CAZyme Information: MGYG000001393_00489

Basic Information

• Species: Hafnia paralvei
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Hafnia; Hafnia paralvei
• CAZyme ID: MGYG000001393_00489
• CAZy Family: GT2
• CAZyme Description: Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
338	MGYG000001393_9|CGC2	37976.04	6.308

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001393	4880992	Isolate	not provided	not provided

• Gene Location: Start: 124763; End: 125779 Strand: -

Full Sequence      

MSNNEVIKNEADEIKKVSIVIPVFNEQESLPILIKRTHAACELLNKPYEIILIDDGSHDD
SAEILTRAAEIPENHIVAVLLNRNYGQHSAIMAGFNQVSGDLIITLDADLQNPPEEIPRL
VATAEQGYDVVGTVRAKRKDTWFRKTASKMINMMIQKATGKSMGDYGCMLRAYRRPIIEA
MLHCHERSTFIPILANTFARRTIEIDVRHDEREFGESKYSFLKLINLMYDLVTCLTTTPL
RLLSIVGSVIALSGFTLAVLLIAMRLIFGPTWAAEGVFTLFAVLFTFIGAQFVGLGLLGE
YIGRIYNDVRARPRYFVQKIVSADALKTHVSVEQQEEE

Enzyme Prediction     

EC	2.4.1.-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT2	18	177	2.2e-31	0.9647058823529412

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK10714	PRK10714	0.0	10	336	1	325	undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
cd04187	DPM1_like_bac	5.17e-78	19	195	1	176	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.
cd04179	DPM_DPG-synthase_like	3.97e-56	19	192	1	177	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.
COG0463	WcaA	3.20e-31	15	281	3	267	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
cd06442	DPM1_like	9.03e-30	19	218	1	208	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AMH19242.1	2.52e-238	1	338	1	338
AJQ99190.1	1.03e-237	1	338	1	338
QQE45936.1	3.73e-234	7	338	1	332
QIP55939.1	2.48e-229	1	338	1	338
AWV44884.1	2.48e-229	1	338	1	338

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5EKP_A	3.68e-42	16	320	27	329	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]
5EKE_A	5.15e-42	16	320	27	329	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]
5MLZ_A	1.16e-20	16	218	24	230	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
A1JPP5	2.32e-191	9	333	2	326	Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase OS=Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 / 8081) OX=393305 GN=arnC PE=3 SV=1
Q93PD9	9.53e-184	12	333	5	326	Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase OS=Yersinia pseudotuberculosis serotype I (strain IP32953) OX=273123 GN=arnC PE=2 SV=1
B2K5L4	9.53e-184	12	333	5	326	Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase OS=Yersinia pseudotuberculosis serotype IB (strain PB1/+) OX=502801 GN=arnC PE=3 SV=1
B1JJ29	9.53e-184	12	333	5	326	Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase OS=Yersinia pseudotuberculosis serotype O:3 (strain YPIII) OX=502800 GN=arnC PE=3 SV=1
A4TIM3	9.53e-184	12	333	5	326	Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase OS=Yersinia pestis (strain Pestoides F) OX=386656 GN=arnC 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
1.000072	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
245	267
277	299