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CAZyme Information: P168DRAFT_292143-t37_1-p1

You are here: Home > Sequence: P168DRAFT_292143-t37_1-p1

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 Aspergillus campestris
Lineage Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus campestris
CAZyme ID P168DRAFT_292143-t37_1-p1
CAZy Family GH43
CAZyme Description alpha
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1048 114363.50 6.3409
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AcampestrisIBT28561 9929 1392248 173 9756
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.28:5 -

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH65 405 768 6.6e-80 0.9838709677419355

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
224471 ATH1 1.51e-61 62 796 9 726
Trehalose and maltose hydrolase (possible phosphorylase) [Carbohydrate transport and metabolism].
397616 Glyco_hydro_65N 1.54e-40 67 336 1 240
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.
281612 Glyco_hydro_65m 3.06e-20 405 699 3 329
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.
237517 PRK13807 2.13e-08 62 627 8 538
maltose phosphorylase; Provisional

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 24 1047 19 1037
0.0 24 1047 27 1045
0.0 22 1047 61 1078
0.0 24 1039 25 1028
0.0 24 1040 27 1045

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5.99e-38 335 768 251 642
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]
1.35e-15 431 796 326 722
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]
7.08e-08 417 781 301 703
Chain A, Glycoside hydrolase family 65 central catalytic [[Bacillus] selenitireducens MLS10],4KTP_B Chain B, Glycoside hydrolase family 65 central catalytic [[Bacillus] selenitireducens MLS10]
1.60e-07 417 781 301 703
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 24 1047 27 1045
Acid trehalase OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=treA PE=3 SV=1
0.0 50 1039 53 1051
Cell wall acid trehalase ARB_03719 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_03719 PE=1 SV=1
3.59e-116 62 939 107 959
Cell wall acid trehalase ATC1 OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=ATC1 PE=1 SV=2
2.76e-108 54 944 157 1055
Periplasmic/secreted acid trehalase ATH1 OS=Candida glabrata OX=5478 GN=ATH1 PE=1 SV=1
6.31e-98 54 946 121 1036
Periplasmic acid trehalase ATC1 OS=Saccharomyces cerevisiae (strain CEN.PK113-7D) OX=889517 GN=CENPK1137D_1727 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000341 0.999640 CS pos: 19-20. Pr: 0.9778

TMHMM  Annotations      help

There is no transmembrane helices in P168DRAFT_292143-t37_1-p1.