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Basic Information | |
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Species | Selaginella moellendorffii |
Cazyme ID | 437348 |
Family | GH13 |
Protein Properties | Length: 1133 Molecular Weight: 127718 Isoelectric Point: 6.2958 |
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 | 345 | 667 | 9.9e-28 |
LPRIKGLGYNAVQLMAVMEHAYYGSFGYHITNFFAVSSRCGTPDELKSLIDKAHELGLFVLMDVVHSHCSNNVLDGLNMFDGTDSQYFHSGARGYHWMWD SRLFDYSSWEVLRFLLSNLRWWMEEYKFDGFRFDGITSMMYTHHGLQMTFTGQYSEYFGMTTDVDAVVYLMLANDLLHALYPQTITVAEDVSGMPTLCIP VADGGIGFDYRLQMAIADKWIDILEKLKDEEWNMGNIVFTLTNRRWMEKCISYAESHDQALVGDKTLAFWLMDKDMYDHMALDRPSTPRIDRGIALHKMI RLITMALGGEGYLNFMGNEFGHP |
Full Sequence |
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Protein Sequence Length: 1133 Download |
MAWSVTQAPA GRASCICPRG IGGSGGIGAA ASSSQALRSS ARRRKRVALC CGSPLLGRAL 60 SLSCHVHGKH YSRPSTRVSC ADPVSPAEST AASTATASKD LLEPSKADHS MEEQTMEIAK 120 QIQAFRDGSL KLKEQDAALP KVVPPPGDGQ RIYEIDPYLK NYRDHLEYRY SQYKAKVDAI 180 NKHEGGLEAF SRGYEKFGFN RTAAGITYRE WAPAAKSASL MGDFNNWNPN ADMMKKNEYG 240 VWELFLPNNA DGSAAIPHGS RVKIHMETAS GVKDAIPAWI KFAVQAPGEI PYNGIYYDPP 300 PEERYEFKHP RPKRPNSLRV YEAHVGMSST EPKVNSYSAF RDDVLPRIKG LGYNAVQLMA 360 VMEHAYYGSF GYHITNFFAV SSRCGTPDEL KSLIDKAHEL GLFVLMDVVH SHCSNNVLDG 420 LNMFDGTDSQ YFHSGARGYH WMWDSRLFDY SSWEVLRFLL SNLRWWMEEY KFDGFRFDGI 480 TSMMYTHHGL QMTFTGQYSE YFGMTTDVDA VVYLMLANDL LHALYPQTIT VAEDVSGMPT 540 LCIPVADGGI GFDYRLQMAI ADKWIDILEK LKDEEWNMGN IVFTLTNRRW MEKCISYAES 600 HDQALVGDKT LAFWLMDKDM YDHMALDRPS TPRIDRGIAL HKMIRLITMA LGGEGYLNFM 660 GNEFGHPEWI DFPRSDQKLP NGKFVPGNKN SFDKCRRRFD LGDADYLRYR GLQEFDRAMQ 720 QLEAKYEFMV APHEYVSRKN EGDKIIVFEK GDLVFVFNFH WQKSYTDYRV GCLKPGNYKV 780 VLDTDERLFG GFGRLDHSAV FHTNEGWYDD RPQSFQVYSP CRTAVVYAPG LSQRVAMADS 840 SWDDAALITA FNSAVGKYQE RHSSKESDGK SSHQEKIESA SQQDQAAAEG SSQHADSSFV 900 DPSSYYPYPY PQPHPSYPYP AFVYPVPAYA CAPPPSHCCH HSCCHSSSTQ SSRSDDPSFE 960 TLKLAILQSL SQLPPDKQLS LEDNAEVLIA WFNAGFRTAR SPSRVVPISL FLIYWAERWL 1020 DQGFLPRTSE SKKEAFRKYL EASGVLDSLT KVLVALYEEN DKPPLAIDFI QHNLGGYTNE 1080 EYTKLKGERD ELQLKYNELV AAHEELGRKF EELQLQLPPP EEAPPVEGAP PA* 1140 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02960 | PLN02960 | 2.0e-6 | 160 | 246 | 93 | + alpha-amylase | ||
PLN03244 | PLN03244 | 2.0e-137 | 255 | 827 | 577 | + alpha-amylase; Provisional | ||
PLN02447 | PLN02447 | 0 | 104 | 829 | 729 | + 1,4-alpha-glucan-branching enzyme | ||
cd11321 | AmyAc_bac_euk_BE | 0 | 301 | 717 | 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 | 255 | 827 | 576 | + alpha-amylase |
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 | 152 | 827 | 13 | 690 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3aml_A | 0 | 152 | 827 | 13 | 690 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3vu2_B | 0 | 152 | 827 | 13 | 690 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 3vu2_A | 0 | 152 | 827 | 13 | 690 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 3k1d_A | 5.60519e-45 | 168 | 829 | 95 | 721 | 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 |
Sequence Alignments (This image is cropped. Click for full image.) |
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