| Basic Information | |
|---|---|
| Species | Aquilegia coerulea |
| Cazyme ID | Aquca_002_00786.1 |
| Family | GT35 |
| Protein Properties | Length: 974 Molecular Weight: 110591 Isoelectric Point: 5.0782 |
| Chromosome | Chromosome/Scaffold: 2 Start: 5974528 End: 5981183 |
| Description | Glycosyl transferase, family 35 |
| View CDS | |
| External Links |
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| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GT35 | 179 | 967 | 0 |
| ALSKLGHDLENVAKQEPDAALGNGGLGRLASCFLDSLATLNYPAWGYGLRYKYGLFKQNITKDGQEEVAENWLEMANPWEIVRNDVSYPVKFFGKVVAGS DGKKHWIGGEDIKAVAYDVPIPGYKTKTTINLRLWSTKAPSQDFDLSAFNSGNHAKAYEAQTNAEKICYILYPGDDSVEGKILRLKQQYTLCSASLQDII ARFEKRCGGSLNWEEFPEKVAVQLNDTHPTLCIPELMRILIDVKGMSWKQAWEITQRTVAYTNHTVLPEALEKWSYDIMQKLLPRHVEIIESIDEQLLHT IILESGVEDLELLQKKLKEMRILDNFDLPDSVLELLFPPEENSIMDSNEEVNIYDEDEDSNEEADSDEEKESEGENNWNKTMALFKPAPKAEKIVRMANL CVVGGHAVNGVAEIHSEIVKEEVFNEFFKLWPHKFQNKTNGVTPRRWILFCNPDLSSIISKWTGTEDWVLDTEKLAELRKFVDNKDLQTEWRAAKRNNKM KIVSFIKERTGYTVSPDAMFDVQVKRIHEYKRQLLNIMGIVYRYKKMKEMSAEERKDKFVPRVCIFGGKAFSTYVQAKRIVKFITDVGATVNHDPEIGDL LKVVFVPDYNVSVAELLIPASELSQHISTAGMEASGTSNMKFSMNGCVLIGTLDGANVEIREEVGEDNFFLFGAQAHEIAELRKERAEGKFVPDPRFEEV KTYIRSGVFGSSNYDELMGSLEGNEGYGRADYFLVGEDFPSYIECQEKVDEAYRDQKRWTRMSILNTAGSYKFSSDRTIREYAKDIWNI | |||
| Full Sequence |
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| Protein Sequence Length: 974 Download |
| MATSNISATM KTSPSSTTRS HCNSLSRFIT FTSNNNIHHS NHLFFTKTSN SSLRSKRSLS 60 LYVNNVISDQ KLTEPIPQQE VNDDPSSFSP NSISIASNIK YHAEFTPSFS PEKFEVSKAY 120 FATAESVRDA LIANWNATYD YYDKLNMKQA YYLSMEFLQG RALLNAIGNL ELSGPYAEAL 180 SKLGHDLENV AKQEPDAALG NGGLGRLASC FLDSLATLNY PAWGYGLRYK YGLFKQNITK 240 DGQEEVAENW LEMANPWEIV RNDVSYPVKF FGKVVAGSDG KKHWIGGEDI KAVAYDVPIP 300 GYKTKTTINL RLWSTKAPSQ DFDLSAFNSG NHAKAYEAQT NAEKICYILY PGDDSVEGKI 360 LRLKQQYTLC SASLQDIIAR FEKRCGGSLN WEEFPEKVAV QLNDTHPTLC IPELMRILID 420 VKGMSWKQAW EITQRTVAYT NHTVLPEALE KWSYDIMQKL LPRHVEIIES IDEQLLHTII 480 LESGVEDLEL LQKKLKEMRI LDNFDLPDSV LELLFPPEEN SIMDSNEEVN IYDEDEDSNE 540 EADSDEEKES EGENNWNKTM ALFKPAPKAE KIVRMANLCV VGGHAVNGVA EIHSEIVKEE 600 VFNEFFKLWP HKFQNKTNGV TPRRWILFCN PDLSSIISKW TGTEDWVLDT EKLAELRKFV 660 DNKDLQTEWR AAKRNNKMKI VSFIKERTGY TVSPDAMFDV QVKRIHEYKR QLLNIMGIVY 720 RYKKMKEMSA EERKDKFVPR VCIFGGKAFS TYVQAKRIVK FITDVGATVN HDPEIGDLLK 780 VVFVPDYNVS VAELLIPASE LSQHISTAGM EASGTSNMKF SMNGCVLIGT LDGANVEIRE 840 EVGEDNFFLF GAQAHEIAEL RKERAEGKFV PDPRFEEVKT YIRSGVFGSS NYDELMGSLE 900 GNEGYGRADY FLVGEDFPSY IECQEKVDEA YRDQKRWTRM SILNTAGSYK FSSDRTIREY 960 AKDIWNINPV DLQ* 1020 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam00343 | Phosphorylase | 5.0e-135 | 179 | 479 | 301 | + 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 | 569 | 967 | 408 | + 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 | 100 | 476 | 381 | + 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 | 569 | 969 | 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. | ||
| TIGR02093 | P_ylase | 0 | 569 | 967 | 404 | + 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 | |
|---|---|
| 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 |
| EMBL | CAA36612.1 | 0 | 10 | 972 | 1 | 965 | unnamed protein product [Solanum tuberosum] |
| EMBL | CBI22291.1 | 0 | 20 | 972 | 17 | 981 | unnamed protein product [Vitis vinifera] |
| Swiss-Prot | P04045 | 0 | 10 | 972 | 1 | 965 | PHSL1_SOLTU RecName: Full=Alpha-1,4 glucan phosphorylase L-1 isozyme, chloroplastic/amyloplastic; AltName: Full=Starch phosphorylase L-1; Flags: Precursor |
| RefSeq | XP_002279075.1 | 0 | 20 | 972 | 17 | 957 | PREDICTED: similar to Alpha-1,4 glucan phosphorylase L-1 isozyme, chloroplastic/amyloplastic [Vitis vinifera] |
| RefSeq | XP_002526085.1 | 0 | 13 | 972 | 2 | 976 | 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 | 1xoi_B | 0 | 120 | 973 | 52 | 833 | A Chain A, Human Liver Glycogen Phosphorylase A Complexed With Chloroindoloyl Glycine Amide |
| PDB | 1xoi_A | 0 | 120 | 973 | 52 | 833 | A Chain A, Human Liver Glycogen Phosphorylase A Complexed With Chloroindoloyl Glycine Amide |
| PDB | 2ati_B | 0 | 120 | 973 | 52 | 833 | A Chain A, Human Liver Glycogen Phosphorylase A Complexed With Chloroindoloyl Glycine Amide |
| PDB | 2ati_A | 0 | 120 | 973 | 52 | 833 | A Chain A, Human Liver Glycogen Phosphorylase A Complexed With Chloroindoloyl Glycine Amide |
| PDB | 1fc0_B | 0 | 120 | 973 | 52 | 833 | A Chain A, Human Liver Glycogen Phosphorylase Complexed With N-Acetyl-Beta-D- Glucopyranosylamine |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| HO778303 | 867 | 114 | 972 | 0 |
| HO797178 | 399 | 574 | 972 | 0 |
| HO418036 | 593 | 305 | 893 | 0 |
| HO613954 | 401 | 572 | 972 | 0 |
| HO613954 | 59 | 456 | 514 | 0.062 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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