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CAZyme Information: KAF5689534.1

You are here: Home > Sequence: KAF5689534.1

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 Fusarium circinatum
Lineage Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium circinatum
CAZyme ID KAF5689534.1
CAZy Family GT32
CAZyme Description beta-glucosidase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
727 81373.75 5.5417
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_FcircinatumNRRL25331 13905 N/A 0 13905
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.21:13

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH1 3 445 5.3e-148 0.9184149184149184

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
395176 Glyco_hydro_1 3.87e-163 3 445 4 421
Glycosyl hydrolase family 1.
274539 BGL 2.64e-151 5 445 1 404
beta-galactosidase.
225343 BglB 2.14e-142 1 445 1 423
Beta-glucosidase/6-phospho-beta-glucosidase/beta-galactosidase [Carbohydrate transport and metabolism].
187654 DR_C-13_KR_SDR_c_like 1.13e-130 467 724 6 260
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs. Daunorubicin is a clinically important therapeutic compound used in some cancer treatments. Daunorubicin C-13 ketoreductase is member of the classical SDR family with a canonical glycine-rich NAD(P)-binding motif, but lacking a complete match to the active site tetrad characteristic of this group. The critical Tyr, plus the Lys and upstream Asn are present, but the catalytic Ser is replaced, generally by Gln. 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.
215455 PLN02849 4.10e-99 5 442 31 449
beta-glucosidase

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 1 445 3 447
0.0 1 445 1 445
0.0 1 445 1 445
0.0 1 445 1 445
0.0 1 445 1 445

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.19e-264 3 445 7 449
Trichoderma harzianum GH1 beta-glucosidase ThBgl2 [Trichoderma harzianum]
1.90e-260 3 445 20 462
Chain A, Glycoside hydrolase family 1 [Trichoderma reesei QM6a],6KHT_B Chain B, Glycoside hydrolase family 1 [Trichoderma reesei QM6a],6KHT_C Chain C, Glycoside hydrolase family 1 [Trichoderma reesei QM6a]
4.87e-167 3 445 25 465
Chain A, Beta-glucosidase [[Humicola] grisea var. thermoidea],4MDP_A Chain A, Beta-glucosidase [[Humicola] grisea var. thermoidea]
1.83e-163 4 445 3 432
Crystal structure of the double mutant L167W / P172L of the beta-glucosidase from Trichoderma harzianum [Trichoderma harzianum],6EFU_B Crystal structure of the double mutant L167W / P172L of the beta-glucosidase from Trichoderma harzianum [Trichoderma harzianum]
6.63e-161 4 445 3 432
Trichoderma harzianum GH1 beta-glucosidase ThBgl1 [Trichoderma harzianum],5JBK_B Trichoderma harzianum GH1 beta-glucosidase ThBgl1 [Trichoderma harzianum]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.79e-163 4 442 11 442
Beta-glucosidase 1B OS=Phanerodontia chrysosporium OX=2822231 GN=BGL1B PE=1 SV=1
3.56e-144 4 445 6 430
Beta-glucosidase 1A OS=Phanerodontia chrysosporium OX=2822231 GN=BGL1A PE=1 SV=1
4.16e-131 5 445 23 484
Raucaffricine-O-beta-D-glucosidase OS=Rauvolfia serpentina OX=4060 GN=RG PE=1 SV=1
2.21e-128 3 445 49 492
Beta-glucosidase 6 OS=Oryza sativa subsp. japonica OX=39947 GN=BGLU6 PE=1 SV=1
3.53e-125 468 725 1 257
Short-chain dehydrogenase chyC OS=Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255) OX=500485 GN=chyC PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000061 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in KAF5689534.1.