CAZyme Information: MGYG000001507_01623

Basic Information

• Species: Paenibacillus ihuae
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus; Paenibacillus ihuae
• CAZyme ID: MGYG000001507_01623
• CAZy Family: GT4
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
335		38268.19	7.0909

Genome Property

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

• Gene Location: Start: 1770286; End: 1771293 Strand: -

Full Sequence      

MSCRRGGDISYEVHSTVHRTNHTVLRESDFPASDIIVSNFYTTVSVSEAASLNGKGMHVR
LSLCYEPLFLPDNSVSFPSYNTTSRLIVLSEWQREIIALNHGITGSIVPVGISSSFSNRH
IRHRLQEPMNITAILRKVENGFSWHREQDYLVRQLDIVKQNLPDVKINFISPPDEFYSSE
SLQNMKASGKYRFFTPQNDEELCYHYNGADIFVSSSIFDSGSLPGLEAMRCGAAFVTVYS
GGNMEYARHEENCLLSYRYENRLAEDIIRLVRDHVLRIRLASQGEADSKSWTWENSVRIM
ERTVTHFLQGIPFVDPPRSVQAMLRRTDSMPTTRK

Enzyme Prediction     

No EC number prediction in MGYG000001507_01623.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT4	142	278	4.4e-17	0.8625

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd03801	GT4_PimA-like	2.89e-21	80	302	138	363	phosphatidyl-myo-inositol mannosyltransferase. This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.
pfam00534	Glycos_transf_1	1.90e-14	142	285	11	156	Glycosyl transferases group 1. Mutations in this domain of PIGA lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.
COG0438	RfaB	8.64e-14	80	310	148	380	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
cd01635	Glycosyltransferase_GTB-type	1.02e-09	108	255	81	234	glycosyltransferase family 1 and related proteins with GTB topology. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.
cd03809	GT4_MtfB-like	5.18e-09	85	301	141	361	glycosyltransferases MtfB, WbpX, and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. MtfB (mannosyltransferase B) in E. coli has been shown to direct the growth of the O9-specific polysaccharide chain. It transfers two mannoses into the position 3 of the previously synthesized polysaccharide.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QSF46890.1	3.09e-232	6	335	40	369
AIQ46642.1	3.30e-192	7	310	41	344
CQR55119.1	6.20e-181	6	326	40	358
QUL57251.1	8.07e-179	6	319	40	353
AIQ73748.1	6.58e-165	7	308	41	342

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
0.999948	0.000082	0.000007	0.000000	0.000000	0.000002

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001507_01623.