CAZyme Information: MGYG000004379_00596

Basic Information

• Species: CAG-628 sp000438415
• Lineage: Bacteria; Firmicutes; Bacilli; RF39; UBA660; CAG-628; CAG-628 sp000438415
• CAZyme ID: MGYG000004379_00596
• CAZy Family: GT2
• CAZyme Description: Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
796		93902.75	8.4605

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004379	1274831	MAG	Israel	Asia

• Gene Location: Start: 135; End: 2525 Strand: +

Full Sequence      

MCVFNLKKQLIGELSLNSKNAINVNKEDNYIFAIKVFPHSSVKIKKIVLEESLKTEDDFM
FENIDNDNKILVITPSYPSLENKYLCGFVHSRLKSYKDHGINFDVVCCHNYNGICKYNYE
GIDVLRVNFSNLRQILQHKKYDKILVHFFDDLYAKVFDACYLDETELYLWVHGPETLYWD
WSKFTTEYFKNEQPLSYDLINKFKNNDEIIRNYNEKSNVHWIFVSNWIKQRSEELINIKF
KNYDVIPNIIDSETFKYVEKNPEQRKNVFFIRRFDDCNKYAIDLNVRAILELSKRKCFEN
MNFNIYGTGDTYDKLIEPLLKFKNVHFYRKFLTHEEIAKKHKENGIAFFPTRYDAQGVSM
CEAAMSGLAVVTSDNDAVKEFLPKDKIYANTENYVEYADIIENLYNNPELFKKISKDCHD
SVYNKCNFNETTGKEIELFKQTKKLDITKKKIIKEKQPVLSIVIPCYNVEKYIEKTISTI
VTCKNADKIEIIPVNDGSKDNTAKIINRLINEYSEDKKTSIFNFIDKENGGHGSTINAGL
KVATGKYFRVIDGDDWINSQEMDKLIDKLENETSDIVITDYSEDLAFSNILNHKKIYDFM
IPNIKYDFEDLCIPNYGFGEWGPILATGNYKTEVLKKTNFKLSEKSFYVDMEYNVYSIEK
AKTITYYPYDIYRYFIGRSGQSVSKKSFIKNRFQHEKVLLNMITYVENNKNISELKKQYI
YEKLINPMANAHYIILTEYQKKPSEFKAFDKLLKSHPEVYYSKILTRKFIRLNRKTNGLI
LPISPLIIKLYKFVRR

Enzyme Prediction     

No EC number prediction in MGYG000004379_00596.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT2	461	579	2.1e-24	0.6647058823529411

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd04179	DPM_DPG-synthase_like	3.41e-21	462	578	1	113	DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily. DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. The UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate. This protein family belongs to Glycosyltransferase 2 superfamily.
pfam00535	Glycos_transf_2	4.43e-21	461	612	1	147	Glycosyl transferase family 2. Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.
cd03801	GT4_PimA-like	1.28e-20	69	416	1	342	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.
cd00761	Glyco_tranf_GTA_type	4.78e-18	462	579	1	112	Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold. Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.
PRK11204	PRK11204	6.60e-18	458	554	54	144	N-glycosyltransferase; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QOS67183.1	2.89e-263	12	789	83	860
AJC12300.1	8.38e-102	9	440	76	510
QKF06692.1	1.89e-77	70	642	17	587
AIW87108.1	7.82e-70	69	437	2	368
QWG53197.1	1.22e-69	102	438	4	328

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3BCV_A	1.62e-12	458	579	5	119	Crystalstructure of a putative glycosyltransferase from Bacteroides fragilis [Bacteroides fragilis NCTC 9343],3BCV_B Crystal structure of a putative glycosyltransferase from Bacteroides fragilis [Bacteroides fragilis NCTC 9343]
5HEA_A	2.56e-12	459	629	6	158	CgTstructure in hexamer [Streptococcus parasanguinis FW213],5HEA_B CgT structure in hexamer [Streptococcus parasanguinis FW213],5HEA_C CgT structure in hexamer [Streptococcus parasanguinis FW213],5HEC_A CgT structure in dimer [Streptococcus parasanguinis FW213],5HEC_B CgT structure in dimer [Streptococcus parasanguinis FW213]
5TZE_C	2.99e-06	461	578	4	117	Crystalstructure of S. aureus TarS in complex with UDP-GlcNAc [Staphylococcus aureus],5TZE_E Crystal structure of S. aureus TarS in complex with UDP-GlcNAc [Staphylococcus aureus],5TZI_C Crystal structure of S. aureus TarS 1-349 [Staphylococcus aureus],5TZJ_A Crystal structure of S. aureus TarS 1-349 in complex with UDP-GlcNAc [Staphylococcus aureus],5TZJ_C Crystal structure of S. aureus TarS 1-349 in complex with UDP-GlcNAc [Staphylococcus aureus],5TZK_C Crystal structure of S. aureus TarS 1-349 in complex with UDP [Staphylococcus aureus]
6P61_A	4.05e-06	455	581	10	130	Structureof a Glycosyltransferase from Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Leptospira borgpetersenii serovar Hardjo-bovis str. JB197],6P61_B Structure of a Glycosyltransferase from Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Leptospira borgpetersenii serovar Hardjo-bovis str. JB197],6P61_C Structure of a Glycosyltransferase from Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Leptospira borgpetersenii serovar Hardjo-bovis str. JB197],6P61_D Structure of a Glycosyltransferase from Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Leptospira borgpetersenii serovar Hardjo-bovis str. JB197]
5TZ8_A	4.23e-06	461	578	4	117	Crystalstructure of S. aureus TarS [Staphylococcus aureus],5TZ8_B Crystal structure of S. aureus TarS [Staphylococcus aureus],5TZ8_C Crystal structure of S. aureus TarS [Staphylococcus aureus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P71059	1.23e-12	458	577	3	115	Uncharacterized glycosyltransferase EpsJ OS=Bacillus subtilis (strain 168) OX=224308 GN=epsJ PE=2 SV=1
P47306	2.67e-10	460	684	3	215	Uncharacterized glycosyltransferase MG060 OS=Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195) OX=243273 GN=MG060 PE=3 SV=1
P75042	2.10e-09	460	696	3	225	Uncharacterized glycosyltransferase MG060 homolog OS=Mycoplasma pneumoniae (strain ATCC 29342 / M129) OX=272634 GN=MPN_075 PE=3 SV=1
Q57022	9.75e-09	458	564	4	104	Uncharacterized glycosyltransferase HI_0868 OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=HI_0868 PE=3 SV=1
P22639	1.08e-08	460	589	3	124	Uncharacterized glycosyltransferase alr2836 OS=Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) OX=103690 GN=alr2836 PE=3 SV=2

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
1.000044	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004379_00596.