CAZyme Information: MGYG000001507_05444

Basic Information

• Species: Paenibacillus ihuae
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus; Paenibacillus ihuae
• CAZyme ID: MGYG000001507_05444
• CAZy Family: GT2
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
302	MGYG000001507_5|CGC2	34329.78	9.6188

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001507	6631509	Isolate	not provided	not provided

• Gene Location: Start: 82714; End: 83622 Strand: +

Full Sequence      

MQGLSVAICTRNRVQDLTRCIHSITKQSIGRTYPIEVIIIDDGEIPKEVLNNFEALLAAS
GYPLIYFSKITDRGLWMSRIKAVELSNMDKILFLDDDVEIPGHYLATLYQTYLDHPNCAG
VGGVAIGMRNSFLGTIRCLLSFQQSLSSGKLSLSGQAGSMYNWHKARKIFKTEFQHGCNM
SFKKEAIRDLQPVPWLKSYSVGEDILMSRIARRTGPLYINPELKLLHHESPASRDNLEDV
AYTRVLNHVHLLKDERSGPIGYLALIWTTLYLILREQPKKNFPAIRGYKKGLREIFSRQT
AR

Enzyme Prediction     

No EC number prediction in MGYG000001507_05444.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT2	5	131	1.2e-16	0.7235294117647059

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00761	Glyco_tranf_GTA_type	3.50e-18	6	128	1	118	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	5	124	1	114	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.
pfam13641	Glyco_tranf_2_3	2.61e-09	4	215	4	198	Glycosyltransferase like family 2. Members of this family of prokaryotic proteins include putative glucosyltransferase, which are involved in bacterial capsule biosynthesis.
COG0463	WcaA	4.02e-08	1	105	2	101	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
cd06420	GT2_Chondriotin_Pol_N	5.34e-08	6	188	1	140	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
QSF45363.1	1.43e-219	1	302	1	302
AIQ15488.1	1.56e-200	1	301	1	300
AIQ66475.1	5.20e-199	1	301	1	300
QQZ62854.1	2.12e-198	1	301	1	300
CQR51605.1	2.12e-198	1	301	1	300

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
1.000068	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001507_05444.