Basic Information | |
---|---|
Species | Chlamydomonas reinhardtii |
Cazyme ID | Cre06.g289850.t1.3 |
Family | GH13 |
Protein Properties | Length: 770 Molecular Weight: 86227.6 Isoelectric Point: 6.2759 |
Chromosome | Chromosome/Scaffold: 6 Start: 6089722 End: 6100307 |
Description | starch branching enzyme 2.2 |
View CDS |
External Links |
---|
NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
---|---|---|---|
Family | Start | End | Evalue |
GH13 | 239 | 563 | 9.2e-30 |
LPRVQALGYNAIQLMAIQEHAYYGSFGYHVTNPFAVSSRSGTPEELKALIDEAHRRGIAVLLDVVHSHISGNQDDGLAGFDMGQREQDNYFKQGEAGYHK LWDSRCLNYANWECQRYLLSNLRYWLEEYQFDGFRFDGVTSMLYHHHGIHTSFSGDYNEYLGTSTNVDAVVYLMMANRLVHDLVPSAVTIAEDVSGMPAL CRPVAEGGVGFDARLNMSIPDTWIKLLKHVRDEHWRMQDIVSALCNRRYTEKSIGYAESHDQALVGDQTIAFRLMGPEMYSGMSALTEATPVVSRGVALH KLIRLVTMALGGEGWLSFMGNEFGH |
Full Sequence |
---|
Protein Sequence Length: 770 Download |
MAARPLQGPR ALLPVPTAST AAPLRATAQA PASTSSSAAD EGDGLGVIAV DPALANFKGH 60 LEYRWAQYRR TLDSITAGAG SLAAFAEGYK YFGFNREDGA IVYREWAPAA QAAALIGDFS 120 KWEPVWMTRD EWGVWSVRLE DVDGKPAIPH RSRVKVRLQH PHGWWMDRVP AWIKWAAAEQ 180 RMDAKYDGIY WDPPAAERHQ WRHQRPPRPA ALRIYEAHVG MSSETGKVAS YSEFTDTVLP 240 RVQALGYNAI QLMAIQEHAY YGSFGYHVTN PFAVSSRSGT PEELKALIDE AHRRGIAVLL 300 DVVHSHISGN QDDGLAGFDM GQREQDNYFK QGEAGYHKLW DSRCLNYANW ECQRYLLSNL 360 RYWLEEYQFD GFRFDGVTSM LYHHHGIHTS FSGDYNEYLG TSTNVDAVVY LMMANRLVHD 420 LVPSAVTIAE DVSGMPALCR PVAEGGVGFD ARLNMSIPDT WIKLLKHVRD EHWRMQDIVS 480 ALCNRRYTEK SIGYAESHDQ ALVGDQTIAF RLMGPEMYSG MSALTEATPV VSRGVALHKL 540 IRLVTMALGG EGWLSFMGNE FGHPEWIDFP RDGNGWSHHY CRRQWSLADT DHLRYKFLQA 600 WDAAMMALDN HYGFLASPHQ WVTHMDEPEQ ILVFERGPLL FVFNWSPIAD REAYRVAVPA 660 PGKWRVALDS DAWDYGGAGR VFHDADHFSD PEPAGTSRDR EHSIRVLAPA RTCAVYYNAD 720 THTHWRERPQ AQQQEGGAEA EAPHHTYGLA PAATQTAGGL SVGSGDEVV* |
Functional Domains Download unfiltered results here | ||||||||
---|---|---|---|---|---|---|---|---|
Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02960 | PLN02960 | 3.0e-7 | 51 | 142 | 105 | + alpha-amylase | ||
PLN03244 | PLN03244 | 1.0e-121 | 146 | 716 | 572 | + alpha-amylase; Provisional | ||
PLN02960 | PLN02960 | 1.0e-166 | 146 | 717 | 577 | + alpha-amylase | ||
PLN02447 | PLN02447 | 0 | 40 | 725 | 689 | + 1,4-alpha-glucan-branching enzyme | ||
cd11321 | AmyAc_bac_euk_BE | 0 | 210 | 602 | 393 | + Alpha amylase catalytic domain found in bacterial and eukaryotic branching enzymes. Branching enzymes (BEs) catalyze the formation of alpha-1,6 branch points in either glycogen or starch by cleavage of the alpha-1,4 glucosidic linkage yielding a non-reducing end oligosaccharide chain, and subsequent attachment to the alpha-1,6 position. By increasing the number of non-reducing ends, glycogen is more reactive to synthesis and digestion as well as being more soluble. This group includes bacterial and eukaryotic proteins. 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. |
Annotations - NR Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
GenBank | ABN05321.1 | 0 | 34 | 720 | 81 | 775 | starch branching enzyme I [Populus trichocarpa] |
EMBL | CAA54308.1 | 0 | 8 | 720 | 51 | 776 | 1,4-alpha-glucan branching enzyme [Manihot esculenta] |
EMBL | CBI18866.1 | 0 | 33 | 720 | 84 | 779 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_001695391.1 | 0 | 33 | 720 | 1 | 690 | starch branching enzyme [Chlamydomonas reinhardtii] |
RefSeq | XP_002284841.1 | 0 | 20 | 720 | 48 | 756 | PREDICTED: hypothetical protein [Vitis vinifera] |
Annotations - PDB Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 3amk_A | 0 | 37 | 720 | 3 | 694 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3aml_A | 0 | 37 | 720 | 3 | 694 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3vu2_B | 0 | 37 | 720 | 3 | 694 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 3vu2_A | 0 | 37 | 720 | 3 | 694 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 1m7x_D | 7.00649e-44 | 106 | 709 | 32 | 605 | A Chain A, The X-Ray Crystallographic Structure Of Branching Enzyme |
Metabolic Pathways | |||
---|---|---|---|
Pathway Name | Reaction | EC | Protein Name |
starch biosynthesis | RXN-7710 | EC-2.4.1.18 | 1,4-α-glucan branching enzyme |
EST Download unfiltered results here | ||||
---|---|---|---|---|
Hit | Length | Start | End | EValue |
HO619167 | 599 | 129 | 720 | 0 |
HO794536 | 693 | 42 | 720 | 0 |
HO777638 | 635 | 100 | 720 | 0 |
HO458123 | 401 | 332 | 716 | 0 |
HO777638 | 47 | 50 | 96 | 0.007 |
Sequence Alignments (This image is cropped. Click for full image.) |
---|