| Basic Information | |
|---|---|
| Species | Cucumis sativus |
| Cazyme ID | Cucsa.284600.1 |
| Family | GT35 |
| Protein Properties | Length: 986 Molecular Weight: 111378 Isoelectric Point: 4.9553 |
| Chromosome | Chromosome/Scaffold: 02653 Start: 1305547 End: 1311987 |
| Description | Glycosyl transferase, family 35 |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
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| Family | Start | End | Evalue |
| GT35 | 179 | 979 | 0 |
| ALRVLGFNLEEVARQESDAALGNGGLGRLASCFLDSLATLNYPAWGYGLRYKYGLFKQLITKNGQEEVAENWLEMGNPWEIARNDISYPVKFYGEVISGA DGSKQWVGGENITAVAYDVPIPGYKTKTTINLRLWSTKVAPEEFDLSSFNVGNHADAYAAIKKAEKICYVLYPGDDSLEGKTLRLKQQYTLCSASLQDIV ARFERRSGEALDWESFPEKVAVQMNDTHPTLCIPELIRILMDVKALTWKEAWDITSRTVAYTNHTVLPEALEKWGFPLMQELLPRHVQIIEMIDEELIHS IVAKYGTKDHELLQQKLKEMRVLENFELPDSVMELLVNSAESAVAVDAIEEAEILDEESLPSKEEEEAEILDEESLPGKEEEESEDKSIAKKIDVSFKVD PKQPKMIRMANLSVVGGYSVNGVAEIHSEIVRTEVFSDFYELWPEKFQNKTNGVTPRRWIRFCNPDLSKIITKWTGTEHWVTDTEKLAILRKFADNEDLQ SMWKEAKRINKLKVVSFLKEKTGYLVSPDAMFDVQVKRIHEYKRQLLNILGIVYRYKQMKEMTLEEREAKFVPRVCIFGGKAFATYVQAKRIVKFIADVG ATVNNDPDIGDLLKVVFVPDYNVSVAEVLIPGSDLSQHISTAGMEASGTSNMKFAMNGCVLIGTLDGANVEIREEVGEDNFFLFGARAHEIANLRKERAQ GKFVPDPRFEEVKAFVRSGVFGSNNYEELIGSLEGNEGYGRADYFLVGKDFPSYIECQDRVDEAYRDQKRWTKMSILNTAGSYKFSSDRTIHEYAKDIWK I | |||
| Full Sequence |
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| Protein Sequence Length: 986 Download |
| MAPFRLSSSS INSNNPHLSK FNFPSTAAIT SDSGFRTNWT TTRLLLFRTT SVPSSTRRKL 60 WISNVAKDQQ KELKDPVNGG VVDDSDSFLP DSASIAASIK YHSEFTPSFS PEGFGLSKAY 120 YATAESVRDM LIINWNATYE YYERMNVKQA YYLSMEFLQG RALLNAIGNL ELSGNYGDAL 180 RVLGFNLEEV ARQESDAALG NGGLGRLASC FLDSLATLNY PAWGYGLRYK YGLFKQLITK 240 NGQEEVAENW LEMGNPWEIA RNDISYPVKF YGEVISGADG SKQWVGGENI TAVAYDVPIP 300 GYKTKTTINL RLWSTKVAPE EFDLSSFNVG NHADAYAAIK KAEKICYVLY PGDDSLEGKT 360 LRLKQQYTLC SASLQDIVAR FERRSGEALD WESFPEKVAV QMNDTHPTLC IPELIRILMD 420 VKALTWKEAW DITSRTVAYT NHTVLPEALE KWGFPLMQEL LPRHVQIIEM IDEELIHSIV 480 AKYGTKDHEL LQQKLKEMRV LENFELPDSV MELLVNSAES AVAVDAIEEA EILDEESLPS 540 KEEEEAEILD EESLPGKEEE ESEDKSIAKK IDVSFKVDPK QPKMIRMANL SVVGGYSVNG 600 VAEIHSEIVR TEVFSDFYEL WPEKFQNKTN GVTPRRWIRF CNPDLSKIIT KWTGTEHWVT 660 DTEKLAILRK FADNEDLQSM WKEAKRINKL KVVSFLKEKT GYLVSPDAMF DVQVKRIHEY 720 KRQLLNILGI VYRYKQMKEM TLEEREAKFV PRVCIFGGKA FATYVQAKRI VKFIADVGAT 780 VNNDPDIGDL LKVVFVPDYN VSVAEVLIPG SDLSQHISTA GMEASGTSNM KFAMNGCVLI 840 GTLDGANVEI REEVGEDNFF LFGARAHEIA NLRKERAQGK FVPDPRFEEV KAFVRSGVFG 900 SNNYEELIGS LEGNEGYGRA DYFLVGKDFP SYIECQDRVD EAYRDQKRWT KMSILNTAGS 960 YKFSSDRTIH EYAKDIWKIS PLLIS* |
| Functional Domains Download unfiltered results here | ||||||||
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam00343 | Phosphorylase | 8.0e-130 | 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. | ||
| cd04300 | GT1_Glycogen_Phosphorylase | 0 | 582 | 979 | 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 | 96 | 503 | 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. | ||
| pfam00343 | Phosphorylase | 0 | 577 | 981 | 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 | 583 | 979 | 402 | + 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 | 34 | 984 | 27 | 932 | unnamed protein product [Vitis vinifera] |
| Swiss-Prot | P53535 | 0 | 66 | 982 | 54 | 971 | 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 | 34 | 984 | 27 | 980 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002316098.1 | 0 | 25 | 984 | 7 | 952 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002512108.1 | 0 | 42 | 984 | 29 | 972 | 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 | 583 | 978 | 402 | 793 | A Chain A, Solution Nmr Structure Of Proteorhodopsin |
| PDB | 2azd_B | 0 | 146 | 472 | 57 | 375 | A Chain A, Solution Nmr Structure Of Proteorhodopsin |
| PDB | 2azd_A | 0 | 583 | 978 | 402 | 793 | A Chain A, Solution Nmr Structure Of Proteorhodopsin |
| PDB | 2azd_A | 0 | 146 | 472 | 57 | 375 | A Chain A, Solution Nmr Structure Of Proteorhodopsin |
| PDB | 2aw3_B | 0 | 583 | 978 | 402 | 793 | A Chain A, Solution Nmr Structure Of Proteorhodopsin |
| Hydropathy |
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| EST Download unfiltered results here | ||||
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| Hit | Length | Start | End | EValue |
| HO797178 | 396 | 586 | 981 | 0 |
| HO778303 | 396 | 586 | 981 | 0 |
| HO778303 | 401 | 117 | 517 | 0 |
| HO613954 | 398 | 584 | 981 | 0 |
| HO778303 | 55 | 68 | 120 | 0.0003 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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