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CAZyme Information: OTA31315.1

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Basic Information help

Species

Hortaea werneckii

Lineage

Ascomycota; Dothideomycetes; ; Teratosphaeriaceae; Hortaea; Hortaea werneckii

CAZyme ID

OTA31315.1

CAZy Family

GH28

CAZyme Description

Arabinogalactan endo-beta-1,4-galactanase [Source:UniProtKB/TrEMBL;Acc:A0A1Z5T5N0]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
593		66014.46	5.9487

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_HwerneckiiEXF-2000	15649	1157616	29	15620

Gene Location

Full Sequence Download help

Enzyme Prediction help

EC	3.2.1.89:16

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH53	234	577	2.7e-82	0.9824561403508771

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
311610	Glyco_hydro_53	6.09e-91	234	570	1	321	Glycosyl hydrolase family 53. This domain belongs to family 53 of the glycosyl hydrolase classification. These enzymes are enzymes are endo-1,4- beta-galactanases (EC:3.2.1.89). The structure of this domain is known and has a TIM barrel fold.
226385	GanB	4.90e-64	233	582	39	391	Arabinogalactan endo-1,4-beta-galactosidase [Carbohydrate transport and metabolism].
240034	Nudix_Hydrolase_19	7.09e-59	47	186	1	129	Members of the Nudix hydrolase superfamily catalyze the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+, for their activity and contain a highly conserved 23-residue nudix motif (GX5EX7REUXEEXGU, where U = I, L or V), which functions as a metal binding and catalytic site. Substrates of nudix hydrolases include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the nudix hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance & "house-cleaning" enzymes. Substrate specificity is used to define families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required.
215184	PLN02325	7.02e-44	45	186	6	135	nudix hydrolase
223979	YjhB	3.58e-26	39	182	1	141	ADP-ribose pyrophosphatase YjhB, NUDIX family [Nucleotide transport and metabolism].

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start
2.20e-224	202	593	1	397
2.76e-218	207	593	7	389
4.87e-164	207	590	3	384
2.48e-162	213	591	8	380
2.48e-162	214	591	9	380

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
1.31e-81	234	584	4	331	Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Humicola insolens]
5.13e-81	234	584	4	331	Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Thermothelomyces thermophilus],1HJS_B Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Thermothelomyces thermophilus],1HJS_C Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Thermothelomyces thermophilus],1HJS_D Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Thermothelomyces thermophilus],1HJU_A Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Thermothelomyces thermophilus],1HJU_B Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Thermothelomyces thermophilus],1HJU_C Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Thermothelomyces thermophilus],1HJU_D Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Thermothelomyces thermophilus]
2.32e-79	234	570	4	318	Crystal Structure Of Beta-1,4-galactanase From Aspergillus Aculeatus At 293k [Aspergillus aculeatus],1FOB_A Crystal Structure Of Beta-1,4-galactanase From Aspergillus Aculeatus At 100k [Aspergillus aculeatus],6Q3R_A ASPERGILLUS ACULEATUS GALACTANASE [Aspergillus aculeatus],6Q3R_B ASPERGILLUS ACULEATUS GALACTANASE [Aspergillus aculeatus]
2.76e-75	234	590	21	347	Emericilla nidulans endo-beta-1,4-galactanase [Aspergillus nidulans]
8.89e-36	233	582	50	391	Chain A, Arabinogalactan endo-1,4-beta-galactosidase [Ignisphaera aggregans DSM 17230],7OSK_B Chain B, Arabinogalactan endo-1,4-beta-galactosidase [Ignisphaera aggregans DSM 17230]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
5.46e-82	234	575	20	339	Probable arabinogalactan endo-beta-1,4-galactanase A OS=Aspergillus tubingensis OX=5068 GN=galA PE=2 SV=1
6.75e-81	234	584	4	331	Arabinogalactan endo-beta-1,4-galactanase OS=Humicola insolens OX=34413 PE=1 SV=1
2.64e-80	234	584	4	331	Arabinogalactan endo-beta-1,4-galactanase OS=Thermothelomyces thermophilus OX=78579 PE=1 SV=1
4.59e-80	234	575	20	339	Arabinogalactan endo-beta-1,4-galactanase A OS=Aspergillus niger OX=5061 GN=galA PE=1 SV=1
4.59e-80	234	575	20	339	Probable arabinogalactan endo-beta-1,4-galactanase A OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=galA PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000014	0.000003

TMHMM Annotations help

There is no transmembrane helices in OTA31315.1.