dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Aspergillus ochraceoroseus

Lineage

Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus ochraceoroseus

CAZyme ID

P175DRAFT_0506547-t39_1-p1

CAZy Family

GH54|CBM42

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
312	MSFN02000001\|CGC24	35079.49	6.1690

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AochraceoroseusIBT24754	9070	1392256	153	8917

Gene Location

Enzyme Prediction help

EC	3.2.1.8:31

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH10	28	292	2.6e-70	0.8085808580858086

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395262	Glyco_hydro_10	1.44e-90	28	292	1	254	Glycosyl hydrolase family 10.
214750	Glyco_10	7.04e-76	74	292	1	213	Glycosyl hydrolase family 10.
226217	XynA	7.46e-60	65	299	58	286	Endo-1,4-beta-xylanase, GH35 family [Carbohydrate transport and metabolism].
187656	KR_2_SDR_x	0.002	212	293	270	357	ketoreductase (KR), subgroup 2, complex (x) SDRs. Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes both KR domains of the Bacillus subtilis Pks J,-L, and PksM, and all three KR domains of PksN, components of the megacomplex bacillaene synthase, which synthesizes the antibiotic bacillaene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start
1.30e-150	1	310	1	310
3.12e-150	1	296	1	296
3.23e-150	1	310	1	306
1.08e-116	28	296	41	310
1.05e-87	28	296	87	357

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
1.26e-149	27	310	3	281	Penicillium canescens endo-1,4-beta-xylanase XylE [Penicillium canescens]
2.44e-90	28	296	3	273	Chain A, Beta-xylanase [Bispora sp. MEY-1],5XZO_B Chain B, Beta-xylanase [Bispora sp. MEY-1],5XZU_A Chain A, Beta-xylanase [Bispora sp. MEY-1],5XZU_B Chain B, Beta-xylanase [Bispora sp. MEY-1]
1.00e-74	28	292	3	259	Crystal structure of GH10 family xylanase XynAF1 from Aspergillus fumigatus Z5 [Aspergillus fumigatus Z5],6JDT_B Crystal structure of GH10 family xylanase XynAF1 from Aspergillus fumigatus Z5 [Aspergillus fumigatus Z5],6JDY_A Ligand complex structure of GH10 family xylanase XynAF1, soaking for 120 minutes [Aspergillus fumigatus Z5],6JDY_B Ligand complex structure of GH10 family xylanase XynAF1, soaking for 120 minutes [Aspergillus fumigatus Z5],6JDZ_A Ligand complex structure of GH10 family xylanase XynAF1, soaking for 20 minutes [Aspergillus fumigatus Z5],6JDZ_B Ligand complex structure of GH10 family xylanase XynAF1, soaking for 20 minutes [Aspergillus fumigatus Z5],6JE0_A Ligand complex structure of GH10 family xylanase XynAF1, soaking for 30 minutes [Aspergillus fumigatus Z5],6JE0_B Ligand complex structure of GH10 family xylanase XynAF1, soaking for 30 minutes [Aspergillus fumigatus Z5],6JE1_A Ligand complex structure of GH10 family xylanase XynAF1, soaking for 40 minutes [Aspergillus fumigatus Z5],6JE1_B Ligand complex structure of GH10 family xylanase XynAF1, soaking for 40 minutes [Aspergillus fumigatus Z5],6JE2_A Ligand complex structure of GH10 family xylanase XynAF1, soaking for 80 minutes [Aspergillus fumigatus Z5],6JE2_B Ligand complex structure of GH10 family xylanase XynAF1, soaking for 80 minutes [Aspergillus fumigatus Z5]
5.32e-62	28	294	25	288	GH10 endo-xylanase [Aspergillus aculeatus ATCC 16872],6Q8M_B GH10 endo-xylanase [Aspergillus aculeatus ATCC 16872],6Q8N_A GH10 endo-xylanase in complex with xylobiose epoxide inhibitor [Aspergillus aculeatus ATCC 16872],6Q8N_B GH10 endo-xylanase in complex with xylobiose epoxide inhibitor [Aspergillus aculeatus ATCC 16872]
3.60e-55	28	296	5	258	The mutant crystal structure of b-1,4-Xylanase (XynAS9_V43P/G44E) from Streptomyces sp. 9 [Streptomyces sp.],3WUG_A The mutant crystal structure of b-1,4-Xylanase (XynAS9_V43P/G44E) with xylobiose from Streptomyces sp. 9 [Streptomyces sp.]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
7.38e-75	16	292	9	276	Endo-1,4-beta-xylanase D OS=Talaromyces funiculosus OX=28572 GN=xynD PE=1 SV=1
2.93e-60	28	292	38	295	Endo-1,4-beta-xylanase 5 OS=Magnaporthe grisea OX=148305 GN=XYL5 PE=3 SV=1
2.93e-60	28	292	38	295	Endo-1,4-beta-xylanase 5 OS=Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) OX=242507 GN=XYL5 PE=3 SV=1
1.35e-58	28	293	94	349	Endo-1,4-beta-xylanase A OS=Phanerodontia chrysosporium OX=2822231 GN=xynA PE=1 SV=1
9.99e-56	28	296	84	343	Endo-1,4-beta-xylanase C OS=Phanerodontia chrysosporium OX=2822231 GN=xynC PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000304	0.999648	CS pos: 17-18. Pr: 0.9796

TMHMM Annotations help

There is no transmembrane helices in P175DRAFT_0506547-t39_1-p1.

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