CAZyme Information: MGYG000004856_01528

Basic Information

• Species: Raoultibacter timonensis
• Lineage: Bacteria; Actinobacteriota; Coriobacteriia; Coriobacteriales; Eggerthellaceae; Raoultibacter; Raoultibacter timonensis
• CAZyme ID: MGYG000004856_01528
• CAZy Family: GT4
• CAZyme Description: D-inositol-3-phosphate glycosyltransferase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
393		42554.27	6.8188

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004856	3534823	MAG	China	Asia

• Gene Location: Start: 2760; End: 3941 Strand: +

Full Sequence      

MPTETKPCICIFSALYSPAVGGVETYTGNLARAIADLGYRVIIVTSNTHDAAPRENDGTI
EIVRLPCRPLLGGRYPVPRADRSFKELWSWLGQQQIDYIIVNTRFYLLSNRGLRFSRERG
ITPILIEHGSAHLTMGNPLIDKGVAFVEHALTSIGKRYRASYWAVSAKSSAWLKHFGIAS
QGELSNSIDADAYCAQASKRSYKDELGLSASDFVVAFVGRLVPEKGVKELAQASRLLEDR
TDISFIVAGDGPLSEAASQQASSRMHLLGRLDPPDIAALLAQSDILCLPSRSEGFATSLL
EAAACCTTAVATEVGGGRELMPDEAYGTIIPNAEPQTIADAIRRAADHPGQTADKGRLLG
KLVRTDYSWEKTARRAISACERAQREAAGEATE

Enzyme Prediction     

No EC number prediction in MGYG000004856_01528.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT4	210	349	1.1e-29	0.90625

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd03801	GT4_PimA-like	1.74e-46	9	375	2	360	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	1.46e-43	9	386	3	380	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
cd03798	GT4_WlbH-like	1.08e-31	9	379	1	372	Bordetella parapertussis WlbH and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. Staphylococcus aureus CapJ may be involved in capsule polysaccharide biosynthesis. WlbH in Bordetella parapertussis has been shown to be required for the biosynthesis of a trisaccharide that, when attached to the B. pertussis lipopolysaccharide (LPS) core (band B), generates band A LPS.
cd03814	GT4-like	3.12e-30	9	381	2	365	glycosyltransferase family 4 proteins. This family is most closely related to the GT4 family of glycosyltransferases and includes a sequence annotated as alpha-D-mannose-alpha(1-6)phosphatidyl myo-inositol monomannoside transferase from Bacillus halodurans. 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 bacteria and eukaryotes.
cd03811	GT4_GT28_WabH-like	1.28e-28	8	361	3	340	family 4 and family 28 glycosyltransferases similar to Klebsiella WabH. This family is most closely related to the GT1 family of glycosyltransferases. WabH in Klebsiella pneumoniae has been shown to transfer a GlcNAc residue from UDP-GlcNAc onto the acceptor GalUA residue in the cellular outer core.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QOS67171.1	6.06e-141	23	384	1	362
CBL03246.1	5.93e-120	4	383	11	391
QOY61384.1	6.19e-103	6	373	4	373
BAN76660.1	1.79e-94	6	379	2	376
AEB07231.1	5.50e-92	9	386	3	383

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3OKA_A	1.02e-14	16	370	14	366	Crystalstructure of Corynebacterium glutamicum PimB' in complex with GDP-Man (triclinic crystal form) [Corynebacterium glutamicum],3OKA_B Crystal structure of Corynebacterium glutamicum PimB' in complex with GDP-Man (triclinic crystal form) [Corynebacterium glutamicum]
3OKC_A	1.09e-14	16	370	14	366	Crystalstructure of Corynebacterium glutamicum PimB' bound to GDP (orthorhombic crystal form) [Corynebacterium glutamicum],3OKP_A Crystal structure of Corynebacterium glutamicum PimB' bound to GDP-Man (orthorhombic crystal form) [Corynebacterium glutamicum]
6KIH_A	4.44e-11	19	373	50	414	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]
6TVP_A	3.78e-09	205	377	206	393	Structureof Mycobacterium smegmatis alpha-maltose-1-phosphate synthase GlgM [Mycolicibacterium smegmatis MC2 155],6TVP_B Structure of Mycobacterium smegmatis alpha-maltose-1-phosphate synthase GlgM [Mycolicibacterium smegmatis MC2 155]
4N9W_A	2.71e-08	21	342	19	327	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
A0JZ09	2.37e-17	21	373	26	395	D-inositol 3-phosphate glycosyltransferase OS=Arthrobacter sp. (strain FB24) OX=290399 GN=mshA PE=3 SV=1
P37287	1.02e-16	9	387	35	405	Phosphatidylinositol N-acetylglucosaminyltransferase subunit A OS=Homo sapiens OX=9606 GN=PIGA PE=1 SV=1
Q64323	1.37e-16	9	386	35	405	Phosphatidylinositol N-acetylglucosaminyltransferase subunit A OS=Mus musculus OX=10090 GN=Piga PE=2 SV=1
A6ZW78	2.19e-16	9	343	5	335	Phosphatidylinositol N-acetylglucosaminyltransferase GPI3 subunit OS=Saccharomyces cerevisiae (strain YJM789) OX=307796 GN=SPT14 PE=3 SV=1
B5VSZ6	3.94e-16	9	343	5	335	Phosphatidylinositol N-acetylglucosaminyltransferase GPI3 subunit OS=Saccharomyces cerevisiae (strain AWRI1631) OX=545124 GN=SPT14 PE=3 SV=2

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
0.999250	0.000790	0.000004	0.000002	0.000001	0.000002

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004856_01528.