y
Basic Information | |
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Species | Glycine max |
Cazyme ID | Glyma13g30920.3 |
Family | GT35 |
Protein Properties | Length: 861 Molecular Weight: 98001.1 Isoelectric Point: 6.992 |
Chromosome | Chromosome/Scaffold: 13 Start: 33407618 End: 33418684 |
Description | alpha-glucan phosphorylase 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 |
GT35 | 284 | 839 | 0 |
ALSQLGFEFEVVAEQEGDAALGNGGLARLSACQMDSLATLDYPAWGYGLRYEYGLFRQIIVDGFQHEQPDYWLNYGNPWEIERIHVTYEVKFYGTVEEVE MNGEKHQVWVPGETVEAVAYDNPIPGYGTRNTINLRLWAAKPSNKFDLEAYNTGDYINSVVNRQRAETISNVLYPDDRNHQGKELRLKQQYFFVSASLQD IIRRFKEAHNNFDELPDKVALHLNDTHPSLSIAEIMRILVDEEHLVWNKAWDIACKVFSFTTHTVVAEGLEKIPVDLLGSLLPRHLQILYEINFKFMEEL KKKIGLDYNRLSRMSIVEEGAVKSIRMANLSIVGSHAVNGVSKLHLDTLKMNTFKDFYELWPEKFQYKTNGVTQRRWIVVSNPSLCALISKWLGTEAWIR NADLLTGLRDLVDNTDFHQEWKMVKKVNKMRLAEYIETMSGVKVSLDAMFDVQVKRIHEYKRQLLNILGIIHRYDCIKNMDKNDRRKVVPRVCIIGGKAA PGYEIAKKIIKLSHAVAEKINNDTDIGDLLKLVFIPDYNVSVAELVIPGADLSQHL |
Full Sequence |
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Protein Sequence Length: 861 Download |
MQTIISFPHL TPFPNQLSPV PFPSLTHFSS LSIPRSLTVA HWRILLRAST SESISTSTST 60 IAVDNSDSAD STAFVIRARN QIGLLQVITR VFKVLGLTVD RATVEFEGDF FVKTFFVTDS 120 HGNKIEDSDS LQRIKRALAE AIAGEDDGGN GTISVTRSAA NRGIVVRRPG LAEAIGERRA 180 KAERMFSLMD GFLKNDPLTL QKDILNHVEY TVARSRFSFD DFEAYQALSH SVRDRLIERW 240 HDTHVYVKRT KPKRLYFLSL EFLMGRSLSN SVINLGIQDQ YAEALSQLGF EFEVVAEQEG 300 DAALGNGGLA RLSACQMDSL ATLDYPAWGY GLRYEYGLFR QIIVDGFQHE QPDYWLNYGN 360 PWEIERIHVT YEVKFYGTVE EVEMNGEKHQ VWVPGETVEA VAYDNPIPGY GTRNTINLRL 420 WAAKPSNKFD LEAYNTGDYI NSVVNRQRAE TISNVLYPDD RNHQGKELRL KQQYFFVSAS 480 LQDIIRRFKE AHNNFDELPD KVALHLNDTH PSLSIAEIMR ILVDEEHLVW NKAWDIACKV 540 FSFTTHTVVA EGLEKIPVDL LGSLLPRHLQ ILYEINFKFM EELKKKIGLD YNRLSRMSIV 600 EEGAVKSIRM ANLSIVGSHA VNGVSKLHLD TLKMNTFKDF YELWPEKFQY KTNGVTQRRW 660 IVVSNPSLCA LISKWLGTEA WIRNADLLTG LRDLVDNTDF HQEWKMVKKV NKMRLAEYIE 720 TMSGVKVSLD AMFDVQVKRI HEYKRQLLNI LGIIHRYDCI KNMDKNDRRK VVPRVCIIGG 780 KAAPGYEIAK KIIKLSHAVA EKINNDTDIG DLLKLVFIPD YNVSVAELVI PGADLSQHLR 840 FANLTFVIVP FLRLIDVTNE * 900 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd04300 | GT1_Glycogen_Phosphorylase | 0 | 201 | 838 | 638 | + This is a family of oligosaccharide phosphorylases. It includes yeast and mammalian glycogen phosphorylases, plant starch/glucan phosphorylase, as well as the maltodextrin phosphorylases of bacteria. The members of this family catalyze the breakdown of oligosaccharides into glucose-1-phosphate units. They are important allosteric enzymes in carbohydrate metabolism. The allosteric control mechanisms of yeast and mammalian members of this family are different from that of bacterial members. The members of this family belong to the GT-B structural superfamily of glycoslytransferases, which have characteristic N- and C-terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. | ||
TIGR02093 | P_ylase | 0 | 204 | 842 | 639 | + glycogen/starch/alpha-glucan phosphorylases. This family consists of phosphorylases. Members use phosphate to break alpha 1,4 linkages between pairs of glucose residues at the end of long glucose polymers, releasing alpha-D-glucose 1-phosphate. The nomenclature convention is to preface the name according to the natural substrate, as in glycogen phosphorylase, starch phosphorylase, maltodextrin phosphorylase, etc. Name differences among these substrates reflect differences in patterns of branching with alpha 1,6 linkages. Members include allosterically regulated and unregulated forms. A related family, TIGR02094, contains examples known to act well on particularly small alpha 1,4 glucans, as may be found after import from exogenous sources [Energy metabolism, Biosynthesis and degradation of polysaccharides]. | ||
pfam00343 | Phosphorylase | 0 | 284 | 842 | 559 | + Carbohydrate phosphorylase. The members of this family catalyze the formation of glucose 1-phosphate from one of the following polyglucoses; glycogen, starch, glucan or maltodextrin. | ||
PRK14986 | PRK14986 | 0 | 231 | 842 | 612 | + glycogen phosphorylase; Provisional | ||
COG0058 | GlgP | 0 | 192 | 844 | 655 | + Glucan phosphorylase [Carbohydrate transport and metabolism] |
Gene Ontology | |
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GO Term | Description |
GO:0004645 | phosphorylase activity |
GO:0005975 | carbohydrate metabolic process |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
EMBL | CBI30609.1 | 0 | 189 | 843 | 1 | 655 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_001757919.1 | 0 | 189 | 839 | 1 | 651 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_002273615.1 | 0 | 185 | 843 | 1 | 659 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002305114.1 | 0 | 185 | 843 | 1 | 659 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002509431.1 | 0 | 13 | 839 | 6 | 786 | glycogen phosphorylase, putative [Ricinus communis] |
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 | 1ygp_B | 0 | 200 | 848 | 44 | 731 | A Chain A, Phosphorylated Form Of Yeast Glycogen Phosphorylase With Phosphate Bound In The Active Site. |
PDB | 1ygp_A | 0 | 200 | 848 | 44 | 731 | A Chain A, Phosphorylated Form Of Yeast Glycogen Phosphorylase With Phosphate Bound In The Active Site. |
PDB | 1c50_A | 0 | 200 | 842 | 15 | 657 | A Chain A, Identification And Structural Characterization Of A Novel Allosteric Binding Site Of Glycogen Phosphorylase B |
PDB | 1abb_D | 0 | 200 | 842 | 18 | 660 | A Chain A, Control Of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies On R-State Glycogen Phosphorylase Reconstituted With Pyridoxal 5'-Diphosphate |
PDB | 1abb_C | 0 | 200 | 842 | 18 | 660 | A Chain A, Control Of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies On R-State Glycogen Phosphorylase Reconstituted With Pyridoxal 5'-Diphosphate |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
starch degradation I | RXN-1826 | EC-2.4.1.1 | phosphorylase |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO779924 | 621 | 92 | 709 | 0 |
HO586252 | 383 | 460 | 842 | 0 |
CO095011 | 285 | 416 | 700 | 0 |
ES340735 | 339 | 283 | 620 | 0 |
HO779924 | 30 | 62 | 91 | 0.00002 |
Sequence Alignments (This image is cropped. Click for full image.) |
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