| Basic Information | |
|---|---|
| Species | Oryza sativa |
| Cazyme ID | LOC_Os02g38260.1 |
| Family | GH5 |
| Protein Properties | Length: 583 Molecular Weight: 61517.6 Isoelectric Point: 5.8849 |
| Chromosome | Chromosome/Scaffold: 2 Start: 23142015 End: 23144272 |
| Description | Cellulase (glycosyl hydrolase family 5) protein |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH5 | 39 | 352 | 6.8e-40 |
| AGGRRVKLACVNWPSHLEPVVTEGLGMQPVDAISKKVASLGFNCVRLTYPIALATNASLSSLTVRRSLLAHGLAGAVAGVEANNPGLLDLTLIESFRAVV DSLGESGVMVILDNHVSRPGWCCADDDGNGFFGDRHFDPDAWVRGLGAMAALFAGVPNVVGMSLRNELRGPRQNADDWYRYMQMGAEAVHAANPAALVIM GGLGYDTDLSFLAARPVDVSFAAAERGKLVFELHWYSFADARAWESEDANEVCGRVARGVARRGGFLLDAGFPLFLSEFGADTRGGSRKDDRYLPCAAAV AAELDLDWALWALQ | |||
| Full Sequence |
|---|
| Protein Sequence Length: 583 Download |
| MRRRVALCLV LFAFAGLHAA AVEAVTLSTS SRWIVDDEAG GRRVKLACVN WPSHLEPVVT 60 EGLGMQPVDA ISKKVASLGF NCVRLTYPIA LATNASLSSL TVRRSLLAHG LAGAVAGVEA 120 NNPGLLDLTL IESFRAVVDS LGESGVMVIL DNHVSRPGWC CADDDGNGFF GDRHFDPDAW 180 VRGLGAMAAL FAGVPNVVGM SLRNELRGPR QNADDWYRYM QMGAEAVHAA NPAALVIMGG 240 LGYDTDLSFL AARPVDVSFA AAERGKLVFE LHWYSFADAR AWESEDANEV CGRVARGVAR 300 RGGFLLDAGF PLFLSEFGAD TRGGSRKDDR YLPCAAAVAA ELDLDWALWA LQGSYALRQG 360 VAGADEVYGV LDWSWSKPRN ATALSRIQSL QRPLRGPGYD EARPYTVLFH PLTGRCVVRR 420 AADDAAAAAA TLELGRCEDT DAWAYTQPAS TLAMRGAGRG SPPLCLRAEG SGRPARLATS 480 DAGGCRGDAL STWRLVSGST MHVAVNATTT TTPSRDGGGG LLCLDVGDDG RSVVTNPCRC 540 LDDAAAGECD PETQWFKLVT STRSPATGAA AAATVARGLI AA* 600 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd11353 | AmyAc_euk_bac_CMD_like | 0.004 | 132 | 180 | 70 | + Alpha amylase catalytic domain found in eukaryotic and bacterial 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). This group of CMDs is mainly bacterial. 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. | ||
| pfam00150 | Cellulase | 1.0e-13 | 67 | 330 | 271 | + Cellulase (glycosyl hydrolase family 5). | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0003824 | catalytic activity |
| GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
| GO:0005488 | binding |
| GO:0005623 | cell |
| GO:0005975 | carbohydrate metabolic process |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | EAY86525.1 | 0 | 1 | 582 | 1 | 582 | hypothetical protein OsI_07905 [Oryza sativa Indica Group] |
| GenBank | EAZ23667.1 | 0 | 1 | 420 | 1 | 420 | hypothetical protein OsJ_07369 [Oryza sativa Japonica Group] |
| GenBank | EAZ23667.1 | 1e-31 | 506 | 582 | 507 | 583 | hypothetical protein OsJ_07369 [Oryza sativa Japonica Group] |
| RefSeq | NP_001047320.1 | 0 | 1 | 357 | 1 | 357 | Os02g0596200 [Oryza sativa (japonica cultivar-group)] |
| RefSeq | XP_002452393.1 | 0 | 18 | 563 | 23 | 560 | hypothetical protein SORBIDRAFT_04g024910 [Sorghum bicolor] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1ece_B | 0.00000001 | 29 | 350 | 8 | 320 | A Chain A, Acidothermus Cellulolyticus Endocellulase E1 Catalytic Domain In Complex With A Cellotetraose |
| PDB | 1ece_A | 0.00000001 | 29 | 350 | 8 | 320 | A Chain A, Acidothermus Cellulolyticus Endocellulase E1 Catalytic Domain In Complex With A Cellotetraose |
| PDB | 1vrx_B | 0.00000001 | 29 | 350 | 8 | 320 | A Chain A, Endocellulase E1 From Acidothermus Cellulolyticus Mutant Y245g |
| PDB | 1vrx_A | 0.00000001 | 29 | 350 | 8 | 320 | A Chain A, Endocellulase E1 From Acidothermus Cellulolyticus Mutant Y245g |
| PDB | 4dm1_C | 0.005 | 44 | 205 | 28 | 168 | A Chain A, Contribution Of Disulfide Bond Toward Thermostability In Hyperthermostable Endocellulase |
