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CAZyme Information: MGYG000004265_01119

You are here: Home > Sequence: MGYG000004265_01119

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 UMGS263 sp900540535
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; UMGS263; UMGS263 sp900540535
CAZyme ID MGYG000004265_01119
CAZy Family GT0
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
542 61575.29 4.8961
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004265 2478899 MAG China Asia
Gene Location Start: 176476;  End: 178104  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004265_01119.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd02513 CMP-NeuAc_Synthase 5.46e-75 2 217 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 4.84e-57 1 220 2 225
CMP-N-acetylneuraminic acid synthetase [Cell wall/membrane/envelope biogenesis].
COG3980 SpsG 4.49e-28 221 541 2 309
Spore coat polysaccharide biosynthesis protein SpsG, predicted glycosyltransferase [Cell wall/membrane/envelope biogenesis].
pfam02348 CTP_transf_3 4.14e-18 4 180 1 166
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.
PRK13368 PRK13368 5.34e-11 1 124 1 114
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ACV55877.1 7.13e-183 2 542 6 546
API89863.1 3.37e-164 1 541 1 543
AMB92172.1 8.69e-157 1 541 1 544
AMB95295.1 1.40e-155 1 541 1 544
QGS37541.1 5.70e-152 1 542 6 553

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6IFD_A 2.05e-27 4 222 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 7.26e-26 2 215 3 218
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 4.41e-13 4 220 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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q0P8U6 1.85e-26 1 209 1 216
Pseudaminic acid cytidylyltransferase OS=Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168) OX=192222 GN=pseF PE=3 SV=1
Q2M5Q2 4.27e-25 1 209 1 216
Pseudaminic acid cytidylyltransferase OS=Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176) OX=354242 GN=pseF PE=3 SV=1
Q8NFW8 6.05e-25 2 278 44 325
N-acylneuraminate cytidylyltransferase OS=Homo sapiens OX=9606 GN=CMAS PE=1 SV=2
Q5R6R5 6.05e-25 2 278 44 325
N-acylneuraminate cytidylyltransferase OS=Pongo abelii OX=9601 GN=CMAS PE=2 SV=1
P69060 1.97e-24 2 278 42 323
N-acylneuraminate cytidylyltransferase OS=Rattus norvegicus OX=10116 GN=Cmas PE=2 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
1.000062 0.000001 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004265_01119.