CAZyme Information: MGYG000002006_01756

Basic Information

• Species: Lawsonibacter sp900754605
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Oscillospiraceae; Lawsonibacter; Lawsonibacter sp900754605
• CAZyme ID: MGYG000002006_01756
• CAZy Family: GT2
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
366		42617.31	5.6963

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002006	3005540	MAG	Spain	Europe

• Gene Location: Start: 16989; End: 18089 Strand: -

Full Sequence      

MGNCKVCVYAICKNEEKFVDRWMDSMGEADLVVVLDTGSKDGTVERLRARGAQVTEEQIQ
PWRFDAARNRSLELIPEDVDLCVCTDLDEVFHPGWREALERAWKPGCNRVSYRYTWSFQQ
DGSEGVVFWSDKIHARRGYRWVHPVHEVLQWVEAGAPGPTVAAEGIQLDHHPDPEKSRGQ
YLPLLELSVEEDPEDDRNMHYLGREYLFRGQWEDSIRTLKRHLAMPKAVWRDERAASMRF
LARACLALSRQSEALEWYLRAAAEAPYLREPWVELARLLYQREEWDGVLYATGQALTIRE
RPRTYICEPEAWGSLPYDLRCQAFYHTGRIALALEEARQALVLSPTNLRLQKNMRLLERQ
LEANRV

Enzyme Prediction     

No EC number prediction in MGYG000002006_01756.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd02511	Beta4Glucosyltransferase	1.93e-13	5	172	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	5.51e-07	5	102	4	107	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
cd00761	Glyco_tranf_GTA_type	4.06e-06	6	99	3	98	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	4.42e-06	199	286	4	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.
sd00006	TPR	1.54e-04	235	341	1	96	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ANU42689.1	4.92e-176	5	354	2	351
QQR04409.1	4.92e-176	5	354	2	351
QIA29496.1	5.71e-175	5	354	2	351
AQS58818.1	4.26e-146	1	364	1	363
CAB1239995.1	8.62e-145	1	361	1	360

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

has no Swissprot hit.

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
1.000078	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002006_01756.