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CAZyme Information: EEP77607.1
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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 | Uncinocarpus reesii | |||||||||||
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| Lineage | Ascomycota; Eurotiomycetes; ; Onygenaceae; Uncinocarpus; Uncinocarpus reesii | |||||||||||
| CAZyme ID | EEP77607.1 | |||||||||||
| CAZy Family | GH16 | |||||||||||
| CAZyme Description | 3-isopropylmalate dehydratase | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | ||||||||||||
Enzyme Prediction help
| EC | 2.4.1.183:18 | 2.4.1.-:2 | 2.4.1.183:36 | 2.4.1.-:11 |
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CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH13 | 1484 | 1691 | 3.4e-83 | 0.5175 |
| GH13 | 2346 | 2808 | 8.3e-69 | 0.98 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| 183543 | PRK12466 | 0.0 | 427 | 889 | 14 | 468 | 3-isopropylmalate dehydratase large subunit. |
| 153133 | IPMI | 0.0 | 443 | 870 | 1 | 370 | 3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate. Aconatase-like catalytic domain of 3-isopropylmalate dehydratase and related uncharacterized proteins. 3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate 3-isopropylmalate. IPMI is involved in fungal and bacterial leucine biosynthesis and is also found in eukaryotes. |
| 272940 | leuC | 0.0 | 427 | 888 | 13 | 465 | 3-isopropylmalate dehydratase, large subunit. Members of this family are 3-isopropylmalate dehydratase, large subunit, or the large subunit domain of single-chain forms. Homoaconitase, aconitase, and 3-isopropylmalate dehydratase have similar overall structures. All are dehydratases (EC 4.2.1.-) and bind a Fe-4S iron-sulfur cluster. 3-isopropylmalate dehydratase is split into large (leuC) and small (leuD) chains in eubacteria. Several pairs of archaeal proteins resemble the leuC and leuD pair in length and sequence but even more closely resemble the respective domains of homoaconitase, and their identity is uncertain. These homologs are now described by a separate model of subfamily (rather than equivalog) homology type, and the priors and cutoffs for this model have been changed to focus this equivalog family more narrowly. [Amino acid biosynthesis, Pyruvate family] |
| 395261 | Aconitase | 0.0 | 426 | 870 | 6 | 448 | Aconitase family (aconitate hydratase). |
| 200462 | AmyAc_AGS | 0.0 | 1304 | 1771 | 1 | 569 | Alpha amylase catalytic domain found in Alpha 1,3-glucan synthase (also called uridine diphosphoglucose-1,3-alpha-glucan glucosyltransferase and 1,3-alpha-D-glucan synthase). Alpha 1,3-glucan synthase (AGS, EC 2.4.1.183) is an enzyme that catalyzes the reversible chemical reaction of UDP-glucose and [alpha-D-glucosyl-(1-3)]n to form UDP and [alpha-D-glucosyl-(1-3)]n+1. AGS is a component of fungal cell walls. The cell wall of filamentous fungi is composed of 10-15% chitin and 10-35% alpha-1,3-glucan. AGS is triggered in fungi as a response to cell wall stress and elongates the glucan chains in cell wall synthesis. This group includes proteins from Ascomycetes and Basidomycetes. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| 0.0 | 1298 | 3314 | 4 | 2289 | |
| 0.0 | 1298 | 3314 | 4 | 2285 | |
| 0.0 | 1298 | 3314 | 4 | 2285 | |
| 0.0 | 1296 | 3314 | 1 | 2299 | |
| 0.0 | 1299 | 3340 | 3 | 2329 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 1.31e-84 | 2 | 350 | 60 | 377 | Crystal structure of human UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase (DPAGT1) [Homo sapiens] |
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| 1.67e-84 | 2 | 350 | 59 | 376 | Human GPT (DPAGT1) in complex with tunicamycin [Homo sapiens],6BW5_B Human GPT (DPAGT1) in complex with tunicamycin [Homo sapiens],6BW5_C Human GPT (DPAGT1) in complex with tunicamycin [Homo sapiens],6BW5_D Human GPT (DPAGT1) in complex with tunicamycin [Homo sapiens] |
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| 1.12e-83 | 2 | 350 | 60 | 377 | Crystal structure of human UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase (DPAGT1) (V264G mutant) [Homo sapiens],5O5E_A Crystal structure of human UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase (DPAGT1) (V264G mutant) in complex with tunicamycin [Homo sapiens],6FWZ_A Crystal structure of human UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase (DPAGT1) (V264G mutant) in complex with UDP-GlcNAc [Homo sapiens] |
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| 2.65e-83 | 2 | 350 | 59 | 376 | Human GPT (DPAGT1) H129 variant in complex with tunicamycin [Homo sapiens],6BW6_B Human GPT (DPAGT1) H129 variant in complex with tunicamycin [Homo sapiens],6BW6_C Human GPT (DPAGT1) H129 variant in complex with tunicamycin [Homo sapiens],6BW6_D Human GPT (DPAGT1) H129 variant in complex with tunicamycin [Homo sapiens] |
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| 6.31e-70 | 437 | 887 | 44 | 442 | The reduced form of MJ0499 [Methanocaldococcus jannaschii DSM 2661],4NQY_B The reduced form of MJ0499 [Methanocaldococcus jannaschii DSM 2661] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 0.0 | 1298 | 3340 | 11 | 2308 | Cell wall alpha-1,3-glucan synthase ags1 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=ags1 PE=1 SV=3 |
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| 0.0 | 1313 | 3340 | 20 | 2295 | Cell wall alpha-1,3-glucan synthase mok11 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=mok11 PE=3 SV=2 |
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| 0.0 | 426 | 1147 | 12 | 733 | 3-isopropylmalate dehydratase OS=Rhizomucor pusillus OX=4840 GN=LEUA PE=3 SV=1 |
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| 0.0 | 1293 | 3310 | 5 | 2217 | Cell wall alpha-1,3-glucan synthase mok12 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=mok12 PE=3 SV=1 |
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| 0.0 | 1318 | 3340 | 24 | 2256 | Cell wall alpha-1,3-glucan synthase mok13 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=mok13 PE=3 SV=2 |
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | CS Position |
|---|---|---|
| 0.783896 | 0.216096 |
TMHMM Annotations download full data without filtering help
| Start | End |
|---|---|
| 5 | 22 |
| 65 | 84 |
| 97 | 119 |
| 139 | 161 |
| 166 | 188 |
| 198 | 220 |
| 233 | 255 |
| 2262 | 2284 |
| 3015 | 3037 |
| 3057 | 3075 |
| 3080 | 3102 |
| 3112 | 3134 |
| 3147 | 3169 |
| 3189 | 3211 |
| 3235 | 3254 |
| 3269 | 3291 |