGSKGIKLKNLAEIGGSSLLARTIMTIKNSTCFRHIWVSTDDKRIAIEAQKYGA 91
Cdd:cd02517     1 KVIVVIPARYASSRLPGKPLADIAGKPMIQHVYERAKKAKGLDEVVVATDDERIADAVESFGG 63
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 32-161 1.10e-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: 41.41  E-value: 1.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199467  32 ALILARGGSK---GIKLknLAEIGGSSLLARTIMTIKnsTCFRHIWVSTDDKRIAIEAQKYGAiihhrpeKFARDDTP-- 106
Cdd:pfam12804   1 AVILAGGRSSrmgGDKA--LLPLGGKPLLERVLERLR--PAGDEVVVVANDEEVLAALAGLGV-------PVVPDPDPgq 69

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1834199467 107 -SLHAISEFLDVHRSIHDFALFQCTSVFLKTKYIQEAVRKFESHDC-----VFAAKRSHYL 161
Cdd:pfam12804  70 gPLAGLLAALRAAPGADAVLVLACDMPFLTPELLRRLLAAAEESGAdivvpVYDGGRGHPL 130
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 30-99 6.68e-04

GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133025 [Multi-domain]  Cd Length: 186  Bit Score: 39.47  E-value: 6.68e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1834199467  30 IHALILARGGSK---GIKLknLAEIGGSSLLARTIMTIKNStCFRHIWVSTDDKRIAIEAQKYG----AIIHHRPEK 99
Cdd:cd04182     1 IAAIILAAGRSSrmgGNKL--LLPLDGKPLLRHALDAALAA-GLSRVIVVLGAEADAVRAALAGlpvvVVINPDWEE 74
PRK05450 PRK05450
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
 30-91 5.17e-03

3-deoxy-manno-octulosonate cytidylyltransferase; Provisional


Pssm-ID: 235473  Cd Length: 245  Bit Score: 37.40  E-value: 5.17e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1834199467  30 IHALILARGGSKGIKLKNLAEIGGSSLLARTIMTIKNSTcFRHIWVSTDDKRIAIEAQKYGA 91
Cdd:PRK05450    3 FLIIIPARYASTRLPGKPLADIGGKPMIVRVYERASKAG-ADRVVVATDDERIADAVEAFGG 63
PLN02917 PLN02917
CMP-KDO synthetase
 33-91 5.83e-03

CMP-KDO synthetase


Pssm-ID: 215495  Cd Length: 293  Bit Score: 37.12  E-value: 5.83e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1834199467  33 LILARGGSKGIKLKNLAEIGGSSLLARTIMTIKNSTCFRHIWVSTDDKRIAIEAQKYGA 91
Cdd:PLN02917   51 IIPARFASSRFEGKPLVHILGKPMIQRTWERAKLATTLDHIVVATDDERIAECCRGFGA 109
PRK13368 PRK13368
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
 32-91 6.89e-03

3-deoxy-manno-octulosonate cytidylyltransferase; Provisional


Pssm-ID: 184007  Cd Length: 238  Bit Score: 36.87  E-value: 6.89e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199467  32 ALILARGGSKGIKLKNLAEIGGSSLLARTIMTIKNSTCFRHIWVSTDDKRIAIEAQKYGA 91
Cdd:PRK13368    5 VVIPARYGSSRLPGKPLLDILGKPMIQHVYERAAQAAGVEEVYVATDDQRIEDAVEAFGG 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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