dbCAN-seq: a database of CAZyme sequence and annotation

You are browsing environment: HUMAN GUT

help

CAZyme Information: MGYG000000514_01783

You are here: Home > Sequence: MGYG000000514_01783

Basic Information help

Species

CAG-590 sp900769115

Lineage

Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; CAG-590; CAG-590 sp900769115

CAZyme ID

MGYG000000514_01783

CAZy Family

GT101

CAZyme Description

2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-acetyltransferase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
683		77834.16	4.5517

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000514	3147233	MAG	Fiji	Oceania

Gene Location

Start: 25014; End: 27065 Strand: +

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000000514_01783.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GT101	433	659	1e-75	0.9955357142857143

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam08759	GT-D	4.22e-102	434	660	1	223	Glycosyltransferase GT-D fold. This domain is found at the C-terminus of proteins such as the probable glycosyltransferase Gly that also contain the glycosyl transferase domain at the N-terminus. It is also found N-terminal in numerous putative glycosyltransferases such as GalT1. GalT1 has been shown to catalyze the third step of Fap1 glycosylation. This domain is structurally distinct from all known GT folds of glycosyltransferases and contains a metal binding site. This new glycosyltransferase fold has been named GT-D.
TIGR03728	glyco_access_1	3.94e-97	416	681	1	263	glycosyltransferase, SP_1767 family. Members of this protein family are putative glycosyltransferases. Some members are found close to genes for the accessory secretory (SecA2) system, and are suggested by Partial Phylogenetic Profiling to correlate with SecA2 systems. Glycosylation, therefore, may occur in the cytosol prior to secretion.
cd03349	LbH_XAT	9.17e-37	32	174	2	144	Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of a large number of microbial enzymes that catalyze the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. Members of this class of enzymes include Enterococcus faecium streptogramin A acetyltransferase and Pseudomonas aeruginosa chloramphenicol acetyltransferase. They contain repeated copies of a six-residue hexapeptide repeat sequence motif (X-[STAV]-X-[LIV]-[GAED]-X) and adopt a left-handed parallel beta helix (LbH) structure. The active enzyme is a trimer with CoA and substrate binding sites at the interface of two separate LbH subunits. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients.
cd04647	LbH_MAT_like	1.23e-20	32	154	2	109	Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, galactoside O-acetyltransferase (GAT), xenobiotic acyltransferase (XAT) and similar proteins. MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively while GAT specifically acetylates galactopyranosides. XAT catalyzes the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients. Members of this family contain a a left-handed parallel beta-helix (LbH) domain with at least 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). They are trimeric in their active form.
COG0110	WbbJ	7.89e-14	21	169	21	190	Acetyltransferase (isoleucine patch superfamily) [General function prediction only].

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QNL99919.1	0.0	1	683	1	683
QIK61699.1	6.49e-71	380	679	4	297
QIK56277.1	9.09e-71	380	679	4	297
QQA15849.1	2.42e-68	414	680	43	305
QWG41831.1	2.42e-68	414	680	43	305

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4PFX_A	9.26e-52	421	681	19	275	Thehighly conserved domain of unknown function 1792 has a distinct glycosyltransferase fold [Streptococcus parasanguinis FW213]
4PHR_A	9.26e-52	421	681	19	275	Domainof unknown function 1792 (DUF1792) with manganese [Streptococcus parasanguinis FW213]
4PHS_A	4.74e-51	421	681	19	275	Selenomethioninesubstituted structure of domain of unknown function 1792 (DUF1792) [Streptococcus parasanguinis FW213]
5V4A_A	7.93e-49	415	680	7	269	ANew Glycosyltransferase (DUF1792) from Streptococcus sanguinis [Streptococcus sanguinis SK36],5V4A_B A New Glycosyltransferase (DUF1792) from Streptococcus sanguinis [Streptococcus sanguinis SK36]
6MFK_A	1.63e-12	15	191	14	207	ChainA, Chloramphenicol acetyltransferase [Elizabethkingia anophelis]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9AEU2	3.19e-47	405	680	407	677	Probable glycosyl transferase Gly OS=Streptococcus gordonii OX=1302 GN=gly PE=3 SV=2
A0A0H2URB1	4.11e-44	405	681	535	811	Glycosyltransferase GlyD OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=glyD PE=1 SV=1
P50868	9.98e-15	15	186	6	193	Chloramphenicol acetyltransferase OS=Klebsiella aerogenes OX=548 GN=catB4 PE=3 SV=1
P26840	1.13e-13	57	179	24	153	Probable macrolide acetyltransferase (Fragment) OS=Lysinibacillus sphaericus OX=1421 PE=3 SV=1
P50869	1.14e-13	15	186	6	193	Chloramphenicol acetyltransferase OS=Morganella morganii OX=582 GN=cat PE=3 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
1.000054	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000000514_01783.