dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000003387_00672

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Basic Information help

Species

Pseudomonas_R sp900766265

Lineage

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

CAZyme ID

MGYG000003387_00672

CAZy Family

GT4

CAZyme Description

Alginate biosynthesis protein AlgA

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
483		53151.25	4.9521

Genome Property

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

Gene Location

Start: 270271; End: 271722 Strand: -

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000003387_00672.

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR01479	GMP_PMI	0.0	1	468	1	468	mannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase. This enzyme is known to be bifunctional, as both mannose-6-phosphate isomerase (EC 5.3.1.8) (PMI) and mannose-1-phosphate guanylyltransferase (EC 2.7.7.22) in Pseudomonas aeruginosa, Xanthomonas campestris, and Gluconacetobacter xylinus. The literature on the enzyme from E. coli attributes mannose-6-phosphate isomerase activity to an adjacent gene, but the present sequence has not been shown to lack the activity. The PMI domain is C-terminal. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
PRK15460	cpsB	0.0	1	468	6	477	mannose-1-phosphate guanyltransferase; Provisional
COG0836	CpsB	5.84e-164	1	332	2	333	Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis].
cd02509	GDP-M1P_Guanylyltransferase	3.85e-129	1	277	1	274	GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose. GDP-mannose-1-phosphate guanylyltransferase, also called GDP-mannose pyrophosphorylase (GDP-MP), catalyzes the formation of GDP-Mannose from mannose-1-phosphate and GTP. Mannose is a key monosaccharide for glycosylation of proteins and lipids. GDP-Mannose is the activated donor for mannosylation of various biomolecules. This enzyme is known to be bifunctional, as both mannose-6-phosphate isomerase and mannose-1-phosphate guanylyltransferase. This CD covers the N-terminal GDP-mannose-1-phosphate guanylyltransferase domain, whereas the isomerase function is located at the C-terminal half. GDP-MP is a member of the nucleotidyltransferase family of enzymes.
pfam01050	MannoseP_isomer	4.22e-95	314	464	1	151	Mannose-6-phosphate isomerase. All of the members of this Pfam entry belong to family 2 of the mannose-6-phosphate isomerases. The type II phosphomannose isomerases are bifunctional enzymes. This Pfam entry covers the isomerase domain. The guanosine diphospho-D-mannose pyrophosphorylase domain is in another Pfam entry, see pfam00483.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AGN91810.2	3.78e-164	1	467	2	472
ACC75758.1	1.18e-55	1	273	32	312
BCF92878.1	8.41e-52	1	289	29	325
AFM26073.1	7.56e-26	355	477	336	458
QCQ21102.1	2.18e-24	361	468	342	449

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2QH5_A	2.04e-57	4	289	8	287	Crystalstructure of mannose-6-phosphate isomerase from Helicobacter pylori [Helicobacter pylori 26695],2QH5_B Crystal structure of mannose-6-phosphate isomerase from Helicobacter pylori [Helicobacter pylori 26695]
2X5S_A	2.22e-51	1	346	2	332	Crystalstructure of T. maritima GDP-mannose pyrophosphorylase in apo state. [Thermotoga maritima MSB8],2X5S_B Crystal structure of T. maritima GDP-mannose pyrophosphorylase in apo state. [Thermotoga maritima MSB8],2X5Z_A Crystal structure of T. maritima GDP-mannose pyrophosphorylase in complex with GDP-mannose. [Thermotoga maritima MSB8],2X5Z_B Crystal structure of T. maritima GDP-mannose pyrophosphorylase in complex with GDP-mannose. [Thermotoga maritima MSB8],2X60_A Crystal structure of T. maritima GDP-mannose pyrophosphorylase in complex with GTP. [Thermotoga maritima MSB8],2X60_B Crystal structure of T. maritima GDP-mannose pyrophosphorylase in complex with GTP. [Thermotoga maritima MSB8],2X65_A Crystal structure of T. maritima GDP-mannose pyrophosphorylase in complex with mannose-1-phosphate. [Thermotoga maritima MSB8],2X65_B Crystal structure of T. maritima GDP-mannose pyrophosphorylase in complex with mannose-1-phosphate. [Thermotoga maritima MSB8]
2CU2_A	7.29e-46	4	347	6	334	Crystalstructure of mannose-1-phosphate geranyltransferase from Thermus thermophilus HB8 [Thermus thermophilus HB8]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P07874	2.36e-245	1	471	1	471	Alginate biosynthesis protein AlgA OS=Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) OX=208964 GN=algA PE=1 SV=3
Q88ND5	7.01e-241	1	480	2	484	Alginate biosynthesis protein AlgA OS=Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440) OX=160488 GN=algA PE=3 SV=1
Q887Q9	1.24e-238	1	483	1	483	Alginate biosynthesis protein AlgA OS=Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000) OX=223283 GN=algA PE=3 SV=1
P59785	3.03e-232	1	480	1	482	Alginate biosynthesis protein AlgA OS=Pseudomonas fluorescens OX=294 GN=algA PE=3 SV=1
B0RVK6	4.34e-192	1	469	4	467	Xanthan biosynthesis protein XanB OS=Xanthomonas campestris pv. campestris (strain B100) OX=509169 GN=xanB 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
1.000034	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000003387_00672.