CAZyme Information: MGYG000001500_03317

Basic Information

• Species: Lawsonibacter asaccharolyticus
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Oscillospiraceae; Lawsonibacter; Lawsonibacter asaccharolyticus
• CAZyme ID: MGYG000001500_03317
• CAZy Family: GT2
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
366	MGYG000001500_10|CGC9	42102.44	5.096

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001500	3446570	Isolate	not provided	not provided

• Gene Location: Start: 3208075; End: 3209175 Strand: +

Full Sequence      

MRIAVYAICKNESQFVDRWMDSMSEADQVVVLDTGSTDDTVERLKKRGAQVTVELISPWR
FDVARNRSLDLVSEDTDICVCTDLDEVFHPGWRAALERAWQPGAGQATYRYTWSFNPDGS
EGVVFWYEKAHARYGYQWIHPVHEVLKWVGEGVPGPTVTVEGMQLDHHPDPTKSRGQYLP
LLELSVEEEPEDDRNTHYLGREYMYRGRWDDCIRTLEHHLSMPTATWKDERAASMRYIAL
SWLRKGDRARARDWYLRAIAEAPHLREPYMDLARMLYDMEEWDGVLYFTGCALSITIRPK
TYICEADSWGSLPHDLRCQALFQTGRRALALDEARAALACAPSDPRLRGNVAVLEQLLGE
TERSAP

Enzyme Prediction     

No EC number prediction in MGYG000001500_03317.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd02511	Beta4Glucosyltransferase	1.72e-11	2	169	1	165	UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of lipooligosaccharide. UDP-glucose: lipooligosaccharide (LOS) beta-1-4-glucosyltransferase catalyzes the addition of the first residue, glucose, of the lacto-N-neotetrase structure to HepI of the LOS inner core. LOS is the major constituent of the outer leaflet of the outer membrane of gram-positive bacteria. It consists of a short oligosaccharide chain of variable composition (alpha chain) attached to a branched inner core which is lined in turn to lipid A. Beta 1,4 glucosyltransferase is required to attach the alpha chain to the inner core.
COG0463	WcaA	5.96e-08	1	99	3	107	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
cd00761	Glyco_tranf_GTA_type	2.59e-07	9	139	5	143	Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold. Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.
sd00006	TPR	1.91e-06	197	283	5	86	Tetratricopeptide repeat. The Tetratricopeptide repeat (TPR) typically contains 34 amino acids and is found in a variety of organisms including bacteria, cyanobacteria, yeast, fungi, plants, and humans. It is present in a variety of proteins including those involved in chaperone, cell-cycle, transcription, and protein transport complexes. The number of TPR motifs varies among proteins. Those containing 5-6 tandem repeats generate a right-handed helical structure with an amphipathic channel that is thought to accommodate an alpha-helix of a target protein. It has been proposed that TPR proteins preferentially interact with WD-40 repeat proteins, but in many instances several TPR-proteins seem to aggregate to multi-protein complexes.
TIGR02917	PEP_TPR_lipo	3.52e-05	198	365	95	250	putative PEP-CTERM system TPR-repeat lipoprotein. This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ANU42689.1	3.85e-180	1	354	1	354
QQR04409.1	3.85e-180	1	354	1	354
QIA29496.1	2.22e-179	1	354	1	354
AQS58818.1	2.30e-143	1	355	4	357
QNK42027.1	4.01e-143	2	361	5	363

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9XC90	1.12e-08	2	140	4	148	Lipopolysaccharide core biosynthesis glycosyltransferase WaaE OS=Klebsiella pneumoniae OX=573 GN=waaE PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000062	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001500_03317.