CAZyme Information: CAWG_01617-T-p1

Basic Information

• Species: Candida albicans
• Lineage: Ascomycota; Saccharomycetes; ; Debaryomycetaceae; Candida; Candida albicans
• CAZyme ID: CAWG_01617-T-p1
• CAZy Family: GH17
• CAZyme Description: Protein of unknown function

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
286		32563.40	7.5693

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CalbicansWO1	6160	294748	0	6160

• Gene Location: location=Supercontig_1.2_C_albicans_WO-1:634492-635352(-)

Full Sequence      

MIYYILAFFIFISLSIYATVIFFSHKPRKPFPSELTYKTNDSTDKSHPLPPRINTNSKFQ
DDGIDISLVIPCYNETQRLGKMLDEAIEYLEKNHQSKYEIIVVDDGSSDGTDEYALQKAN
EFKLPSHIMRVVQLKQNRGKGGAVTHGLLHSRGKYALFADADGATSFPDVAKLVNYLANA
NGQPSIAIGSRAHMVNTDAVVKRSFIRNFLMYGLHALVFVFGIRDVRDTQCGFKMFNFEA
VKNIFPHMHTERWIFDVEVLLLGEIQKFNMKELPVNWQEIDGSKVI

Enzyme Prediction     

No EC number prediction in CAWG_01617-T-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT2	67	244	5.1e-27	0.9882352941176471

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
133031	DPG_synthase	2.04e-103	68	284	1	211	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.
240336	PTZ00260	1.13e-83	56	285	62	296	dolichyl-phosphate beta-glucosyltransferase; Provisional
133022	DPM_DPG-synthase_like	2.10e-54	68	261	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.
395426	Glycos_transf_2	1.65e-26	67	241	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.
133062	DPM1_like	1.13e-24	68	275	1	197	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
AOW31021.1|GT2	4.56e-204	1	285	1	285
CAX39788.1|GT2	1.05e-193	1	285	1	285
CAG88571.2|GT2	1.88e-144	1	285	1	287
ABN65654.1|GT2	1.02e-138	16	285	16	287
CCE41571.1|GT2	4.61e-137	16	285	17	286

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5MLZ_A	6.37e-11	66	267	25	213	Dolichyl phosphate 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]
6YV7_B	1.69e-07	66	179	44	154	Mannosyltransferase PcManGT from Pyrobaculum calidifontis [Pyrobaculum calidifontis JCM 11548],6YV8_B Mannosyltransferase PcManGT from Pyrobaculum calidifontis in complex with GDP and Mn2+ [Pyrobaculum calidifontis JCM 11548],6YV9_A Mannosyltransferase PcManGT from Pyrobaculum calidifontis in complex with GDP-Man and Mn2+ [Pyrobaculum calidifontis JCM 11548]
6YV7_A	1.70e-07	66	179	45	155	Mannosyltransferase PcManGT from Pyrobaculum calidifontis [Pyrobaculum calidifontis JCM 11548],6YV8_A Mannosyltransferase PcManGT from Pyrobaculum calidifontis in complex with GDP and Mn2+ [Pyrobaculum calidifontis JCM 11548],6YV9_B Mannosyltransferase PcManGT from Pyrobaculum calidifontis in complex with GDP-Man and Mn2+ [Pyrobaculum calidifontis JCM 11548]
5HEA_A	6.06e-07	61	162	2	94	CgT structure in hexamer [Streptococcus parasanguinis FW213],5HEA_B CgT structure in hexamer [Streptococcus parasanguinis FW213],5HEA_C CgT structure in hexamer [Streptococcus parasanguinis FW213],5HEC_A CgT structure in dimer [Streptococcus parasanguinis FW213],5HEC_B CgT structure in dimer [Streptococcus parasanguinis FW213]
5EKE_A	1.68e-06	56	162	17	119	Structure of 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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P40350|ALG5_YEAST	2.14e-96	14	285	24	303	Dolichyl-phosphate beta-glucosyltransferase OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=ALG5 PE=1 SV=1
sp|O60061|ALG5_SCHPO	8.23e-75	24	285	27	288	Dolichyl-phosphate beta-glucosyltransferase OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=alg5 PE=3 SV=1
sp|Q54J42|ALG5_DICDI	1.27e-66	45	285	57	298	Dolichyl-phosphate beta-glucosyltransferase OS=Dictyostelium discoideum OX=44689 GN=alg5 PE=2 SV=1
sp|Q9VLQ1|ALG5_DROME	1.74e-66	13	285	20	291	Dolichyl-phosphate beta-glucosyltransferase OS=Drosophila melanogaster OX=7227 GN=wol PE=1 SV=1
sp|Q9Y673|ALG5_HUMAN	1.65e-63	66	286	67	291	Dolichyl-phosphate beta-glucosyltransferase OS=Homo sapiens OX=9606 GN=ALG5 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999841	0.000204

TMHMM  Annotations     

Start	End
2	24