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CAZyme Information: MGYG000000180_00064
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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 | Collinsella sp003459505 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Actinobacteriota; Coriobacteriia; Coriobacteriales; Coriobacteriaceae; Collinsella; Collinsella sp003459505 | |||||||||||
| CAZyme ID | MGYG000000180_00064 | |||||||||||
| CAZy Family | GH13 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 69250; End: 72546 Strand: + | |||||||||||
Full Sequence Download help
| MRLIHNSRLP QFRTPFGAVT TGTSVSLSVI LEDADPNQAT LTLRTWVDEI GESRYPMTHE | 60 |
| GDGIFSVELE CTEPCLIWYS FICNIEGQPE VRLGAPQGRT GGEGVTYDYA EVPSFQVTVY | 120 |
| KHRENRPTWY ECGMVYQIFP DRYARDENWR ERTLAEVEKP RNGIQRRMVE DWNEPPVYER | 180 |
| AEDGSIKTWD FYGGSLKGIQ NDLPRIAELG FTAIYLNPIF EAASNHRYDT ADYTKIDPIL | 240 |
| GTEQDFTELC QAAEKLGISI ILDGVFNHTG DDSIYFNRYG NYPGVGAWQS EDSPWRDAFY | 300 |
| FHEDGSYDCW WGVGNMPAIN ESSELVRERL LGKDGVIRKW LRAGAHGWRL DVADELSDDF | 360 |
| LAEIKKAVLA EKPDALLLGE VWEDASNKIS YGHLRRYLQG SELDSAMDYP FRDMVIGFLM | 420 |
| GYKNAYQAAE EIETLRENYP REALSCALNL LSSHDRPRII SVLGGGPDES QLPECERSKW | 480 |
| RLDENSMGLA KSRFWLATLM QMTFPGVPSI YYGDEYGLEG LTDPGNRRTL PTKDQLHDFD | 540 |
| TLAIVKNASA VRRALPFMID GEIKAFALND EVLAYNRTGR DGESATVIIN RSLRNSHRVT | 600 |
| IPALDECASD VISGHEREIH NGTVTLDLYP LGSSIIYHHA EQRLQEPLDH GAGVVCHITS | 660 |
| VPTDDGKPGT IGAPTRRFID HLAAMGMRYW QVLPVNPTDF FRSPYAGPSA FAGNIDLLPE | 720 |
| SHEELAADFE TWKARGGEDA DPLYTAFKHR NADWLEKYCV YMAVKKYFEG ESRHDWPADV | 780 |
| ARYNEHLIDD KRFHDEAELQ AYMQYRFDLA WCELMNYAHK KGIEVIGDIP MYVSDDSADA | 840 |
| WSEPENFWLS DTGKAIEISG APPDNFAPEG QVWGNPTFRW DHMKQNGYSW WMDRLRRAFS | 900 |
| LYDRVRLDHF LGFHSYFSIP TGKACADGRW LAGPGKDLFQ TAYDELGPLN FIAEDLGYLT | 960 |
| PGVRAMASTC GFPGMDVLEF SDYDVRSGVH PTPGKILYTS THDTSTLAGW CTRSFAGGDE | 1020 |
| PSGVEVAAKL MSDALASDAP LVMMPLQDVL GLSDDARMNV PGVATGNWTW QADEADVAAA | 1080 |
| EGKTAQLLRN THRFWGEA | 1098 |
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH13 | 194 | 524 | 5.1e-122 | 0.9936708860759493 |
| GH77 | 729 | 1082 | 2e-100 | 0.7449392712550608 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| PRK14510 | PRK14510 | 0.0 | 1 | 1071 | 1 | 1191 | bifunctional glycogen debranching protein GlgX/4-alpha-glucanotransferase. |
| cd11338 | AmyAc_CMD | 2.64e-175 | 133 | 563 | 2 | 389 | Alpha amylase catalytic domain found in cyclomaltodextrinases and related proteins. Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). 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. |
| PRK14508 | PRK14508 | 3.30e-150 | 647 | 1070 | 2 | 472 | 4-alpha-glucanotransferase; Provisional |
| pfam02446 | Glyco_hydro_77 | 2.65e-136 | 657 | 1070 | 2 | 455 | 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. |
| PRK10785 | PRK10785 | 2.35e-98 | 127 | 603 | 116 | 568 | maltodextrin glucosidase; Provisional |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| AZH69620.1 | 0.0 | 1 | 1098 | 1 | 1098 |
| ATP53560.1 | 0.0 | 1 | 1098 | 1 | 1098 |
| QIA33253.1 | 0.0 | 1 | 1098 | 1 | 1098 |
| AEB07182.1 | 0.0 | 1 | 1094 | 1 | 1094 |
| QOY60572.1 | 0.0 | 1 | 1093 | 1 | 1083 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 1CWY_A | 3.02e-86 | 648 | 1088 | 3 | 493 | 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 | 3.02e-86 | 648 | 1088 | 3 | 493 | 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 | 4.42e-86 | 648 | 1088 | 6 | 495 | 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 | 3.87e-84 | 648 | 1088 | 3 | 493 | Crystalstructure of Thermus aquaticus amylomaltase (GH77) in complex with a 34-meric cycloamylose [Thermus aquaticus] |
| 2X1I_A | 5.34e-84 | 653 | 1083 | 8 | 488 | glycosidehydrolase family 77 4-alpha-glucanotransferase from thermus brockianus [Thermus brockianus] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P36905 | 1.98e-98 | 3 | 647 | 256 | 931 | Amylopullulanase OS=Thermoanaerobacterium saccharolyticum OX=28896 GN=apu PE=3 SV=2 |
| P16950 | 3.33e-94 | 3 | 647 | 253 | 929 | Amylopullulanase OS=Thermoanaerobacter thermohydrosulfuricus OX=1516 GN=apu PE=1 SV=1 |
| P38939 | 5.29e-93 | 3 | 647 | 253 | 928 | Amylopullulanase OS=Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) OX=340099 GN=apu PE=1 SV=2 |
| P38536 | 2.20e-92 | 3 | 647 | 256 | 930 | Amylopullulanase OS=Thermoanaerobacterium thermosulfurigenes OX=33950 GN=amyB PE=3 SV=2 |
| P0A3Q0 | 2.95e-89 | 652 | 1080 | 6 | 481 | 4-alpha-glucanotransferase OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=malQ PE=3 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 |
|---|---|---|---|---|---|
| 1.000070 | 0.000001 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |