CAZyme Information: MGYG000004385_00169

Basic Information

• Species: Lachnospira sp900545725
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Lachnospira; Lachnospira sp900545725
• CAZyme ID: MGYG000004385_00169
• CAZy Family: GT4
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
428	MGYG000004385_2|CGC1	49337.15	4.842

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004385	2735315	MAG	Israel	Asia

• Gene Location: Start: 23087; End: 24373 Strand: -

Full Sequence      

MSFSKFVLDTANKLRPVLTRIVPAGLLSAVKAKIVEKNTSNLGNVHIEPFDRTIYKDGIN
LVGNIRGDNGLGQSMRLIADIIDSDNIPFTINNFYVPPGGSMTNHTYDYKITEQAEYNIN
IIHVNASEFTLCYMDRGNKLWDYRYNIAYWLWELEDFPEEWLNNIMLADEIWTPAEFISN
TLRKYTDKPVTTVPYSVTAPTDDKYDRKYFNLPEDKFLFLMMFASGSIMERKNPIGTIEA
FKKAFDKDNKDVGIVIKINELEQSESDIEYIREIFDGYDNIYIITGTFSNIEVNSLTKCV
DVFVSLHRAEGFGLVLAEAMYVGTPTIATNWSANTEFMNSDVACMVDYKMIEIKEDIPPF
KKGYRWADADINQAAGYMKRLYEDKAFYQEIKDNAYKYVRKRLSMERSAKIVADRISEIY
SKKNGEEK

Enzyme Prediction     

No EC number prediction in MGYG000004385_00169.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT4	223	390	4.1e-16	0.9

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd03801	GT4_PimA-like	1.38e-24	121	420	85	365	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	7.60e-24	105	423	88	381	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
cd03809	GT4_MtfB-like	3.46e-15	168	414	139	362	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	4.33e-15	183	346	74	234	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.
cd03817	GT4_UGDG-like	9.41e-15	71	414	30	371	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ACR71127.1	1.01e-173	1	420	1	427
BBI36185.1	1.14e-106	5	419	7	424
ANY70499.1	3.04e-106	5	421	12	426
QQZ62154.1	6.87e-105	11	425	16	428
AZS17521.1	2.58e-99	3	425	10	431

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
1.000054	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004385_00169.