CAZyme Information: MGYG000000060_01482

Basic Information

• Species: Lachnospira eligens_A
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Lachnospira; Lachnospira eligens_A
• CAZyme ID: MGYG000000060_01482
• CAZy Family: GT4
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
430	MGYG000000060_4|CGC3	49096.08	5.0123

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000060	3236509	Isolate	United Kingdom	Europe

• Gene Location: Start: 78228; End: 79520 Strand: +

Full Sequence      

MGLSKFFLNTGEALRPVLTKIIPMKLLSKMKAGIINNATDKLSADSIEKYEAGRYKCGAN
IIGNIKGDNGLGQSARIMCRLLDENKEPHVIRDFFVPPGGSRSNDTYDDRLTEELPFDVN
IIHVNASEFMVAYLSLGKEVWDYRYNIGYWAWELETFPEEWLPAFKLVDEVWTPSDFVTN
TLKKYTDKPVITVPHCVAPQTDIVKFDRKHFNLPEDKFLFLVMYNSGSVMERKNPLAAIK
AFKEAFCKDEQMKEKYKDVGLVIKISEAELSAEDEKIIGSVIEDCDNIYYMCGHMGRCEV
NTLLADVDVYVSLHRSEGFGLVMAESMYVGTPVIATDWSGNTEFMNSDTACMVGYDMIEL
DKDYEPFKKGNVWADAHVDEAADYMRRLYEDKDFYERIAGNGQKYVKEHLAYKRSADIVS
ERLRKIHGKS

Enzyme Prediction     

No EC number prediction in MGYG000000060_01482.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd03801	GT4_PimA-like	2.56e-28	71	424	30	366	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.
COG0438	RfaB	2.86e-26	121	430	104	381	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
cd03809	GT4_MtfB-like	4.17e-16	166	407	137	349	glycosyltransferases MtfB, WbpX, and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. MtfB (mannosyltransferase B) in E. coli has been shown to direct the growth of the O9-specific polysaccharide chain. It transfers two mannoses into the position 3 of the previously synthesized polysaccharide.
cd01635	Glycosyltransferase_GTB-type	2.40e-15	111	344	4	225	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.
pfam00534	Glycos_transf_1	1.45e-13	216	404	1	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ACR71127.1	0.0	1	430	1	430
BBI36185.1	1.12e-98	5	426	7	424
QQZ62154.1	8.46e-98	14	423	19	419
QTE67074.1	7.84e-96	50	429	12	381
ANY70499.1	1.20e-94	5	408	12	406

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
1.000029	0.000005	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000060_01482.