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CAZyme Information: MGYG000001173_00338

You are here: Home > Sequence: MGYG000001173_00338

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 Collinsella sp900759335
Lineage Bacteria; Actinobacteriota; Coriobacteriia; Coriobacteriales; Coriobacteriaceae; Collinsella; Collinsella sp900759335
CAZyme ID MGYG000001173_00338
CAZy Family GT0
CAZyme Description 3-deoxy-manno-octulosonate cytidylyltransferase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
549 60903.46 4.7228
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001173 2216826 MAG Austria Europe
Gene Location Start: 3652;  End: 5301  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001173_00338.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd02513 CMP-NeuAc_Synthase 1.09e-73 7 221 1 220
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 1.85e-58 8 228 4 226
CMP-N-acetylneuraminic acid synthetase [Cell wall/membrane/envelope biogenesis].
COG3980 SpsG 1.19e-30 228 479 2 258
Spore coat polysaccharide biosynthesis protein SpsG, predicted glycosyltransferase [Cell wall/membrane/envelope biogenesis].
pfam02348 CTP_transf_3 1.72e-20 9 137 1 121
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.
cd02517 CMP-KDO-Synthetase 3.13e-13 7 152 1 135
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ACV55877.1 7.31e-239 7 549 6 548
API89863.1 1.73e-163 7 545 2 542
QGS37541.1 1.83e-160 1 547 1 553
AMB95295.1 3.74e-160 7 545 2 543
AMB92172.1 4.85e-158 8 545 3 543

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1QWJ_A 6.13e-22 6 226 2 222
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 3.83e-20 9 229 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 2.38e-18 9 228 6 227
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 2.73e-17 9 228 6 227
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
Q45982 7.28e-26 8 229 4 230
Post-translational flagellin modification protein B OS=Campylobacter coli OX=195 GN=ptmB PE=3 SV=1
Q58462 6.03e-24 228 479 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
Q0P8U6 3.03e-22 9 234 4 227
Pseudaminic acid cytidylyltransferase OS=Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168) OX=192222 GN=pseF PE=3 SV=1
Q57140 9.55e-22 9 227 8 227
Probable N-acylneuraminate cytidylyltransferase OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=neuA PE=3 SV=1
Q0E671 1.04e-21 2 285 27 311
N-acylneuraminate cytidylyltransferase A OS=Danio rerio OX=7955 GN=cmasa 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
1.000041 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001173_00338.