You are browsing environment: HUMAN GUT
CAZyme Information: MGYG000002022_00105
You are here: Home > Sequence: MGYG000002022_00105
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 | Centipeda artemidis | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_C; Negativicutes; Selenomonadales; Selenomonadaceae; Centipeda; Centipeda artemidis | |||||||||||
| CAZyme ID | MGYG000002022_00105 | |||||||||||
| CAZy Family | GH13 | |||||||||||
| CAZyme Description | Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase | |||||||||||
| CAZyme Property |
|
|||||||||||
| Genome Property |
|
|||||||||||
| Gene Location | Start: 106297; End: 109746 Strand: + | |||||||||||
Full Sequence Download help
| MLEQYQVEHN SQDIYYRSIV GAAEAGARLR LGIRIRTYEP IRQVLVRLWQ DRTGERLVPL | 60 |
| ETKDTEGEQH FYTCWVNLPD HGCLLWYYFI ITAESGTYFY GNNEEMLGGV GTLSRTAPAS | 120 |
| YQITIYNKGA HTPDWFKNAV MYQIFPDRFA RAGDEIVRKK GAVIRTDWTD DPMYLKDPDT | 180 |
| KEIIAYDFFG GNLKGIIGKL DYLADLGISC IYFNPVFESE SNHHYDTGDY HKIDPMLGDI | 240 |
| EDFRTLVKEA RARGIRIILD GVFSHTGSNS IYFNRRAQYG SLGAYQSEES PYYSWYHFRN | 300 |
| YPNEYDCWWN FDTLPNVNET DPAYMDFIIT SENSVLHHWM NEGIAGWRLD VIDELPPAFS | 360 |
| KTFFSELKKH DPDAVMIGEV WEDASNKVAY GTPREYLSGN EMDSAMNYPL RTILFDFLTG | 420 |
| SADGTLTARR LASQIENYPK ENLYAMMNLI GSHDVQRAVT VLAGVPYYEG MPAIEQSRVR | 480 |
| MTPEQFDLGS RRLLMATLWQ MTYPGVPSVY YGDEIGMQGF KDPFNRRPYD WTHGNKEIRG | 540 |
| WVERFIEIRN KNDALRTGDI LPLYGAGDVV AYARTIRSGY DVFNHEKEDG VFIAAFNRNT | 600 |
| EESITIELDV SDFACGTFED CFKPSRTYEV ERGRLRVKIP PLYGLLLHER KEPRRYERKA | 660 |
| GILLHPTSLP SKYGVGDFGK EVYRFVDFLA EAGQKVWQIL PLSPVGCGYS PYQSISAFAG | 720 |
| NIMLVDPEPL VARGWLTERD LFLPYEANTA FIDFDRVKQF KKDLLEKACA AFRTDGKDDP | 780 |
| DYRAFCEKEA YWLDDYALFH AAKKEYDRAP WTEWPEKIRR RDPAALKELA EKQRDEIELD | 840 |
| RFKQYIFHTQ WNRLHDYAKK KGIEILGDMP IFIARDSADV WAHAQLFDLN EDGTPRTVAG | 900 |
| VPPDYFAASG QLWGNPQYDW DAMAKEHYAW WKDRFRKLSQ QVDIIRIDHF RGFESYWSID | 960 |
| GKAETAINGR WIKGPGKVFF DEIEKELGTL DIVAEDLGII TSEVDRLRED CGFPGMKVIQ | 1020 |
| FMLAPNEAGR VGFAVPENTI IYTGTHDNNT TVGWYMHDID EVMRETLANM VGTTSDRPQT | 1080 |
| ICKRLIKTAY ASHSRMAIIP MQDLLALDER ARMNTPGTVG INWRWSLKKD YLLQLDPQKL | 1140 |
| RALCIQYHR | 1149 |
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH77 | 664 | 1140 | 4.7e-168 | 0.97165991902834 |
| GH13 | 191 | 523 | 4.7e-134 | 0.9936708860759493 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| pfam02446 | Glyco_hydro_77 | 0.0 | 664 | 1125 | 1 | 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. |
| PRK14510 | PRK14510 | 0.0 | 9 | 1128 | 5 | 1193 | bifunctional glycogen debranching protein GlgX/4-alpha-glucanotransferase. |
| cd11338 | AmyAc_CMD | 0.0 | 138 | 560 | 1 | 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 | 0.0 | 658 | 1149 | 5 | 496 | 4-alpha-glucanotransferase; Provisional |
| PLN02635 | PLN02635 | 1.71e-171 | 639 | 1149 | 12 | 525 | disproportionating enzyme |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QNH53465.1 | 0.0 | 1 | 1149 | 1 | 1149 |
| ANR69627.1 | 0.0 | 1 | 1149 | 1 | 1149 |
| AOH47405.1 | 0.0 | 1 | 1149 | 1 | 1149 |
| AKT53142.1 | 0.0 | 1 | 1149 | 1 | 1149 |
| AME04250.1 | 0.0 | 1 | 1149 | 1 | 1149 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 2X1I_A | 9.98e-136 | 661 | 1143 | 8 | 493 | glycosidehydrolase family 77 4-alpha-glucanotransferase from thermus brockianus [Thermus brockianus] |
| 2OWC_A | 2.09e-135 | 658 | 1143 | 8 | 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] |
| 1CWY_A | 2.74e-135 | 658 | 1143 | 5 | 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 | 3.85e-135 | 658 | 1143 | 5 | 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] |
| 5JIW_A | 1.57e-133 | 658 | 1143 | 5 | 493 | 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 | 4.75e-145 | 657 | 1149 | 3 | 495 | 4-alpha-glucanotransferase OS=Streptococcus pneumoniae (strain ATCC BAA-255 / R6) OX=171101 GN=malQ PE=3 SV=1 |
| P0A3Q0 | 4.75e-145 | 657 | 1149 | 3 | 495 | 4-alpha-glucanotransferase OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=malQ PE=3 SV=1 |
| O87172 | 1.50e-134 | 658 | 1143 | 5 | 493 | 4-alpha-glucanotransferase OS=Thermus thermophilus OX=274 GN=malQ PE=1 SV=1 |
| P72785 | 8.03e-131 | 657 | 1132 | 4 | 482 | 4-alpha-glucanotransferase OS=Synechocystis sp. (strain PCC 6803 / Kazusa) OX=1111708 GN=malQ PE=3 SV=1 |
| O66937 | 9.15e-129 | 658 | 1131 | 2 | 467 | 4-alpha-glucanotransferase OS=Aquifex aeolicus (strain VF5) OX=224324 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 |
|---|---|---|---|---|---|
| 1.000032 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |