CAZyme Information: MGYG000000337_01808

Basic Information

• Species: Morganella morganii_B
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Morganella; Morganella morganii_B
• CAZyme ID: MGYG000000337_01808
• CAZy Family: GT2
• CAZyme Description: Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
288	MGYG000000337_90|CGC1	32144.3	7.8105

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000337	3835549	MAG	Sweden	Europe

• Gene Location: Start: 24; End: 890 Strand: +

Full Sequence      

MGRVDAGSRDRSAELLTQAAEIPENHVVAVLLNRNYGQHSAIMAGFRQADGDLVITMDAD
LQNPPEEIPRLVEKAEEGYDVVGTRRANRQDSWFRKTASKMINKMIIAATGSAMGDYGCM
LRAYRRHIIDAMLQCHERSTFIPILANTFARKTIEIDVKHAEREFGDSKYSFLKLINLMY
DLLTCLTTAPLRLLSIVGSIIAASGFLLALLLIILRVAFGALWAAEGVFTLFAILFMFIG
AQFVAMGLLGEYIGRIYNDVRARPRYFIQKVVGAQAKETSETETQEKN

Enzyme Prediction     

EC	2.4.1.-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT2	4	128	1.1e-22	0.7705882352941177

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK10714	PRK10714	0.0	4	285	44	325	undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
cd04187	DPM1_like_bac	4.97e-64	4	146	35	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	3.62e-43	4	143	34	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.
cd06442	DPM1_like	7.92e-20	4	169	33	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.
pfam00535	Glycos_transf_2	9.97e-20	4	129	33	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
QXO71399.1	3.76e-195	4	288	45	329
QWL91143.1	3.76e-195	4	288	45	329
QQO71047.1	3.76e-195	4	288	45	329
AWC94897.1	1.53e-194	4	288	45	329
QXO48493.1	2.17e-194	4	288	45	329

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5EKP_A	7.40e-35	4	273	64	331	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	1.03e-34	4	273	64	331	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	5.67e-12	4	169	59	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
B4ETL6	1.94e-165	4	273	46	315	Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase OS=Proteus mirabilis (strain HI4320) OX=529507 GN=arnC PE=3 SV=1
Q7N3Q6	7.63e-165	4	273	45	314	Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase OS=Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 / TT01) OX=243265 GN=arnC PE=2 SV=1
A1JPP5	3.68e-154	4	281	46	323	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
Q6D2F0	5.23e-154	4	274	44	314	Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase OS=Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) OX=218491 GN=arnC PE=3 SV=1
C6DAW6	8.62e-153	4	274	44	314	Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase OS=Pectobacterium carotovorum subsp. carotovorum (strain PC1) OX=561230 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
1.000084	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
193	215
230	252