CAZyme Information: MGYG000001263_02168

Basic Information

• Species: Acidovorax sp000302535
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Burkholderiales; Burkholderiaceae; Acidovorax; Acidovorax sp000302535
• CAZyme ID: MGYG000001263_02168
• CAZy Family: GT4
• CAZyme Description: Mannosylfructose-phosphate synthase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
315	MGYG000001263_75|CGC1	34627.71	6.9737

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001263	5662192	MAG	Italy	Europe

• Gene Location: Start: 11589; End: 12536 Strand: +

Full Sequence      

MAMKTWAVEVYDVVSEAWRSQLLRGAQGALYHSPNYFLAPHDGPSVATVHDLSITRYPQT
HPAARRRYFELAFRRSLDRASMLITDTEAVRQELLVDYGVAPEKVRSIHLGVSEHFGPIP
PEATAGVLQARGLKHGGYALSVATLEPRKKLDRLIAAYGQLPVAVRTAYPLVLIGSMGWL
NSPLQRLIEQAQSQGWLRFLGYVPQDELPVLYAGARAYAMTSMYEGFGLPVLEAMASGVP
VLTSSVSCMPEVAGGAALLAHPDDPDELRAQLHRLLTDETWRSQAVPLGLARAQQLTWDR
CVAETVAVYRQVAGE

Enzyme Prediction     

No EC number prediction in MGYG000001263_02168.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT4	138	283	1.1e-35	0.90625

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd03809	GT4_MtfB-like	6.99e-99	17	307	74	362	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.
cd03801	GT4_PimA-like	7.54e-43	36	310	99	366	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	3.43e-39	36	315	103	380	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
cd03800	GT4_sucrose_synthase	7.26e-34	16	307	85	398	sucrose-phosphate synthase and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. The sucrose-phosphate synthases in this family may be unique to plants and photosynthetic bacteria. This enzyme catalyzes the synthesis of sucrose 6-phosphate from fructose 6-phosphate and uridine 5'-diphosphate-glucose, a key regulatory step of sucrose metabolism. The activity of this enzyme is regulated by phosphorylation and moderated by the concentration of various metabolites and light.
pfam00534	Glycos_transf_1	5.87e-30	138	279	4	145	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QJW78489.1	4.41e-102	18	314	80	374
AYQ87397.1	1.29e-101	27	314	88	375
QKM46169.1	1.67e-100	27	313	6	292
AWY56583.1	5.94e-100	27	314	88	375
ASD78174.1	5.94e-100	27	314	88	375

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6KIH_A	1.09e-14	140	312	248	424	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]
3C4Q_A	1.21e-11	44	315	127	409	Structureof the retaining glycosyltransferase MshA : The first step in mycothiol biosynthesis. Organism : Corynebacterium glutamicum- Complex with UDP [Corynebacterium glutamicum],3C4Q_B Structure of the retaining glycosyltransferase MshA : The first step in mycothiol biosynthesis. Organism : Corynebacterium glutamicum- Complex with UDP [Corynebacterium glutamicum],3C4V_A Structure of the retaining glycosyltransferase MshA:The first step in mycothiol biosynthesis. Organism: Corynebacterium glutamicum : Complex with UDP and 1L-INS-1-P. [Corynebacterium glutamicum],3C4V_B Structure of the retaining glycosyltransferase MshA:The first step in mycothiol biosynthesis. Organism: Corynebacterium glutamicum : Complex with UDP and 1L-INS-1-P. [Corynebacterium glutamicum]
3C48_A	1.24e-11	44	315	147	429	Structureof the retaining glycosyltransferase MshA: The first step in mycothiol biosynthesis. Organism: Corynebacterium glutamicum- APO (OPEN) structure. [Corynebacterium glutamicum],3C48_B Structure of the retaining glycosyltransferase MshA: The first step in mycothiol biosynthesis. Organism: Corynebacterium glutamicum- APO (OPEN) structure. [Corynebacterium glutamicum]
4N9W_A	6.80e-09	146	314	203	369	Crystalstructure of phosphatidyl mannosyltransferase PimA [Mycolicibacterium smegmatis MC2 155],4NC9_A Crystal structure of phosphatidyl mannosyltransferase PimA [Mycolicibacterium smegmatis MC2 155],4NC9_B Crystal structure of phosphatidyl mannosyltransferase PimA [Mycolicibacterium smegmatis MC2 155],4NC9_C Crystal structure of phosphatidyl mannosyltransferase PimA [Mycolicibacterium smegmatis MC2 155],4NC9_D Crystal structure of phosphatidyl mannosyltransferase PimA [Mycolicibacterium smegmatis MC2 155]
2GEJ_A	7.04e-09	146	314	219	385	CrystalStructure of phosphatidylinositol mannosyltransferase (PimA) from Mycobacterium smegmatis in complex with GDP-Man [Mycolicibacterium smegmatis MC2 155],2GEK_A Crystal Structure of phosphatidylinositol mannosyltransferase (PimA) from Mycobacterium smegmatis in complex with GDP [Mycolicibacterium smegmatis MC2 155]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
A1SP12	2.09e-16	11	315	142	453	D-inositol 3-phosphate glycosyltransferase OS=Nocardioides sp. (strain ATCC BAA-499 / JS614) OX=196162 GN=mshA PE=3 SV=1
D7C367	2.27e-15	45	311	171	442	D-inositol 3-phosphate glycosyltransferase OS=Streptomyces bingchenggensis (strain BCW-1) OX=749414 GN=mshA PE=3 SV=1
P26402	1.17e-14	48	264	110	308	Protein RfbU OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=rfbU PE=3 SV=1
Q59002	1.60e-13	44	310	114	382	Uncharacterized glycosyltransferase MJ1607 OS=Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) OX=243232 GN=MJ1607 PE=3 SV=1
C3PK12	1.06e-12	42	309	125	402	D-inositol 3-phosphate glycosyltransferase OS=Corynebacterium aurimucosum (strain ATCC 700975 / DSM 44827 / CIP 107346 / CN-1) OX=548476 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
1.000068	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001263_02168.