You are browsing environment: HUMAN GUT
CAZyme Information: MGYG000000088_00132
You are here: Home > Sequence: MGYG000000088_00132
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 | Streptococcus lutetiensis | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; Streptococcus; Streptococcus lutetiensis | |||||||||||
| CAZyme ID | MGYG000000088_00132 | |||||||||||
| CAZy Family | GH77 | |||||||||||
| CAZyme Description | 4-alpha-glucanotransferase | |||||||||||
| CAZyme Property |
|
|||||||||||
| Genome Property |
|
|||||||||||
| Gene Location | Start: 129729; End: 131231 Strand: - | |||||||||||
Full Sequence Download help
| MKKRASGVLM HITSLPGKQG VGTFGQEAYN FVDFLVETDQ TYWQILPLTT TSYGDSPYQS | 60 |
| FSATAGNTHL IDLELLCKQG YLAKEDYETV NFGDDLENVD YARIFEARRP ILEKAVAEFM | 120 |
| QSADNQKALA EFEKEATWVK DYAEFMAIKE FFGNKALQEW DDKAVVRREE AALETYREKL | 180 |
| KDVITYHKVT QYFFYQQWAD LKAYANEKGI KIIGDMPIYV SADSVEVWTM PELFKVDAEK | 240 |
| TPLCIAGVPA DSFSDDGQLW GNPIYDWENH KKTNYAWWVY RIKEGIKLYD LLRIDHFKGF | 300 |
| SDYWEIRGDY KTANDGSWQP GPGRALFDVV RDELGELPII AENLGYIDAK AEQLLTDTAF | 360 |
| PGMKILEFGF YDTEGKSIDA PHNCNKNSVA YNGTHDNEVV NGWYDNLTDE QKAFVDAYTH | 420 |
| RHEGEPITQT MLRTLFATVS DIAIATMQDI LDKPAESRMN IPNTVGGNWQ WRILKEDLTD | 480 |
| ERKAFLKDIT ALYCRKNTFK | 500 |
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH77 | 10 | 493 | 4.5e-156 | 0.9939271255060729 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| PRK14508 | PRK14508 | 0.0 | 1 | 495 | 2 | 496 | 4-alpha-glucanotransferase; Provisional |
| pfam02446 | Glyco_hydro_77 | 0.0 | 10 | 473 | 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 | 2.55e-172 | 1 | 495 | 11 | 514 | 4-alpha-glucanotransferase [Carbohydrate transport and metabolism]. |
| PLN02635 | PLN02635 | 1.22e-157 | 2 | 495 | 26 | 525 | disproportionating enzyme |
| TIGR00217 | malQ | 5.74e-125 | 2 | 495 | 12 | 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 |
|---|---|---|---|---|---|
| ALT82789.1 | 0.0 | 1 | 500 | 1 | 500 |
| QQE31261.1 | 0.0 | 1 | 500 | 1 | 500 |
| VTT00955.1 | 0.0 | 1 | 500 | 1 | 500 |
| SQF42592.1 | 0.0 | 1 | 500 | 1 | 500 |
| SQG57150.1 | 0.0 | 1 | 500 | 1 | 500 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 6M6T_A | 1.72e-277 | 2 | 497 | 3 | 498 | 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] |
| 1TZ7_A | 1.82e-133 | 4 | 496 | 22 | 504 | Aquifexaeolicus amylomaltase [Aquifex aeolicus],1TZ7_B Aquifex aeolicus amylomaltase [Aquifex aeolicus] |
| 2OWC_A | 7.51e-132 | 4 | 487 | 8 | 493 | 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] |
| 1FP8_A | 2.00e-131 | 4 | 487 | 5 | 491 | 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] |
| 1CWY_A | 7.98e-131 | 4 | 487 | 5 | 491 | 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] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P0A3Q0 | 1.51e-196 | 1 | 497 | 1 | 497 | 4-alpha-glucanotransferase OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=malQ PE=3 SV=1 |
| P0A3Q1 | 1.51e-196 | 1 | 497 | 1 | 497 | 4-alpha-glucanotransferase OS=Streptococcus pneumoniae (strain ATCC BAA-255 / R6) OX=171101 GN=malQ PE=3 SV=1 |
| Q59266 | 7.70e-152 | 10 | 495 | 1 | 485 | 4-alpha-glucanotransferase OS=Clostridium butyricum OX=1492 GN=malQ PE=1 SV=1 |
| O66937 | 3.72e-133 | 4 | 496 | 2 | 484 | 4-alpha-glucanotransferase OS=Aquifex aeolicus (strain VF5) OX=224324 GN=malQ PE=1 SV=1 |
| O87172 | 4.37e-130 | 4 | 487 | 5 | 491 | 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 |
|---|---|---|---|---|---|
| 1.000043 | 0.000011 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |