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Basic Information | |
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Species | Populus trichocarpa |
Cazyme ID | Potri.010G160200.1 |
Family | GT35 |
Protein Properties | Length: 980 Molecular Weight: 111220 Isoelectric Point: 5.5631 |
Chromosome | Chromosome/Scaffold: 10 Start: 16616169 End: 16622716 |
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 | |||
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Family | Start | End | Evalue |
GT35 | 187 | 974 | 0 |
ALRKLGHELEDVAGQEPDAALGNGGLGRLASCFLDSLATLNYPAWGYGLRYKYGLFKQLITKDGQEEVAENWLEMGNPWEIVRNDVSYSVKFYGEVISKP DGSKEWIGGENITAVAYDVPIPGYKTKTTINLRLWSTKVAPNEFDLRAYNAGDHAKACAALKNAEKICYILYPGDESTEGKILRLKQQYTLCSASLQDII AHFERRSGKPVNWENFPDKVAVQMNDTHPTLCIPELIRILIDLKGLSWKESWYITQRTVAYTNHTVLPEALEKWSLDLLQKLLPRHVEIIRMIDEELIHT IIAEYGTGDLDLLQHKLKQMRILDNIELPDSVLELLVKQEESSSVDSIKEVKVSDAETESTDEEQSEEQDTDAKDVVTFDPDPNLPKMVRMANLCVVGGY AVNGVAEIHSEIVKNEVFNEFYKASKLLWPEKFQNKTNGVTPRRWIRFCNPDLSKIITKWTGTDDWVLNTEKLSTLAEFSDNEDLQSEWREAKKRNKIKV ADFLKEKTGYIVNPDAMFDVQVKRIHEYKRQLLNIMGIVYRYKKMKEMSPEERKARYVPRVCIFGGKAFATYVQAKRIVKFITDVGTTVNHDADIGDLLK VVFVPDYNVSVAEVLIPGSELSQHISTAGMEASGTSNMKFAMNGCILIGTLDGANVEIRQEVGEDNFFLFGAEAHEIAGLRKERAEGKFIPDPRFEEVKA FVRNGVFGHYNYEELMGSLEGNEGYGRADYFLVGKDFPSYVECQEKVDEAYKDQKRWTKMSILNTAGSYKFSSDRTIHEYARDIWRIQ |
Full Sequence |
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Protein Sequence Length: 980 Download |
EDKTLLSLSL IFCSLHLTKS REQKQSMATL PFSAAQSSSV SGFNYRASHS NLFFVRTPRF 60 FNRLKRRNLS VKNITSDQRQ ELKDPSVNGE ASLETLEPDS ASIAASIQYH AEFTPLFSPE 120 HFDLPKAFVA TAESVRDSLI INWNATYKYY EKMNVKQAYY LSMEYLQGRA LLNAIGNLEL 180 SGAYADALRK LGHELEDVAG QEPDAALGNG GLGRLASCFL DSLATLNYPA WGYGLRYKYG 240 LFKQLITKDG QEEVAENWLE MGNPWEIVRN DVSYSVKFYG EVISKPDGSK EWIGGENITA 300 VAYDVPIPGY KTKTTINLRL WSTKVAPNEF DLRAYNAGDH AKACAALKNA EKICYILYPG 360 DESTEGKILR LKQQYTLCSA SLQDIIAHFE RRSGKPVNWE NFPDKVAVQM NDTHPTLCIP 420 ELIRILIDLK GLSWKESWYI TQRTVAYTNH TVLPEALEKW SLDLLQKLLP RHVEIIRMID 480 EELIHTIIAE YGTGDLDLLQ HKLKQMRILD NIELPDSVLE LLVKQEESSS VDSIKEVKVS 540 DAETESTDEE QSEEQDTDAK DVVTFDPDPN LPKMVRMANL CVVGGYAVNG VAEIHSEIVK 600 NEVFNEFYKA SKLLWPEKFQ NKTNGVTPRR WIRFCNPDLS KIITKWTGTD DWVLNTEKLS 660 TLAEFSDNED LQSEWREAKK RNKIKVADFL KEKTGYIVNP DAMFDVQVKR IHEYKRQLLN 720 IMGIVYRYKK MKEMSPEERK ARYVPRVCIF GGKAFATYVQ AKRIVKFITD VGTTVNHDAD 780 IGDLLKVVFV PDYNVSVAEV LIPGSELSQH ISTAGMEASG TSNMKFAMNG CILIGTLDGA 840 NVEIRQEVGE DNFFLFGAEA HEIAGLRKER AEGKFIPDPR FEEVKAFVRN GVFGHYNYEE 900 LMGSLEGNEG YGRADYFLVG KDFPSYVECQ EKVDEAYKDQ KRWTKMSILN TAGSYKFSSD 960 RTIHEYARDI WRIQPVLLP* 1020 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd04300 | GT1_Glycogen_Phosphorylase | 1.0e-180 | 104 | 511 | 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. | ||
TIGR02093 | P_ylase | 0 | 107 | 973 | 875 | + 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 | 95 | 975 | 891 | + Glucan phosphorylase [Carbohydrate transport and metabolism] | ||
cd04300 | GT1_Glycogen_Phosphorylase | 0 | 570 | 973 | 409 | + 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 | 975 | 413 | + 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 | 27 | 979 | 1 | 933 | unnamed protein product [Vitis vinifera] |
Swiss-Prot | P53535 | 0 | 76 | 979 | 55 | 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 | 27 | 979 | 1 | 981 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002316098.1 | 0 | 27 | 979 | 1 | 953 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002512108.1 | 0 | 27 | 979 | 1 | 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 | 1xoi_B | 0 | 76 | 975 | 5 | 829 | A Chain A, Human Liver Glycogen Phosphorylase A Complexed With Chloroindoloyl Glycine Amide |
PDB | 1xoi_A | 0 | 76 | 975 | 5 | 829 | A Chain A, Human Liver Glycogen Phosphorylase A Complexed With Chloroindoloyl Glycine Amide |
PDB | 2zb2_B | 0 | 76 | 975 | 8 | 832 | A Chain A, Human Liver Glycogen Phosphorylase A Complexed With Glcose And 5- Chloro-N-[4-(1,2-Dihydroxyethyl)phenyl]-1h-Indole-2-Carboxamide |
PDB | 2zb2_A | 0 | 76 | 975 | 8 | 832 | A Chain A, Human Liver Glycogen Phosphorylase A Complexed With Glcose And 5- Chloro-N-[4-(1,2-Dihydroxyethyl)phenyl]-1h-Indole-2-Carboxamide |
PDB | 2ati_B | 0 | 76 | 975 | 5 | 829 | A Chain A, Human Liver Glycogen Phosphorylase A Complexed With Glcose And 5- Chloro-N-[4-(1,2-Dihydroxyethyl)phenyl]-1h-Indole-2-Carboxamide |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
starch degradation I | RXN-1826 | EC-2.4.1.1 | phosphorylase |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO797178 | 405 | 576 | 980 | 0 |
HO778303 | 405 | 576 | 980 | 0 |
HO778303 | 407 | 127 | 533 | 0 |
HO613954 | 517 | 464 | 980 | 0 |
HO778303 | 113 | 23 | 129 | 0.000000000003 |
Sequence Alignments (This image is cropped. Click for full image.) |
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