| Basic Information | |
|---|---|
| Species | Linum usitatissimum |
| Cazyme ID | Lus10037093 |
| Family | GT35 |
| Protein Properties | Length: 956 Molecular Weight: 108740 Isoelectric Point: 4.9284 |
| Chromosome | Chromosome/Scaffold: 462 Start: 172246 End: 176193 |
| Description | Glycosyl transferase, family 35 |
| View CDS | |
| External Links |
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| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GT35 | 163 | 948 | 0 |
| ALKTLGYSLEDVAKQEPDAALGNGGLGRLASCFLDSLATLNYPAWGYGLRYKYGLFKQLITKDGQEEVAESWLEMGNPWEIVRNDVSYPVKFYGEVKVNP DGSKEWIGGEDITAVAYDVPIPGYKTKTTLNLRLWSTKLDPQAFDLHAFNTGDHVKAYAAMNNAEKICYVLYPGDESREGKTLRLKQQYTLCSASLQDII ARFERRSCLGDESSSNWEEFPEKVAVQMNDTHPTLCIPELIRILVDVKGLSWREAWNITRRTVAYTNHTVLPEALEKWSLDLVQELLPRHVEIIKMIDEG LIHTIIEEYGAEDVDLLHKKLKEMRILDNFELPESVLELLVPPVEETPKLEEKEKQESEEQEEEEEEVDVTEETEERNELFEPDTSLPKLVRMANLCIAG GFAVNGVAEIHSEIVKNEVFNDFYKLWPEKFQNKTNGVTPRRWIRFCNPDLSGIITKWTGTEDWILDTEKLVKLRNFADDEELQTEWRQSKRRNKAKVAD FLKEKTGYTVSPDAMFDVQVKRIHEYKRQLLNILGIVYRYKKMKEMASDEERRSSYVPRVCIFGGKAFATYVQAKRIVKFITDVGATINHDPEIGDLLKV VFVPDYNVSVAEVLIPGSELSQHISTAGMEASGTSNMKFSMNGCVLIGTLDGANVEIREEVGEDNFFLFGAKAHEIASLREERTDGKFVPDPRFEEVKEY VRSGAFGSYNYNELMGSLEGNEGYGRADYFLVGKDFPSYIECQDQVDLAYKDQKRWTKMSIMNTAGSFKFSSDRTIHQYANEIWRI | |||
| Full Sequence |
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| Protein Sequence Length: 956 Download |
| MADFLFSPVA QSASQQPITS LHSPKLFFTS FTPSRSKQFL FPRRRTIKLF SVKSIASSDQ 60 KQELKDPLTS LQNGSHSAPN SSSLVSSINY HAEFTPAFSP ERFELPKAYV ATAQSVRDSL 120 IVNWNTTYDH HEKMNVKQAY YLSMEALLNA IGNLELSGAY ADALKTLGYS LEDVAKQEPD 180 AALGNGGLGR LASCFLDSLA TLNYPAWGYG LRYKYGLFKQ LITKDGQEEV AESWLEMGNP 240 WEIVRNDVSY PVKFYGEVKV NPDGSKEWIG GEDITAVAYD VPIPGYKTKT TLNLRLWSTK 300 LDPQAFDLHA FNTGDHVKAY AAMNNAEKIC YVLYPGDESR EGKTLRLKQQ YTLCSASLQD 360 IIARFERRSC LGDESSSNWE EFPEKVAVQM NDTHPTLCIP ELIRILVDVK GLSWREAWNI 420 TRRTVAYTNH TVLPEALEKW SLDLVQELLP RHVEIIKMID EGLIHTIIEE YGAEDVDLLH 480 KKLKEMRILD NFELPESVLE LLVPPVEETP KLEEKEKQES EEQEEEEEEV DVTEETEERN 540 ELFEPDTSLP KLVRMANLCI AGGFAVNGVA EIHSEIVKNE VFNDFYKLWP EKFQNKTNGV 600 TPRRWIRFCN PDLSGIITKW TGTEDWILDT EKLVKLRNFA DDEELQTEWR QSKRRNKAKV 660 ADFLKEKTGY TVSPDAMFDV QVKRIHEYKR QLLNILGIVY RYKKMKEMAS DEERRSSYVP 720 RVCIFGGKAF ATYVQAKRIV KFITDVGATI NHDPEIGDLL KVVFVPDYNV SVAEVLIPGS 780 ELSQHISTAG MEASGTSNMK FSMNGCVLIG TLDGANVEIR EEVGEDNFFL FGAKAHEIAS 840 LREERTDGKF VPDPRFEEVK EYVRSGAFGS YNYNELMGSL EGNEGYGRAD YFLVGKDFPS 900 YIECQDQVDL AYKDQKRWTK MSIMNTAGSF KFSSDRTIHQ YANEIWRINP LQLPN* 960 |
| Functional Domains Download unfiltered results here | ||||||
|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description |
| pfam00343 | Phosphorylase | 1.0e-132 | 163 | 490 | 328 | + 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 | 1.0e-175 | 87 | 491 | 414 | + 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 | 550 | 948 | 408 | + 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 | 546 | 950 | 410 | + 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 | 551 | 948 | 403 | + 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 | |
|---|---|
| GO Term | Description |
| GO:0004645 | phosphorylase activity |
| GO:0005975 | carbohydrate metabolic process |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| EMBL | CBI27267.1 | 0 | 44 | 954 | 49 | 933 | unnamed protein product [Vitis vinifera] |
| Swiss-Prot | P53535 | 0 | 34 | 954 | 24 | 974 | 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 | 44 | 954 | 49 | 981 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002316098.1 | 0 | 1 | 954 | 1 | 953 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002512108.1 | 0 | 1 | 954 | 1 | 973 | glycogen phosphorylase, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1xoi_B | 0 | 74 | 953 | 17 | 832 | A Chain A, Human Liver Glycogen Phosphorylase A Complexed With Chloroindoloyl Glycine Amide |
| PDB | 1xoi_A | 0 | 74 | 953 | 17 | 832 | A Chain A, Human Liver Glycogen Phosphorylase A Complexed With Chloroindoloyl Glycine Amide |
| PDB | 3cem_B | 0 | 80 | 950 | 1 | 807 | A Chain A, Human Liver Glycogen Phosphorylase A Complexed With Chloroindoloyl Glycine Amide |
| PDB | 3cem_A | 0 | 80 | 950 | 1 | 807 | A Chain A, Human Liver Glycogen Phosphorylase A Complexed With Chloroindoloyl Glycine Amide |
| PDB | 3cej_B | 0 | 80 | 950 | 1 | 807 | A Chain A, Human Liver Glycogen Phosphorylase A Complexed With Chloroindoloyl Glycine Amide |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| HO797178 | 401 | 554 | 954 | 0 |
| HO778303 | 401 | 554 | 954 | 0 |
| HO778303 | 389 | 108 | 491 | 0 |
| HO613954 | 403 | 552 | 954 | 0 |
| HO778303 | 80 | 35 | 110 | 0.0000003 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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