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Basic Information | |
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Species | Chlamydomonas reinhardtii |
Cazyme ID | Cre06.g270100.t1.3 |
Family | GH13 |
Protein Properties | Length: 870 Molecular Weight: 98644.2 Isoelectric Point: 6.588 |
Chromosome | Chromosome/Scaffold: 6 Start: 2660766 End: 2669981 |
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 | 351 | 675 | 1e-27 |
LPRIRALGYNAIQIMAIQEHAYYGSFGYHVTNFFAPSSRCGTPEELKALIDEAHRLGIIVLMDIVHSHASKNTNDGINMFDGTDAMYFHGGPRGFHWMWD SRCFDYGNWETLRFLLSNTRYWMDEFKFDGYRFDGVTSMMYHHHGLSYSFTGNYDEYFGMNTDVDAVVYLMLVNQLLHDMFPNAITIGEDVSGMPAFCRP WHEGGVGFDYRLQMAIADKWIEVLKSHDDHSWDMTAITHTLTNRRYAESCVSYAESHDQALVGDKTIAFWLMDKDMYDKMSVPGKGPASAIVDRGIALHK MIRLVTLALGGESYLNFMGNEFGHP |
Full Sequence |
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Protein Sequence Length: 870 Download |
MLFRGPTKAN PSRVSSHSVE SQRCAQAIPR GVPTPGRVVA CRAASAYAGS AYSADPAGAL 60 AALEEENKLL KTTISDAKAA IMELETQLKA SGIPLPAPEN SPDLMPTQPE DFWSPAMEVP 120 YNYEYKDRYG AISPIPGHDG TECFSWDATL WGFAEHFRYR WRRLRSIRQA IEDNEGGLDN 180 FTKSYNRFGL NRGMHEGRQG IWYREWAPGA KALSLIGDFN NWTPKDAHWA FKNTYGVWEL 240 FLPDGPDGTP AIPHRSKVKC RLETPDGQWV ERIPAWIKWA TQAWNEIQFN GVHWDPPETG 300 SPGEIASDKK YTFKYPRPPR PRSLRIYECH VGMSSQEPKV NSYLEFRRDV LPRIRALGYN 360 AIQIMAIQEH AYYGSFGYHV TNFFAPSSRC GTPEELKALI DEAHRLGIIV LMDIVHSHAS 420 KNTNDGINMF DGTDAMYFHG GPRGFHWMWD SRCFDYGNWE TLRFLLSNTR YWMDEFKFDG 480 YRFDGVTSMM YHHHGLSYSF TGNYDEYFGM NTDVDAVVYL MLVNQLLHDM FPNAITIGED 540 VSGMPAFCRP WHEGGVGFDY RLQMAIADKW IEVLKSHDDH SWDMTAITHT LTNRRYAESC 600 VSYAESHDQA LVGDKTIAFW LMDKDMYDKM SVPGKGPASA IVDRGIALHK MIRLVTLALG 660 GESYLNFMGN EFGHPEWIDF PRDNTYDPST GRFIQGNGGS MDKCRRRWDL ADSESLKYKW 720 LLAFDRAMCH LDKAFGFQGA PHQWISRADS ADKMIVCERG DLLFVFNFHP TRSYTDYRVG 780 CNASGPYKIV LSSDEEVFGG YRNCSKDAGV TFVAQPMAHD NRPFSFLVYA PSRTCVVYAP 840 AGWVDSEADR KPHGIAGLAV RDLGPYFAR* 900 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02960 | PLN02960 | 6.0e-8 | 153 | 244 | 97 | + alpha-amylase | ||
PLN03244 | PLN03244 | 6.0e-138 | 250 | 838 | 594 | + alpha-amylase; Provisional | ||
PLN02960 | PLN02960 | 4.0e-178 | 250 | 838 | 592 | + alpha-amylase | ||
PLN02447 | PLN02447 | 0 | 82 | 868 | 789 | + 1,4-alpha-glucan-branching enzyme | ||
cd11321 | AmyAc_bac_euk_BE | 0 | 307 | 726 | 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 | 81 | 868 | 82 | 879 | starch branching enzyme II [Parachlorella kessleri] |
GenBank | EAY86110.1 | 0 | 136 | 841 | 140 | 824 | hypothetical protein OsI_07480 [Oryza sativa Indica Group] |
RefSeq | NP_195985.3 | 0 | 132 | 841 | 115 | 802 | SBE2.2 (starch branching enzyme 2.2); 1,4-alpha-glucan branching enzyme [Arabidopsis thaliana] |
RefSeq | XP_001690322.1 | 0 | 124 | 869 | 2 | 747 | starch branching enzyme [Chlamydomonas reinhardtii] |
RefSeq | XP_001696229.1 | 0 | 82 | 869 | 1 | 788 | starch branching enzyme [Chlamydomonas reinhardtii] |
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 | 132 | 838 | 2 | 690 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3aml_A | 0 | 132 | 838 | 2 | 690 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3vu2_B | 0 | 132 | 838 | 2 | 690 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 3vu2_A | 0 | 132 | 838 | 2 | 690 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 3k1d_A | 0 | 199 | 841 | 136 | 722 | 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 | 702 | 140 | 841 | 0 |
HO777638 | 642 | 200 | 841 | 0 |
HO458123 | 406 | 441 | 846 | 0 |
HO458123 | 302 | 139 | 439 | 0 |
HO777638 | 56 | 147 | 202 | 7.8 |
Sequence Alignments (This image is cropped. Click for full image.) |
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