CAZyme Information: MGYG000001388_01486

Basic Information

• Species: Desulfitobacterium hafniense
• Lineage: Bacteria; Firmicutes_B; Desulfitobacteriia; Desulfitobacteriales; Desulfitobacteriaceae; Desulfitobacterium; Desulfitobacterium hafniense
• CAZyme ID: MGYG000001388_01486
• CAZy Family: GT2
• CAZyme Description: Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
385	MGYG000001388_29|CGC2	43789.42	10.0488

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001388	5194328	Isolate	not provided	not provided

• Gene Location: Start: 92234; End: 93391 Strand: +

Full Sequence      

MLSLVIPVFNEKDNIDELIQRVEKSLKDYSYEIIFVDDSNDETTAIISQFACGDQRIKLI
HRKNKTGLASAVICGFENAQGDILAVMDGDLQHPPEILPKMMKEIEQGADLVVPSRFIPG
GSDGGLNHFRKLVSATARYIGKILIKSLRRASDHTGGMFMLRKEVIQGKQLNPVGWKILM
EIMVMGSYQNLVEIPYVFSTRNLGQSKLNLKVQLQYVWHIIGLLKRSESDRRFYVFCLVG
GSGVLVDMLIFAILGYRFPGMSVNAKAVVSAFIAMVSNYTLNNLFTWKEIRGIKFNYKAF
LVNLRRFSKYLMVSSFGILIKSIILFLLYYFLHINKYWGNFAGIVCASFSNYFLSKLWVW
REEKASFPIYKRVGEKNSSGVSAKK

Enzyme Prediction     

No EC number prediction in MGYG000001388_01486.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT2	3	166	8e-34	0.9705882352941176

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06442	DPM1_like	3.19e-82	4	223	1	224	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	1.58e-50	4	184	1	183	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.
cd04187	DPM1_like_bac	2.42e-41	4	167	1	160	Bacterial DPM1_like enzymes are related to eukaryotic DPM1. A family of bacterial enzymes related to eukaryotic DPM1; Although the mechanism of eukaryotic enzyme is well studied, the mechanism of the bacterial enzymes is not well understood. The eukaryotic 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. 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. This protein family belongs to Glycosyltransferase 2 superfamily.
PLN02726	PLN02726	3.52e-40	3	224	12	240	dolichyl-phosphate beta-D-mannosyltransferase
pfam00535	Glycos_transf_2	3.91e-35	3	166	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CDX02485.1	6.49e-229	1	322	1	322
AWI06118.1	1.71e-137	1	372	1	371
AKN31736.1	6.90e-137	1	360	1	359
AKA67428.1	2.26e-135	1	372	1	371
ABI69448.1	7.41e-109	2	385	6	378

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5MLZ_A	3.37e-70	3	360	26	372	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]
5EKE_A	6.20e-13	2	116	28	145	Structureof the polyisoprenyl-phosphate glycosyltransferase GtrB (F215A mutant) [Synechocystis sp. PCC 6803 substr. Kazusa],5EKE_B Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB (F215A mutant) [Synechocystis sp. PCC 6803 substr. Kazusa],5EKE_C Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB (F215A mutant) [Synechocystis sp. PCC 6803 substr. Kazusa],5EKE_D Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB (F215A mutant) [Synechocystis sp. PCC 6803 substr. Kazusa]
5EKP_A	6.20e-13	2	116	28	145	Structureof the polyisoprenyl-phosphate glycosyltransferase GtrB (WT) [Synechocystis sp. PCC 6803 substr. Kazusa],5EKP_B Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB (WT) [Synechocystis sp. PCC 6803 substr. Kazusa],5EKP_C Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB (WT) [Synechocystis sp. PCC 6803 substr. Kazusa],5EKP_D Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB (WT) [Synechocystis sp. PCC 6803 substr. Kazusa]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P14020	1.50e-28	3	217	6	228	Dolichol-phosphate mannosyltransferase OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=DPM1 PE=1 SV=3
Q9LM93	6.70e-28	3	224	16	243	Dolichol-phosphate mannosyltransferase subunit 1 OS=Arabidopsis thaliana OX=3702 GN=DPMS1 PE=1 SV=1
Q9VIU7	5.69e-25	3	223	9	237	Dolichol-phosphate mannosyltransferase subunit 1 OS=Drosophila melanogaster OX=7227 GN=Dpm1 PE=3 SV=1
P54856	6.34e-25	3	225	31	261	Dolichol-phosphate mannosyltransferase OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=DPM1 PE=3 SV=2
Q54LP3	1.32e-22	3	228	21	254	Dolichol-phosphate mannosyltransferase subunit 1 OS=Dictyostelium discoideum OX=44689 GN=dpm1 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
1.000073	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
233	255
265	287
310	332
337	359