y
Basic Information | |
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Species | Chlamydomonas reinhardtii |
Cazyme ID | Cre10.g444700.t1.1 |
Family | GH13 |
Protein Properties | Length: 869 Molecular Weight: 98283.5 Isoelectric Point: 6.196 |
Chromosome | Chromosome/Scaffold: 10 Start: 3445284 End: 3453070 |
Description | starch branching enzyme 2.2 |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH13 | 350 | 673 | 1.4e-27 |
LPRIRALGYNAIQIMAIQEHAYYGSFGYHVTNFFGVSSRCGTPEELKALVDEAHRMGIIVLMDIVHSHASKNTNDGINMFDGTDGMYFHGGPRGNHWMWD SRCFNYGNWETMRFLLSNARWWMDEYKFDGYRFDGVTSMMYHHHGLSYTFTGNYGEYFGMNTDVDAVVYLMLVNNLLHDLFPNCVTIGEDVSGMPAFCRP WQEGGVGFDYRLQMAIADKWIEVMKLHDDYAWNMGNLVHTLTNRRYAEACVGYAESHDQALVGDKTIAFWLMDKDMYDFMAVPGHGAQSLVVDRGVALHK MIRLLTIALGGESYLNFMGNEFGH |
Full Sequence |
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Protein Sequence Length: 869 Download |
MQLGKFHHVQ AGGVAQRPRR GALPRSVVTA AAPGEKLSAL ELLRRENELL RQTLDVANVP 60 VDSVVEPRAS STATAPRPTA PKSAGSSLTN ASGAELALLG EAGAVAGPED FWSPTVEVPE 120 NMEYVDEYGP ISPIPNHDGT MCFKWDNTLW SAAEHFKYRW NVFKNIRAAI DQNEGGFEKF 180 SQGYKYYGFN RGECNGQTGI WYREWAPGAK ALALVGDFNN WAPAEGHWAF KNQYGTWELF 240 LPDKPDGTSA IPHRTKVKAR IEGADGSWQD KIPAWIKWST QEWNEVLFNG VYWDPPEKGA 300 PGEVDPDKQY TFKYPRPPKP RALRIYECHV GMSSEEPKVN SYLEFRRDVL PRIRALGYNA 360 IQIMAIQEHA YYGSFGYHVT NFFGVSSRCG TPEELKALVD EAHRMGIIVL MDIVHSHASK 420 NTNDGINMFD GTDGMYFHGG PRGNHWMWDS RCFNYGNWET MRFLLSNARW WMDEYKFDGY 480 RFDGVTSMMY HHHGLSYTFT GNYGEYFGMN TDVDAVVYLM LVNNLLHDLF PNCVTIGEDV 540 SGMPAFCRPW QEGGVGFDYR LQMAIADKWI EVMKLHDDYA WNMGNLVHTL TNRRYAEACV 600 GYAESHDQAL VGDKTIAFWL MDKDMYDFMA VPGHGAQSLV VDRGVALHKM IRLLTIALGG 660 ESYLNFMGNE FGHPEWIDFP RVDSYDPSTG KFVPGNGGSL HLCRRRWDLA DADFLKYKFL 720 NAFDRAMCHL DKAFGYMSAP NTYISRKDEG DKMIVFERGD LVFVFNFHPG QSYQDYRVGC 780 REAGPYKLVL SSDEEVFGGY RNNTKENDVT FQTQSGNFDN RPHSFQVYAP ARTCAVYAPA 840 EWADKDADRK PHGIPGLGIK DLGPYFSR* 900 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02960 | PLN02960 | 1.0e-8 | 153 | 244 | 97 | + alpha-amylase | ||
PLN03244 | PLN03244 | 2.0e-133 | 250 | 837 | 592 | + alpha-amylase; Provisional | ||
PLN02960 | PLN02960 | 6.0e-176 | 250 | 837 | 589 | + alpha-amylase | ||
PLN02447 | PLN02447 | 0 | 110 | 867 | 760 | + 1,4-alpha-glucan-branching enzyme | ||
cd11321 | AmyAc_bac_euk_BE | 0 | 306 | 725 | 420 | + 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 | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
DDBJ | BAF98234.1 | 0 | 108 | 866 | 120 | 878 | starch branching enzyme II [Parachlorella kessleri] |
GenBank | EAY86110.1 | 0 | 81 | 841 | 84 | 825 | hypothetical protein OsI_07480 [Oryza sativa Indica Group] |
RefSeq | XP_001690322.1 | 0 | 122 | 868 | 1 | 747 | starch branching enzyme [Chlamydomonas reinhardtii] |
RefSeq | XP_001696229.1 | 0 | 108 | 868 | 28 | 788 | starch branching enzyme [Chlamydomonas reinhardtii] |
RefSeq | XP_002453926.1 | 0 | 135 | 841 | 118 | 803 | hypothetical protein SORBIDRAFT_04g021540 [Sorghum bicolor] |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 3amk_A | 0 | 131 | 837 | 2 | 690 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3vu2_B | 0 | 131 | 837 | 2 | 690 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 3vu2_A | 0 | 131 | 837 | 2 | 690 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 3aml_A | 0 | 131 | 837 | 2 | 690 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3k1d_A | 0 | 198 | 799 | 136 | 684 | A Chain A, Crystal Structure Of Glycogen Branching Enzyme Synonym: 1,4- Glucan:1,4-Alpha-D-Glucan 6-Glucosyl-Transferase From Mycob Tuberculosis H3 |
Metabolic Pathways | |||
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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 | ||||
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Hit | Length | Start | End | EValue |
HO794536 | 703 | 139 | 841 | 0 |
HO777638 | 644 | 198 | 841 | 0 |
HO458123 | 401 | 440 | 840 | 0 |
HO458123 | 301 | 138 | 438 | 0 |
HO777638 | 56 | 146 | 201 | 0.46 |
Sequence Alignments (This image is cropped. Click for full image.) |
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