Basic Information | |
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Species | Brachypodium distachyon |
Cazyme ID | Bradi5g09170.2 |
Family | GH13 |
Protein Properties | Length: 849 Molecular Weight: 95021.4 Isoelectric Point: 4.9896 |
Chromosome | Chromosome/Scaffold: 5 Start: 12406074 End: 12415848 |
Description | starch branching enzyme 2.2 |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH13 | 363 | 683 | 3e-31 |
LPRIKRLGYNAVQIMAIQEHSYYASFGYHVTNFFAPSSRFGTPEDLKSLIDRAHELGLLVLMDIVHSHSSNNTLDGLNGFDGTDTHYFHGGPRGHHWMWD SRLFNYGSWEVLRFLLSNARWWLEEYKFDGFRFDGVTSMMYTHHGLQVSFTGNYGEYFGFATDVDAVVYLMLVNDMIHGLYPDAVAIGEDVSGMPTFCLP VQDGGVGFDYRLHMAVADKWIELLKQSDESWKMGDIVHTLTNRRWSEKCVTYAESHDQALVGDKTIAFWLMDKDMYDFMALDRPSTPRIDRGIALHKMIR LVTMGLGGEGYLNFMGNEFGH |
Full Sequence |
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Protein Sequence Length: 849 Download |
MASFAVSGAT LGVVLAGSGG GGLSSTARSA RAGVDLPSLL LRKKDSSSPQ VVALLLTVGA 60 IFAFAGAVLS CAGAPGKVLV PGGGSDDLLS SAEPVSTTPA QPEESQIPED ISEQTAEAST 120 SVDAEDKLES SEPTQGIVET ITDSVTEGVK ELVVEEKPRV IQPPGDGQKI YQIDPMLEGF 180 RSHLDYRYSE YKRIRAAIDQ YEGGLDGFSR GYEKLGFIRS AEGITYREWA PGAHSAALVG 240 DFNNWNPNAD TMTRNEYGVW EIFLPNNADG SPAIPHGSRV KIRMDTPSGV KDSISAWIKF 300 SVQAPGEIPY NGIYYDPPEE EKYVFQHPQP KQPKSLRIYE SHIGMSSPEP KINTYANFRD 360 EVLPRIKRLG YNAVQIMAIQ EHSYYASFGY HVTNFFAPSS RFGTPEDLKS LIDRAHELGL 420 LVLMDIVHSH SSNNTLDGLN GFDGTDTHYF HGGPRGHHWM WDSRLFNYGS WEVLRFLLSN 480 ARWWLEEYKF DGFRFDGVTS MMYTHHGLQV SFTGNYGEYF GFATDVDAVV YLMLVNDMIH 540 GLYPDAVAIG EDVSGMPTFC LPVQDGGVGF DYRLHMAVAD KWIELLKQSD ESWKMGDIVH 600 TLTNRRWSEK CVTYAESHDQ ALVGDKTIAF WLMDKDMYDF MALDRPSTPR IDRGIALHKM 660 IRLVTMGLGG EGYLNFMGNE FGHPEWIDFP RGPQTLPNGS VLPGNNNSYD KCRRRFDLGD 720 ADFLRYHGMQ EFDQAMQHLE EKYGFMTSEH QYVSRKHEED KVIIFERGDL VFVFNFHWSN 780 SFFDYRVGCS KPGKYKVALD SDDVLFGGFS RLDHDVEYFT TEDPHDNRPR SFSVYTPSRT 840 VVVYALTE* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02960 | PLN02960 | 9.0e-9 | 180 | 264 | 91 | + alpha-amylase | ||
PLN03244 | PLN03244 | 1.0e-136 | 272 | 847 | 582 | + alpha-amylase; Provisional | ||
PLN02447 | PLN02447 | 0 | 100 | 848 | 753 | + 1,4-alpha-glucan-branching enzyme | ||
cd11321 | AmyAc_bac_euk_BE | 0 | 319 | 734 | 417 | + 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. | ||
PLN02960 | PLN02960 | 0 | 272 | 847 | 580 | + alpha-amylase |
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 | AAG27623.1 | 0 | 1 | 848 | 1 | 823 | AF286319_1 starch branching enzyme 2 [Triticum aestivum] |
GenBank | AAK26821.1 | 0 | 1 | 848 | 1 | 819 | starch branching enzyme IIa [Aegilops tauschii] |
EMBL | CAA72154.1 | 0 | 1 | 848 | 1 | 823 | 1,4-alpha-glucan branching enzyme II [Triticum aestivum] |
EMBL | CAR95900.1 | 0 | 1 | 848 | 1 | 823 | starch branching enzyme IIa [Triticum aestivum] |
EMBL | CAX51366.1 | 0 | 1 | 848 | 1 | 821 | starch branching enzyme [Hordeum vulgare subsp. vulgare] |
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 | 166 | 844 | 9 | 690 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3aml_A | 0 | 166 | 844 | 9 | 690 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3vu2_B | 0 | 166 | 844 | 9 | 690 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 3vu2_A | 0 | 166 | 844 | 9 | 690 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 1m7x_D | 4.2039e-45 | 210 | 808 | 9 | 577 | A Chain A, The X-Ray Crystallographic Structure Of Branching Enzyme |
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 |