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CAZyme Information: MGYG000002969_00279

You are here: Home > Sequence: MGYG000002969_00279

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 Succiniclasticum sp900544275
Lineage Bacteria; Firmicutes_C; Negativicutes; Acidaminococcales; Acidaminococcaceae; Succiniclasticum; Succiniclasticum sp900544275
CAZyme ID MGYG000002969_00279
CAZy Family GT9
CAZyme Description Lipopolysaccharide heptosyltransferase 1
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
344 MGYG000002969_1|CGC1 38313.65 8.0316
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002969 1973557 MAG United States North America
Gene Location Start: 299521;  End: 300555  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002969_00279.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT9 80 316 2.4e-65 0.9511111111111111

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG0859 RfaF 6.73e-84 4 331 2 325
ADP-heptose:LPS heptosyltransferase [Cell wall/membrane/envelope biogenesis].
cd03789 GT9_LPS_heptosyltransferase 3.63e-74 5 334 1 277
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.
TIGR02193 heptsyl_trn_I 1.17e-55 5 300 1 299
lipopolysaccharide heptosyltransferase I. This family consists of examples of ADP-heptose:LPS heptosyltransferase I, an enzyme of LPS inner core region biosynthesis. LPS, composed of lipid A, a core region, and O antigen, is found in the outer membrane of Gram-negative bacteria. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
pfam01075 Glyco_transf_9 1.98e-47 74 314 2 241
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.
TIGR02195 heptsyl_trn_II 5.35e-43 5 334 1 331
lipopolysaccharide heptosyltransferase II. This family consists of examples of ADP-heptose:LPS heptosyltransferase II, an enzyme of LPS inner core region biosynthesis. LPS, composed of lipid A, a core region, and O antigen, is found in the outer membrane of Gram-negative bacteria. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QTV78223.1 4.44e-174 1 338 3 348
QNP77240.1 1.83e-167 1 335 1 340
BBG62450.1 5.24e-167 1 335 1 340
ADB48008.1 1.09e-153 1 335 1 344
AEQ22075.1 1.99e-147 17 338 1 329

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2GT1_A 7.50e-26 5 298 2 296
E.coli heptosyltransferase WaaC. [Escherichia coli UTI89],2GT1_B E. coli heptosyltransferase WaaC. [Escherichia coli UTI89]
6DFE_A 7.50e-26 5 298 2 296
Thestructure of a ternary complex of E. coli WaaC [Escherichia coli],6DFE_B The structure of a ternary complex of E. coli WaaC [Escherichia coli]
2H1F_A 8.53e-26 5 298 2 296
E.coli heptosyltransferase WaaC with ADP [Escherichia coli O6],2H1F_B E. coli heptosyltransferase WaaC with ADP [Escherichia coli O6],2H1H_A E. coli heptosyltransferase WaaC with ADP-2-deoxy-2-fluoro heptose [Escherichia coli RS218],2H1H_B E. coli heptosyltransferase WaaC with ADP-2-deoxy-2-fluoro heptose [Escherichia coli RS218]
3TOV_A 4.22e-22 1 299 6 305
Thecrystal structure of the glycosyl transferase family 9 from Veillonella parvula DSM 2008 [Veillonella parvula DSM 2008],3TOV_B The crystal structure of the glycosyl transferase family 9 from Veillonella parvula DSM 2008 [Veillonella parvula DSM 2008]
1PSW_A 2.47e-20 5 299 2 305
Structureof E. coli ADP-heptose lps heptosyltransferase II [Escherichia coli]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q57336 5.70e-25 4 301 9 301
Lipopolysaccharide core heptosyltransferase OpsX OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=opsX PE=3 SV=1
P24173 6.98e-25 5 298 2 296
Lipopolysaccharide heptosyltransferase 1 OS=Escherichia coli (strain K12) OX=83333 GN=rfaC PE=1 SV=1
Q9R9D5 6.27e-23 15 284 5 279
Lipopolysaccharide core heptosyltransferase RfaQ OS=Escherichia coli OX=562 GN=rfaQ PE=1 SV=1
P45042 2.43e-22 5 299 2 305
ADP-heptose--LPS heptosyltransferase 2 OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=rfaF PE=3 SV=1
P37692 8.85e-22 5 299 2 305
ADP-heptose--LPS heptosyltransferase 2 OS=Escherichia coli (strain K12) OX=83333 GN=rfaF 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
1.000056 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002969_00279.