CAZyme Information: MGYG000004851_01278

Basic Information

• Species: Nitratidesulfovibrio vulgaris
• Lineage: Bacteria; Desulfobacterota; Desulfovibrionia; Desulfovibrionales; Desulfovibrionaceae; Nitratidesulfovibrio; Nitratidesulfovibrio vulgaris
• CAZyme ID: MGYG000004851_01278
• CAZy Family: GT4
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
353		38272.22	6.5821

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004851	3102739	MAG	China	Asia

• Gene Location: Start: 2175; End: 3236 Strand: +

Full Sequence      

MRTRIFIPPLPRMSGGLAVLYRMASHLHQAGHDVALVPRDTAPCLDEAARELPVVSWESI
DLSGDDLWLVPEGWVNALAPGLKAGARNVVYVQNWAYLLSALPSGVQWPQLDVSFMAVSD
PVAWFTRETTGREAVVLRPGIDTALFHPARPDDTDVCPPRDRIRVCWMPRKNKALAIQIR
AILEARLSLAPPCGSAGPLPVEWVEIHGLRQPEVAAALRSAHIFLATGFPEGCPLPPLEA
MASGALVVGFAGMGGWDYMRQAMPGGYLPWYILREVPWGGNGLFAADADVTGAAFALEHA
IRMIAAADPRVDALRKAGLHTAATYDLAAQRDALLALWTRAAEGDLFHAARRP

Enzyme Prediction     

No EC number prediction in MGYG000004851_01278.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd03801	GT4_PimA-like	4.57e-22	5	338	4	365	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	4.50e-08	1	344	1	380	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
pfam13692	Glyco_trans_1_4	8.50e-08	204	305	58	137	Glycosyl transferases group 1.
cd03809	GT4_MtfB-like	7.01e-05	169	248	203	297	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.
cd01635	Glycosyltransferase_GTB-type	2.65e-04	5	258	3	225	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
ADP88100.1	1.91e-261	1	353	1	353
ABM27210.1	2.09e-252	1	353	60	412
ABB36876.1	2.43e-141	1	347	1	342
BBD08803.1	9.32e-128	2	340	3	333
ADU61252.1	2.05e-117	1	338	4	327

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
0.999943	0.000110	0.000002	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004851_01278.