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CAZyme Information: MGYG000002022_01289
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Basic Information |
Genomic context |
Full Sequence |
Enzyme annotations |
CAZy signature domains |
CDD domains |
CAZyme hits |
PDB hits |
Swiss-Prot hits |
SignalP and Lipop annotations |
TMHMM annotations
Basic Information help
| Species | Centipeda artemidis | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_C; Negativicutes; Selenomonadales; Selenomonadaceae; Centipeda; Centipeda artemidis | |||||||||||
| CAZyme ID | MGYG000002022_01289 | |||||||||||
| CAZy Family | GT0 | |||||||||||
| CAZyme Description | 3-deoxy-manno-octulosonate cytidylyltransferase | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 32947; End: 34599 Strand: + | |||||||||||
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd02513 | CMP-NeuAc_Synthase | 1.59e-76 | 2 | 218 | 1 | 223 | 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. |
| COG1083 | NeuA | 4.73e-52 | 1 | 217 | 2 | 221 | CMP-N-acetylneuraminic acid synthetase [Cell wall/membrane/envelope biogenesis]. |
| TIGR03584 | PseF | 2.95e-41 | 4 | 220 | 1 | 222 | 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. |
| COG3980 | SpsG | 4.38e-30 | 222 | 533 | 2 | 300 | Spore coat polysaccharide biosynthesis protein SpsG, predicted glycosyltransferase [Cell wall/membrane/envelope biogenesis]. |
| pfam02348 | CTP_transf_3 | 9.71e-22 | 4 | 130 | 1 | 120 | Cytidylyltransferase. This family consists of two main Cytidylyltransferase activities: 1) 3-deoxy-manno-octulosonate cytidylyltransferase,, EC:2.7.7.38 catalyzing the reaction:- CTP + 3-deoxy-D-manno-octulosonate <=> diphosphate + CMP-3-deoxy-D-manno-octulosonate, 2) acylneuraminate cytidylyltransferase EC:2.7.7.43, catalyzing 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. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| ACV55877.1 | 3.28e-178 | 3 | 543 | 7 | 546 |
| API89863.1 | 4.15e-175 | 1 | 542 | 1 | 543 |
| AMB92172.1 | 2.50e-166 | 1 | 541 | 1 | 543 |
| QGS37541.1 | 2.80e-165 | 1 | 544 | 6 | 554 |
| AMB95295.1 | 4.82e-161 | 1 | 541 | 1 | 543 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 1QWJ_A | 4.37e-30 | 3 | 220 | 4 | 222 | TheCrystal Structure of Murine CMP-5-N-Acetylneuraminic Acid Synthetase [Mus musculus],1QWJ_B The Crystal Structure of Murine CMP-5-N-Acetylneuraminic Acid Synthetase [Mus musculus],1QWJ_C The Crystal Structure of Murine CMP-5-N-Acetylneuraminic Acid Synthetase [Mus musculus],1QWJ_D The Crystal Structure of Murine CMP-5-N-Acetylneuraminic Acid Synthetase [Mus musculus] |
| 6IFD_A | 7.56e-27 | 4 | 223 | 23 | 249 | CrystalStructure of CMP-N-acetylneuraminate Synthetase from Vibrio cholerae in complex with CDP and Mg2+. [Vibrio cholerae],6IFD_B Crystal Structure of CMP-N-acetylneuraminate Synthetase from Vibrio cholerae in complex with CDP and Mg2+. [Vibrio cholerae],6IFD_C Crystal Structure of CMP-N-acetylneuraminate Synthetase from Vibrio cholerae in complex with CDP and Mg2+. [Vibrio cholerae],6IFD_D Crystal Structure of CMP-N-acetylneuraminate Synthetase from Vibrio cholerae in complex with CDP and Mg2+. [Vibrio cholerae],6IFI_A Crystal Structure of the Apo form of CMP-N-acetylneuraminate Synthetase from Vibrio cholerae [Vibrio cholerae],6IFI_B Crystal Structure of the Apo form of CMP-N-acetylneuraminate Synthetase from Vibrio cholerae [Vibrio cholerae] |
| 6CKJ_A | 1.29e-18 | 4 | 221 | 6 | 226 | N.meningitidis CMP-sialic acid synthetase, ligand-free [Neisseria meningitidis],6CKK_A N. meningitidis CMP-sialic acid synthetase in the presence of CTP and Ca2+ [Neisseria meningitidis],6CKK_B N. meningitidis CMP-sialic acid synthetase in the presence of CTP and Ca2+ [Neisseria meningitidis],6CKL_A N. meningitidis CMP-sialic acid synthetase in the presence of CMP and Neu5Ac2en [Neisseria meningitidis],6CKL_B N. meningitidis CMP-sialic acid synthetase in the presence of CMP and Neu5Ac2en [Neisseria meningitidis],6CKL_C N. meningitidis CMP-sialic acid synthetase in the presence of CMP and Neu5Ac2en [Neisseria meningitidis],6CKM_A N. meningitidis CMP-sialic acid synthetase in the presence of CMP-sialic acid and Ca2+ [Neisseria meningitidis] |
| 1EYR_A | 2.74e-17 | 4 | 221 | 6 | 226 | Structureof a sialic acid activating synthetase, CMP acylneuraminate synthetase in the presence and absence of CDP [Neisseria meningitidis],1EYR_B Structure of a sialic acid activating synthetase, CMP acylneuraminate synthetase in the presence and absence of CDP [Neisseria meningitidis],1EZI_A Structure of a sialic acid activating synthetase, CMP acylneuraminate synthetase in the presence and absence of CDP [Neisseria meningitidis],1EZI_B Structure of a sialic acid activating synthetase, CMP acylneuraminate synthetase in the presence and absence of CDP [Neisseria meningitidis] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q5R6R5 | 1.12e-31 | 3 | 311 | 45 | 361 | N-acylneuraminate cytidylyltransferase OS=Pongo abelii OX=9601 GN=CMAS PE=2 SV=1 |
| Q8NFW8 | 1.12e-31 | 3 | 311 | 45 | 361 | N-acylneuraminate cytidylyltransferase OS=Homo sapiens OX=9606 GN=CMAS PE=1 SV=2 |
| P69060 | 1.48e-31 | 3 | 311 | 43 | 359 | N-acylneuraminate cytidylyltransferase OS=Rattus norvegicus OX=10116 GN=Cmas PE=2 SV=1 |
| Q99KK2 | 1.48e-31 | 3 | 311 | 43 | 359 | N-acylneuraminate cytidylyltransferase OS=Mus musculus OX=10090 GN=Cmas PE=1 SV=2 |
| Q58462 | 1.60e-31 | 222 | 496 | 2 | 312 | Uncharacterized protein MJ1062 OS=Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) OX=243232 GN=MJ1062 PE=1 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000071 | 0.000001 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |