CAZyme Information: MGYG000001676_00024

Basic Information

• Species: RUG705 sp900759875
• Lineage: Bacteria; Firmicutes; Bacilli; RF39; UBA660; RUG705; RUG705 sp900759875
• CAZyme ID: MGYG000001676_00024
• CAZy Family: GT2
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
357		42966.85	6.6072

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001676	1153275	MAG	United States	North America

• Gene Location: Start: 22712; End: 23785 Strand: +

Full Sequence      

MTKYKICVYAICKNEEKFVDRWVKSMMEADDIYVLDTGSTDNTVKKLEEYNVHVSKDIIK
PWRFDVARNKSLELIPNKYDIYVCTDLDEVFLPGWRKHLEENWSKDYTRARYNYNWSLDK
DNKPLVNFYLDKIHIYGYKWVNPVHEVLCYDELEKYLTIDEIVLNHYPDSSKSRSSYLPL
LELSVKEDSDNDRNMHYLGREYMYYKRWNECIDTLKKHLSMKKATWKDERCASMRFIARS
YIALGDRNLAREWYKKAIREAPYLRDAYVELGILDYQYENYEAAIYYLEKALLIKGNRKS
YINEIFSYNETPYDILSICYYNLGDYERAYTNVLKAYEINSNDERIKNNLNIIKGAL

Enzyme Prediction     

No EC number prediction in MGYG000001676_00024.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd02511	Beta4Glucosyltransferase	2.92e-12	5	168	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.
sd00006	TPR	5.53e-09	237	338	7	97	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.
cd00761	Glyco_tranf_GTA_type	3.61e-06	6	95	3	94	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.
COG2956	YciM	1.12e-05	202	344	151	283	Lipopolysaccharide biosynthesis regulator YciM, contains six TPR domains and a predicted metal-binding C-terminal domain [Cell wall/membrane/envelope biogenesis].
sd00006	TPR	1.22e-05	266	350	2	75	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
AQS58819.1	1.71e-126	1	357	1	360
QOX65321.1	2.52e-125	1	357	1	360
CAB1239995.1	9.21e-125	1	357	1	360
QHQ60865.1	2.45e-124	1	357	1	360
QAT50106.1	1.47e-122	1	354	1	357

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
1.000029	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001676_00024.