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CAZyme Information: MGYG000001876_00237

You are here: Home > Sequence: MGYG000001876_00237

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Acetatifactor sp900760705
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Acetatifactor; Acetatifactor sp900760705
CAZyme ID MGYG000001876_00237
CAZy Family GT2
CAZyme Description Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
530 60026.06 8.1069
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001876 3172346 MAG Denmark Europe
Gene Location Start: 87735;  End: 89327  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001876_00237.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT2 223 386 6.7e-31 0.9823529411764705

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd04187 DPM1_like_bac 9.86e-59 224 401 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 2.00e-49 225 402 2 181
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.
PRK10714 PRK10714 4.34e-47 215 522 1 309
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
COG1670 RimL 5.99e-30 8 168 12 179
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, Posttranslational modification, protein turnover, chaperones].
pfam13302 Acetyltransf_3 3.04e-26 6 143 2 139
Acetyltransferase (GNAT) domain. This domain catalyzes N-acetyltransferase reactions.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QNM02137.1 2.75e-175 217 524 2 308
AOZ97444.1 1.95e-148 218 525 2 310
ADL35280.1 5.74e-148 219 529 3 314
QUI96750.1 4.33e-130 222 526 3 306
ADL25130.1 7.49e-112 222 525 3 305

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5EKP_A 6.22e-33 222 523 28 328
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 8.54e-33 222 523 28 328
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 3.35e-16 222 423 25 229
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]
6ERD_A 2.36e-13 1 158 39 196
Crystalstructure of a putative acetyltransferase from Bacillus cereus species. [Bacillus cereus ATCC 14579],6ERD_B Crystal structure of a putative acetyltransferase from Bacillus cereus species. [Bacillus cereus ATCC 14579]
6ERD_C 2.36e-13 1 158 39 196
Crystalstructure of a putative acetyltransferase from Bacillus cereus species. [Bacillus cereus ATCC 14579],6ERD_D Crystal structure of a putative acetyltransferase from Bacillus cereus species. [Bacillus cereus ATCC 14579]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
A1JPP5 7.36e-45 217 523 5 312
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
B5XTK8 1.43e-43 220 529 8 318
Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase OS=Klebsiella pneumoniae (strain 342) OX=507522 GN=arnC PE=3 SV=1
Q7N3Q6 7.02e-43 217 529 4 317
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
B2K5L4 1.02e-42 220 523 8 312
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 1.02e-42 220 523 8 312
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

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
1.000056 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      download full data without filtering help

start end
447 469
484 506