CAZyme Information: MGYG000001265_01750

Basic Information

• Species: Methylobacterium sp002778835
• Lineage: Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Beijerinckiaceae; Methylobacterium; Methylobacterium sp002778835
• CAZyme ID: MGYG000001265_01750
• CAZy Family: GT4
• CAZyme Description: D-inositol-3-phosphate glycosyltransferase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
132	MGYG000001265_105|CGC1	13838.56	4.44

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001265	4213059	MAG	Italy	Europe

• Gene Location: Start: 8950; End: 9348 Strand: -

Full Sequence      

MLSPFVRDPSPLYRWADVVVVPSQRPESLGRVAIEAMSYGIPPVVSRIGGLTETVEDGRS
GWVVEPGDADSLSATLARIVAEPEAWRSYPAAAHARYESVFSEAAAAEGIGAVLREAGLA
CVTESPSAGARA

Enzyme Prediction     

No EC number prediction in MGYG000001265_01750.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT4	9	87	2.9e-21	0.48125

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd03823	GT4_ExpE7-like	2.10e-24	8	96	253	341	glycosyltransferase ExpE7 and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. ExpE7 in Sinorhizobium meliloti has been shown to be involved in the biosynthesis of galactoglucans (exopolysaccharide II).
cd03801	GT4_PimA-like	4.28e-22	11	102	263	353	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	6.62e-22	12	84	75	146	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.
cd03808	GT4_CapM-like	6.79e-21	5	102	253	349	capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. CapM in Staphylococcus aureus is required for the synthesis of type 1 capsular polysaccharides.
COG0438	RfaB	1.32e-20	12	102	273	362	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ACB27303.1	4.35e-44	2	115	283	396
QGY02674.1	4.79e-44	2	115	289	402
QEE42856.1	8.50e-44	2	115	264	377
AWV19269.1	1.35e-43	2	115	253	366
APT33945.1	1.65e-43	2	115	263	376

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6KIH_A	1.53e-10	13	116	321	423	Sucrose-phosphatesynthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_B Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_C Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_D Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_E Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_F Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_G Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_H Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_I Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_J Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_K Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_L Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus]
6N1X_A	6.01e-09	10	80	268	337	ChainA, Glycosyltransferase [Staphylococcus aureus subsp. aureus CN1]
6D9T_A	6.11e-09	10	80	284	353	BshAfrom Staphylococcus aureus complexed with UDP [Staphylococcus aureus]
2R60_A	1.03e-07	27	116	369	458	Structureof apo Sucrose Phosphate Synthase (SPS) of Halothermothrix orenii [Halothermothrix orenii],2R66_A Complex Structure of Sucrose Phosphate Synthase (SPS)-F6P of Halothermothrix orenii [Halothermothrix orenii H 168],2R68_A Complex Structure of Sucrose Phosphate Synthase (SPS)-S6P of Halothermothrix orenii [Halothermothrix orenii H 168]
5D00_A	1.33e-07	12	102	271	360	Crystalstructure of BshA from B. subtilis complexed with N-acetylglucosaminyl-malate and UMP [Bacillus subtilis subsp. subtilis str. 168],5D00_B Crystal structure of BshA from B. subtilis complexed with N-acetylglucosaminyl-malate and UMP [Bacillus subtilis subsp. subtilis str. 168],5D01_A Crystal structure of BshA from B. subtilis complexed with N-acetylglucosaminyl-malate [Bacillus subtilis subsp. subtilis str. 168],5D01_B Crystal structure of BshA from B. subtilis complexed with N-acetylglucosaminyl-malate [Bacillus subtilis subsp. subtilis str. 168]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
D7AW65	2.01e-11	13	88	315	388	D-inositol 3-phosphate glycosyltransferase OS=Nocardiopsis dassonvillei (strain ATCC 23218 / DSM 43111 / CIP 107115 / JCM 7437 / KCTC 9190 / NBRC 14626 / NCTC 10488 / NRRL B-5397 / IMRU 509) OX=446468 GN=mshA PE=3 SV=1
C7QKE8	1.13e-09	13	76	309	374	D-inositol 3-phosphate glycosyltransferase 2 OS=Catenulispora acidiphila (strain DSM 44928 / JCM 14897 / NBRC 102108 / NRRL B-24433 / ID139908) OX=479433 GN=mshA2 PE=3 SV=1
D5USX8	1.14e-09	12	110	313	409	D-inositol 3-phosphate glycosyltransferase OS=Tsukamurella paurometabola (strain ATCC 8368 / DSM 20162 / CCUG 35730 / CIP 100753 / JCM 10117 / KCTC 9821 / NBRC 16120 / NCIMB 702349 / NCTC 13040) OX=521096 GN=mshA PE=3 SV=1
D1BD84	5.28e-09	10	84	309	385	D-inositol 3-phosphate glycosyltransferase OS=Sanguibacter keddieii (strain ATCC 51767 / DSM 10542 / NCFB 3025 / ST-74) OX=446469 GN=mshA PE=3 SV=1
A1SP12	7.33e-09	12	102	344	435	D-inositol 3-phosphate glycosyltransferase OS=Nocardioides sp. (strain ATCC BAA-499 / JS614) OX=196162 GN=mshA PE=3 SV=1

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
1.000050	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001265_01750.