You are browsing environment: FUNGIDB
CAZyme Information: Z517_03799-t43_1-p1
You are here: Home > Sequence: Z517_03799-t43_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 | Fonsecaea pedrosoi | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Fonsecaea; Fonsecaea pedrosoi | |||||||||||
| CAZyme ID | Z517_03799-t43_1-p1 | |||||||||||
| CAZy Family | GH125 | |||||||||||
| CAZyme Description | glycogen debranching enzyme | |||||||||||
| CAZyme Property |
|
|||||||||||
| Genome Property |
|
|||||||||||
| Gene Location | Start: 5020916; End:5027790 Strand: - | |||||||||||
Full Sequence Download help
| MPPKTHQSTR QVYLLPLTDA GAPDVPNEYI YLPAPTEPAY YLRFAIEGTS SICRQGSLWV | 60 |
| NFPLKGQPFD RKRYHEFKLH PDFNRTLEID IPITSAGAFS FYTTYSPLPE FATGDVESPE | 120 |
| PTRTPTYYVD IEPSLRLGGS CLPLDALGIF SVVSKFMGNY PGDWKKHLRG ISARGYNMVH | 180 |
| FTPLQQRGES NSPYSLYDQL AFDADLFPGG EDDVARMVKS MEEEHELLGL TDVVFNHTAN | 240 |
| NSKWLEEHPE AGYSVETAPW LESALDVDNA LLEYSNNLTS LGLPTVFNST SDLDLVVAGI | 300 |
| NEHVIHKIRL WEYFVCDVKS DTQAVTEAWK KGAVKLPPEG FENAIGGGLD SLKSWSLSQK | 360 |
| AAFILDKGML DSLRVDGQYS RLRIDGRFSR KVDPGVGAAI LTTLFGRYKD GADTKPAEEE | 420 |
| ITAIINELNL PFYKEFDADC AAILDQTKGR LQYTRMDSHG PRLGPITKEN PLIETYFARL | 480 |
| PQNKTTAKHD PKALSLAVNG WIWAADAMKD NAGPDWRPYL RRELIPWSDC VKLRYGKGPE | 540 |
| DNPYLWEHMT KYVRLMAKYF TAFRIDNCHS TPIHVAEYLL DEARKVQPNL AVFAELFTGN | 600 |
| EQMDYVFVKR LGLSALIREA MQAWSTQELS RVVHRHCGRP IGSFELNVPS SLHNKLENGS | 660 |
| VNGDGPQTRE VVKHIRESPV HALFMDCTHD NEMPAQKRDA RDTLPTAALV NMCGCATGSV | 720 |
| MGFDEIYPKL VDLVNENRRY ASISSEGEVH TGAGEGGIAG VKKLMNHIHT MMGKDGYDET | 780 |
| FLHHEGELIT LHRVHPDSRK GYFLIAHTAF PGFGNGNGGM SPVHLAGTKV RPLGAWVLEV | 840 |
| DQSEQAKKEA LGDKEYLVGL PSRVRNIKGS TIHTENGDTT ITIADFFPPG SIALFETWVP | 900 |
| SAEHSLGLGA FISSGTDEAF GELDLIDLNF VLYRCEAEER DTSDGQDGVY NVPNHGPLVY | 960 |
| AGLQGWWSVL EPIVRRNDLG HPLCNHLRQG QWALDFLVGR MERIAKKEEY TRLQKPAQWL | 1020 |
| KERFDAVRVI PSFLLPRYFA LILQTAYDAA FKRAIELMSP NIQHGQNFLQ SLAVVSIQQT | 1080 |
| GYVKSASLWP DKSVPSLAAG LPHFSVSWAR CWGRDVFISL RGLYLCTGRF AEAKEHIKAF | 1140 |
| GSVLKHGMIP NLLSSGAAPR YNSRDSPWFF LQNIQDYTKI APDGLSILQE KVPRRFLPYD | 1200 |
| DTWFPWDDPR AYSKESTVQE IIQEILQRHA SGLSFREHNA GPQLDMQMRP EGFQIEVHVD | 1260 |
| WKTGIIFGGS QWNCGTWMDK MGESERAGSK GVPGTPRDGA AVEITGLLYS ALRWVGHLHE | 1320 |
| AGNYPWSGVE TDSGEKISFI EWADRIRANF EKCYWIPVNP KDDIDDDVDP KIINRRGIYK | 1380 |
| DLYKSGKEYE DYQLRPNFPI AMVVAPDLFT PERALHALKV ADDVLRGPTG MATLDPSDLN | 1440 |
| YRPYYNNSED STDFATSKGR NYHQGPEWLW PTGFFLRALL YFDLKRRTDS AGRMESYQQV | 1500 |
| TRRLEGCKQA IKDSPWKGLT ELTNKNGSFC ADSSYYITNP NVGNKESTED WRIRGYNPLT | 1560 |
| PPDLLQHEIP QTPASKSTVL AGRSDCVSVV QDRDPLRRLL VIVGPCSIHD PVSALEYCDR | 1620 |
| LLKMKEKYKD ELVIVMRSYL EKPRTTVGWK GLINDPEIDG SFLINKGLRL SRQLFVDLTS | 1680 |
| KGMPIASEML DTISPQFLAD LLSIGAVGAR TTESQLHREL ASGLSFPVGF KNGTDGTLGV | 1740 |
| AIDAIGAVKH PHHFLSVTKP GVVAIVGTVG NEDCFVILRG GTTGTNYDAT SIKNAKEMLR | 1800 |
| KKGLNERVMV DCSHGNSEKQ HKNQPKVAKV LADQIAAGEE AIMGVMIESH INEGNQKVPP | 1860 |
| EGKAGLKYGV SITDACIGWE DTETVLETLA DAVRRRRDLL GKKEVNGAAG PQQNGHA | 1917 |
Enzyme Prediction help
| EC | 2.4.1.25:2 | 3.2.1.33:2 | 2.4.1.25:2 | 3.2.1.33:2 | 2.4.1.25:22 | 3.2.1.33:21 |
|---|
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH13 | 1094 | 1534 | 1.8e-198 | 0.9700460829493087 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| 237190 | PRK12755 | 0.0 | 1545 | 1897 | 3 | 351 | phospho-2-dehydro-3-deoxyheptonate aldolase; Provisional |
| 223794 | AroG1 | 0.0 | 1544 | 1897 | 1 | 350 | 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) synthase [Amino acid transport and metabolism]. |
| 236435 | PRK09261 | 0.0 | 1544 | 1897 | 1 | 348 | phospho-2-dehydro-3-deoxyheptonate aldolase; Validated |
| 200466 | AmyAc_Glg_debranch_2 | 0.0 | 126 | 623 | 1 | 478 | Alpha amylase catalytic domain found in glycogen debranching enzymes. Debranching enzymes facilitate the breakdown of glycogen through glucosyltransferase and glucosidase activity. These activities are performed by a single enzyme in mammals, yeast, and some bacteria, but by two distinct enzymes in Escherichia coli and other bacteria. Debranching enzymes perform two activities, 4-alpha-D-glucanotransferase (EC 2.4.1.25) and amylo-1,6-glucosidase (EC 3.2.1.33). 4-alpha-D-glucanotransferase catalyzes the endohydrolysis of 1,6-alpha-D-glucoside linkages at points of branching in chains of 1,4-linked alpha-D-glucose residues. Amylo-alpha-1,6-glucosidase catalyzes the endohydrolysis of 1,6-alpha-D-glucoside linkages at points of branching in chains of 1,4-linked alpha-D-glucose residues. The catalytic triad (DED), which is highly conserved in other debranching enzymes, is not present in this group. 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. |
| 273673 | glyc_debranch | 0.0 | 32 | 1534 | 10 | 1447 | glycogen debranching enzymye. glycogen debranching enzyme possesses two different catalytic activities; oligo-1,4-->1,4-glucantransferase (EC 2.4.1.25) and amylo-1,6-glucosidase (EC 3.2.1.33). Site directed mutagenesis studies in S. cerevisiae indicate that the transferase and glucosidase activities are independent and located in different regions of the polypeptide chain. Proteins in this model belong to the larger alpha-amylase family. The model covers eukaryotic proteins with a seed composed of human, nematode and yeast sequences. Yeast seed sequence is well characterized. The model is quite rigorous; either query sequence yields large bit score or it fails to hit the model altogether. There doesn't appear to be any middle ground. [Energy metabolism, Biosynthesis and degradation of polysaccharides] |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QGA17275.1|GH13_25|GH133 | 0.0 | 7 | 1534 | 2 | 1500 |
| APA06511.1|GH13_25|GH133 | 0.0 | 9 | 1534 | 3 | 1524 |
| ATZ46434.1|GH13_25|GH133 | 0.0 | 9 | 1534 | 3 | 1524 |
| QKX54581.1|GH13_25|GH133 | 0.0 | 8 | 1534 | 3 | 1500 |
| QSZ35219.1|GH13_25|GH133 | 0.0 | 9 | 1534 | 3 | 1524 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 7EKU_A | 0.0 | 8 | 1534 | 2 | 1505 | Chain A, 4-alpha-glucanotransferase [[Candida] glabrata CBS 138],7EKU_B Chain B, 4-alpha-glucanotransferase [[Candida] glabrata CBS 138] |
| 5D06_A | 0.0 | 8 | 1534 | 2 | 1505 | Crystal Structure of the Candida Glabrata Glycogen Debranching Enzyme [[Candida] glabrata CBS 138],5D06_B Crystal Structure of the Candida Glabrata Glycogen Debranching Enzyme [[Candida] glabrata CBS 138] |
| 5D0F_A | 0.0 | 8 | 1534 | 2 | 1505 | Crystal Structure of the Candida Glabrata Glycogen Debranching Enzyme (E564Q) in complex with maltopentaose [[Candida] glabrata CBS 138],5D0F_B Crystal Structure of the Candida Glabrata Glycogen Debranching Enzyme (E564Q) in complex with maltopentaose [[Candida] glabrata CBS 138] |
| 7EIM_A | 0.0 | 8 | 1534 | 2 | 1505 | Chain A, 4-alpha-glucanotransferase [[Candida] glabrata CBS 138],7EIM_B Chain B, 4-alpha-glucanotransferase [[Candida] glabrata CBS 138],7EJP_A Chain A, 4-alpha-glucanotransferase [[Candida] glabrata CBS 138],7EJP_B Chain B, 4-alpha-glucanotransferase [[Candida] glabrata CBS 138],7EJT_A Chain A, 4-alpha-glucanotransferase [[Candida] glabrata CBS 138],7EJT_B Chain B, 4-alpha-glucanotransferase [[Candida] glabrata CBS 138] |
| 7EKW_A | 0.0 | 8 | 1534 | 2 | 1505 | Chain A, 4-alpha-glucanotransferase [[Candida] glabrata CBS 138],7EKW_B Chain B, 4-alpha-glucanotransferase [[Candida] glabrata CBS 138] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| sp|Q06625|GDE_YEAST | 0.0 | 14 | 1534 | 6 | 1511 | Glycogen debranching enzyme OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=GDB1 PE=1 SV=1 |
| sp|A8BQB4|GDE_HORSE | 1.31e-310 | 37 | 1530 | 26 | 1512 | Glycogen debranching enzyme OS=Equus caballus OX=9796 GN=AGL PE=2 SV=1 |
| sp|Q2PQH8|GDE_CANLF | 1.66e-307 | 37 | 1530 | 26 | 1512 | Glycogen debranching enzyme OS=Canis lupus familiaris OX=9615 GN=AGL PE=2 SV=1 |
| sp|P35573|GDE_HUMAN | 4.31e-303 | 37 | 1530 | 26 | 1511 | Glycogen debranching enzyme OS=Homo sapiens OX=9606 GN=AGL PE=1 SV=3 |
| sp|P35574|GDE_RABIT | 2.33e-302 | 37 | 1530 | 49 | 1534 | Glycogen debranching enzyme OS=Oryctolagus cuniculus OX=9986 GN=AGL PE=1 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | CS Position |
|---|---|---|
| 1.000054 | 0.000000 |