CAZyme Information: MGYG000003627_00156

Basic Information

• Lineage: Bacteria; Verrucomicrobiota; Lentisphaeria; Victivallales; UBA1829; UBA1732
• CAZyme ID: MGYG000003627_00156
• CAZy Family: GT2
• CAZyme Description: Polyprenol monophosphomannose synthase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
252		28036.51	8.1446

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003627	1872155	MAG	Fiji	Oceania

• Gene Location: Start: 1753; End: 2511 Strand: -

Full Sequence      

MKYSIILPTYNESENIQETLRKLAQYCPESTEVIVVDDNSPDGTAKIAEQVATAINIPVH
VLKNPGVRGLSPSVIFGFNHASGAYLACMDADGQHRPEDLPGLLETMERQDAIFMIGSRH
VPGGGFTEHWSLSRTLASRSAAIAARICLGVPIQDPMSGFFVIRRDIFQFVKDELSPSGF
KIMLELAWLLHIAGLQPIEEYPITFAMRKFGKSKLSAQVIQQYIGMLLRCMRTKASIQKK
LKQRLEQSTSNL

Enzyme Prediction     

No EC number prediction in MGYG000003627_00156.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT2	4	169	2.6e-35	0.9764705882352941

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06442	DPM1_like	1.36e-82	5	229	1	223	DPM1_like represents putative enzymes similar to eukaryotic DPM1. Proteins similar to eukaryotic DPM1, including enzymes from bacteria and archaea; 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. This protein family belongs to Glycosyltransferase 2 superfamily.
cd04179	DPM_DPG-synthase_like	2.74e-55	5	186	1	181	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.
PLN02726	PLN02726	1.06e-41	1	233	9	242	dolichyl-phosphate beta-D-mannosyltransferase
pfam00535	Glycos_transf_2	1.66e-40	4	168	1	164	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.
COG0463	WcaA	1.17e-29	1	245	3	249	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AVM44821.1	7.47e-64	1	234	2	234
ASJ08444.1	5.27e-47	1	242	1	236
AHL23598.1	5.61e-46	1	242	1	236
BAD86098.1	5.75e-46	1	242	1	236
CAT70652.1	5.75e-46	1	242	1	236

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5MLZ_A	1.21e-43	1	242	23	258	Dolichylphosphate mannose synthase in complex with GDP and Mg2+ [Pyrococcus furiosus DSM 3638],5MM0_A Dolichyl phosphate mannose synthase in complex with GDP-mannose and Mn2+ (donor complex) [Pyrococcus furiosus DSM 3638],5MM1_A Dolichyl phosphate mannose synthase in complex with GDP and dolichyl phosphate mannose [Pyrococcus furiosus DSM 3638]
5TZE_C	1.94e-08	1	147	1	147	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]
5TZ8_A	2.43e-08	1	147	1	147	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]
3BCV_A	2.53e-06	2	92	6	94	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P14020	5.86e-39	1	227	3	231	Dolichol-phosphate mannosyltransferase OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=DPM1 PE=1 SV=3
A0QZ12	1.55e-34	5	222	26	243	Polyprenol monophosphomannose synthase OS=Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) OX=246196 GN=ppm1 PE=1 SV=1
C5CBV8	1.38e-33	1	224	1	222	Undecaprenyl-phosphate mannosyltransferase OS=Micrococcus luteus (strain ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 / NCIMB 9278 / NCTC 2665 / VKM Ac-2230) OX=465515 GN=Mlut_12000 PE=1 SV=1
P54856	1.25e-32	4	232	31	261	Dolichol-phosphate mannosyltransferase OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=DPM1 PE=3 SV=2
O53493	1.61e-32	5	222	614	831	Bifunctional apolipoprotein N-acyltransferase/polyprenol monophosphomannose synthase OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=ppm1 PE=1 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
1.000069	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003627_00156.