CAZyme Information: MGYG000000562_00942

Basic Information

• Species: Lachnospira sp000437735
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Lachnospira; Lachnospira sp000437735
• CAZyme ID: MGYG000000562_00942
• CAZy Family: GT4
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
393	MGYG000000562_3|CGC6	45238.79	5.3571

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000562	2986625	MAG	China	Asia

• Gene Location: Start: 234250; End: 235431 Strand: -

Full Sequence      

MKRKLAFVVQRYGLEVNGGAELLSRQLVEHLQQQYDIEVLTTKAIEYTTWKNEYTNDVDV
INGVTVRRFGVDKPRDLNRFGKFSGKVIGNPEHTMEQEEQWFEMQGPHVPELIDYIKDHA
DDYEAFIFMTYLYYTTVKGLPLVKDKAILISTAHDEPPIYLKTFDTLFQMPKALFYLTVE
EKKFVERKFRNERIINNDGYGGSGVEVPDTIDSQFCKNKYGIDNYMVYAGRIDEAKGCKE
LFDYFLRYKKENQNDLKLVMMGKPVIPIPKSDDIVSLGFVSDQEKFDVMSGAKFLIMPSP
FESLSIVVLEAMTLSVPVVVNGRCDVLKGHCVRSNGGLYYKSYYEFEGCVNYMLTHPDTA
AGMGANGRKYVDANYTWEKITDRFIDIVERVCN

Enzyme Prediction     

No EC number prediction in MGYG000000562_00942.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd03801	GT4_PimA-like	2.17e-29	4	389	1	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	1.29e-25	4	393	1	379	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
cd03809	GT4_MtfB-like	2.94e-15	131	383	86	359	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.
cd03821	GT4_Bme6-like	4.24e-13	225	386	206	377	Brucella melitensis Bme6 and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. Bme6 in Brucella melitensis has been shown to be involved in the biosynthesis of a polysaccharide.
cd01635	Glycosyltransferase_GTB-type	2.93e-11	227	339	114	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
AKB49876.1	8.63e-149	4	391	2	386
AKB73989.1	1.51e-148	4	388	2	383
AKJ39142.1	3.87e-148	4	393	2	388
AKB58354.1	3.87e-148	4	393	2	388
AKB53538.1	3.87e-148	4	393	2	388

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q4JAK2	5.55e-08	14	387	12	347	Archaeal glycosylation protein 16 OS=Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770) OX=330779 GN=agl16 PE=3 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
1.000054	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000562_00942.