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CAZyme Information: MGYG000001234_00062
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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 | Peptostreptococcus sp900759325 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Peptostreptococcales; Peptostreptococcaceae; Peptostreptococcus; Peptostreptococcus sp900759325 | |||||||||||
| CAZyme ID | MGYG000001234_00062 | |||||||||||
| CAZy Family | GH77 | |||||||||||
| CAZyme Description | 4-alpha-glucanotransferase | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 76836; End: 78314 Strand: - | |||||||||||
Full Sequence Download help
| MTNTRKAGIL LPIFSLPSKY GVGSLGHCAY EFVDFLVRTG QSVWQILPIT ATAAIDEYSP | 60 |
| YKSVCAFSGN YDLIDIDMLV GKGLVDWNFI NSVYQGYYQA DPRYADYAKA RSLKMIIFRE | 120 |
| AFSNFDPKHD QAYKDFKKEN AFWLDDFAKY MALKEANDEK PYWEWPNPAN KPNPDTIDFH | 180 |
| CFLQYLFFDQ WHQLKKYAND RGIEIFGDMP IYVSRDSSDF YYNRDMFLTD EKGEPHQISG | 240 |
| VPPDEFSATG QVWGNPLYDW DYLKKHKFDW WVKRIQKSLE LYDILRIDHF RGFESFYSID | 300 |
| PVTRDAMNGR WIKAPGKELF DQVKKEIKNA NIVAEDLGII TDEVRDLLDY TGFPGMKIVQ | 360 |
| FGFSSDADNL NLPHNYPKNS VAYTGTHDNT SLAEWLKTCS PSEFSYAEAY LRMSAYDRYT | 420 |
| ECLIRAVMMT NSYMAIIPLQ DWYDFEGWSR INTPGIDEGN WIFRMLPHEM YNHDLEGYIS | 480 |
| YITGLYGRFK NR | 492 |
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH77 | 11 | 481 | 3.7e-149 | 0.9838056680161943 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| PRK14508 | PRK14508 | 0.0 | 1 | 488 | 1 | 496 | 4-alpha-glucanotransferase; Provisional |
| pfam02446 | Glyco_hydro_77 | 0.0 | 11 | 465 | 1 | 457 | 4-alpha-glucanotransferase. These enzymes EC:2.4.1.25 transfer a segment of a (1,4)-alpha-D-glucan to a new 4-position in an acceptor, which may be glucose or (1,4)-alpha-D-glucan. |
| COG1640 | MalQ | 1.51e-141 | 5 | 488 | 14 | 514 | 4-alpha-glucanotransferase [Carbohydrate transport and metabolism]. |
| PLN02635 | PLN02635 | 3.03e-141 | 5 | 465 | 28 | 500 | disproportionating enzyme |
| TIGR00217 | malQ | 9.68e-125 | 1 | 488 | 10 | 513 | 4-alpha-glucanotransferase. This enzyme is known as amylomaltase and disproportionating enzyme. [Energy metabolism, Biosynthesis and degradation of polysaccharides] |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QIP48587.1 | 8.81e-149 | 5 | 488 | 4 | 495 |
| SQG33199.1 | 8.81e-149 | 5 | 488 | 4 | 495 |
| AYF53877.1 | 8.97e-149 | 5 | 488 | 4 | 492 |
| QPW60579.1 | 1.80e-148 | 5 | 488 | 4 | 492 |
| QPW55448.1 | 2.55e-148 | 5 | 488 | 4 | 492 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 6M6T_A | 1.22e-129 | 1 | 488 | 1 | 496 | ChainA, 4-alpha-glucanotransferase [Streptococcus agalactiae],6M6T_B Chain B, 4-alpha-glucanotransferase [Streptococcus agalactiae],6M6T_C Chain C, 4-alpha-glucanotransferase [Streptococcus agalactiae],6M6T_D Chain D, 4-alpha-glucanotransferase [Streptococcus agalactiae],6M6T_E Chain E, 4-alpha-glucanotransferase [Streptococcus agalactiae],6M6T_F Chain F, 4-alpha-glucanotransferase [Streptococcus agalactiae],6M6T_G Chain G, 4-alpha-glucanotransferase [Streptococcus agalactiae],6M6T_H Chain H, 4-alpha-glucanotransferase [Streptococcus agalactiae] |
| 1CWY_A | 3.24e-122 | 5 | 470 | 5 | 482 | CrystalStructure Of Amylomaltase From Thermus Aquaticus, A Glycosyltransferase Catalysing The Production Of Large Cyclic Glucans [Thermus aquaticus],1ESW_A X-Ray Structure Of Acarbose Bound To Amylomaltase From Thermus Aquaticus. Implications For The Synthesis Of Large Cyclic Glucans [Thermus aquaticus] |
| 1FP8_A | 3.24e-122 | 5 | 470 | 5 | 482 | StructureOf The Amylomaltase From Thermus Thermophilus Hb8 In Space Group P21212 [Thermus thermophilus],1FP9_A Structure Of Amylomaltase From Thermus Thermophilus Hb8 In Space Group C2 [Thermus thermophilus] |
| 2OWC_A | 2.19e-120 | 5 | 470 | 8 | 484 | Structureof a covalent intermediate in Thermus thermophilus amylomaltase [Thermus thermophilus],2OWW_A Covalent intermediate in amylomaltase in complex with the acceptor analog 4-deoxyglucose [Thermus thermophilus],2OWX_A THERMUS THERMOPHILUS AMYLOMALTASE AT pH 5.6 [Thermus thermophilus] |
| 5JIW_A | 4.12e-120 | 5 | 470 | 5 | 482 | Crystalstructure of Thermus aquaticus amylomaltase (GH77) in complex with a 34-meric cycloamylose [Thermus aquaticus] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P0A3Q1 | 7.80e-141 | 5 | 488 | 4 | 495 | 4-alpha-glucanotransferase OS=Streptococcus pneumoniae (strain ATCC BAA-255 / R6) OX=171101 GN=malQ PE=3 SV=1 |
| P0A3Q0 | 7.80e-141 | 5 | 488 | 4 | 495 | 4-alpha-glucanotransferase OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=malQ PE=3 SV=1 |
| Q59266 | 4.70e-135 | 13 | 488 | 3 | 485 | 4-alpha-glucanotransferase OS=Clostridium butyricum OX=1492 GN=malQ PE=1 SV=1 |
| P72785 | 2.30e-123 | 1 | 488 | 1 | 499 | 4-alpha-glucanotransferase OS=Synechocystis sp. (strain PCC 6803 / Kazusa) OX=1111708 GN=malQ PE=3 SV=1 |
| O87172 | 1.78e-121 | 5 | 470 | 5 | 482 | 4-alpha-glucanotransferase OS=Thermus thermophilus OX=274 GN=malQ PE=1 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000056 | 0.000007 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |