dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Pseudomonas_E extremaustralis

Lineage

Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Pseudomonas_E; Pseudomonas_E extremaustralis

CAZyme ID

MGYG000003208_03457

CAZy Family

GT4

CAZyme Description

D-inositol-3-phosphate glycosyltransferase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
504	MGYG000003208_62\|CGC1	56255.09	5.1508

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003208	6254364	MAG	United States	North America

Gene Location

Start: 12713; End: 14227 Strand: -

Enzyme Prediction help

No EC number prediction in MGYG000003208_03457.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GT4	316	469	1.5e-24	0.9

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
NF038011	PelF	0.0	11	497	1	489	GT4 family glycosyltransferase PelF. Proteins of this family are components of the exopolysaccharide Pel transporter. It has been reported that PelF is a soluble glycosyltransferase that uses UDP-glucose as the substrate for the synthesis of exopolysaccharide Pel, whereas PelG is a Wzx-like and PST family exopolysaccharide transporter.
cd03813	GT4-like	0.0	11	497	1	473	glycosyltransferase family 4 proteins. This family is most closely related to the GT4 family of glycosyltransferases. 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, while some of them are also found in Archaea and eukaryotes.
pfam11997	DUF3492	9.74e-108	10	288	1	278	Domain of unknown function (DUF3492). This presumed domain is functionally uncharacterized. This domain is found in bacteria, archaea and eukaryotes. This domain is typically between 259 to 282 amino acids in length. This domain is found associated with pfam00534. This domain has two conserved sequence motifs: GGVS and EHGIY.
cd03801	GT4_PimA-like	7.26e-40	179	498	82	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	6.28e-37	183	504	89	381	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].

CAZyme Hits help

Hit ID	Query Start	Query End	Hit Start	Hit End
SDF91447.1	1	504	1	504
QXH84364.1	1	504	1	504
AKS06975.1	1	504	1	504
ASV36134.1	1	504	1	504
SDO46969.1	1	504	1	504

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4N9W_A	5.66e-08	247	483	126	351	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	5.92e-08	247	483	142	367	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]
5D00_A	2.86e-06	326	502	213	377	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 download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
C0ZUT0	3.06e-10	169	433	98	352	D-inositol 3-phosphate glycosyltransferase OS=Rhodococcus erythropolis (strain PR4 / NBRC 100887) OX=234621 GN=mshA PE=3 SV=1
Q9R9N2	6.59e-10	292	484	138	333	Lipopolysaccharide core biosynthesis mannosyltransferase LpsB OS=Rhizobium meliloti (strain 1021) OX=266834 GN=lpsB PE=3 SV=1
Q0SF06	9.75e-10	169	433	108	362	D-inositol 3-phosphate glycosyltransferase OS=Rhodococcus jostii (strain RHA1) OX=101510 GN=mshA PE=3 SV=1
D5UJ42	1.26e-09	168	502	126	441	D-inositol 3-phosphate glycosyltransferase OS=Cellulomonas flavigena (strain ATCC 482 / DSM 20109 / BCRC 11376 / JCM 18109 / NBRC 3775 / NCIMB 8073 / NRS 134) OX=446466 GN=mshA PE=3 SV=1
C7QKE8	1.60e-09	191	496	119	423	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

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000011	0.000010	0.000000	0.000000	0.000000	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000003208_03457.

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