dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Pseudomonas_R sp900766265

Lineage

Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Pseudomonas_R; Pseudomonas_R sp900766265

CAZyme ID

MGYG000003387_02887

CAZy Family

GT4

CAZyme Description

D-inositol-3-phosphate glycosyltransferase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
354	MGYG000003387_13\|CGC5	39910.48	6.373

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003387	4465621	MAG	United States	North America

Gene Location

Start: 629452; End: 630516 Strand: -

Enzyme Prediction help

No EC number prediction in MGYG000003387_02887.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GT4	170	308	3.6e-27	0.8875

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd03802	GT4_AviGT4-like	1.22e-135	2	337	1	330	UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. aviGT4 in Streptomyces viridochromogenes has been shown to be involved in biosynthesis of oligosaccharide antibiotic avilamycin A. Inactivation of aviGT4 resulted in a mutant that accumulated a novel avilamycin derivative lacking the terminal eurekanate residue.
cd03801	GT4_PimA-like	6.25e-38	2	337	1	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	5.99e-33	1	344	1	381	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
cd03823	GT4_ExpE7-like	1.87e-28	2	337	1	355	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).
cd03811	GT4_GT28_WabH-like	3.88e-23	19	337	12	349	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 help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AYN95333.1	1.36e-195	1	343	1	343
QEU29821.1	5.52e-195	1	343	1	343
QGW84865.1	6.59e-185	1	342	1	341
ARP90132.1	1.94e-181	1	340	1	340
ARP86111.1	1.94e-181	1	340	1	340

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5ZE7_A	2.24e-29	19	332	21	343	UDPGlucose alpha tetrahydrobiopterin glycosyltransferase from Synechococcus species PCC 7942 - apo form [Synechococcus elongatus PCC 7942 = FACHB-805],5ZE7_B UDP Glucose alpha tetrahydrobiopterin glycosyltransferase from Synechococcus species PCC 7942 - apo form [Synechococcus elongatus PCC 7942 = FACHB-805],5ZES_A UDP Glucose alpha tetrahydrobiopterin glycosyltransferase from Synechococcus species PCC 7942 - UDP complex [Synechococcus elongatus PCC 7942 = FACHB-805],5ZES_B UDP Glucose alpha tetrahydrobiopterin glycosyltransferase from Synechococcus species PCC 7942 - UDP complex [Synechococcus elongatus PCC 7942 = FACHB-805],5ZFK_B UDP Glucose alpha tetrahydrobiopterin glycosyltransferase from Synechococcus species PCC 7942 - UDP-BH2 complex [Synechococcus elongatus PCC 7942 = FACHB-805]
5ZER_A	2.28e-29	19	332	21	343	UDPGlucose alpha tetrahydrobiopterin glycosyltransferase from Synechococcus species PCC 7942 - BH2 complex form [Synechococcus elongatus PCC 7942 = FACHB-805],5ZER_B UDP Glucose alpha tetrahydrobiopterin glycosyltransferase from Synechococcus species PCC 7942 - BH2 complex form [Synechococcus elongatus PCC 7942 = FACHB-805],5ZFK_A UDP Glucose alpha tetrahydrobiopterin glycosyltransferase from Synechococcus species PCC 7942 - UDP-BH2 complex [Synechococcus elongatus PCC 7942 = FACHB-805]
2IV3_A	1.38e-14	12	341	23	336	Crystalstructure of AviGT4, a glycosyltransferase involved in Avilamycin A biosynthesis [Streptomyces viridochromogenes],2IV3_B Crystal structure of AviGT4, a glycosyltransferase involved in Avilamycin A biosynthesis [Streptomyces viridochromogenes],2IV3_C Crystal structure of AviGT4, a glycosyltransferase involved in Avilamycin A biosynthesis [Streptomyces viridochromogenes],2IV3_D Crystal structure of AviGT4, a glycosyltransferase involved in Avilamycin A biosynthesis [Streptomyces viridochromogenes]
2IUY_A	2.51e-14	12	341	23	336	Crystalstructure of AviGT4, a glycosyltransferase involved in Avilamycin A biosynthesis [Streptomyces viridochromogenes],2IUY_B Crystal structure of AviGT4, a glycosyltransferase involved in Avilamycin A biosynthesis [Streptomyces viridochromogenes]
4N9W_A	2.16e-09	1	325	5	345	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 download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
A0QQZ8	5.48e-11	176	318	234	375	D-inositol 3-phosphate glycosyltransferase OS=Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) OX=246196 GN=mshA PE=1 SV=1
Q0RS49	2.17e-10	172	329	213	377	D-inositol 3-phosphate glycosyltransferase OS=Frankia alni (strain ACN14a) OX=326424 GN=mshA PE=3 SV=1
B2HQV2	5.90e-10	170	302	252	391	D-inositol 3-phosphate glycosyltransferase OS=Mycobacterium marinum (strain ATCC BAA-535 / M) OX=216594 GN=mshA PE=3 SV=1
C7MSY6	7.34e-10	176	328	236	399	D-inositol 3-phosphate glycosyltransferase OS=Saccharomonospora viridis (strain ATCC 15386 / DSM 43017 / JCM 3036 / NBRC 12207 / P101) OX=471857 GN=mshA PE=3 SV=1
A1UAM8	7.47e-10	171	349	231	417	D-inositol 3-phosphate glycosyltransferase OS=Mycobacterium sp. (strain KMS) OX=189918 GN=mshA 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
1.000048	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000003387_02887.

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