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CAZyme Information: MGYG000002031_00237

You are here: Home > Sequence: MGYG000002031_00237

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 UBA5905 sp900549155
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; UBA5905; UBA5905 sp900549155
CAZyme ID MGYG000002031_00237
CAZy Family GT0
CAZyme Description 3-deoxy-manno-octulosonate cytidylyltransferase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
543 61243.09 5.6543
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002031 2138143 MAG Spain Europe
Gene Location Start: 122245;  End: 123876  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002031_00237.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd02513 CMP-NeuAc_Synthase 6.78e-71 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 9.51e-53 1 222 2 226
CMP-N-acetylneuraminic acid synthetase [Cell wall/membrane/envelope biogenesis].
TIGR03590 PseG 7.55e-36 222 473 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.
COG3980 SpsG 3.45e-29 222 519 2 301
Spore coat polysaccharide biosynthesis protein SpsG, predicted glycosyltransferase [Cell wall/membrane/envelope biogenesis].
pfam02348 CTP_transf_3 5.69e-18 4 139 1 129
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 7.53e-193 3 541 7 546
API89863.1 2.67e-179 1 540 1 543
QGS37541.1 1.26e-177 1 541 6 553
AMB92172.1 1.03e-176 1 539 1 543
AMB95295.1 4.14e-176 1 539 1 543

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6IFD_A 5.88e-28 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]
1QWJ_A 2.72e-23 5 218 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]
4FCU_A 1.75e-06 6 118 5 110
ChainA, 3-deoxy-manno-octulosonate cytidylyltransferase [Acinetobacter baumannii ATCC 17978]
3POL_A 2.07e-06 6 118 28 133
ChainA, 3-deoxy-manno-octulosonate cytidylyltransferase [Acinetobacter baumannii ATCC 17978]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q58462 3.03e-28 222 476 2 275
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 1.18e-27 2 221 3 233
Post-translational flagellin modification protein B OS=Campylobacter coli OX=195 GN=ptmB PE=3 SV=1
Q0P8U6 3.50e-26 1 210 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 2.29e-25 1 210 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 1.31e-22 5 239 47 292
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
1.000049 0.000004 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002031_00237.