CAZyme Information: MGYG000000633_01064

Basic Information

• Species: Victivallis sp900768515
• Lineage: Bacteria; Verrucomicrobiota; Lentisphaeria; Victivallales; Victivallaceae; Victivallis; Victivallis sp900768515
• CAZyme ID: MGYG000000633_01064
• CAZy Family: GT4
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
348	MGYG000000633_10|CGC2	39530.58	8.8904

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000633	2845403	MAG	Madagascar	Africa

• Gene Location: Start: 59071; End: 60117 Strand: -

Full Sequence      

MNIPLGICTRYDRLGASSRCRYYQYEDAFRKEGFLPEFHPFFPNRYLEKLYAGNGRSRRS
ALAACFRRFQDSFRFPERLLIEYELLPGLPAAVELVLIGKRRFVLNYDDDVWVRYAGKPF
LENKYDTLIRHAAGVVTANTLLEKRAQALCPNVIKVPTAVDLDDYTPEKFPKFPRFTVVW
IGTPVTYAYLEQAAEALRSMAQHTDFELLVIARRSLEARAIPGVPMRFEEWSPENEAELL
CRSHVGIMPLPAEDPFARGKSAFKLIQYMAAGIPAIASGVGENRRVLLHGETGFLADTPA
EWNAALLCLAGDDGCRNRMAAAARRRAFEYSTQKYAPILTGFLRRTLL

Enzyme Prediction     

No EC number prediction in MGYG000000633_01064.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd03801	GT4_PimA-like	3.57e-13	28	313	38	334	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.
COG0438	RfaB	1.23e-09	1	313	1	343	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
pfam13692	Glyco_trans_1_4	2.23e-09	175	312	1	138	Glycosyl transferases group 1.
cd03794	GT4_WbuB-like	2.78e-08	120	312	155	362	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.
cd01635	Glycosyltransferase_GTB-type	8.02e-07	87	295	66	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AVM46441.1	7.61e-147	1	347	1	345
QSH42203.1	2.55e-98	5	344	3	341
ASG22108.1	2.84e-62	4	343	11	366
QXG82513.1	5.09e-58	3	344	2	348
ABC24599.1	5.09e-58	3	344	2	348

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
1.000032	0.000002	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000633_01064.