CAZyme Information: MGYG000001897_00625

Basic Information

• Lineage: Bacteria; Firmicutes; Bacilli; RF39; UBA660; CAG-1000
• CAZyme ID: MGYG000001897_00625
• CAZy Family: GT2
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
355		42659.5	9.6917

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001897	1342627	MAG	Denmark	Europe

• Gene Location: Start: 17635; End: 18702 Strand: -

Full Sequence      

MKKYKICIYAICKNESKFIKRWYESIKGADYICVLDTGSEDDSLKILKSLNIKVKQKLIK
PWRFDVARNESLKLIPKDADICICLDLDEIMLPGWKDELLKIWNNDITRVSYKYNWSLDK
NDKPIISFYANKIHKNNYYKWTHPVHEILISLKEEKSVTSNNITINHYPDNTKSRSNYLP
LLELSVKEDPTDDRNMHYLGREYMYYRKWNKCIDTLIKHLALPSSTWKDERCASMRFIAT
SYINLKRYDEARMWLDKAMKEAPYLRDAFTERMILEYNLKKYEESIKYGKKALKIKTRVY
TYINSEHSWNETIYDIMSINYYMIGNKKEGLKYLNKALKINPNNERIKNNKKYFM

Enzyme Prediction     

No EC number prediction in MGYG000001897_00625.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd02511	Beta4Glucosyltransferase	2.81e-13	5	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.
sd00006	TPR	3.69e-08	238	339	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.
pfam00535	Glycos_transf_2	2.98e-07	7	146	1	150	Glycosyl transferase family 2. Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.
cd00761	Glyco_tranf_GTA_type	2.18e-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.
sd00006	TPR	3.31e-05	267	351	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
QOX65321.1	1.16e-115	1	352	1	354
AQS58819.1	1.68e-113	1	350	1	352
AQS58818.1	2.23e-113	1	350	1	352
QHQ60865.1	1.27e-108	1	350	1	352
QAT50106.1	3.22e-108	1	350	1	352

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
1.000032	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001897_00625.