y
Basic Information | |
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Species | Linum usitatissimum |
Cazyme ID | Lus10036892 |
Family | GT35 |
Protein Properties | Length: 775 Molecular Weight: 88622.5 Isoelectric Point: 4.953 |
Chromosome | Chromosome/Scaffold: 31 Start: 1118576 End: 1122925 |
Description | Glycosyl transferase, family 35 |
View CDS |
External Links |
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CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GT35 | 58 | 767 | 0 |
QMGNPWEIVRNDVSYPVKFYGEVKVNPDGSKEWIGGEDITAVAYDVPIPGYKTKTTLNLRLWSTKLDPQAFDLHAFNTGDHVKAYAAMNNAEKICYVLYP GDESREGKTLRLKQQYTLCSASLQDIIARFERRSCSGDESSSNWEDFPEKVAVQMNDTHPTLCIPELIRILVDVKGLSWREAWNITRRTVAYTNHTVLPE ALEKWSLDLVQELLPRHVEIIKLIDEELIHTIIEEYGAEDVDLWHKNLKEMRILDNFELPESVLELLVPPVEETPKLEEKEKQEQEEQEEDADVAEEKEE TNELFEPDPSLPKQVRMANLCIAGGFAVNGVAEIHSEIVKNEVFNDFYKLWPEKFQNKTNGVTPRRWIRFCNPDLSGIITKWTGTEHWILDAEKLVKLRN FADDEELQTEWRESKRRNKAKVADFLKEKTGYTVSPDAMFDVQVKRIHEYKRQLLNILGIVYRYKKMKEMASDEERRSSYVPRVCIFGGKAFATYVQAKR IVKFITDVGATINHDPEIGDLLKVVFVPDYNVSVAEVLIPGSELSQHISTAGMEASGTSNMKFSMNGCVLIGTLDGANVEIREEVGEDNFFLFGAKAHEI ATLREERAKGKFVPDPRFEEVKQYVRSGAFGSYNYNELMGSLEGNEGYGRADYFLVGKDFPSYIECQDQVDLAYKDQKRWTKMSIMNTAGSFKFSSDRTI HQYANEIWRI |
Full Sequence |
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Protein Sequence Length: 775 Download |
MTQNAIRDKD CRFFPHPLRS PKMVDRALLN AIGNLELSGA YADALKTLGY SLEDVAKQMG 60 NPWEIVRNDV SYPVKFYGEV KVNPDGSKEW IGGEDITAVA YDVPIPGYKT KTTLNLRLWS 120 TKLDPQAFDL HAFNTGDHVK AYAAMNNAEK ICYVLYPGDE SREGKTLRLK QQYTLCSASL 180 QDIIARFERR SCSGDESSSN WEDFPEKVAV QMNDTHPTLC IPELIRILVD VKGLSWREAW 240 NITRRTVAYT NHTVLPEALE KWSLDLVQEL LPRHVEIIKL IDEELIHTII EEYGAEDVDL 300 WHKNLKEMRI LDNFELPESV LELLVPPVEE TPKLEEKEKQ EQEEQEEDAD VAEEKEETNE 360 LFEPDPSLPK QVRMANLCIA GGFAVNGVAE IHSEIVKNEV FNDFYKLWPE KFQNKTNGVT 420 PRRWIRFCNP DLSGIITKWT GTEHWILDAE KLVKLRNFAD DEELQTEWRE SKRRNKAKVA 480 DFLKEKTGYT VSPDAMFDVQ VKRIHEYKRQ LLNILGIVYR YKKMKEMASD EERRSSYVPR 540 VCIFGGKAFA TYVQAKRIVK FITDVGATIN HDPEIGDLLK VVFVPDYNVS VAEVLIPGSE 600 LSQHISTAGM EASGTSNMKF SMNGCVLIGT LDGANVEIRE EVGEDNFFLF GAKAHEIATL 660 REERAKGKFV PDPRFEEVKQ YVRSGAFGSY NYNELMGSLE GNEGYGRADY FLVGKDFPSY 720 IECQDQVDLA YKDQKRWTKM SIMNTAGSFK FSSDRTIHQY ANEIWRINPL QLPN* 780 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR02093 | P_ylase | 7.0e-102 | 60 | 313 | 257 | + 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 | 8.0e-111 | 60 | 313 | 257 | + 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 | 60 | 769 | 715 | + 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 | 0 | 369 | 767 | 411 | + 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 | 370 | 767 | 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 | |
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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 | 26 | 773 | 152 | 933 | unnamed protein product [Vitis vinifera] |
Swiss-Prot | P53535 | 0 | 26 | 773 | 148 | 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 | 26 | 773 | 173 | 981 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002316098.1 | 0 | 26 | 773 | 143 | 953 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002512108.1 | 0 | 26 | 773 | 148 | 973 | 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 | 49 | 770 | 203 | 878 | A Chain A, Phosphorylated Form Of Yeast Glycogen Phosphorylase With Phosphate Bound In The Active Site. |
PDB | 1ygp_A | 0 | 49 | 770 | 203 | 878 | A Chain A, Phosphorylated Form Of Yeast Glycogen Phosphorylase With Phosphate Bound In The Active Site. |
PDB | 1xoi_B | 0 | 60 | 772 | 186 | 832 | A Chain A, Human Liver Glycogen Phosphorylase A Complexed With Chloroindoloyl Glycine Amide |
PDB | 1xoi_A | 0 | 60 | 772 | 186 | 832 | A Chain A, Human Liver Glycogen Phosphorylase A Complexed With Chloroindoloyl Glycine Amide |
PDB | 2qll_A | 0 | 60 | 772 | 187 | 833 | A Chain A, Human Liver Glycogen Phosphorylase- Gl Complex |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO797178 | 401 | 373 | 773 | 0 |
HO778303 | 401 | 373 | 773 | 0 |
HO778303 | 347 | 26 | 313 | 0 |
HO613954 | 402 | 372 | 773 | 0 |
HO620767 | 402 | 372 | 773 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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