CAZyme Information: MGYG000000765_01023

Basic Information

• Species: Porphyromonas_A bennonis
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae; Porphyromonas_A; Porphyromonas_A bennonis
• CAZyme ID: MGYG000000765_01023
• CAZy Family: GT4
• CAZyme Description: D-inositol-3-phosphate glycosyltransferase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
388		44111.49	5.4921

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000765	2007181	MAG	Bangladesh	Asia

• Gene Location: Start: 47032; End: 48198 Strand: +

Full Sequence      

MTGKKPEILCISHKYPPSTGGMERQSYELIKGLRAYYKVHSFTYKKGDQPKVVWLAALKR
HIMECLESHPEIRLIHLNDGAMASASLWMQKELDIPVVVTYHGLDVTFPLDFYQDKLIPK
LEQYDAAICVSEYTRQQCLKRGFDPEHTYTVPNGVDVSLADKPDRREEITEELLSRGVDV
RGKRVIIASGRSVRRKGFSWFIKNVMPSLGSDVVLLMTGPRRQEQSFMQSVTRYIPWNDL
RLFLGAPTDEAELDELLETTHGVYPLGRVSFDDLMSLYSLADLFVMPNIPVEGDQEGFGL
VALEASVRGTWVVASGIEGITEAVIEGANGTLLPPEEPDRWIAKIRELLSMSQQELAEWG
RRGQSYTTDHFSWERMVDGYKAVFDRFI

Enzyme Prediction     

No EC number prediction in MGYG000000765_01023.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT4	181	355	4.2e-22	0.925

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd03801	GT4_PimA-like	1.04e-55	8	384	2	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	9.02e-35	8	388	3	378	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
cd03800	GT4_sucrose_synthase	2.26e-31	74	380	104	396	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.
cd05844	GT4-like	2.98e-29	73	371	83	353	glycosyltransferase family 4 proteins. 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 glycosyltransferase family 4 (GT4). 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.
cd03809	GT4_MtfB-like	4.40e-27	19	378	13	358	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BBD45797.1	8.10e-141	7	388	3	385
QRQ99900.1	1.11e-96	7	388	2	387
QQD14713.1	2.33e-92	7	388	2	385
QBR12593.1	1.43e-91	6	380	7	385
AIM35737.1	5.77e-91	7	384	2	381

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4N9W_A	6.37e-11	74	353	94	335	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	6.72e-11	74	353	110	351	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]
6TVP_A	2.09e-10	8	378	17	390	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]
3OKA_A	6.18e-10	7	376	6	368	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	6.45e-10	7	376	6	368	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
D1BD84	1.16e-13	245	386	279	416	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
A8LZG1	2.29e-13	201	384	252	429	D-inositol 3-phosphate glycosyltransferase OS=Salinispora arenicola (strain CNS-205) OX=391037 GN=mshA PE=3 SV=1
B1VEI4	5.14e-12	217	383	235	406	D-inositol 3-phosphate glycosyltransferase OS=Corynebacterium urealyticum (strain ATCC 43042 / DSM 7109) OX=504474 GN=mshA PE=3 SV=1
A4X1R6	5.97e-12	144	377	241	456	D-inositol 3-phosphate glycosyltransferase OS=Salinispora tropica (strain ATCC BAA-916 / DSM 44818 / CNB-440) OX=369723 GN=mshA PE=3 SV=1
D6Z995	3.11e-11	88	382	153	430	D-inositol 3-phosphate glycosyltransferase OS=Segniliparus rotundus (strain ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM 44985 / JCM 13578) OX=640132 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
1.000053	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000765_01023.