CAZyme Information: MGYG000001040_01215

Basic Information

• Species: Prevotella sp900554045
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900554045
• CAZyme ID: MGYG000001040_01215
• CAZy Family: GT2
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
234	MGYG000001040_119|CGC1	26175.11	8.2863

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001040	2860396	MAG	Denmark	Europe

• Gene Location: Start: 8798; End: 9502 Strand: +

Full Sequence      

MISVCMATYNGAKYIRQQLCSIISQIGEGDEVIISDDGSTDSTLDTIRSMADGRIRIVEG
PCRQSPTLNFENALSHAKGDYIFLADQDDVWLPGKVSACMKWLNRYDCVVSDAEMADESL
RVIEKSYYSVHRTKPGRWYNLLVKNGYMGCCMAFTRRVLDAALPFPKGIAMHDLWIGNVA
AFRFSVKFISNTLVTYRCHGGNASFTANMKSGFSLPEKLSIRLQTAVNLLARRQ

Enzyme Prediction     

No EC number prediction in MGYG000001040_01215.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT2	3	159	4.6e-26	0.9705882352941176

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd04196	GT_2_like_d	2.26e-78	3	204	1	210	Subfamily of Glycosyltransferase Family GT2 of unknown function. GT-2 includes diverse families of glycosyltransferases 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. 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.
pfam00535	Glycos_transf_2	1.35e-23	3	157	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	3.01e-20	4	116	1	118	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.
cd06433	GT_2_WfgS_like	3.30e-19	3	204	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.
COG0463	WcaA	1.60e-17	1	183	4	185	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QNT67204.1	3.61e-93	1	230	1	229
QFQ12908.1	6.99e-82	1	229	1	227
ADU24285.1	2.04e-75	1	232	1	230
QLK83838.1	3.40e-75	1	233	1	231
QCQ50453.1	3.40e-75	1	233	1	231

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1H7L_A	4.51e-08	2	106	3	116	dTDP-MAGNESIUMCOMPLEX OF SPSA FROM BACILLUS SUBTILIS [Bacillus subtilis],1H7Q_A dTDP-MANGANESE COMPLEX OF SPSA FROM BACILLUS SUBTILIS [Bacillus subtilis],1QG8_A Native (Magnesium-Containing) Spsa From Bacillus Subtilis [Bacillus subtilis],1QGQ_A Udp-manganese Complex Of Spsa From Bacillus Subtilis [Bacillus subtilis],1QGS_A Udp-Magnesium Complex Of Spsa From Bacillus Subtilis [Bacillus subtilis]
5HEA_A	8.82e-06	1	89	6	95	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P22639	2.34e-12	2	207	3	218	Uncharacterized glycosyltransferase alr2836 OS=Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) OX=103690 GN=alr2836 PE=3 SV=2
Q077R2	1.16e-11	1	204	3	202	UDP-Glc:alpha-D-GlcNAc-diphosphoundecaprenol beta-1,3-glucosyltransferase WfaP OS=Escherichia coli OX=562 GN=wfaP PE=1 SV=1
B5L3F2	5.11e-10	1	166	5	166	UDP-Glc:alpha-D-GlcNAc-diphosphoundecaprenol beta-1,3-glucosyltransferase WfgD OS=Escherichia coli OX=562 GN=wfgD PE=1 SV=1
Q57022	9.28e-10	1	116	5	122	Uncharacterized glycosyltransferase HI_0868 OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=HI_0868 PE=3 SV=1
P9WLV4	1.59e-09	2	199	1	203	Uncharacterized protein MT1570 OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=MT1570 PE=4 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000021	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001040_01215.