CAZyme Information: MGYG000002897_00964

Basic Information

• Species: Varibaculum cambriense
• Lineage: Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Actinomycetaceae; Varibaculum; Varibaculum cambriense
• CAZyme ID: MGYG000002897_00964
• CAZy Family: GT4
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
385		42453.7	9.366

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002897	2017891	MAG	United States	North America

• Gene Location: Start: 28711; End: 29868 Strand: -

Full Sequence      

MRSNPNILVISFSDIRRDARLLRQLSVVKDFGHVTTLGYGSQPAGSDEHLQIPSNLPSLP
QTVPGVLKLALHLHGASEFAAPALRRARELLQGRQFDLVISNDARALPVAFYAAGDSTPV
WADLHEWAPEERTHITSWRILVAPYIRYICKKYLPRTSSQTTVAGRIAHLYQENFGVQPQ
VMRNSCPFQNLLPTETGSEQIRLVHSGGAVPGRALETTIKAVVAAGERFTLDLYLVPAND
GGKYLRELKSLAEGSPRIVFHDPVKPAELPKTLNQYDVGVFWIPPFNTNARLTLPNKLFD
FVQARLAVAVGPTVEMVDVVKQYNLGIVSAGFTVEQIVESLNTLTTKSIATYKQNVDAAA
RELSFDKDAEVAKGIIGRLLTTNRL

Enzyme Prediction     

No EC number prediction in MGYG000002897_00964.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd03794	GT4_WbuB-like	1.44e-10	56	328	64	343	Escherichia coli WbuB and similar proteins. This family is most closely related to the GT1 family of glycosyltransferases. WbuB in E. coli is involved in the biosynthesis of the O26 O-antigen. It has been proposed to function as an N-acetyl-L-fucosamine (L-FucNAc) transferase.
cd03801	GT4_PimA-like	4.76e-10	65	344	52	330	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.
cd04950	GT4_TuaH-like	1.76e-04	263	376	260	369	teichuronic acid biosynthesis glycosyltransferase TuaH and similar proteins. Members of this family may function in teichuronic acid biosynthesis/cell wall biogenesis. 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
SDT98650.1	1.78e-156	1	380	1	380
QPZ39397.1	3.14e-154	3	381	2	379
QYB16409.1	1.48e-150	3	380	2	379
ATG53173.1	1.53e-150	9	380	1	371
QHO91465.1	3.62e-142	1	379	1	379

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
1.000082	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002897_00964.