You are browsing environment: FUNGIDB
CAZyme Information: ASPBRDRAFT_57943-t33_1-p1
You are here: Home > Sequence: ASPBRDRAFT_57943-t33_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 brasiliensis | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus brasiliensis | |||||||||||
| CAZyme ID | ASPBRDRAFT_57943-t33_1-p1 | |||||||||||
| CAZy Family | GT20 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
|
|||||||||||
| Genome Property |
|
|||||||||||
| Gene Location | ||||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| AA7 | 333 | 536 | 7.1e-46 | 0.4410480349344978 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| 212491 | SDR_c | 1.06e-42 | 38 | 274 | 1 | 232 | 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. |
| 223959 | FabG | 2.15e-40 | 35 | 273 | 5 | 244 | NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism, General function prediction only]. |
| 226674 | YdfG | 1.25e-38 | 35 | 262 | 6 | 227 | NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]. |
| 395056 | adh_short | 4.75e-36 | 36 | 234 | 1 | 187 | short chain dehydrogenase. This family contains a wide variety of dehydrogenases. |
| 237220 | PRK12828 | 1.62e-32 | 32 | 273 | 4 | 230 | short chain dehydrogenase; Provisional |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| 2.33e-30 | 13 | 271 | 461 | 721 | |
| 1.14e-23 | 284 | 755 | 5 | 491 | |
| 1.14e-23 | 284 | 755 | 5 | 491 | |
| 1.14e-23 | 284 | 755 | 5 | 491 | |
| 1.14e-23 | 284 | 755 | 5 | 491 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 2.20e-22 | 345 | 755 | 63 | 488 | Chain AAA, Chitooligosaccharide oxidase [Fusarium graminearum PH-1] |
|
| 6.25e-20 | 372 | 756 | 77 | 469 | Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens],6EO4_B Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens] |
|
| 8.26e-20 | 34 | 243 | 6 | 202 | Clavulanic Acid Dehydrogenase: Structural and Biochemical Analysis of the Final Step in the Biosynthesis of the beta-Lactamase Inhibitor Clavulanic acid [Streptomyces clavuligerus],2JAP_B Clavulanic Acid Dehydrogenase: Structural and Biochemical Analysis of the Final Step in the Biosynthesis of the beta-Lactamase Inhibitor Clavulanic acid [Streptomyces clavuligerus],2JAP_C Clavulanic Acid Dehydrogenase: Structural and Biochemical Analysis of the Final Step in the Biosynthesis of the beta-Lactamase Inhibitor Clavulanic acid [Streptomyces clavuligerus],2JAP_D Clavulanic Acid Dehydrogenase: Structural and Biochemical Analysis of the Final Step in the Biosynthesis of the beta-Lactamase Inhibitor Clavulanic acid [Streptomyces clavuligerus] |
|
| 1.11e-19 | 372 | 756 | 77 | 469 | Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens],6EO5_B Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens] |
|
| 2.37e-19 | 327 | 668 | 53 | 416 | Chain A, FAD-binding PCMH-type domain-containing protein [Fusarium graminearum PH-1] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 4.94e-76 | 8 | 271 | 5 | 262 | Short chain dehydrogenase mpl6 OS=Monascus purpureus OX=5098 GN=mpl6 PE=1 SV=1 |
|
| 4.94e-76 | 8 | 271 | 5 | 262 | Short chain dehydrogenase citE OS=Monascus ruber OX=89489 GN=citE PE=1 SV=1 |
|
| 1.92e-65 | 319 | 756 | 50 | 496 | FAD-linked oxidoreductase srdI OS=Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) OX=367110 GN=srdI PE=2 SV=1 |
|
| 3.08e-56 | 328 | 756 | 63 | 503 | FAD-linked oxidoreductase OXR1 OS=Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) OX=242507 GN=OXR1 PE=1 SV=1 |
|
| 1.15e-55 | 319 | 756 | 5 | 451 | FAD-linked oxidoreductase virF (Fragment) OS=Hypocrea virens (strain Gv29-8 / FGSC 10586) OX=413071 GN=virF PE=3 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | CS Position |
|---|---|---|
| 1.000066 | 0.000000 |