dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Acetatifactor sp900066365

Lineage

Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Acetatifactor; Acetatifactor sp900066365

CAZyme ID

MGYG000000041_01578

CAZy Family

GT2

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
543	MGYG000000041_10\|CGC1	61715.99	8.8492

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000041	3646137	Isolate	United Kingdom	Europe

Gene Location

Start: 47378; End: 49009 Strand: -

Enzyme Prediction help

No EC number prediction in MGYG000000041_01578.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GT2	302	448	2e-32	0.7764705882352941

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06433	GT_2_WfgS_like	2.62e-69	302	501	1	201	WfgS and WfeV are involved in O-antigen biosynthesis. Escherichia coli WfgS and Shigella dysenteriae WfeV are glycosyltransferase 2 family enzymes involved in O-antigen biosynthesis. GT-2 enzymes have GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.
cd05232	UDP_G4E_4_SDR_e	1.41e-49	3	276	1	283	UDP-glucose 4 epimerase, subgroup 4, extended (e) SDRs. UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), is a homodimeric extended SDR. It catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. This subgroup is comprised of bacterial proteins, and includes the Staphylococcus aureus capsular polysaccharide Cap5N, which may have a role in the synthesis of UDP-N-acetyl-d-fucosamine. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
pfam00535	Glycos_transf_2	2.93e-29	302	478	1	161	Glycosyl transferase family 2. Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.
cd00761	Glyco_tranf_GTA_type	1.35e-27	303	421	1	117	Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold. Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.
cd02525	Succinoglycan_BP_ExoA	2.65e-21	300	495	1	209	ExoA is involved in the biosynthesis of succinoglycan. Succinoglycan Biosynthesis Protein ExoA catalyzes the formation of a beta-1,3 linkage of the second sugar (glucose) of the succinoglycan with the galactose on the lipid carrie. Succinoglycan is an acidic exopolysaccharide that is important for invasion of the nodules. Succinoglycan is a high-molecular-weight polymer composed of repeating octasaccharide units. These units are synthesized on membrane-bound isoprenoid lipid carriers, beginning with galactose followed by seven glucose molecules, and modified by the addition of acetate, succinate, and pyruvate. ExoA is a membrane protein with a transmembrance domain at c-terminus.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
VCV20929.1	6.52e-85	1	279	1	281
AOH47322.1	5.24e-62	301	541	3	245
QMW80818.1	2.63e-60	2	277	338	606
QIB56408.1	2.63e-60	2	277	338	606
QMX59845.1	2.97e-56	298	539	2	245

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3BCV_A	2.93e-13	299	452	5	154	Crystalstructure of a putative glycosyltransferase from Bacteroides fragilis [Bacteroides fragilis NCTC 9343],3BCV_B Crystal structure of a putative glycosyltransferase from Bacteroides fragilis [Bacteroides fragilis NCTC 9343]
5HEA_A	1.11e-12	301	438	7	140	CgTstructure in hexamer [Streptococcus parasanguinis FW213],5HEA_B CgT structure in hexamer [Streptococcus parasanguinis FW213],5HEA_C CgT structure in hexamer [Streptococcus parasanguinis FW213],5HEC_A CgT structure in dimer [Streptococcus parasanguinis FW213],5HEC_B CgT structure in dimer [Streptococcus parasanguinis FW213]
2Z86_A	1.44e-09	299	408	375	480	Crystalstructure of chondroitin polymerase from Escherichia coli strain K4 (K4CP) complexed with UDP-GlcUA and UDP [Escherichia coli],2Z86_B Crystal structure of chondroitin polymerase from Escherichia coli strain K4 (K4CP) complexed with UDP-GlcUA and UDP [Escherichia coli],2Z86_C Crystal structure of chondroitin polymerase from Escherichia coli strain K4 (K4CP) complexed with UDP-GlcUA and UDP [Escherichia coli],2Z86_D Crystal structure of chondroitin polymerase from Escherichia coli strain K4 (K4CP) complexed with UDP-GlcUA and UDP [Escherichia coli]
2Z87_A	1.44e-09	299	408	374	479	Crystalstructure of chondroitin polymerase from Escherichia coli strain K4 (K4CP) complexed with UDP-GalNAc and UDP [Escherichia coli],2Z87_B Crystal structure of chondroitin polymerase from Escherichia coli strain K4 (K4CP) complexed with UDP-GalNAc and UDP [Escherichia coli]
6P61_A	3.95e-08	299	400	13	110	Structureof a Glycosyltransferase from Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Leptospira borgpetersenii serovar Hardjo-bovis str. JB197],6P61_B Structure of a Glycosyltransferase from Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Leptospira borgpetersenii serovar Hardjo-bovis str. JB197],6P61_C Structure of a Glycosyltransferase from Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Leptospira borgpetersenii serovar Hardjo-bovis str. JB197],6P61_D Structure of a Glycosyltransferase from Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Leptospira borgpetersenii serovar Hardjo-bovis str. JB197]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q56623	3.23e-18	2	292	10	317	UDP-glucose 4-epimerase OS=Vibrio cholerae OX=666 GN=galE PE=3 SV=1
P9WMX8	1.01e-14	299	506	5	213	Uncharacterized glycosyltransferase MT1564 OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=MT1564 PE=3 SV=1
P9WMX9	1.01e-14	299	506	5	213	Uncharacterized glycosyltransferase Rv1514c OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=Rv1514c PE=1 SV=1
P71239	1.47e-14	301	529	3	233	Putative colanic acid biosynthesis glycosyl transferase WcaE OS=Escherichia coli (strain K12) OX=83333 GN=wcaE PE=4 SV=2
Q9CMP0	4.16e-12	299	525	433	665	Chondroitin synthase OS=Pasteurella multocida (strain Pm70) OX=272843 GN=fcbD 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
1.000056	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000000041_01578.

You are here: Home > Sequence: MGYG000000041_01578