| Basic Information | |
|---|---|
| Species | Carica papaya |
| Cazyme ID | evm.model.supercontig_112.64 |
| Family | GT35 |
| Protein Properties | Length: 745 Molecular Weight: 84414.9 Isoelectric Point: 6.2614 |
| Chromosome | Chromosome/Scaffold: 112 Start: 554452 End: 560917 |
| 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 | 117 | 357 | 0 |
| ALQKFGYELEEIVEQEKDAALGNGGLGRLASCFLDSMASLNLPAWGYGLRYKYGLFKQQITMEGQQEIAEDWLEVHIHYKAMSHIVFDIRKWIGGEVLLA LAYDVPIPGYKTKNTISLRLWEAKARAEDFDLFLFNDGQYESAAQLHSRAQQICAVLYPGDATEDGKLLRLKQQFFLCSASLQDLIFRFKERKTGESPRH WSEFPKKVAVQLNDTHPTLAIPELMRLLMDDEGLGWDEAWD | |||
| GT35 | 358 | 739 | 0 |
| VNGVARLHSDILKSELFADYVSLWPTKFQNKTNGITPRRWLRFCSPELSDIITKWLKTDQWITKLDLLVGLRKFADNADFQAEWASAKMANKHRLAQYIL RVTGVSIDPTSLFDIQIKRIHEYKRQLLNILGAIYRYKKLKEMSPEERKKTTPRTIMIGGKAFATYTNAKRIVKLVNDVGVVVNNDPEVNNYLKVVFVPN YNVSVAEVLIPGSELSQHISTAGMEASGTSNMKFSLNGCLIIGTLDGANVEIREEIGEENFFLFGATADEVPKLRKERENGLFQPDPRFEEAKQFIRSGI FGNYDYTQLLDSLEGNSGYGRGDYFLVGHDFPSYMDAQARVDEAYKDQKRWLKMSILSTAGSGKFSSDRTISQYAKEIWNIE | |||
| Full Sequence |
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| Protein Sequence Length: 745 Download |
| MAATGKANGA TVSSVPAKVQ VAANPLADEP AQIASNINYH AQYSPHFSPF KFEPEQAYYA 60 AAESVCDRLI QQWNETYCHF HKVDPKQTYY LSMEYLQGRA LNNAIGNLDI QGAYAEALQK 120 FGYELEEIVE QEKDAALGNG GLGRLASCFL DSMASLNLPA WGYGLRYKYG LFKQQITMEG 180 QQEIAEDWLE VHIHYKAMSH IVFDIRKWIG GEVLLALAYD VPIPGYKTKN TISLRLWEAK 240 ARAEDFDLFL FNDGQYESAA QLHSRAQQIC AVLYPGDATE DGKLLRLKQQ FFLCSASLQD 300 LIFRFKERKT GESPRHWSEF PKKVAVQLND THPTLAIPEL MRLLMDDEGL GWDEAWDVNG 360 VARLHSDILK SELFADYVSL WPTKFQNKTN GITPRRWLRF CSPELSDIIT KWLKTDQWIT 420 KLDLLVGLRK FADNADFQAE WASAKMANKH RLAQYILRVT GVSIDPTSLF DIQIKRIHEY 480 KRQLLNILGA IYRYKKLKEM SPEERKKTTP RTIMIGGKAF ATYTNAKRIV KLVNDVGVVV 540 NNDPEVNNYL KVVFVPNYNV SVAEVLIPGS ELSQHISTAG MEASGTSNMK FSLNGCLIIG 600 TLDGANVEIR EEIGEENFFL FGATADEVPK LRKERENGLF QPDPRFEEAK QFIRSGIFGN 660 YDYTQLLDSL EGNSGYGRGD YFLVGHDFPS YMDAQARVDE AYKDQKRWLK MSILSTAGSG 720 KFSSDRTISQ YAKEIWNIEE CRVP* |
| Functional Domains Download unfiltered results here | ||||||||
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam00343 | Phosphorylase | 5.0e-103 | 117 | 358 | 256 | + 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. | ||
| cd04300 | GT1_Glycogen_Phosphorylase | 3.0e-138 | 34 | 358 | 346 | + 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. | ||
| cd04300 | GT1_Glycogen_Phosphorylase | 0 | 358 | 738 | 386 | + 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. | ||
| pfam00343 | Phosphorylase | 0 | 358 | 740 | 388 | + 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. | ||
| TIGR02093 | P_ylase | 0 | 358 | 738 | 386 | + 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]. | ||
| 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 |
| Swiss-Prot | P32811 | 0 | 298 | 744 | 402 | 838 | PHSH_SOLTU RecName: Full=Alpha-glucan phosphorylase, H isozyme; AltName: Full=Starch phosphorylase H |
| RefSeq | XP_002280732.1 | 0 | 1 | 358 | 1 | 371 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002280732.1 | 0 | 355 | 744 | 454 | 843 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002313399.1 | 0 | 2 | 358 | 13 | 381 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002313399.1 | 0 | 358 | 744 | 467 | 853 | predicted protein [Populus trichocarpa] |
| 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 | 2gj4_A | 0 | 358 | 742 | 441 | 820 | A Chain A, Structure Of Rabbit Muscle Glycogen Phosphorylase In Complex With Ligand |
| PDB | 2gj4_A | 0 | 20 | 358 | 1 | 356 | A Chain A, Structure Of Rabbit Muscle Glycogen Phosphorylase In Complex With Ligand |
| PDB | 1z8d_A | 0 | 358 | 742 | 453 | 832 | A Chain A, Crystal Structure Of Human Muscle Glycogen Phosphorylase A With Amp And Glucose |
| PDB | 1z8d_A | 0 | 20 | 358 | 13 | 368 | A Chain A, Crystal Structure Of Human Muscle Glycogen Phosphorylase A With Amp And Glucose |
| PDB | 3nc4_A | 0 | 358 | 742 | 451 | 830 | A Chain A, The Binding Of Beta-D-Glucopyranosyl-Thiosemicarbazone Derivatives To Glycogen Phosphorylase: A New Class Of Inhibit |
| Metabolic Pathways | |||
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| Pathway Name | Reaction | EC | Protein Name |
| starch degradation I | RXN-1826 | EC-2.4.1.1 | phosphorylase |
| Hydropathy |
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| EST Download unfiltered results here | ||||
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| Hit | Length | Start | End | EValue |
| GT044838 | 338 | 378 | 715 | 0 |
| GT043461 | 329 | 364 | 692 | 0 |
| HO780010 | 310 | 436 | 745 | 0 |
| HO613954 | 389 | 358 | 745 | 0 |
| HO780010 | 37 | 391 | 427 | 0.00000000004 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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