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CAZyme Information: MGYG000001700_01614

You are here: Home > Sequence: MGYG000001700_01614

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 Citrobacter_A sedlakii
Lineage Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Citrobacter_A; Citrobacter_A sedlakii
CAZyme ID MGYG000001700_01614
CAZy Family GT2
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
563 MGYG000001700_3|CGC3 63837.65 8.6982
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001700 4631466 Isolate not provided not provided
Gene Location Start: 144713;  End: 146404  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001700_01614.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT2 8 131 3.2e-20 0.7294117647058823

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG4261 COG4261 1.21e-151 247 563 1 308
Predicted acyltransferase, LPLAT superfamily [General function prediction only].
cd04179 DPM_DPG-synthase_like 2.07e-37 9 190 1 185
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.
cd07984 LPLAT_LABLAT-like 2.33e-19 358 555 13 192
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LABLAT-like. Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are such LPLATs as lipid A biosynthesis lauroyl/myristoyl (LABLAT, HtrB) acyltransferases and similar proteins.
cd04188 DPG_synthase 7.79e-18 9 190 1 190
DPG_synthase is involved in protein N-linked glycosylation. 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.
pfam00535 Glycos_transf_2 4.91e-17 8 142 1 137
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      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QUC30464.1 0.0 1 563 1 563
QBY30608.1 0.0 1 563 1 563
CBG91030.1 0.0 1 563 1 563
SAZ24087.1 0.0 1 563 1 563
QIO37808.1 0.0 1 563 1 563

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5MLZ_A 8.50e-08 9 159 27 181
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      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
C5CBV8 7.08e-10 10 162 6 161
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
Q57964 1.43e-09 10 161 4 161
Uncharacterized protein MJ0544 OS=Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) OX=243232 GN=MJ0544 PE=4 SV=1
A0QZ12 1.03e-07 9 162 26 184
Polyprenol monophosphomannose synthase OS=Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) OX=246196 GN=ppm1 PE=1 SV=1
Q54J42 3.82e-07 9 187 78 273
Dolichyl-phosphate beta-glucosyltransferase OS=Dictyostelium discoideum OX=44689 GN=alg5 PE=2 SV=1
B3VA58 5.51e-06 9 188 8 202
UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminyltransferase OS=Methanococcus voltae OX=2188 GN=aglK PE=1 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
1.000060 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001700_01614.