logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000003131_00250

You are here: Home > Sequence: MGYG000003131_00250

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species UMGS1260 sp900550105
Lineage Bacteria; Firmicutes_C; Negativicutes; UMGS1260; UMGS1260; UMGS1260; UMGS1260 sp900550105
CAZyme ID MGYG000003131_00250
CAZy Family GT112
CAZyme Description Glycosyltransferase TibC
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
430 MGYG000003131_2|CGC1 48690.49 6.2337
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003131 3664514 MAG United States North America
Gene Location Start: 27224;  End: 28516  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 2.4.99.-

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT112 40 405 2.9e-171 0.9866310160427807

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 42 407 8 374
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 3.76e-22 128 409 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 5.07e-09 237 407 175 329
ADP-heptose:LPS heptosyltransferase [Cell wall/membrane/envelope biogenesis].
pfam01075 Glyco_transf_9 4.08e-07 238 358 106 233
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.
PRK10422 PRK10422 2.45e-05 239 410 185 345
lipopolysaccharide core biosynthesis protein; Provisional

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QDR80265.1 3.02e-215 31 415 19 403
QNP78359.1 5.43e-196 30 430 1 405
BBG64539.1 3.22e-195 10 411 8 417
BBG64536.1 3.54e-195 30 421 33 428
QNP78211.1 4.68e-195 30 415 1 390

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4RB4_A 5.60e-142 40 407 18 386
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 3.20e-141 40 407 18 386
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q9S4K6 1.88e-142 40 407 18 386
Glycosyltransferase TibC OS=Escherichia coli O78:H11 (strain H10407 / ETEC) OX=316401 GN=tibC PE=1 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
1.000078 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003131_00250.