Species | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae; Porphyromonas; | |||||||||||
CAZyme ID | MGYG000003813_00278 | |||||||||||
CAZy Family | GH77 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 43536; End: 45275 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH77 | 45 | 576 | 4.5e-120 | 0.9291497975708503 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
PLN02950 | PLN02950 | 6.93e-132 | 17 | 575 | 249 | 892 | 4-alpha-glucanotransferase |
pfam02446 | Glyco_hydro_77 | 1.52e-130 | 29 | 577 | 1 | 459 | 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. |
PLN03236 | PLN03236 | 6.10e-115 | 3 | 575 | 43 | 715 | 4-alpha-glucanotransferase; Provisional |
COG1640 | MalQ | 4.10e-85 | 20 | 576 | 9 | 493 | 4-alpha-glucanotransferase [Carbohydrate transport and metabolism]. |
PRK14508 | PRK14508 | 3.63e-77 | 40 | 576 | 14 | 475 | 4-alpha-glucanotransferase; Provisional |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QEH41274.1 | 1.34e-117 | 26 | 579 | 208 | 707 |
AEE12916.1 | 1.80e-117 | 23 | 576 | 6 | 580 |
SCM57389.1 | 2.23e-116 | 21 | 579 | 235 | 869 |
AAQ65928.1 | 5.01e-115 | 23 | 579 | 3 | 634 |
ANH81313.1 | 6.71e-115 | 14 | 579 | 221 | 868 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1TZ7_A | 5.05e-36 | 40 | 575 | 31 | 483 | Aquifexaeolicus amylomaltase [Aquifex aeolicus],1TZ7_B Aquifex aeolicus amylomaltase [Aquifex aeolicus] |
1FP8_A | 2.54e-32 | 40 | 575 | 14 | 477 | 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 | 2.54e-32 | 40 | 575 | 14 | 477 | 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] |
2OWC_A | 6.46e-32 | 40 | 575 | 17 | 479 | 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 | 1.76e-30 | 40 | 575 | 14 | 477 | Crystalstructure of Thermus aquaticus amylomaltase (GH77) in complex with a 34-meric cycloamylose [Thermus aquaticus] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q8RXD9 | 2.42e-103 | 17 | 579 | 258 | 905 | 4-alpha-glucanotransferase DPE2 OS=Arabidopsis thaliana OX=3702 GN=DPE2 PE=1 SV=1 |
Q69Q02 | 1.52e-102 | 17 | 579 | 252 | 899 | 4-alpha-glucanotransferase DPE2 OS=Oryza sativa subsp. japonica OX=39947 GN=DPE2 PE=2 SV=1 |
Q9Z8L2 | 2.11e-52 | 26 | 575 | 26 | 502 | 4-alpha-glucanotransferase OS=Chlamydia pneumoniae OX=83558 GN=malQ PE=3 SV=1 |
Q9PKU9 | 1.02e-49 | 26 | 575 | 30 | 506 | 4-alpha-glucanotransferase OS=Chlamydia muridarum (strain MoPn / Nigg) OX=243161 GN=malQ PE=3 SV=1 |
O34022 | 4.62e-46 | 26 | 575 | 30 | 506 | 4-alpha-glucanotransferase OS=Chlamydia caviae (strain ATCC VR-813 / DSM 19441 / 03DC25 / GPIC) OX=227941 GN=malQ PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000022 | 0.000003 | 0.000001 | 0.000000 | 0.000000 | 0.000000 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.