CAZyme Information: MGYG000002414_05124

Basic Information

• Species: Paenibacillus odorifer
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus; Paenibacillus odorifer
• CAZyme ID: MGYG000002414_05124
• CAZy Family: GT2
• CAZyme Description: putative protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
245		29273.89	5.3785

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002414	6802552	Isolate	South Korea	Asia

• Gene Location: Start: 5762407; End: 5763144 Strand: -

Full Sequence      

MSSHRGPLRKTSGNRLTAIMQVRNEAGRYLEQVLEELSELVDDIVIVDDGSTDNTAQLCL
SFAKVKKLVTLQSSLFNREWELRQTLWELAVSTNPDWLLSVDADEFYEESAKREMRRLID
QDVYDWVSFRLFDFWGGTTHYREDEHWNIHTKHTRTLVRYLPNFHYFFPKMDHHVPRLPL
SYSVLPGFLTELRVKHYGWAISPEELRRKYSRYLELDPEGRWGSLEQYESILDEQPHLVE
WQEEH

Enzyme Prediction     

No EC number prediction in MGYG000002414_05124.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd02511	Beta4Glucosyltransferase	4.54e-19	15	227	1	198	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.
pfam00535	Glycos_transf_2	3.52e-11	17	171	1	156	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	4.17e-08	18	122	1	105	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.
COG0463	WcaA	4.19e-08	15	211	4	199	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
cd04179	DPM_DPG-synthase_like	2.73e-07	22	71	5	58	DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily. DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. The UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate. This protein family belongs to Glycosyltransferase 2 superfamily.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AWV35702.1	6.68e-185	1	245	1	245
AIQ76415.1	2.24e-183	1	245	1	245
AIQ37755.1	1.44e-172	3	244	2	243
AIQ25952.1	7.73e-170	1	243	1	243
AIQ54712.1	4.88e-158	7	242	6	241

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P0A5H2	1.61e-09	15	223	2	213	Uncharacterized protein Mb3815c OS=Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97) OX=233413 GN=BQ2027_MB3815C PE=3 SV=1
P9WKW8	1.61e-09	15	223	2	213	Uncharacterized protein MT3894 OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=MT3894 PE=3 SV=1
P9WKW9	1.61e-09	15	223	2	213	Uncharacterized protein Rv3786c OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=Rv3786c PE=1 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
1.000058	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002414_05124.