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Basic Information | |
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Species | Gossypium raimondii |
Cazyme ID | Gorai.013G092200.2 |
Family | GT35 |
Protein Properties | Length: 769 Molecular Weight: 87754.8 Isoelectric Point: 4.8797 |
Chromosome | Chromosome/Scaffold: 13 Start: 14807197 End: 14813532 |
Description | Glycosyl transferase, family 35 |
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 | 162 | 760 | 0 |
ALKKLGHNLEDVAREEPDAALGNGGLGRLASCFLDSLATLNYPAWGYGLRYKYGLFKQYITKDGQEEVAENWLEMGNPWEIVRNDVSYPVKFYGEVISGP EGIKEWVGGEDITAVAYDVPIPGYKTKTTINLRLWSTKVAPEKFDLSAFNAGDHAKAYSAMNNAEKICYILYPGDESLEGKTLRLKQQYTLCSASLQDII ARYERRSGEFLNWEIFPEKVAVQMNDTHPTLCIPELIRILIDVKGLSWEQAWNITQRTVAYTNHTVLPEALEKWSLELMEKLLPRHVEIIKMIDEELVQT IIDEYGTEDLDLLQEKLKQMRILDNIELPESVVEMIAKPEKSLVEAIESTEEDDVSDEETEPTAEEDELEEEEIEEENEVPPIIEPDPKLPKLVRMANLC VAGGYAVNGVAEIHSEIVKNEVFNDFYEMWPEKFQNKTNGVTPRRWIRFCNPDLSKIITKWTGSEDWVVNTEKLLTLRKFSDNEDLQSEWREAKRRNKVK VASFLREKTGYIVNPDAMFDVQVKRIHEYKRQLLNIMGIVYRYKKMKGMSHEERKASFAPRVCIFGGKAFATYVQAKRIVKFITDVGATVNHDPEIGDL |
Full Sequence |
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Protein Sequence Length: 769 Download |
MASLPFSATS FHSTFICFNY KARNPNLFFL KKGSSFTFSR RKFIIKSVAS DQRQDLKEEG 60 QITEEASLDT FVPDSASVAS SIKYHSEFTP SFAPDHFELP KAFKATAESV RDSLIINWNA 120 TYAYYEKINV KQAYYLSMEY LQGRALLNAI GNLELTGAYA EALKKLGHNL EDVAREEPDA 180 ALGNGGLGRL ASCFLDSLAT LNYPAWGYGL RYKYGLFKQY ITKDGQEEVA ENWLEMGNPW 240 EIVRNDVSYP VKFYGEVISG PEGIKEWVGG EDITAVAYDV PIPGYKTKTT INLRLWSTKV 300 APEKFDLSAF NAGDHAKAYS AMNNAEKICY ILYPGDESLE GKTLRLKQQY TLCSASLQDI 360 IARYERRSGE FLNWEIFPEK VAVQMNDTHP TLCIPELIRI LIDVKGLSWE QAWNITQRTV 420 AYTNHTVLPE ALEKWSLELM EKLLPRHVEI IKMIDEELVQ TIIDEYGTED LDLLQEKLKQ 480 MRILDNIELP ESVVEMIAKP EKSLVEAIES TEEDDVSDEE TEPTAEEDEL EEEEIEEENE 540 VPPIIEPDPK LPKLVRMANL CVAGGYAVNG VAEIHSEIVK NEVFNDFYEM WPEKFQNKTN 600 GVTPRRWIRF CNPDLSKIIT KWTGSEDWVV NTEKLLTLRK FSDNEDLQSE WREAKRRNKV 660 KVASFLREKT GYIVNPDAMF DVQVKRIHEY KRQLLNIMGI VYRYKKMKGM SHEERKASFA 720 PRVCIFGGKA FATYVQAKRI VKFITDVGAT VNHDPEIGDL LKYGRNGG* 780 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR02093 | P_ylase | 1.0e-93 | 553 | 762 | 210 | + 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]. | ||
cd04300 | GT1_Glycogen_Phosphorylase | 4.0e-107 | 552 | 762 | 211 | + 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 | 3.0e-136 | 162 | 496 | 335 | + 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 | 6.0e-171 | 82 | 486 | 408 | + 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]. | ||
cd04300 | GT1_Glycogen_Phosphorylase | 0 | 79 | 496 | 422 | + 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. |
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 | CBI27267.1 | 0 | 1 | 762 | 1 | 740 | unnamed protein product [Vitis vinifera] |
Swiss-Prot | P53535 | 0 | 32 | 762 | 25 | 781 | PHSL2_SOLTU RecName: Full=Alpha-1,4 glucan phosphorylase L-2 isozyme, chloroplastic/amyloplastic; AltName: Full=Starch phosphorylase L-2; Flags: Precursor |
RefSeq | XP_002274575.1 | 0 | 1 | 762 | 1 | 788 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002316098.1 | 0 | 1 | 762 | 1 | 760 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002512108.1 | 0 | 1 | 762 | 1 | 780 | 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 | 1z8d_A | 0 | 105 | 762 | 55 | 642 | A Chain A, Crystal Structure Of Human Muscle Glycogen Phosphorylase A With Amp And Glucose |
PDB | 2ffr_A | 0 | 105 | 762 | 43 | 630 | A Chain A, Crystallographic Studies On N-Azido-Beta-D-Glucopyranosylamine, An Inhibitor Of Glycogen Phosphorylase: Comparison With N-Acetyl-Beta-D- Glucopyranosylam |
PDB | 2gj4_A | 0 | 105 | 762 | 43 | 630 | A Chain A, Structure Of Rabbit Muscle Glycogen Phosphorylase In Complex With Ligand |
PDB | 4el5_A | 0 | 105 | 762 | 43 | 630 | A Chain A, Structure Of Rabbit Muscle Glycogen Phosphorylase In Complex With Ligand |
PDB | 4el0_A | 0 | 105 | 762 | 43 | 630 | A Chain A, Structure Of Rabbit Muscle Glycogen Phosphorylase In Complex With Ligand |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO778303 | 402 | 102 | 503 | 0 |
HO778303 | 207 | 556 | 762 | 0 |
CO100137 | 297 | 193 | 489 | 0 |
ES816557 | 326 | 177 | 502 | 0 |
HO778303 | 87 | 20 | 103 | 0.000000002 |
Sequence Alignments (This image is cropped. Click for full image.) |
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