Species | RUG115 sp900066395 | |||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; RUG115; RUG115 sp900066395 | |||||||||||
CAZyme ID | MGYG000000154_02445 | |||||||||||
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: 599458; End: 601089 Strand: + |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd02513 | CMP-NeuAc_Synthase | 2.09e-77 | 1 | 214 | 1 | 221 | 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 | 3.61e-56 | 3 | 219 | 5 | 225 | CMP-N-acetylneuraminic acid synthetase [Cell wall/membrane/envelope biogenesis]. |
COG3980 | SpsG | 3.99e-33 | 220 | 495 | 2 | 279 | Spore coat polysaccharide biosynthesis protein SpsG, predicted glycosyltransferase [Cell wall/membrane/envelope biogenesis]. |
TIGR03590 | PseG | 1.29e-30 | 220 | 473 | 1 | 272 | 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 | 6.31e-23 | 3 | 209 | 1 | 195 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
ACV55877.1 | 4.63e-199 | 2 | 541 | 7 | 546 |
AMB92172.1 | 1.23e-195 | 2 | 540 | 3 | 544 |
AMB95295.1 | 6.11e-191 | 2 | 540 | 3 | 544 |
API89863.1 | 3.35e-185 | 2 | 539 | 3 | 542 |
QGS37541.1 | 2.21e-178 | 2 | 542 | 8 | 554 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6IFD_A | 1.22e-28 | 3 | 221 | 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] |
1QWJ_A | 2.26e-24 | 4 | 216 | 6 | 220 | 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 | 9.08e-17 | 3 | 219 | 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 | 2.57e-15 | 3 | 219 | 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] |
4FCU_A | 7.27e-07 | 5 | 118 | 5 | 111 | ChainA, 3-deoxy-manno-octulosonate cytidylyltransferase [Acinetobacter baumannii ATCC 17978] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q58462 | 2.35e-30 | 220 | 473 | 2 | 272 | 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 |
Q45982 | 3.90e-30 | 2 | 221 | 4 | 230 | Post-translational flagellin modification protein B OS=Campylobacter coli OX=195 GN=ptmB PE=3 SV=1 |
Q90WG6 | 7.24e-26 | 2 | 283 | 32 | 317 | N-acylneuraminate cytidylyltransferase OS=Oncorhynchus mykiss OX=8022 GN=cmas PE=2 SV=1 |
Q0P8U6 | 1.23e-25 | 3 | 208 | 4 | 216 | Pseudaminic acid cytidylyltransferase OS=Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168) OX=192222 GN=pseF PE=3 SV=1 |
P69060 | 1.98e-24 | 4 | 309 | 45 | 359 | N-acylneuraminate cytidylyltransferase OS=Rattus norvegicus OX=10116 GN=Cmas PE=2 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
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1.000043 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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