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CAZyme Information: MGYG000002355_02522
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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 | Clostridium_F botulinum | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium_F; Clostridium_F botulinum | |||||||||||
| CAZyme ID | MGYG000002355_02522 | |||||||||||
| 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: 2281056; End: 2282717 Strand: - | |||||||||||
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd02513 | CMP-NeuAc_Synthase | 1.34e-77 | 6 | 222 | 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 | 1.41e-43 | 5 | 226 | 2 | 226 | CMP-N-acetylneuraminic acid synthetase [Cell wall/membrane/envelope biogenesis]. |
| COG3980 | SpsG | 6.88e-39 | 226 | 536 | 2 | 316 | Spore coat polysaccharide biosynthesis protein SpsG, predicted glycosyltransferase [Cell wall/membrane/envelope biogenesis]. |
| TIGR03590 | PseG | 1.35e-36 | 226 | 472 | 1 | 267 | UDP-2,4-diacetamido-2,4,6-trideoxy-beta-L-altropyranose hydrolase. This protein is found in association with enzymes involved in the biosynthesis of pseudaminic acid, a component of polysaccharide in certain Pseudomonas strains as well as a modification of flagellin in Campylobacter and Hellicobacter. The role of this protein is unclear, although it may participate in N-acetylation in conjunction with, or in the absence of PseH (TIGR03585) as it often scores above the trusted cutoff to pfam00583 representing a family of acetyltransferases. |
| pfam02348 | CTP_transf_3 | 5.10e-19 | 8 | 141 | 1 | 127 | 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 |
|---|---|---|---|---|---|
| ADG00373.1 | 0.0 | 1 | 553 | 1 | 553 |
| ABS39440.1 | 0.0 | 1 | 553 | 1 | 553 |
| CBZ04581.1 | 0.0 | 1 | 553 | 1 | 553 |
| APH21287.1 | 0.0 | 1 | 553 | 1 | 553 |
| APQ68618.1 | 0.0 | 1 | 553 | 1 | 553 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 6IFD_A | 3.93e-22 | 2 | 227 | 17 | 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] |
| 1QWJ_A | 2.13e-21 | 7 | 224 | 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] |
| 6CKJ_A | 2.64e-15 | 4 | 226 | 2 | 227 | 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 | 8.88e-15 | 4 | 226 | 2 | 227 | 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 |
|---|---|---|---|---|---|---|
| Q58462 | 3.46e-34 | 226 | 477 | 2 | 274 | 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 |
| Q0E671 | 3.44e-21 | 5 | 279 | 29 | 315 | N-acylneuraminate cytidylyltransferase A OS=Danio rerio OX=7955 GN=cmasa PE=1 SV=1 |
| Q99KK2 | 6.30e-21 | 7 | 313 | 43 | 359 | N-acylneuraminate cytidylyltransferase OS=Mus musculus OX=10090 GN=Cmas PE=1 SV=2 |
| P69060 | 6.30e-21 | 7 | 313 | 43 | 359 | N-acylneuraminate cytidylyltransferase OS=Rattus norvegicus OX=10116 GN=Cmas PE=2 SV=1 |
| Q8NFW8 | 1.55e-20 | 7 | 279 | 45 | 321 | N-acylneuraminate cytidylyltransferase OS=Homo sapiens OX=9606 GN=CMAS PE=1 SV=2 |
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 |
|---|---|---|---|---|---|
| 1.000045 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |