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Basic Information | |
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Species | Volvox carteri |
Cazyme ID | Vocar20002436m |
Family | GH13 |
Protein Properties | Length: 766 Molecular Weight: 87892.9 Isoelectric Point: 6.3085 |
Chromosome | Chromosome/Scaffold: 2 Start: 2466177 End: 2476763 |
Description | starch branching enzyme 2.2 |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH13 | 247 | 571 | 2.6e-28 |
LPRVRALGYNAIQIMAIQEHAYYGSFGYHVTNFFAPSSRCGTPEELKALIDEAHRLGLVVLMDIVHSHASKNTNDGINMFDGTDAMYFHGGPRGYHWMWD SRCFDYGNWETLRFLLSNCRYWMDEFKFDGFRFDGVTSMMYHHHGLSYTFTGNYEEYFGLNTDVDAVVYLMLVNNMLHDMFPNCITVGEDVSGMPAFCRP WHEGGVGFDYRLQMAIADKWIDILKGHDDFAWDMGTITHTLTNRRYAEACVAYAESHDQALVGDKTIAFWLMDKEMYHFMSVPGLGPASTIIDRGIALHK MIRLVTLALGGESYLNFMGNEFGHP |
Full Sequence |
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Protein Sequence Length: 766 Download |
MPTQPEDFWS PELEVPYDYV YTDQYGSISP IPGHDGTECF TWDSALWNFA DHFRYRWRRL 60 REIRKAIDDN EGGLDNFTKS YMRFGLNRGE HQGRKGIWYR EWAPGAKALA LVGDFNSWSP 120 RDNHWAFKNS YGVWELFLPD SPDGSPALPH RSKLKCRLET ADGCWVERIP AWIRWATQAW 180 NEIQFNGVYW DPPESGAPGE IDSDKKYVFR YPRPPRPRAL RIYECHVGMS SQEAKVNSYL 240 EFRRDVLPRV RALGYNAIQI MAIQEHAYYG SFGYHVTNFF APSSRCGTPE ELKALIDEAH 300 RLGLVVLMDI VHSHASKNTN DGINMFDGTD AMYFHGGPRG YHWMWDSRCF DYGNWETLRF 360 LLSNCRYWMD EFKFDGFRFD GVTSMMYHHH GLSYTFTGNY EEYFGLNTDV DAVVYLMLVN 420 NMLHDMFPNC ITVGEDVSGM PAFCRPWHEG GVGFDYRLQM AIADKWIDIL KGHDDFAWDM 480 GTITHTLTNR RYAEACVAYA ESHDQALVGD KTIAFWLMDK EMYHFMSVPG LGPASTIIDR 540 GIALHKMIRL VTLALGGESY LNFMGNEFGH PEWIDFPRDN SYDPSTGRLI PGNGGSFDKC 600 RRRWDLADSP NLKYRWLNAF DRAMMHLDKA FGFQCAPHQW VSRADSSDKM IVCERGDLVF 660 VFNFHPATSY TDYRVGCNAN GPYKVVLSSD EEVFGGYRNA TKDAAVTFVA TPTPHDNRPS 720 SFMVYAPSRT VVVYAPAAWV DPDADRKPHG IPGLAVRSLG PYYAR* 780 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02960 | PLN02960 | 4.0e-8 | 49 | 140 | 97 | + alpha-amylase | ||
PLN03244 | PLN03244 | 3.0e-127 | 146 | 734 | 591 | + alpha-amylase; Provisional | ||
PLN02960 | PLN02960 | 8.0e-166 | 146 | 734 | 598 | + alpha-amylase | ||
PLN02447 | PLN02447 | 0 | 1 | 764 | 766 | + 1,4-alpha-glucan-branching enzyme | ||
cd11321 | AmyAc_bac_euk_BE | 0 | 203 | 622 | 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. |
Gene Ontology | |
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GO Term | Description |
GO:0003824 | catalytic activity |
GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
GO:0005975 | carbohydrate metabolic process |
GO:0043169 | cation binding |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
GenBank | AAB03100.1 | 0 | 28 | 737 | 110 | 797 | starch branching enzyme class II [Arabidopsis thaliana] |
DDBJ | BAF98234.1 | 0 | 5 | 764 | 120 | 879 | starch branching enzyme II [Parachlorella kessleri] |
RefSeq | NP_195985.3 | 0 | 28 | 737 | 115 | 802 | SBE2.2 (starch branching enzyme 2.2); 1,4-alpha-glucan branching enzyme [Arabidopsis thaliana] |
RefSeq | XP_001690322.1 | 0 | 21 | 765 | 3 | 747 | starch branching enzyme [Chlamydomonas reinhardtii] |
RefSeq | XP_001696229.1 | 0 | 1 | 765 | 24 | 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 | 28 | 734 | 2 | 690 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3vu2_B | 0 | 28 | 734 | 2 | 690 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 3vu2_A | 0 | 28 | 734 | 2 | 690 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 3aml_A | 0 | 28 | 734 | 2 | 690 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3k1d_A | 0 | 95 | 737 | 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 |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO794536 | 707 | 36 | 742 | 0 |
HO777638 | 647 | 96 | 742 | 0 |
HO458123 | 401 | 337 | 737 | 0 |
HO458123 | 302 | 35 | 335 | 0 |
HO619167 | 642 | 128 | 757 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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