| Basic Information | |
|---|---|
| Species | Selaginella moellendorffii |
| Cazyme ID | 109836 |
| Family | GH77 |
| Protein Properties | Length: 541 Molecular Weight: 60908.9 Isoelectric Point: 4.8437 |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
 | |||
| Family | Start | End | Evalue |
| GH77 | 34 | 510 | 0 |
| LHPTSLPGPHGIGDLGPDAFRFLDWLESTGCRIWQVLPLVPPGRKAGEDGSPYAGQDANCGNTLLISLTELVKDGLLEEEDIPEAIPVEKINYEAVAELK DPLIQKAAKNLVQNGGSLKKDLETFRKSPQIASWLEEAALFAAIDSHLDDGAWWLWPEPLRDRNPSALDKARKEHKDFIDVFIAQQFLFQKQWQALHTYA NERGIKIIGDMPIYVGGHSADVWVHRTQFMMDEKTCEPVLVSGVPPDCFSETGQLWGSPLYNWKAMAKDGYKWWASRMRRAFELYDEFRIDHFRGLAGYW AVPADAETAIDGRWKMGPRVEFFNAIKKAVGKKIDIIAEDLGIITTDVVELRKAIEAPGMVVLHFAFGNNPTNPHILHNHEVDQVVYPGTHDNDTSVGWW SKASEEDKEKARSYLRLEDEDAVSWELMRAAFSSVARTAIIPMQDVLSLDSDARMNTPAVKSGNWAWRIGESSIFDE | |||
| Full Sequence |
|---|
| Protein Sequence Length: 541 Download |
| MASSALSPGD DLPDEYEKDD PSKKAMPRRA GIILHPTSLP GPHGIGDLGP DAFRFLDWLE 60 STGCRIWQVL PLVPPGRKAG EDGSPYAGQD ANCGNTLLIS LTELVKDGLL EEEDIPEAIP 120 VEKINYEAVA ELKDPLIQKA AKNLVQNGGS LKKDLETFRK SPQIASWLEE AALFAAIDSH 180 LDDGAWWLWP EPLRDRNPSA LDKARKEHKD FIDVFIAQQF LFQKQWQALH TYANERGIKI 240 IGDMPIYVGG HSADVWVHRT QFMMDEKTCE PVLVSGVPPD CFSETGQLWG SPLYNWKAMA 300 KDGYKWWASR MRRAFELYDE FRIDHFRGLA GYWAVPADAE TAIDGRWKMG PRVEFFNAIK 360 KAVGKKIDII AEDLGIITTD VVELRKAIEA PGMVVLHFAF GNNPTNPHIL HNHEVDQVVY 420 PGTHDNDTSV GWWSKASEED KEKARSYLRL EDEDAVSWEL MRAAFSSVAR TAIIPMQDVL 480 SLDSDARMNT PAVKSGNWAW RIGESSIFDE LTEEGERIRG LLHEYNRLPR SEEEHRLIEK 540 * |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
 | ||||||||
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| TIGR00217 | malQ | 7.0e-109 | 28 | 527 | 509 | + 4-alpha-glucanotransferase. This enzyme is known as amylomaltase and disproportionating enzyme [Energy metabolism, Biosynthesis and degradation of polysaccharides]. | ||
| COG1640 | MalQ | 1.0e-131 | 23 | 533 | 526 | + 4-alpha-glucanotransferase [Carbohydrate transport and metabolism] | ||
| pfam02446 | Glyco_hydro_77 | 7.0e-177 | 34 | 522 | 505 | + 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. | ||
| PLN02635 | PLN02635 | 0 | 1 | 534 | 534 | + disproportionating enzyme | ||
| PRK14508 | PRK14508 | 0 | 26 | 528 | 506 | + 4-alpha-glucanotransferase; Provisional | ||
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1x1n_A | 0 | 9 | 528 | 6 | 524 | A Chain A, Structure Determination And Refinement At 1.8 A Resolution Of Disproportionating Enzyme From Potato |
| PDB | 2owx_A | 0 | 22 | 528 | 2 | 503 | A Chain A, Structure Determination And Refinement At 1.8 A Resolution Of Disproportionating Enzyme From Potato |
| PDB | 2oww_A | 0 | 22 | 528 | 2 | 503 | A Chain A, Structure Determination And Refinement At 1.8 A Resolution Of Disproportionating Enzyme From Potato |
| PDB | 2owc_A | 0 | 22 | 528 | 2 | 503 | A Chain A, Structure Of A Covalent Intermediate In Thermus Thermophilus Amylomaltase |
| PDB | 1fp9_A | 0 | 26 | 528 | 3 | 500 | A Chain A, Structure Of A Covalent Intermediate In Thermus Thermophilus Amylomaltase |
| Metabolic Pathways | |||
|---|---|---|---|
| Pathway Name | Reaction | EC | Protein Name |
| starch degradation I | RXN-1828 | EC-2.4.1.25 | 4-α-glucanotransferase |
| starch degradation II | RXN-12391 | EC-2.4.1.25 | 4-α-glucanotransferase |
| Hydropathy |
|---|
 |
| Sequence Alignments (This image is cropped. Click for full image.) |
|---|
 |
