CAZyme Information: MGYG000002108_01450

Basic Information

• Species: Prevotella sp900290275
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900290275
• CAZyme ID: MGYG000002108_01450
• CAZy Family: GT4
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
375	MGYG000002108_45|CGC1	44201.27	9.2915

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002108	2842572	MAG	Mongolia	Asia

• Gene Location: Start: 8849; End: 9976 Strand: -

Full Sequence      

MKLSKKEKRLCFILNIGPHYRFPIFKAIDDRFLASFYFGDHMRLPIKTFDYKKLKGYVSI
LKNRFFSSFYWQSKSLRLVFRNYDMYFMDGESYCLSSWGVLLLCKILGKQTVAWTHGWYG
REGFVKRQIKRLYYSLYTKLMVYNEYSIKLMKREGFNPDKMYCIANSLDTEKDLKIRSEL
RPSNIYRDHFNNDCPTIIYCGRIQKWKRLDLIVHSIAQLKNEGKTVNVVFLGKDIENVAL
DKLAESLGVSKQVWMYGPCYDEQVIGEMFYNADVCLSPGNVGLTAIHALSFGCPVLTHDD
FKYQNPEFEAIVPGETGDFFKKDDMADMKAKIAFWINKDEESRNKTRIKAFNEIDRKWNI
YYQLGIIEKVVNDEK

Enzyme Prediction     

No EC number prediction in MGYG000002108_01450.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT4	190	344	2.9e-18	0.95

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam00534	Glycos_transf_1	4.46e-20	195	352	3	157	Glycosyl transferases group 1. Mutations in this domain of PIGA lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.
COG0438	RfaB	1.52e-19	41	373	42	376	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
cd03801	GT4_PimA-like	9.09e-18	95	357	92	351	phosphatidyl-myo-inositol mannosyltransferase. This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct 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. The members of this family are found mainly in certain bacteria and archaea.
cd03817	GT4_UGDG-like	2.00e-13	117	363	129	370	UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins. This family is most closely related to the GT1 family of glycosyltransferases. UDP-glucose-diacylglycerol glucosyltransferase (EC 2.4.1.337, UGDG; also known as 1,2-diacylglycerol 3-glucosyltransferase) catalyzes the transfer of glucose from UDP-glucose to 1,2-diacylglycerol forming 3-D-glucosyl-1,2-diacylglycerol.
cd01635	Glycosyltransferase_GTB-type	3.49e-13	174	320	98	235	glycosyltransferase family 1 and related proteins with GTB topology. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUI93286.1	1.55e-168	7	374	2	369
AUI56186.1	4.44e-168	5	374	2	371
QUB47006.1	1.59e-164	7	373	6	372
AGB27736.1	6.21e-159	5	371	2	368
QCQ51765.1	6.53e-149	3	370	1	369

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

has no Swissprot hit.

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
0.999967	0.000058	0.000007	0.000000	0.000000	0.000001

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002108_01450.