dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: OTA20481.1

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Basic Information help

Species

Hortaea werneckii

Lineage

Ascomycota; Dothideomycetes; ; Teratosphaeriaceae; Hortaea; Hortaea werneckii

CAZyme ID

OTA20481.1

CAZy Family

AA11

CAZyme Description

unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
635		70920.23	6.9372

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

No EC number prediction in OTA20481.1.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GT17	328	619	8.5e-78	0.9436619718309859

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
235546	fabG	8.10e-69	42	303	1	245	3-oxoacyl-ACP reductase FabG.
212491	SDR_c	2.11e-67	49	299	1	234	classical (c) SDRs. 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 ketoacyl reductases 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.
235975	FabG-like	3.10e-64	42	305	1	251	SDR family oxidoreductase.
404451	adh_short_C2	1.16e-62	59	303	7	236	Enoyl-(Acyl carrier protein) reductase.
223959	FabG	2.59e-62	45	303	4	251	NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism, General function prediction only].

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start
1.20e-133	320	632	77	386
2.12e-128	281	630	25	372
5.78e-128	281	630	25	372
1.63e-127	281	630	25	372
9.17e-127	281	630	25	372

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
4.66e-34	36	306	3	267	Crystal Structure of Levodione Reductase [Leifsonia aquatica],1IY8_B Crystal Structure of Levodione Reductase [Leifsonia aquatica],1IY8_C Crystal Structure of Levodione Reductase [Leifsonia aquatica],1IY8_D Crystal Structure of Levodione Reductase [Leifsonia aquatica],1IY8_E Crystal Structure of Levodione Reductase [Leifsonia aquatica],1IY8_F Crystal Structure of Levodione Reductase [Leifsonia aquatica],1IY8_G Crystal Structure of Levodione Reductase [Leifsonia aquatica],1IY8_H Crystal Structure of Levodione Reductase [Leifsonia aquatica]
4.78e-32	43	309	15	263	Structure of Serratia marcescens 2,3-butanediol dehydrogenase [Serratia marcescens],6XEW_B Structure of Serratia marcescens 2,3-butanediol dehydrogenase [Serratia marcescens]
6.53e-32	43	304	15	256	Structure of Serratia marcescens 2,3-butanediol dehydrogenase mutant Q247A [Serratia marcescens],6VSP_B Structure of Serratia marcescens 2,3-butanediol dehydrogenase mutant Q247A [Serratia marcescens]
3.85e-31	43	302	2	245	Chain A, Glucose/ribitol dehydrogenase [Acetivibrio thermocellus]
4.25e-31	43	304	15	256	Structure of Serratia marcescens 2,3-butanediol dehydrogenase mutant Q247A/V139Q [Serratia marcescens],6XEX_B Structure of Serratia marcescens 2,3-butanediol dehydrogenase mutant Q247A/V139Q [Serratia marcescens]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
2.50e-36	43	302	2	244	3-oxoacyl-[acyl-carrier-protein] reductase FabG OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=fabG PE=3 SV=1
2.40e-33	36	306	3	267	Levodione reductase OS=Leifsonia aquatica OX=144185 GN=lvr PE=1 SV=1
7.67e-33	42	309	30	301	Short-chain dehydrogenase reductase 2a OS=Arabidopsis thaliana OX=3702 GN=SDR2a PE=3 SV=1
9.47e-33	42	303	7	245	Borneol dehydrogenase, mitochondrial OS=Lavandula x intermedia OX=1196215 GN=BDH PE=1 SV=1
8.11e-32	40	308	2	257	Short-chain dehydrogenase reductase 3a OS=Arabidopsis thaliana OX=3702 GN=SDR3a PE=2 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000049	0.000000

TMHMM Annotations help

There is no transmembrane helices in OTA20481.1.