| Basic Information | |
|---|---|
| Species | Volvox carteri |
| Cazyme ID | Vocar20012173m |
| Family | GH13 |
| Protein Properties | Length: 591 Molecular Weight: 65124.3 Isoelectric Point: 7.0476 |
| Chromosome | Chromosome/Scaffold: 53 Start: 40466 End: 49906 |
| Description | starch branching enzyme 2.1 |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH13 | 132 | 449 | 7.6e-34 |
| QGTLAAATSRLEHVASLGFTAVQLMPISEHSDAWGYNPRLLMALHGAYGTPDDLRRFVDKAHSLGLGVIIDVVLHHGAVDGNSLWEYDGWGPDWNGGIYH EGGHDTQWGRGFAFWKREVLAMAEAACATWLCDFRCDGLRFDSANDLPREAIQYLTWSLRQRFPGRILTAEVTPENPQSVHELGFDSVWVHSGYFDIIQQ HRALGRGHHGGGDWAAGWDLPRLRTVMALHPGFTSPTQCIKYLLGSHDQVGCRNGGAWYKDYEMIGGQHRYAVDQYGGGRGDWSARASSRLWYTANVAAA GLPMMFMGTEFAQSGWWD | |||
| Full Sequence |
|---|
| Protein Sequence Length: 591 Download |
| MIQFGNTQVT LSQPPRLLWA YNKRAKTGQA HFSGPPRFEC RQSLRLHRAH APTYLPTMAA 60 FPSAAVDPVT GQAGPTSRSI QNPQVFTLAP QLLAASPFPD CPHGATLMSE AGREVSFKVW 120 APHAASVSLL LQGTLAAATS RLEHVASLGF TAVQLMPISE HSDAWGYNPR LLMALHGAYG 180 TPDDLRRFVD KAHSLGLGVI IDVVLHHGAV DGNSLWEYDG WGPDWNGGIY HEGGHDTQWG 240 RGFAFWKREV LAMAEAACAT WLCDFRCDGL RFDSANDLPR EAIQYLTWSL RQRFPGRILT 300 AEVTPENPQS VHELGFDSVW VHSGYFDIIQ QHRALGRGHH GGGDWAAGWD LPRLRTVMAL 360 HPGFTSPTQC IKYLLGSHDQ VGCRNGGAWY KDYEMIGGQH RYAVDQYGGG RGDWSARASS 420 RLWYTANVAA AGLPMMFMGT EFAQSGWWDV VPDRRLQWSL STDEVGTHSK ALVAGANELR 480 NRFPALRRGW ANILHEDRAN GVVAFERVIE GETRLVAVIN AGRKSWLGGD YGVWVGQAAG 540 QLEEVFCSQA TEFGGNVESG RANNEPRAMY DGKIWINLPD QCTLVFQHTL * 600 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| TIGR02402 | trehalose_TreZ | 5.0e-30 | 133 | 518 | 466 | + malto-oligosyltrehalose trehalohydrolase. Members of this family are the trehalose biosynthetic enzyme malto-oligosyltrehalose trehalohydrolase, formally known as 4-alpha-D-{(1->4)-alpha-D-glucano}trehalose trehalohydrolase (EC 3.2.1.141). It is the TreZ protein of the TreYZ pathway for trehalose biosynthesis, and alternative to the OtsAB system [Energy metabolism, Biosynthesis and degradation of polysaccharides]. | ||
| cd11350 | AmyAc_4 | 2.0e-32 | 132 | 489 | 396 | + Alpha amylase catalytic domain found in an uncharacterized protein family. 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 (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. | ||
| COG0296 | GlgB | 2.0e-42 | 133 | 566 | 484 | + 1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism] | ||
| cd11325 | AmyAc_GTHase | 1.0e-61 | 132 | 448 | 346 | + Alpha amylase catalytic domain found in Glycosyltrehalose trehalohydrolase (also called Maltooligosyl trehalose Trehalohydrolase). Glycosyltrehalose trehalohydrolase (GTHase) was discovered as part of a coupled system for the production of trehalose from soluble starch. In the first half of the reaction, glycosyltrehalose synthase (GTSase), an intramolecular glycosyl transferase, converts the glycosidic bond between the last two glucose residues of amylose from an alpha-1,4 bond to an alpha-1,1 bond, making a non-reducing glycosyl trehaloside. In the second half of the reaction, GTHase cleaves the alpha-1,4 glycosidic bond adjacent to the trehalose moiety to release trehalose and malto-oligosaccharide. Like isoamylase and other glycosidases that recognize branched oligosaccharides, GTHase contains an N-terminal extension and does not have the conserved calcium ion present in other alpha amylase family enzymes. 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. Glycosyltrehalose Trehalohydrolase Maltooligosyltrehalose Trehalohydrolase | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0003824 | catalytic activity |
| GO:0005975 | carbohydrate metabolic process |
| GO:0043169 | cation binding |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | AAU01394.1 | 0 | 139 | 587 | 428 | 859 | putative 1,4-alpha-glucan branching enzyme 2 [Toxoplasma gondii] |
| RefSeq | XP_001694399.1 | 0.0003 | 83 | 131 | 82 | 129 | predicted protein [Chlamydomonas reinhardtii] |
| RefSeq | XP_001694399.1 | 0 | 134 | 590 | 221 | 626 | predicted protein [Chlamydomonas reinhardtii] |
| RefSeq | XP_002367056.1 | 0 | 141 | 587 | 459 | 888 | 1,4-alpha-glucan branching enzyme, putative [Toxoplasma gondii ME49] |
| RefSeq | XP_627714.1 | 0 | 142 | 555 | 189 | 598 | 1,4-alpha-glucan branching enzyme; alpha-amylase; glycogen brancing enzyme [Cryptosporidium parvum Iowa II] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3m07_A | 2e-23 | 132 | 294 | 150 | 306 | A Chain A, 1.4 Angstrom Resolution Crystal Structure Of Putative Alpha Amylase From Salmonella Typhimurium |
| PDB | 1eha_A | 4e-20 | 99 | 446 | 75 | 423 | A Chain A, Crystal Structure Of Glycosyltrehalose Trehalohydrolase From Sulfolobus Solfataricus |
| PDB | 3vgb_A | 8e-20 | 99 | 446 | 75 | 423 | A Chain A, Crystal Structure Of Glycosyltrehalose Trehalohydrolase From Sulfolobus Solfataricus |
| PDB | 1eh9_A | 8e-20 | 99 | 446 | 75 | 423 | A Chain A, Crystal Structure Of Sulfolobus Solfataricus Glycosyltrehalose Trehalohydrolase |
| PDB | 3vgh_A | 2e-19 | 99 | 446 | 75 | 423 | A Chain A, Crystal Structure Of Sulfolobus Solfataricus Glycosyltrehalose Trehalohydrolase |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| FD834000 | 240 | 352 | 591 | 0 |
| FD931574 | 222 | 370 | 591 | 0 |
| HO415417 | 363 | 153 | 515 | 0 |
| GW593495 | 236 | 352 | 587 | 0 |
| BU649873 | 165 | 128 | 292 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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