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CAZyme Information: MGYG000002422_00195

You are here: Home > Sequence: MGYG000002422_00195

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 Campylobacter_D jejuni
Lineage Bacteria; Campylobacterota; Campylobacteria; Campylobacterales; Campylobacteraceae; Campylobacter_D; Campylobacter_D jejuni
CAZyme ID MGYG000002422_00195
CAZy Family GT82
CAZyme Description 3-deoxy-manno-octulosonate cytidylyltransferase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
536 MGYG000002422_1|CGC1 62548.31 8.9724
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002422 1714563 Isolate United Kingdom Europe
Gene Location Start: 189358;  End: 190968  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 2.4.1.-

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT82 20 309 1.3e-141 0.9356913183279743

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam06306 CgtA 3.78e-99 21 310 52 346
Beta-1,4-N-acetylgalactosaminyltransferase (CgtA). This family consists of several beta-1,4-N-acetylgalactosaminyltransferase proteins from Campylobacter jejuni.
COG1083 NeuA 6.64e-99 319 536 5 224
CMP-N-acetylneuraminic acid synthetase [Cell wall/membrane/envelope biogenesis].
cd02513 CMP-NeuAc_Synthase 4.80e-80 317 533 1 222
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.
pfam02348 CTP_transf_3 4.15e-17 319 439 1 119
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.
COG1861 SpsF 2.78e-07 315 383 1 73
Spore coat polysaccharide biosynthesis protein SpsF, cytidylyltransferase family [Cell wall/membrane/envelope biogenesis].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QEP94056.1 0.0 1 536 1 536
ACK29133.1 0.0 1 536 1 536
ATE69119.1 0.0 1 536 1 536
ACE35490.1 0.0 1 536 1 536
AFU43195.1 0.0 1 536 1 536

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6IFD_A 7.37e-46 319 530 23 240
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 3.93e-38 316 533 3 222
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 1.42e-36 316 533 3 222
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]
1QWJ_A 7.38e-11 320 526 6 212
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P0A0Z8 2.15e-37 316 533 3 222
N-acylneuraminate cytidylyltransferase OS=Neisseria meningitidis OX=487 GN=neuA PE=1 SV=1
P0A0Z7 2.15e-37 316 533 3 222
N-acylneuraminate cytidylyltransferase OS=Neisseria meningitidis serogroup B (strain MC58) OX=122586 GN=neuA PE=1 SV=1
P13266 4.43e-36 319 528 6 215
N-acylneuraminate cytidylyltransferase OS=Escherichia coli OX=562 GN=neuA PE=1 SV=1
Q57140 1.91e-33 319 533 8 223
Probable N-acylneuraminate cytidylyltransferase OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=neuA PE=3 SV=1
Q9AFG9 5.60e-28 319 530 4 217
N-acylneuraminate cytidylyltransferase OS=Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R) OX=208435 GN=neuA PE=3 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
1.000003 0.000030 0.000002 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002422_00195.