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Basic Information | |
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Species | Fragaria vesca |
Cazyme ID | mrna29749.1-v1.0-hybrid |
Family | GT35 |
Protein Properties | Length: 1010 Molecular Weight: 113403 Isoelectric Point: 5.9646 |
Chromosome | Chromosome/Scaffold: 3 Start: 4545769 End: 4552981 |
Description | alpha-glucan phosphorylase 2 |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GT35 | 288 | 999 | 0 |
ALSQLGFEFEVLAEQEGDAALGNGGLARLSACQMDSMATLDYPAWGYGLRYQYGLFRQVILDGFQHEQPDFWLNFGNPWETERVHVTYPVKFYGTVDEEI VNGEKCNVWNPGEVVEAVAYDNPIPGYGTRNTITLRLWAGKPSDQRDMEAFNTGDYINAVVSRQKAENISSVLYPDDRSYQGKELRLKQQYFFVSASIQD IIRRFKDAHSNFDEFPDKVALQLNDTHPSLAIVEVMRVLVDEEHLDWKRAWDIVCKLFSFTIHAVIAEGLEKIPVDLLGSLLPRHLQIIYDINFNFVEEL KKRIGLDYDRLSRMSIVEEAAVKSIRMANLAVVCAHTVNGVSQVHSELLRTKLFKDFYELWPEKFQCKTNGVTQRRWIVVSNPSLCALLSKWLGTESWIR NVDLLAGLREYADDADLQQEWMMVKKVNKMRLAEYIEAMSGVKVSLDAMFDVQTKRIHEYKRQLLNILGIIHRYDCIKNMDKSQQSKVVPRVCIIGGKAA PGYEVAKKIIKLCHAVADKINNDSDVGDLLKLIFIPDYNVSLAEVVIPGADLSQHLSTAGHEASGTGSMKFLMNGCLLLATEDGSTVEIVEEIGDENLFL FGTKIHEVPELRERGPAHDMPLQCARVLRLIRDGHFGFQDYFQSLCDSVEGDDFYLLSSDFGSYLEAQAAADKAFVDPKKWAKMSILSTAGSGRFSSDTT IRDYAEKSWGIE |
Full Sequence |
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Protein Sequence Length: 1010 Download |
MSILPSRFLT IPHHPSLAFS HYSPPPLLQT VPRSSLFHAP SNVPRPLRAS ATSPSSSSSS 60 VTVENSSDSE SDAASGGAPA TLFVIRARNR IGLLGIITRV FNVLGLRVEK ATVEFEGDFF 120 VKRFFVTDSR GARIEDRDSL DRIQKALLDA IDDCAGTVSA GPTTTRGVVV RRPGLGLGSG 180 DRAAKAERMF GLMDGFLKND PISLQKDILY HVEYTVARSR FSFDDFEAYQ ALAHSVRDRL 240 IERSHDTQLY FKRKDPKRVY FLSLEFLMGR SLSNSVINLG IRDQYAEALS QLGFEFEVLA 300 EQEGDAALGN GGLARLSACQ MDSMATLDYP AWGYGLRYQY GLFRQVILDG FQHEQPDFWL 360 NFGNPWETER VHVTYPVKFY GTVDEEIVNG EKCNVWNPGE VVEAVAYDNP IPGYGTRNTI 420 TLRLWAGKPS DQRDMEAFNT GDYINAVVSR QKAENISSVL YPDDRSYQGK ELRLKQQYFF 480 VSASIQDIIR RFKDAHSNFD EFPDKVALQL NDTHPSLAIV EVMRVLVDEE HLDWKRAWDI 540 VCKLFSFTIH AVIAEGLEKI PVDLLGSLLP RHLQIIYDIN FNFVEELKKR IGLDYDRLSR 600 MSIVEEAAVK SIRMANLAVV CAHTVNGVSQ VHSELLRTKL FKDFYELWPE KFQCKTNGVT 660 QRRWIVVSNP SLCALLSKWL GTESWIRNVD LLAGLREYAD DADLQQEWMM VKKVNKMRLA 720 EYIEAMSGVK VSLDAMFDVQ TKRIHEYKRQ LLNILGIIHR YDCIKNMDKS QQSKVVPRVC 780 IIGGKAAPGY EVAKKIIKLC HAVADKINND SDVGDLLKLI FIPDYNVSLA EVVIPGADLS 840 QHLSTAGHEA SGTGSMKFLM NGCLLLATED GSTVEIVEEI GDENLFLFGT KIHEVPELRE 900 RGPAHDMPLQ CARVLRLIRD GHFGFQDYFQ SLCDSVEGDD FYLLSSDFGS YLEAQAAADK 960 AFVDPKKWAK MSILSTAGSG RFSSDTTIRD YAEKSWGIEP CRFPSESDG* 1020 |
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 | 205 | 998 | 801 | + 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 | 208 | 998 | 800 | + 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 | 288 | 1000 | 719 | + 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 | 203 | 1002 | 810 | + glycogen phosphorylase; Provisional | ||
COG0058 | GlgP | 0 | 203 | 1000 | 812 | + 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 - 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 | 199 | 1001 | 39 | 878 | A Chain A, Phosphorylated Form Of Yeast Glycogen Phosphorylase With Phosphate Bound In The Active Site. |
PDB | 1ygp_A | 0 | 199 | 1001 | 39 | 878 | A Chain A, Phosphorylated Form Of Yeast Glycogen Phosphorylase With Phosphate Bound In The Active Site. |
PDB | 1c50_A | 0 | 204 | 1002 | 15 | 819 | A Chain A, Identification And Structural Characterization Of A Novel Allosteric Binding Site Of Glycogen Phosphorylase B |
PDB | 1abb_D | 0 | 204 | 1002 | 18 | 822 | 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 | 204 | 1002 | 18 | 822 | A Chain A, Control Of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies On R-State Glycogen Phosphorylase Reconstituted With Pyridoxal 5'-Diphosphate |
Sequence Alignments (This image is cropped. Click for full image.) |
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