CAZyme Information: MGYG000001881_01158

Basic Information

• Species: Akkermansia muciniphila_A
• Lineage: Bacteria; Verrucomicrobiota; Verrucomicrobiae; Verrucomicrobiales; Akkermansiaceae; Akkermansia; Akkermansia muciniphila_A
• CAZyme ID: MGYG000001881_01158
• CAZy Family: GT4
• CAZyme Description: D-inositol-3-phosphate glycosyltransferase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
512	MGYG000001881_10|CGC1	57332.32	10.1136

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001881	2552003	MAG	Denmark	Europe

• Gene Location: Start: 36061; End: 37599 Strand: +

Full Sequence      

MFCHHEKKHLPTPKIPPSHHPPPTFSHSSSRLCRHRNPAFPLSANEKIITLGTACHSSPN
TGSLNFPKTFFFQICRLDGGFLILILPYVAFPQCRTIFQVSHSVSASSAPYRLSDALNRH
IPGLKSTLLLRRRKGIDGLEIHRSPARRAADALRRHLAHGFDILLPARRKDLPFSLNVLG
MGFDTAQMEKADVVHLHWIGGRTVDFSQLRHIRRPLVYTLHDMFACTAGCHCTMDCGLFQ
NECRGNCPQLGAPRLFRNLPAWLFSRKRRAFGRIPSLTLVTPSLWLKREVEKSRMFPGRK
IVQIYNPVDTDLFRPAEDRNAVRASLGIPPGAFVIACGATGLFNPVKGGHFIPLVLEELY
RRGHRNLHLLLFGNQEKNVAYPFPSTNAGFITDMNRLAGLYSAADIFLNPTLQDVLSNVA
LESMACKTPSVTFRTGGVPEAVLDGKTGLVAPQGDLNQMAAHCERLILDGQLLRTLAEEG
RRHAEQTFSYPVIAAQHAALYEETLRERRYKE

Enzyme Prediction     

No EC number prediction in MGYG000001881_01158.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT4	389	474	2.8e-17	0.54375

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd03825	GT4_WcaC-like	3.03e-92	185	504	46	364	putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. Escherichia coli WcaC has been predicted to function in colanic acid biosynthesis. WcfI in Bacteroides fragilis has been shown to be involved in the capsular polysaccharide biosynthesis.
cd03801	GT4_PimA-like	3.60e-44	189	502	81	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	6.82e-35	111	508	22	381	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
cd03814	GT4-like	2.01e-24	248	502	120	365	glycosyltransferase family 4 proteins. This family is most closely related to the GT4 family of glycosyltransferases and includes a sequence annotated as alpha-D-mannose-alpha(1-6)phosphatidyl myo-inositol monomannoside transferase from Bacillus halodurans. 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 bacteria and eukaryotes.
cd04962	GT4_BshA-like	3.45e-24	291	503	155	369	N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins. This family is most closely related to the GT1 family of glycosyltransferases. 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 bacteria, while some of them are also found in Archaea and eukaryotes.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QAA43286.1	0.0	51	512	2	463
AYR34659.1	0.0	51	512	2	463
QHV51660.1	0.0	51	512	2	463
QAA52486.1	0.0	51	512	2	463
QAA50227.1	0.0	51	512	2	463

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3C4Q_A	5.88e-14	302	505	190	406	Structureof the retaining glycosyltransferase MshA : The first step in mycothiol biosynthesis. Organism : Corynebacterium glutamicum- Complex with UDP [Corynebacterium glutamicum],3C4Q_B Structure of the retaining glycosyltransferase MshA : The first step in mycothiol biosynthesis. Organism : Corynebacterium glutamicum- Complex with UDP [Corynebacterium glutamicum],3C4V_A Structure of the retaining glycosyltransferase MshA:The first step in mycothiol biosynthesis. Organism: Corynebacterium glutamicum : Complex with UDP and 1L-INS-1-P. [Corynebacterium glutamicum],3C4V_B Structure of the retaining glycosyltransferase MshA:The first step in mycothiol biosynthesis. Organism: Corynebacterium glutamicum : Complex with UDP and 1L-INS-1-P. [Corynebacterium glutamicum]
3C48_A	6.20e-14	302	505	210	426	Structureof the retaining glycosyltransferase MshA: The first step in mycothiol biosynthesis. Organism: Corynebacterium glutamicum- APO (OPEN) structure. [Corynebacterium glutamicum],3C48_B Structure of the retaining glycosyltransferase MshA: The first step in mycothiol biosynthesis. Organism: Corynebacterium glutamicum- APO (OPEN) structure. [Corynebacterium glutamicum]
6KIH_A	2.07e-13	393	501	313	421	Sucrose-phosphatesynthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_B Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_C Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_D Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_E Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_F Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_G Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_H Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_I Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_J Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_K Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_L Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus]
5D00_A	1.05e-09	297	501	167	372	Crystalstructure of BshA from B. subtilis complexed with N-acetylglucosaminyl-malate and UMP [Bacillus subtilis subsp. subtilis str. 168],5D00_B Crystal structure of BshA from B. subtilis complexed with N-acetylglucosaminyl-malate and UMP [Bacillus subtilis subsp. subtilis str. 168],5D01_A Crystal structure of BshA from B. subtilis complexed with N-acetylglucosaminyl-malate [Bacillus subtilis subsp. subtilis str. 168],5D01_B Crystal structure of BshA from B. subtilis complexed with N-acetylglucosaminyl-malate [Bacillus subtilis subsp. subtilis str. 168]
6TVP_A	2.67e-09	395	501	284	396	Structureof Mycobacterium smegmatis alpha-maltose-1-phosphate synthase GlgM [Mycolicibacterium smegmatis MC2 155],6TVP_B Structure of Mycobacterium smegmatis alpha-maltose-1-phosphate synthase GlgM [Mycolicibacterium smegmatis MC2 155]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
D7C367	1.59e-16	300	509	225	448	D-inositol 3-phosphate glycosyltransferase OS=Streptomyces bingchenggensis (strain BCW-1) OX=749414 GN=mshA PE=3 SV=1
C7QKE8	7.76e-15	297	512	193	422	D-inositol 3-phosphate glycosyltransferase 2 OS=Catenulispora acidiphila (strain DSM 44928 / JCM 14897 / NBRC 102108 / NRRL B-24433 / ID139908) OX=479433 GN=mshA2 PE=3 SV=1
Q8FSH1	3.22e-14	302	503	190	404	D-inositol 3-phosphate glycosyltransferase OS=Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395) OX=196164 GN=mshA PE=3 SV=1
Q8NTA6	3.10e-13	302	505	190	406	D-inositol 3-phosphate glycosyltransferase OS=Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) OX=196627 GN=mshA PE=1 SV=1
A4QB40	3.10e-13	302	505	190	406	D-inositol 3-phosphate glycosyltransferase OS=Corynebacterium glutamicum (strain R) OX=340322 GN=mshA 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
1.000052	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001881_01158.