CAZyme Information: MGYG000000993_01238

Basic Information

• Species: Haemophilus_D sp900756155
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Pasteurellaceae; Haemophilus_D; Haemophilus_D sp900756155
• CAZyme ID: MGYG000000993_01238
• CAZy Family: GT2
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
294	MGYG000000993_6|CGC2	33996.12	8.0755

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000993	1983283	MAG	Denmark	Europe

• Gene Location: Start: 53492; End: 54376 Strand: -

Full Sequence      

MDKAFKYDVIVCTFNGASFISSQLESILSQTILPQKIIVSDDGSCDETLSVVRNTFANAN
FTAYDIIQGPRKGVIANFLFALKYSEADFTFLADQDDIWHINKVAEFAKIAKHKDNAIPT
LIFSDACLIDEQNNEISPSFFTYQALSAKCLSDDSILYKNCVQGAACMINRALRNLALDS
LSYIQLSELYMHDWWLALLARYYGETQFIDKPLLDYRQHCQNQVGVFNHKLRLFYYFIRF
KSYWKNIRQAIRQVKMFEQFATQYGKPHCLPPSSKREYQSVPKLKQWLLSLLVK

Enzyme Prediction     

No EC number prediction in MGYG000000993_01238.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd04196	GT_2_like_d	1.93e-82	8	226	1	212	Subfamily of Glycosyltransferase Family GT2 of unknown function. GT-2 includes diverse families of glycosyltransferases 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. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.
cd00761	Glyco_tranf_GTA_type	8.51e-18	9	117	1	108	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.
pfam00535	Glycos_transf_2	1.44e-12	8	125	1	119	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.
COG0463	WcaA	8.93e-12	6	115	4	111	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
cd06420	GT2_Chondriotin_Pol_N	7.72e-07	9	119	1	106	N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase. Chondroitin polymerase is a two domain, bi-functional protein. The N-terminal domain functions as a GalNAc transferase. The bacterial chondroitin polymerase catalyzes elongation of the chondroitin chain by alternatively transferring the GlcUA and GalNAc moiety from UDP-GlcUA and UDP-GalNAc to the non-reducing ends of the chondroitin chain. The enzyme consists of N-terminal and C-terminal domains in which the two active sites catalyze the addition of GalNAc and GlcUA, respectively. Chondroitin chains range from 40 to over 100 repeating units of the disaccharide. Sulfated chondroitins are involved in the regulation of various biological functions such as central nervous system development, wound repair, infection, growth factor signaling, and morphogenesis, in addition to its conventional structural roles. In Caenorhabditis elegans, chondroitin is an essential factor for the worm to undergo cytokinesis and cell division. Chondroitin is synthesized as proteoglycans, sulfated and secreted to the cell surface or extracellular matrix.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QOR17553.1	6.68e-205	1	294	1	294
AGO01101.1	8.03e-205	1	294	6	299
QTO00968.1	1.33e-192	7	294	4	291
ACX83064.1	1.32e-148	5	294	5	290
BAA28140.1	1.32e-148	5	294	5	290

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P37783	8.27e-12	11	225	1	212	dTDP-rhamnosyl transferase RfbG OS=Shigella flexneri OX=623 GN=rfbG PE=3 SV=1
Q0P9C6	1.45e-06	6	159	3	144	GalNAc(5)-diNAcBac-PP-undecaprenol beta-1,3-glucosyltransferase OS=Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168) OX=192222 GN=pglI 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
1.000053	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000993_01238.