dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Bradyrhizobium sp000015165

Lineage

Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Xanthobacteraceae; Bradyrhizobium; Bradyrhizobium sp000015165

CAZyme ID

MGYG000003137_06709

CAZy Family

GT112

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
645	MGYG000003137_49\|CGC1	71085.01	6.3542

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003137	8388709	MAG	United States	North America

Gene Location

Start: 14092; End: 16029 Strand: -

Enzyme Prediction help

EC	2.4.99.-

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GT112	2	350	1.6e-168	0.9331550802139037

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR04414	hepto_Aah_TibC	0.0	1	354	23	374	autotransporter strand-loop-strand O-heptosyltransferase. Both Aah (autotransporter adhesin heptosyltransferase) and TibC (tib is enterotoxigenic invasion locus B) are protein O-heptosyltransferases that act on multiple sites from repeat regions of proteins exported by autotransporters. Aah glycosylates AIDA, or autotransporter adhesin involved in diffuse adherence, TibC acts on TibA, but TibC can replace Aah. [Protein fate, Protein modification and repair]
cd03789	GT9_LPS_heptosyltransferase	8.39e-19	102	326	18	265	lipopolysaccharide heptosyltransferase and similar proteins. Lipopolysaccharide heptosyltransferase (2.4.99.B6) is involved in the biosynthesis of lipooligosaccharide (LOS). Lipopolysaccharide (LPS) is a major component of the outer membrane of gram-negative bacteria. LPS heptosyltransferase transfers heptose molecules from ADP-heptose to 3-deoxy-D-manno-octulosonic acid (KDO), a part of the inner core component of LPS. This family also contains lipopolysaccharide 1,2-N-acetylglucosaminetransferase EC 2.4.1.56 and belongs to the GT-B structural superfamily of glycoslytransferases, which have characteristic 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.
pfam01075	Glyco_transf_9	7.34e-07	158	306	72	234	Glycosyltransferase family 9 (heptosyltransferase). Members of this family belong to glycosyltransferase family 9. Lipopolysaccharide is a major component of the outer leaflet of the outer membrane in Gram-negative bacteria. It is composed of three domains; lipid A, Core oligosaccharide and the O-antigen. All of these enzymes transfer heptose to the lipopolysaccharide core.
COG0859	RfaF	6.73e-06	165	354	156	329	ADP-heptose:LPS heptosyltransferase [Cell wall/membrane/envelope biogenesis].
pfam13424	TPR_12	0.001	483	554	5	77	Tetratricopeptide repeat.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ABQ36384.1	0.0	1	645	67	711
BAM89986.1	5.94e-270	1	643	68	710
CAL77724.1	1.54e-261	1	645	68	709
SMX58403.1	6.07e-255	1	500	56	549
QPF94610.1	2.36e-187	2	358	74	430

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4RB4_A	3.73e-115	1	351	35	383	Crystalstructure of dodecameric iron-containing heptosyltransferase TibC in complex with ADP-D-beta-D-heptose at 3.9 angstrom resolution [Escherichia coli DEC13E],4RB4_B Crystal structure of dodecameric iron-containing heptosyltransferase TibC in complex with ADP-D-beta-D-heptose at 3.9 angstrom resolution [Escherichia coli DEC13E],4RB4_C Crystal structure of dodecameric iron-containing heptosyltransferase TibC in complex with ADP-D-beta-D-heptose at 3.9 angstrom resolution [Escherichia coli DEC13E],4RB4_D Crystal structure of dodecameric iron-containing heptosyltransferase TibC in complex with ADP-D-beta-D-heptose at 3.9 angstrom resolution [Escherichia coli DEC13E],4RB4_E Crystal structure of dodecameric iron-containing heptosyltransferase TibC in complex with ADP-D-beta-D-heptose at 3.9 angstrom resolution [Escherichia coli DEC13E],4RB4_F Crystal structure of dodecameric iron-containing heptosyltransferase TibC in complex with ADP-D-beta-D-heptose at 3.9 angstrom resolution [Escherichia coli DEC13E],4RB4_G Crystal structure of dodecameric iron-containing heptosyltransferase TibC in complex with ADP-D-beta-D-heptose at 3.9 angstrom resolution [Escherichia coli DEC13E],4RB4_H Crystal structure of dodecameric iron-containing heptosyltransferase TibC in complex with ADP-D-beta-D-heptose at 3.9 angstrom resolution [Escherichia coli DEC13E],4RB4_I Crystal structure of dodecameric iron-containing heptosyltransferase TibC in complex with ADP-D-beta-D-heptose at 3.9 angstrom resolution [Escherichia coli DEC13E],4RB4_J Crystal structure of dodecameric iron-containing heptosyltransferase TibC in complex with ADP-D-beta-D-heptose at 3.9 angstrom resolution [Escherichia coli DEC13E],4RB4_K Crystal structure of dodecameric iron-containing heptosyltransferase TibC in complex with ADP-D-beta-D-heptose at 3.9 angstrom resolution [Escherichia coli DEC13E],4RB4_L Crystal structure of dodecameric iron-containing heptosyltransferase TibC in complex with ADP-D-beta-D-heptose at 3.9 angstrom resolution [Escherichia coli DEC13E]
4RAP_A	5.87e-114	1	351	35	383	Crystalstructure of bacterial iron-containing dodecameric glycosyltransferase TibC from enterotoxigenic E.coli H10407 [Escherichia coli ETEC H10407],4RAP_B Crystal structure of bacterial iron-containing dodecameric glycosyltransferase TibC from enterotoxigenic E.coli H10407 [Escherichia coli ETEC H10407],4RAP_C Crystal structure of bacterial iron-containing dodecameric glycosyltransferase TibC from enterotoxigenic E.coli H10407 [Escherichia coli ETEC H10407],4RAP_D Crystal structure of bacterial iron-containing dodecameric glycosyltransferase TibC from enterotoxigenic E.coli H10407 [Escherichia coli ETEC H10407],4RAP_E Crystal structure of bacterial iron-containing dodecameric glycosyltransferase TibC from enterotoxigenic E.coli H10407 [Escherichia coli ETEC H10407],4RAP_F Crystal structure of bacterial iron-containing dodecameric glycosyltransferase TibC from enterotoxigenic E.coli H10407 [Escherichia coli ETEC H10407],4RAP_G Crystal structure of bacterial iron-containing dodecameric glycosyltransferase TibC from enterotoxigenic E.coli H10407 [Escherichia coli ETEC H10407],4RAP_H Crystal structure of bacterial iron-containing dodecameric glycosyltransferase TibC from enterotoxigenic E.coli H10407 [Escherichia coli ETEC H10407],4RAP_I Crystal structure of bacterial iron-containing dodecameric glycosyltransferase TibC from enterotoxigenic E.coli H10407 [Escherichia coli ETEC H10407],4RAP_J Crystal structure of bacterial iron-containing dodecameric glycosyltransferase TibC from enterotoxigenic E.coli H10407 [Escherichia coli ETEC H10407],4RAP_K Crystal structure of bacterial iron-containing dodecameric glycosyltransferase TibC from enterotoxigenic E.coli H10407 [Escherichia coli ETEC H10407],4RAP_L Crystal structure of bacterial iron-containing dodecameric glycosyltransferase TibC from enterotoxigenic E.coli H10407 [Escherichia coli ETEC H10407]