dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Citrobacter gillenii

Lineage

Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter gillenii

CAZyme ID

MGYG000002535_02353

CAZy Family

GT112

CAZyme Description

Glycosyltransferase TibC

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
406	MGYG000002535_1\|CGC25	46166.4	6.4203

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002535	4885099	Isolate	United States	North America

Gene Location

Start: 2429152; End: 2430372 Strand: +

Enzyme Prediction help

EC	2.4.99.-

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GT112	15	384	1.7e-167	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	13	386	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	7.29e-26	183	388	102	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	6.84e-10	187	342	138	301	ADP-heptose:LPS heptosyltransferase [Cell wall/membrane/envelope biogenesis].
pfam01075	Glyco_transf_9	1.63e-05	217	331	106	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.
cd03801	GT4_PimA-like	0.004	277	315	252	295	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.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ATF49821.1	0.0	1	406	1	406
QCA18747.1	8.73e-317	1	406	1	406
ANO91411.1	7.60e-313	1	406	1	406
QLN03371.1	7.60e-313	1	406	1	406
QGS12532.1	6.25e-312	1	406	1	406

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4RB4_A	8.92e-311	1	406	1	406	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	5.54e-305	2	406	2	406	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]