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CAZyme Information: CAX44942.1

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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 Candida dubliniensis
Lineage Ascomycota; Saccharomycetes; ; Debaryomycetaceae; Candida; Candida dubliniensis
CAZyme ID CAX44942.1
CAZy Family GT71
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1078 FM992688|CGC19 120231.96 4.8659
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_CdubliniensisCD36 6095 573826 235 5860
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.28:7

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH65 441 794 1.7e-87 0.9919354838709677

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
224471 ATH1 1.07e-88 129 851 34 748
Trehalose and maltose hydrolase (possible phosphorylase) [Carbohydrate transport and metabolism].
281612 Glyco_hydro_65m 1.19e-38 441 794 1 383
Glycosyl hydrolase family 65 central catalytic domain. This family of glycosyl hydrolases contains vacuolar acid trehalase and maltose phosphorylase.Maltose phosphorylase (MP) is a dimeric enzyme that catalyzes the conversion of maltose and inorganic phosphate into beta-D-glucose-1-phosphate and glucose. The central domain is the catalytic domain, which binds a phosphate ion that is proximal the the highly conserved Glu. The arrangement of the phosphate and the glutamate is thought to cause nucleophilic attack on the anomeric carbon atom. The catalytic domain also forms the majority of the dimerization interface.
397616 Glyco_hydro_65N 3.56e-16 103 378 5 240
Glycosyl hydrolase family 65, N-terminal domain. This family of glycosyl hydrolases contains vacuolar acid trehalase and maltose phosphorylase.Maltose phosphorylase (MP) is a dimeric enzyme that catalyzes the conversion of maltose and inorganic phosphate into beta-D-glucose-1-phosphate and glucose. This domain is believed to be essential for catalytic activity although its precise function remains unknown.
237517 PRK13807 7.06e-14 353 841 239 729
maltose phosphorylase; Provisional

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 1 1078 1 1078
0.0 1 1078 1 1078
0.0 1 1078 24 1101
0.0 30 1078 25 1070
0.0 17 1078 12 1071

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.18e-48 175 820 62 669
Chain A, Candidate alpha glycoside phosphorylase Glycoside hydrolase family 65 [Flavobacterium johnsoniae UW101],7FE3_B Chain B, Candidate alpha glycoside phosphorylase Glycoside hydrolase family 65 [Flavobacterium johnsoniae UW101],7FE3_C Chain C, Candidate alpha glycoside phosphorylase Glycoside hydrolase family 65 [Flavobacterium johnsoniae UW101],7FE4_A Chain A, Candidate alpha glycoside phosphorylase Glycoside hydrolase family 65 [Flavobacterium johnsoniae UW101],7FE4_B Chain B, Candidate alpha glycoside phosphorylase Glycoside hydrolase family 65 [Flavobacterium johnsoniae UW101],7FE4_C Chain C, Candidate alpha glycoside phosphorylase Glycoside hydrolase family 65 [Flavobacterium johnsoniae UW101]
8.62e-28 386 794 254 696
Crystal structure of kojibiose phosphorylase complexed with kojibiose [Caldicellulosiruptor saccharolyticus DSM 8903],3WIR_A Crystal structure of kojibiose phosphorylase complexed with glucose [Caldicellulosiruptor saccharolyticus DSM 8903],3WIR_B Crystal structure of kojibiose phosphorylase complexed with glucose [Caldicellulosiruptor saccharolyticus DSM 8903],3WIR_C Crystal structure of kojibiose phosphorylase complexed with glucose [Caldicellulosiruptor saccharolyticus DSM 8903],3WIR_D Crystal structure of kojibiose phosphorylase complexed with glucose [Caldicellulosiruptor saccharolyticus DSM 8903]
1.76e-17 327 791 192 689
Chain A, Glycoside hydrolase family 65 central catalytic [[Bacillus] selenitireducens MLS10],4KTP_B Chain B, Glycoside hydrolase family 65 central catalytic [[Bacillus] selenitireducens MLS10]
3.05e-17 327 791 192 689
Chain A, Glycoside hydrolase family 65 central catalytic [[Bacillus] selenitireducens MLS10],4KTR_B Chain B, Glycoside hydrolase family 65 central catalytic [[Bacillus] selenitireducens MLS10],4KTR_C Chain C, Glycoside hydrolase family 65 central catalytic [[Bacillus] selenitireducens MLS10],4KTR_D Chain D, Glycoside hydrolase family 65 central catalytic [[Bacillus] selenitireducens MLS10],4KTR_E Chain E, Glycoside hydrolase family 65 central catalytic [[Bacillus] selenitireducens MLS10],4KTR_F Chain F, Glycoside hydrolase family 65 central catalytic [[Bacillus] selenitireducens MLS10],4KTR_G Chain G, Glycoside hydrolase family 65 central catalytic [[Bacillus] selenitireducens MLS10],4KTR_H Chain H, Glycoside hydrolase family 65 central catalytic [[Bacillus] selenitireducens MLS10]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
0.0 1 1078 1 1078
Cell wall acid trehalase ATC1 OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=ATC1 PE=1 SV=2
9.35e-225 89 977 148 1073
Periplasmic/secreted acid trehalase ATH1 OS=Candida glabrata OX=5478 GN=ATH1 PE=1 SV=1
1.22e-217 89 991 112 1065
Periplasmic acid trehalase ATH1 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=ATH1 PE=1 SV=1
1.22e-217 89 991 112 1065
Periplasmic acid trehalase ATC1 OS=Saccharomyces cerevisiae (strain CEN.PK113-7D) OX=889517 GN=CENPK1137D_1727 PE=1 SV=1
1.63e-121 121 964 79 944
Cell wall acid trehalase ARB_03719 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_03719 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000010 0.000005

TMHMM  Annotations      download full data without filtering help

Start End
34 53