| Basic Information | |
|---|---|
| Species | Thellungiella halophila |
| Cazyme ID | Thhalv10003599m |
| Family | GT35 |
| Protein Properties | Length: 971 Molecular Weight: 109670 Isoelectric Point: 5.3966 |
| Chromosome | Chromosome/Scaffold: 6 Start: 5392362 End: 5397409 |
| 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 | 179 | 965 | 0 |
| ALKSLGFDLESVASQEPDPALGNGGLGRLASCFLDSLATLNYPAWGYGLRYKYGLFKQRITKDGQEEAAEDWLELSNPWEIVRNDVSYPVKFYGKVVFGS DGKKRWIGGEDIVAVAYDVPIPGYKTKSTINLRLWSTKAPSEDFDLSSYNSGKHTEAAEALFNAEKICYVLYPGDESIEGKALRLKQQYTLCSASLQDII ARYETRSGGSINWEEFPEKVAVQMNDTHPTLCIPELMRILMDLKGLSWEDAWKITQRTVAYTNHTVLPEALEKWSLELMEKLLPRHVEIIEMIDEELVRT IVSEYGTADPDLLEEKLKAMRILENVELPSAFADVIVKPKNKPVSAINTIGPFEDSEEDAQTVVKKEQEEERSAGEEEEVIPEPTVKPPKMVRMANLAVV GGHAVNGVAEIHSEIVKKDVFNEFVKLWPDKFQNKTNGVTPRRWIRFCNPYLSDIITNWIGTEDWVLNTEKLSELRKFADNEDLQSEWRAAKKKNKLKVV SLIKERTGYTVNPDAMFDIQIKRIHEYKRQLLNILGIVYRYKKMKEMSASEREKAFVPRVCIFGGKAFATYVQAKRIVKFITDVGSTINHDPEIGDLLKV IFVPDYNVSVAELLIPASELSQHISTAGMEASGTSNMKFSMNGCILIGTLDGANVEIRDEVGEENFFLFGAKAHEIVNLRKERAEGKFVPDPIFEEVKKF VRSGVFGSNNYDELIGSLEGNEGFGRADYFLVGKDFPSYVECQEKVDEAYRDQKRWTRMSIMNTAGSFKFSSDRTIHEYAKDIWNIK | |||
| Full Sequence |
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| Protein Sequence Length: 971 Download |
| MDTMRLSGVS NRAEILVQCN SLSSLVGRRC DNGRWRTRMF PAQSRTWRPA ATRKRFSSVK 60 SVSSEPKEKI ADAVIDSEQE ALTSLSPFAP DAASVASSIK YHSEFTPLFS PEKFELPKAF 120 FATAQSVRDA LIINWNATYE YYNRVNVKQA YYLSMEFLQG RALSNAVGNL GLTGPYAEAL 180 KSLGFDLESV ASQEPDPALG NGGLGRLASC FLDSLATLNY PAWGYGLRYK YGLFKQRITK 240 DGQEEAAEDW LELSNPWEIV RNDVSYPVKF YGKVVFGSDG KKRWIGGEDI VAVAYDVPIP 300 GYKTKSTINL RLWSTKAPSE DFDLSSYNSG KHTEAAEALF NAEKICYVLY PGDESIEGKA 360 LRLKQQYTLC SASLQDIIAR YETRSGGSIN WEEFPEKVAV QMNDTHPTLC IPELMRILMD 420 LKGLSWEDAW KITQRTVAYT NHTVLPEALE KWSLELMEKL LPRHVEIIEM IDEELVRTIV 480 SEYGTADPDL LEEKLKAMRI LENVELPSAF ADVIVKPKNK PVSAINTIGP FEDSEEDAQT 540 VVKKEQEEER SAGEEEEVIP EPTVKPPKMV RMANLAVVGG HAVNGVAEIH SEIVKKDVFN 600 EFVKLWPDKF QNKTNGVTPR RWIRFCNPYL SDIITNWIGT EDWVLNTEKL SELRKFADNE 660 DLQSEWRAAK KKNKLKVVSL IKERTGYTVN PDAMFDIQIK RIHEYKRQLL NILGIVYRYK 720 KMKEMSASER EKAFVPRVCI FGGKAFATYV QAKRIVKFIT DVGSTINHDP EIGDLLKVIF 780 VPDYNVSVAE LLIPASELSQ HISTAGMEAS GTSNMKFSMN GCILIGTLDG ANVEIRDEVG 840 EENFFLFGAK AHEIVNLRKE RAEGKFVPDP IFEEVKKFVR SGVFGSNNYD ELIGSLEGNE 900 GFGRADYFLV GKDFPSYVEC QEKVDEAYRD QKRWTRMSIM NTAGSFKFSS DRTIHEYAKD 960 IWNIKQVELP * |
| Functional Domains Download unfiltered results here | ||||||||
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam00343 | Phosphorylase | 3.0e-151 | 179 | 502 | 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. | ||
| PRK14985 | PRK14985 | 0 | 152 | 965 | 829 | + maltodextrin phosphorylase; Provisional | ||
| cd04300 | GT1_Glycogen_Phosphorylase | 0 | 566 | 964 | 404 | + 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 | 96 | 503 | 412 | + 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 | 568 | 965 | 403 | + 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 |
| GenBank | ACJ11757.1 | 0 | 55 | 970 | 3 | 935 | alpha-1,4 glucan phosphorylase [Gossypium hirsutum] |
| RefSeq | NP_189578.1 | 0 | 1 | 970 | 1 | 962 | glucan phosphorylase, putative [Arabidopsis thaliana] |
| Swiss-Prot | P53536 | 0 | 3 | 969 | 5 | 1002 | PHSL_VICFA RecName: Full=Alpha-1,4 glucan phosphorylase L isozyme, chloroplastic/amyloplastic; AltName: Full=Starch phosphorylase L; Flags: Precursor |
| RefSeq | XP_002279075.1 | 0 | 28 | 970 | 43 | 958 | PREDICTED: similar to Alpha-1,4 glucan phosphorylase L-1 isozyme, chloroplastic/amyloplastic [Vitis vinifera] |
| RefSeq | XP_002526085.1 | 0 | 18 | 970 | 16 | 977 | 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 | 2azd_B | 0 | 146 | 966 | 57 | 796 | A Chain A, Crystal Structure Of Bovine Cd1d With Bound C12-Di-Sulfatide |
| PDB | 2azd_A | 0 | 146 | 966 | 57 | 796 | A Chain A, Crystal Structure Of Bovine Cd1d With Bound C12-Di-Sulfatide |
| PDB | 2aw3_B | 0 | 146 | 966 | 57 | 796 | A Chain A, Crystal Structure Of Bovine Cd1d With Bound C12-Di-Sulfatide |
| PDB | 2aw3_A | 0 | 146 | 966 | 57 | 796 | A Chain A, Crystal Structure Of Bovine Cd1d With Bound C12-Di-Sulfatide |
| PDB | 2av6_B | 0 | 146 | 966 | 57 | 796 | A Chain A, Crystal Structure Of Bovine Cd1d With Bound C12-Di-Sulfatide |
| Hydropathy |
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| EST Download unfiltered results here | ||||
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| Hit | Length | Start | End | EValue |
| HO778303 | 864 | 119 | 971 | 0 |
| HO797178 | 384 | 588 | 971 | 0 |
| HO418036 | 589 | 305 | 890 | 0 |
| HO613954 | 516 | 456 | 971 | 0 |
| HO778303 | 122 | 3 | 121 | 0.00000000003 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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