y
Basic Information | |
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Species | Cucumis sativus |
Cazyme ID | Cucsa.126920.10 |
Family | GT35 |
Protein Properties | Length: 740 Molecular Weight: 84109.2 Isoelectric Point: 6.158 |
Chromosome | Chromosome/Scaffold: 01017 Start: 724870 End: 736485 |
Description | alpha-glucan phosphorylase 2 |
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 |
GT35 | 21 | 733 | 0 |
ALSQLGFEFEVVAEQEGDAALGNGGLARLSACQMDSLATMDFPAWGYGLRYQYGLFRQVILDGFQHEQPDYWLNFGNPWEIERVHVTYPVKFYGTVEEEI LNGEKYKIWIPGETIEAVAYDNPIPGYGTRNTITLRLWAAKPSNQHDMEAYNTGDYIDAVVNRQRAETISSILYPDDRSHQGKELRLKQQYFFVSASLQD IIRRFKDVHKDFNKFPDKVALQLNDIHPALAIPEVMRVFVDEEHLGWNKAFDLTCKIFSFTTHTVQAEALEKIPVDLLESLLPRHLQIIYDINSYFMEEL KKRIGLDYNRLARMSIVEEGAVKSIRVANLSLFCSHTVNGVSKLHSELLQTRVFKDFYELWPEKFQYKTNGVTQRRWIVVSNPNLCALISKWLGTESWIR DIDLLIGLREYATDISLHQEWQMVRRVNKMRLAEYIEATSGLKVSLDAMFDVQIKRIHQYKRQLLNILGIIHRYDCIKNMAKDDRRKVVPRVCIIGGKAA PGYEMAKKMIKLCHAVAEKINNDSDVGDLLKLVFIPDYNVSVAELVIPGADLSQHISTAGHEASGTGSMKFLMNGCLLLATADGSTVEIIEEIGEDNMFL FGAKVHEVPTLREKGSTIKVPLQFARVVRMVRDGYFGFQDYFKSLCDTVEGNSDYYLLGADFGSYLEAQAAADKAFVDQEKWTRMSILSTAGSGRFSSDR TIQDYAEKTWGIE |
Full Sequence |
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Protein Sequence Length: 740 Download |
MGRSLSNSII NLGIRDQCAD ALSQLGFEFE VVAEQEGDAA LGNGGLARLS ACQMDSLATM 60 DFPAWGYGLR YQYGLFRQVI LDGFQHEQPD YWLNFGNPWE IERVHVTYPV KFYGTVEEEI 120 LNGEKYKIWI PGETIEAVAY DNPIPGYGTR NTITLRLWAA KPSNQHDMEA YNTGDYIDAV 180 VNRQRAETIS SILYPDDRSH QGKELRLKQQ YFFVSASLQD IIRRFKDVHK DFNKFPDKVA 240 LQLNDIHPAL AIPEVMRVFV DEEHLGWNKA FDLTCKIFSF TTHTVQAEAL EKIPVDLLES 300 LLPRHLQIIY DINSYFMEEL KKRIGLDYNR LARMSIVEEG AVKSIRVANL SLFCSHTVNG 360 VSKLHSELLQ TRVFKDFYEL WPEKFQYKTN GVTQRRWIVV SNPNLCALIS KWLGTESWIR 420 DIDLLIGLRE YATDISLHQE WQMVRRVNKM RLAEYIEATS GLKVSLDAMF DVQIKRIHQY 480 KRQLLNILGI IHRYDCIKNM AKDDRRKVVP RVCIIGGKAA PGYEMAKKMI KLCHAVAEKI 540 NNDSDVGDLL KLVFIPDYNV SVAELVIPGA DLSQHISTAG HEASGTGSMK FLMNGCLLLA 600 TADGSTVEII EEIGEDNMFL FGAKVHEVPT LREKGSTIKV PLQFARVVRM VRDGYFGFQD 660 YFKSLCDTVE GNSDYYLLGA DFGSYLEAQA AADKAFVDQE KWTRMSILST AGSGRFSSDR 720 TIQDYAEKTW GIEPCRCPL* 780 |
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 | 1 | 732 | 738 | + 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 | 1 | 732 | 738 | + 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 | 21 | 734 | 720 | + 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 | 1 | 736 | 745 | + glycogen phosphorylase; Provisional | ||
COG0058 | GlgP | 0 | 1 | 734 | 747 | + 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 | 1 | 738 | 76 | 813 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_001757919.1 | 0 | 1 | 735 | 76 | 810 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_002273615.1 | 0 | 1 | 738 | 80 | 817 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002305114.1 | 0 | 1 | 739 | 80 | 818 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002509431.1 | 0 | 1 | 739 | 244 | 949 | 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 | 1 | 735 | 108 | 878 | A Chain A, Phosphorylated Form Of Yeast Glycogen Phosphorylase With Phosphate Bound In The Active Site. |
PDB | 1ygp_A | 0 | 1 | 735 | 108 | 878 | A Chain A, Phosphorylated Form Of Yeast Glycogen Phosphorylase With Phosphate Bound In The Active Site. |
PDB | 2gj4_A | 0 | 1 | 736 | 80 | 820 | A Chain A, Structure Of Rabbit Muscle Glycogen Phosphorylase In Complex With Ligand |
PDB | 3nc4_A | 0 | 1 | 736 | 90 | 830 | A Chain A, The Binding Of Beta-D-Glucopyranosyl-Thiosemicarbazone Derivatives To Glycogen Phosphorylase: A New Class Of Inhibit |
PDB | 4el5_A | 0 | 1 | 736 | 80 | 820 | A Chain A, The Binding Of Beta-D-Glucopyranosyl-Thiosemicarbazone Derivatives To Glycogen Phosphorylase: A New Class Of Inhibit |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO779924 | 445 | 2 | 446 | 0 |
HO586252 | 541 | 197 | 735 | 0 |
HO376977 | 448 | 294 | 740 | 0 |
HO417459 | 285 | 348 | 632 | 0 |
HO417459 | 212 | 149 | 354 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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