Basic Information | |
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Species | Eucalyptus grandis |
Cazyme ID | Eucgr.B03166.3 |
Family | GT35 |
Protein Properties | Length: 957 Molecular Weight: 108336 Isoelectric Point: 5.028 |
Chromosome | Chromosome/Scaffold: 2 Start: 56783228 End: 56790952 |
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 | 171 | 951 | 0 |
ALRKLGHNLEDVASQERDAALGNGGLGRLASCFLDSLATLNYPAWGYGLRYKYGLFKQNITKDGQEEVAENWLEMGNPWEIVRNDVSYPVKFYGEVISGP DGSKEWVGGENIVALAYDVPVPGYKTKTTINLRLWSTKVASEEFDLCAFNAGDHATAYAALKNAEKICYILYPGDESIEGKTLRLKQQYTLCSASLQDII TRFERRSGDVVDWGKLPEKVAVQMNDTHPTLCIPELIRILMDVKKLSWEEAWNITKRTVAYTNHTVLPEALEKWSLELMQDLLPRHVEIIKKIDEELVQT IIDEYGQEDLDLLQQKLKEMRILANVELPGTVLELLVKPEEDPIEEVDTAIEESKLVDEVDQPEEEDDPEEKKVIPEPDPELPKMVRMANLCVAGGFAVN GVAEIHSEIVKEEVFNDFFKLWPEKFQNKTNGVTPRRWIRFCNPNLSEIITKWTGTDDWTINTEKLAILRKFADNEDLQSEWREAKRRNKIKVAAFLKEK TGYVVSPDAMFDVQVKRIHEYKRQLLNILGIVHRYKKMKEMTPEERKTRFVPRVCIFGGKAFATYVQAKRIVKFITDVGATVNHDPEIGDLLKVVFVPDY NVSVAEVLIPGSELSQHISTAGMEASGTSNMKFAMNGCVLIGTLDGANVEIREEVGEDNFFLFGARAPEIAGLRKERAEGKFVPDARFEEVKAYVRSGVF GPYNYEELMGSLEGNEGYGRADYFLVGKDFPSYMECQEKVDEAYRDQKRWTKMSILNTAGSYKFSSDRTIHEYARDIWGIE |
Full Sequence |
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Protein Sequence Length: 957 Download |
MAASPFSANC TLPKSIAHSK SVHSSKGCDF GARVTKLFFL QHPRLVCSRR NFYVRNVASD 60 QKQELKEPLA DEVPGTLDTS VPDSASIASS IKYHAEFTPS FSPEKFELPK AYFATAESVR 120 DTLIINWNAT YHYYEKLNVK QAYYLSMEYL QGRALLNAIG NLELSGAYAE ALRKLGHNLE 180 DVASQERDAA LGNGGLGRLA SCFLDSLATL NYPAWGYGLR YKYGLFKQNI TKDGQEEVAE 240 NWLEMGNPWE IVRNDVSYPV KFYGEVISGP DGSKEWVGGE NIVALAYDVP VPGYKTKTTI 300 NLRLWSTKVA SEEFDLCAFN AGDHATAYAA LKNAEKICYI LYPGDESIEG KTLRLKQQYT 360 LCSASLQDII TRFERRSGDV VDWGKLPEKV AVQMNDTHPT LCIPELIRIL MDVKKLSWEE 420 AWNITKRTVA YTNHTVLPEA LEKWSLELMQ DLLPRHVEII KKIDEELVQT IIDEYGQEDL 480 DLLQQKLKEM RILANVELPG TVLELLVKPE EDPIEEVDTA IEESKLVDEV DQPEEEDDPE 540 EKKVIPEPDP ELPKMVRMAN LCVAGGFAVN GVAEIHSEIV KEEVFNDFFK LWPEKFQNKT 600 NGVTPRRWIR FCNPNLSEII TKWTGTDDWT INTEKLAILR KFADNEDLQS EWREAKRRNK 660 IKVAAFLKEK TGYVVSPDAM FDVQVKRIHE YKRQLLNILG IVHRYKKMKE MTPEERKTRF 720 VPRVCIFGGK AFATYVQAKR IVKFITDVGA TVNHDPEIGD LLKVVFVPDY NVSVAEVLIP 780 GSELSQHIST AGMEASGTSN MKFAMNGCVL IGTLDGANVE IREEVGEDNF FLFGARAPEI 840 AGLRKERAEG KFVPDARFEE VKAYVRSGVF GPYNYEELMG SLEGNEGYGR ADYFLVGKDF 900 PSYMECQEKV DEAYRDQKRW TKMSILNTAG SYKFSSDRTI HEYARDIWGI EPVVLP* 960 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR02093 | P_ylase | 0 | 91 | 950 | 870 | + 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]. | ||
COG0058 | GlgP | 0 | 82 | 952 | 878 | + Glucan phosphorylase [Carbohydrate transport and metabolism] | ||
cd04300 | GT1_Glycogen_Phosphorylase | 0 | 553 | 950 | 403 | + 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 | 88 | 471 | 388 | + 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 | 554 | 952 | 404 | + 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. |
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 | 956 | 1 | 933 | unnamed protein product [Vitis vinifera] |
Swiss-Prot | P53535 | 0 | 58 | 956 | 54 | 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 | 1 | 956 | 1 | 981 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002316098.1 | 0 | 10 | 956 | 2 | 953 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002512108.1 | 0 | 10 | 956 | 2 | 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 | 94 | 954 | 51 | 879 | A Chain A, Phosphorylated Form Of Yeast Glycogen Phosphorylase With Phosphate Bound In The Active Site. |
PDB | 1ygp_A | 0 | 94 | 954 | 51 | 879 | A Chain A, Phosphorylated Form Of Yeast Glycogen Phosphorylase With Phosphate Bound In The Active Site. |
PDB | 1z8d_A | 0 | 112 | 952 | 53 | 830 | A Chain A, Crystal Structure Of Human Muscle Glycogen Phosphorylase A With Amp And Glucose |
PDB | 2ffr_A | 0 | 112 | 952 | 41 | 818 | A Chain A, Crystallographic Studies On N-Azido-Beta-D-Glucopyranosylamine, An Inhibitor Of Glycogen Phosphorylase: Comparison With N-Acetyl-Beta-D- Glucopyranosylam |
PDB | 4el5_A | 0 | 112 | 952 | 41 | 818 | A Chain A, Crystallographic Studies On N-Azido-Beta-D-Glucopyranosylamine, An Inhibitor Of Glycogen Phosphorylase: Comparison With N-Acetyl-Beta-D- Glucopyranosylam |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO778303 | 870 | 111 | 957 | 0 |
HO797178 | 401 | 557 | 957 | 0 |
HO613954 | 510 | 448 | 957 | 0 |
HO620767 | 403 | 555 | 957 | 0 |
HO778303 | 89 | 30 | 113 | 0.00000008 |
Sequence Alignments (This image is cropped. Click for full image.) |
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