CAZyme Information: MGYG000000196_03552

Basic Information

• Species: Bacteroides thetaiotaomicron
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides thetaiotaomicron
• CAZyme ID: MGYG000000196_03552
• CAZy Family: GT2
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
326		38956.96	8.9461

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000196	6397474	Isolate	China	Asia

• Gene Location: Start: 36125; End: 37105 Strand: -

Full Sequence      

MKDIANTPLVSIICSTYNHGLYISQCLDGFLMQKTNFPFEILIHDDASTDNTPDIIREYE
HNHPQVIRPIYQKENKYSKKEDIFAKYQCSRVRGKYIAICEGDDYWIDPLKLQKQIDFLE
NNPDYGMIYTTSKVYNQKEGKIEKDIIGREFNGYIELLSGNCIPTLTSCIRSALVMEYLK
EVEPKSKNWLMGDYPMWLWISYYHKIKFIPESTTVYRVLEESASHSNDIQKYERFILSTI
DITAFYIHKFNTPLTEPYLRSLSCFYYDLYDKYMCLGMYKKARHYSKLINPSYVSARMRR
RVRRFHLRFIQIRLAKWFDIKGKERK

Enzyme Prediction     

No EC number prediction in MGYG000000196_03552.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT2	11	147	1.2e-16	0.7647058823529411

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd04196	GT_2_like_d	5.61e-28	11	217	1	203	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.
cd00761	Glyco_tranf_GTA_type	8.82e-18	12	132	1	115	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.
pfam00535	Glycos_transf_2	3.16e-16	11	176	1	159	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.
COG0463	WcaA	1.82e-11	6	321	1	291	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
cd04186	GT_2_like_c	9.37e-11	12	128	1	108	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ALJ44441.1	6.03e-249	1	326	1	326
QUT41283.1	6.03e-249	1	326	1	326
QQA08504.1	6.03e-249	1	326	1	326
AAO78478.1	8.22e-247	1	326	1	326
QMW85764.1	8.22e-247	1	326	1	326

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1H7L_A	3.10e-08	8	141	1	135	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	5.77e-06	6	105	3	96	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
P64864	2.30e-29	10	226	1	210	Uncharacterized protein Mb1547 OS=Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97) OX=233413 GN=BQ2027_MB1547 PE=4 SV=1
P9WLV4	2.30e-29	10	226	1	210	Uncharacterized protein MT1570 OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=MT1570 PE=4 SV=1
P9WLV5	2.30e-29	10	226	1	210	Uncharacterized protein Rv1520 OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=Rv1520 PE=1 SV=1
P22639	4.49e-12	10	250	3	243	Uncharacterized glycosyltransferase alr2836 OS=Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) OX=103690 GN=alr2836 PE=3 SV=2
O32268	4.11e-10	8	170	6	161	Putative teichuronic acid biosynthesis glycosyltransferase TuaG OS=Bacillus subtilis (strain 168) OX=224308 GN=tuaG PE=2 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
1.000037	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000196_03552.