Basic Information | |
---|---|
Species | Physcomitrella patens |
Cazyme ID | Pp1s200_23V6.1 |
Family | GH13 |
Protein Properties | Length: 984 Molecular Weight: 111927 Isoelectric Point: 4.9001 |
Chromosome | Chromosome/Scaffold: 200 Start: 198652 End: 206877 |
Description | Alpha amylase family protein |
View CDS |
External Links |
---|
NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
---|---|---|---|
Family | Start | End | Evalue |
GH13 | 505 | 822 | 4.4e-24 |
TDTVLPRVAKAGYNVIQLFGIQEHADYSSVGYKVTNFFAISSRFGTPEDFKRLVDTAHGLGLMVVMDIVHSHAAPNEGNGLASFDGANDCYFYPGRRGHH KRWGTRMFKYGEYEVLRFLLSNSKWWFMEYKVDGFYFHSVTSMLYTHNGFTPFTSGLDDYCNQYVDKDALIYLSLANEMLHQLSPNMITIAEDATFYPGL VDSINKGGLGFDYYVNSAPSEMWPFLIENVPIQEWSVTEITGTLITTENTTKALVYSENHNQSIVGGQSLAEALLGTSKESSKNISKLEGISLHKIIRLI TLSLAGSAYLNFMGNEFG |
Full Sequence |
---|
Protein Sequence Length: 984 Download |
MALSTGIQCV PAFKSNLVSV EAVTWASQAS LSGVKFRGYE RSGLGLRQSL GYLRDRHVVG 60 GRVIRSIGRR ASRTCKRIGC VRMAGAEEDV AQPTKKGNTQ SKNNVAEEGD TNRGGVNPVG 120 FLKEKGLKTK AFQTFTRERY KALKDLKQLI AERDEDLVEF ANAYEDMGMH RNPGHHVEFY 180 EWAPGARFCS VVGDFNNREH RKHFAREGYF GRDDFGYYHV RIDDVLREGE EEDNATQEYN 240 YDADYDKGDE DIDEDALFER IDQEYWDPGE DEFMSGHKDD LAQELFTTIF GKDLDPMEMV 300 KDISAKYKSK KKKKMYYDDD DSGDDDDDDE YEREPQTLEE FKAAVESHME EWLASNAEAQ 360 KGKDLPSILV EDDGINRDEM ELVDDPVWAK RVEEKEWPEN YWENFVKGRK AWEKKYIPGI 420 SHGDRYRAYL HTPEGPLERV PAWASYVLPD PDGNEVSAIF WDLPKDQQYN WKFDRPSKPQ 480 TLRIYECHVG ISGESPKIAS FNDFTDTVLP RVAKAGYNVI QLFGIQEHAD YSSVGYKVTN 540 FFAISSRFGT PEDFKRLVDT AHGLGLMVVM DIVHSHAAPN EGNGLASFDG ANDCYFYPGR 600 RGHHKRWGTR MFKYGEYEVL RFLLSNSKWW FMEYKVDGFY FHSVTSMLYT HNGFTPFTSG 660 LDDYCNQYVD KDALIYLSLA NEMLHQLSPN MITIAEDATF YPGLVDSINK GGLGFDYYVN 720 SAPSEMWPFL IENVPIQEWS VTEITGTLIT TENTTKALVY SENHNQSIVG GQSLAEALLG 780 TSKESSKNIS KLEGISLHKI IRLITLSLAG SAYLNFMGNE FGHPKWVEFP RAKNNNSFAH 840 AYRRWDLLEE QGPHSQLAAF DQALMEVDET HNILGQGLPN MCHVNDTTKV IVYTRGNLLF 900 AFNFHVTDTY EMYKVGVQVA GEYELVLNSD QPNFGGLGQL QEADKLLNTT RRQSDGLPNT 960 LLLVLPQLSA QVYKLARVFE TSS* |
Functional Domains Download unfiltered results here | ||||||||
---|---|---|---|---|---|---|---|---|
Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02447 | PLN02447 | 2.0e-10 | 132 | 225 | 94 | + 1,4-alpha-glucan-branching enzyme | ||
cd11321 | AmyAc_bac_euk_BE | 2.0e-178 | 466 | 862 | 405 | + 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 | 90 | 981 | 898 | + alpha-amylase | ||
PLN03244 | PLN03244 | 0 | 81 | 979 | 907 | + alpha-amylase; Provisional | ||
PLN02447 | PLN02447 | 0 | 418 | 976 | 574 | + 1,4-alpha-glucan-branching enzyme |
Gene Ontology | |
---|---|
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 | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
DDBJ | BAB02827.1 | 0 | 114 | 979 | 67 | 901 | starch-branching enzyme-like protein [Arabidopsis thaliana] |
EMBL | CBI26672.1 | 0 | 82 | 979 | 43 | 894 | unnamed protein product [Vitis vinifera] |
RefSeq | NP_001154629.1 | 0 | 114 | 979 | 67 | 897 | alpha-amylase/ catalytic/ cation binding [Arabidopsis thaliana] |
RefSeq | XP_001776079.1 | 0 | 83 | 983 | 1 | 865 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_002529457.1 | 0 | 92 | 972 | 48 | 892 | 1,4-alpha-glucan branching enzyme, putative [Ricinus communis] |
Annotations - PDB Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 3amk_A | 0 | 418 | 960 | 114 | 669 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3amk_A | 0.002 | 128 | 225 | 19 | 110 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3aml_A | 0 | 418 | 960 | 114 | 669 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3aml_A | 0.002 | 128 | 225 | 19 | 110 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3vu2_B | 0 | 418 | 960 | 114 | 669 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
Metabolic Pathways | |||
---|---|---|---|
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 | ||||
---|---|---|---|---|
Hit | Length | Start | End | EValue |
FC335449 | 277 | 708 | 984 | 0 |
HO777638 | 586 | 418 | 982 | 0 |
HO794536 | 586 | 418 | 982 | 0 |
FE486732 | 282 | 406 | 687 | 0 |
HO794536 | 59 | 139 | 197 | 1.9 |
Sequence Alignments (This image is cropped. Click for full image.) |
---|