dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

UBA1829 sp900548385

Lineage

Bacteria; Verrucomicrobiota; Lentisphaeria; Victivallales; UBA1829; UBA1829; UBA1829 sp900548385

CAZyme ID

MGYG000000360_02908

CAZy Family

GT112

CAZyme Description

Glycosyltransferase TibC

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
438		50335.49	7.3002

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000360	4492877	MAG	Sweden	Europe

Gene Location

Start: 211; End: 1527 Strand: +

Enzyme Prediction help

EC	2.4.99.-

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GT112	45	417	4.6e-173	0.9946524064171123

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	43	419	1	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	3.20e-22	141	418	10	277	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.
COG0859	RfaF	1.78e-09	202	422	120	332	ADP-heptose:LPS heptosyltransferase [Cell wall/membrane/envelope biogenesis].
pfam01075	Glyco_transf_9	2.35e-06	228	364	76	220	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.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AVM43209.1	8.62e-277	1	423	1	428
AVM45539.1	2.09e-260	28	424	30	426
AVM43989.1	1.02e-184	12	419	2	410
ARQ79249.1	2.42e-168	43	419	3	376
ARQ46048.1	5.64e-168	27	419	20	410

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4RB4_A	7.47e-157	43	419	13	386	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	1.22e-155	43	419	13	386	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]