| Basic Information | |
|---|---|
| Species | Medicago truncatula |
| Cazyme ID | Medtr6g014480.1 |
| Family | GT35 |
| Protein Properties | Length: 965 Molecular Weight: 108440 Isoelectric Point: 4.8121 |
| Chromosome | Chromosome/Scaffold: 6 Start: 3860406 End: 3871111 |
| Description | Glycosyl transferase, family 35 |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GT35 | 160 | 908 | 0 |
| ALSQLGYKLENVAHQEPDAALGNGGLGRLASCFLDSMATLNYPAWGYGLRYKYGLFKQQITKDGQEEVAEDWLEMGNPWEIVRNDVTYPVRFYGKVISGS DGKKHWVGGEDIKAVAHDVPIPGYKTKTTINLRLWSTKAASEEFDLNAFNSGRHTEASEALANAEKICYVLYPGDDSIEGKTLRLKQQYTLCSASLQDII ARFERRSGASVNWEEFPEKVAVQMNDTHPTLCIPELMRILIDIKGLSWKDAWNITQRTVAYTNHTVLPEALEKWSMDLMEKLLPRHVEIIELIDEELVRT IIAEYGTADSDLLEKKLKEMRVLENVELPAEFADVLVKSKEADDISSEEVKISGEEEEDDDGNDDEVVIVEKDGTDKSSVEKKKEELPKPVVEPPKLVRM ANLCVVGGHAVNGVAEIHSEIVKDDVFNAFYKLWPEKFQNKTNGVTPRRWIRFCNPDLSKIITQWIGTEDWVLNTEKLAELRKFADNEDLQKQWREAKLN NKVKVAALIKERTGYSVSPDAMFDIQVKRIHEYKRQLLNIFGIKGKKTFVPRVCIFGGKAFATYVQAKRIVKFITDVGATVNHDPEIGDLLKVIFVPDYN VSVAEMLIPASELSQHISTAGMEASGTSNMKFAMNGCLQIGTLDGANVEIREEVGEDNFFLFGAKAHEITGLRKERAEGKFVPDPRFEEVKEYVRSGVFG SYNYDDLIGSLEGNEGFGRADYFLVGKDFPSYLECQEEVDEAYRNQKTN | |||
| Full Sequence |
|---|
| Protein Sequence Length: 965 Download |
| MTNLVVVGSR LQVVMNENGG IMIHECNSRP PALYYLLLFL MFRFPLLLCS YIGAAWLVLD 60 EATTSLSSFA PDASSIVSSI KYHAEFTPLF SPEKFELPQA FIATAQTVRD ALIINWNATY 120 DYYEKLNVKQ AYYLSMEFLQ GRALLNAIGN LELTGPYAEA LSQLGYKLEN VAHQEPDAAL 180 GNGGLGRLAS CFLDSMATLN YPAWGYGLRY KYGLFKQQIT KDGQEEVAED WLEMGNPWEI 240 VRNDVTYPVR FYGKVISGSD GKKHWVGGED IKAVAHDVPI PGYKTKTTIN LRLWSTKAAS 300 EEFDLNAFNS GRHTEASEAL ANAEKICYVL YPGDDSIEGK TLRLKQQYTL CSASLQDIIA 360 RFERRSGASV NWEEFPEKVA VQMNDTHPTL CIPELMRILI DIKGLSWKDA WNITQRTVAY 420 TNHTVLPEAL EKWSMDLMEK LLPRHVEIIE LIDEELVRTI IAEYGTADSD LLEKKLKEMR 480 VLENVELPAE FADVLVKSKE ADDISSEEVK ISGEEEEDDD GNDDEVVIVE KDGTDKSSVE 540 KKKEELPKPV VEPPKLVRMA NLCVVGGHAV NGVAEIHSEI VKDDVFNAFY KLWPEKFQNK 600 TNGVTPRRWI RFCNPDLSKI ITQWIGTEDW VLNTEKLAEL RKFADNEDLQ KQWREAKLNN 660 KVKVAALIKE RTGYSVSPDA MFDIQVKRIH EYKRQLLNIF GIKGKKTFVP RVCIFGGKAF 720 ATYVQAKRIV KFITDVGATV NHDPEIGDLL KVIFVPDYNV SVAEMLIPAS ELSQHISTAG 780 MEASGTSNMK FAMNGCLQIG TLDGANVEIR EEVGEDNFFL FGAKAHEITG LRKERAEGKF 840 VPDPRFEEVK EYVRSGVFGS YNYDDLIGSL EGNEGFGRAD YFLVGKDFPS YLECQEEVDE 900 AYRNQKTNGS ENEGPNSVTV TPLLTGPTYL AWSRSMKRAL GTKNKFAFLD GSVPIPPMDD 960 LNRN* 1020 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam00343 | Phosphorylase | 7.0e-135 | 160 | 483 | 324 | + 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 | 2.0e-174 | 558 | 907 | 364 | + 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]. | ||
| pfam00343 | Phosphorylase | 3.0e-175 | 558 | 906 | 363 | + 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 | 558 | 907 | 364 | + 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 | 79 | 445 | 371 | + 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 | |
|---|---|
| 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 |
| GenBank | ACJ11757.1 | 0 | 61 | 907 | 26 | 898 | alpha-1,4 glucan phosphorylase [Gossypium hirsutum] |
| Swiss-Prot | P27598 | 0 | 72 | 906 | 68 | 917 | PHSL_IPOBA RecName: Full=Alpha-1,4 glucan phosphorylase L isozyme, chloroplastic/amyloplastic; AltName: Full=Starch phosphorylase L; Flags: Precursor |
| Swiss-Prot | P53536 | 0 | 58 | 906 | 79 | 965 | PHSL_VICFA RecName: Full=Alpha-1,4 glucan phosphorylase L isozyme, chloroplastic/amyloplastic; AltName: Full=Starch phosphorylase L; Flags: Precursor |
| RefSeq | XP_002305367.1 | 0 | 57 | 907 | 33 | 912 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002526085.1 | 0 | 57 | 906 | 70 | 939 | 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 | 3cem_B | 0 | 72 | 906 | 1 | 773 | A Chain A, Hevamine Mutant D125aY183F IN COMPLEX WITH TETRA-Nag |
| PDB | 3cem_A | 0 | 72 | 906 | 1 | 773 | A Chain A, Hevamine Mutant D125aY183F IN COMPLEX WITH TETRA-Nag |
| PDB | 3cej_B | 0 | 72 | 906 | 1 | 773 | A Chain A, Hevamine Mutant D125aY183F IN COMPLEX WITH TETRA-Nag |
| PDB | 3cej_A | 0 | 72 | 906 | 1 | 773 | A Chain A, Hevamine Mutant D125aY183F IN COMPLEX WITH TETRA-Nag |
| PDB | 3ceh_B | 0 | 72 | 906 | 1 | 773 | A Chain A, Human Liver Glycogen Phosphorylase (Tense State) In Complex With The Allosteric Inhibitor Ave5688 |
