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Basic Information | |
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Species | Sorghum bicolor |
Cazyme ID | Sb01g007560.1 |
Family | GT35 |
Protein Properties | Length: 986 Molecular Weight: 109914 Isoelectric Point: 5.2556 |
Chromosome | Chromosome/Scaffold: 1 Start: 6509017 End: 6515545 |
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 | 170 | 522 | 0 |
ALKQLGQNLEDVASQEPDAALGNGGLGRLASCFLDSLATLNYPAWGYGLRYKYGLFKQIITKDGQEEIAENWLEMGYPWEVVRNDVSYPVKFYGKVVEGT DGRKHWIGGENIKAVAHDVPIPGYKTRTTNNLRLWSTTVPAQDFDLAAFNSGDHTKAYEAHLNAEKICHILYPGDESLEGKVLRLKQQYTLCSASLQDII GRFESRAGESLNWEDFPSKVAVQMNDTHPTLCIPELMRILIDVKGLSWSEAWSITERTVAYTNHTVLPEALEKWSLDIMQKLLPRHVEIIETIDEELIND IVSKYGTTDTGLLKKKLKEMRILDNVDLPASISQLFVKPKDKKESPAKSKQKL | |||
GT35 | 580 | 979 | 0 |
KLPRVVRMANLCVVGGHSVNGVAEIHSEIVKQDVFNSFYEMWPTKFQNKTNGVTPRRWIRFCNPELSALISKWIGSDDWVLNTDKLAELKKFADNEDLHS EWRAAKRANKMKVVSLIREKTGYIVSPDAMFDVQVKRIHEYKRQLLNILGIVYRYKKMKEMSAEERAKSFVPRVCIFGGKAFATYIQAKRIVKFITDVAA TVNHDSDVGDLLKVVFVPDYNVSVAEALIPASELSQHISTAGMEASGTSNMKFAMNGCILIGTLDGANVEIREEVGEENFFLFGAEAHEIAGLRKERAEG KFVPDPRFEEVKEFVRSGVFGTYNYDELMGSLEGNEGYGRADYFLVGKDFPSYIECQEKVDKAYRDQKLWTRMSILNTAGSSKFSSDRTIHEYAKDIWDI |
Full Sequence |
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Protein Sequence Length: 986 Download |
MATTASPPLQ LATASRPHAS ASGGGGVGGV LLAGGCGGGV VPGRGRGRMQ RRVSARSVAS 60 DRDVQGPVSP AEGLPSVLNS IGSSAIASNI KHHAEFTPLF SPEHFSPLKA YHATAKSVLD 120 ALLINWNATY DYYNKMNVKQ AYYLSMEFLQ GRALTNAIGN LEITGEYAEA LKQLGQNLED 180 VASQEPDAAL GNGGLGRLAS CFLDSLATLN YPAWGYGLRY KYGLFKQIIT KDGQEEIAEN 240 WLEMGYPWEV VRNDVSYPVK FYGKVVEGTD GRKHWIGGEN IKAVAHDVPI PGYKTRTTNN 300 LRLWSTTVPA QDFDLAAFNS GDHTKAYEAH LNAEKICHIL YPGDESLEGK VLRLKQQYTL 360 CSASLQDIIG RFESRAGESL NWEDFPSKVA VQMNDTHPTL CIPELMRILI DVKGLSWSEA 420 WSITERTVAY TNHTVLPEAL EKWSLDIMQK LLPRHVEIIE TIDEELINDI VSKYGTTDTG 480 LLKKKLKEMR ILDNVDLPAS ISQLFVKPKD KKESPAKSKQ KLLVKSLETI AEDEEKTELE 540 EEEAEVLSEI EEEKLEPEEV EAEEEGSEDE LDPFVKSDPK LPRVVRMANL CVVGGHSVNG 600 VAEIHSEIVK QDVFNSFYEM WPTKFQNKTN GVTPRRWIRF CNPELSALIS KWIGSDDWVL 660 NTDKLAELKK FADNEDLHSE WRAAKRANKM KVVSLIREKT GYIVSPDAMF DVQVKRIHEY 720 KRQLLNILGI VYRYKKMKEM SAEERAKSFV PRVCIFGGKA FATYIQAKRI VKFITDVAAT 780 VNHDSDVGDL LKVVFVPDYN VSVAEALIPA SELSQHISTA GMEASGTSNM KFAMNGCILI 840 GTLDGANVEI REEVGEENFF LFGAEAHEIA GLRKERAEGK FVPDPRFEEV KEFVRSGVFG 900 TYNYDELMGS LEGNEGYGRA DYFLVGKDFP SYIECQEKVD KAYRDQKLWT RMSILNTAGS 960 SKFSSDRTIH EYAKDIWDIS PVILP* 1020 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam00343 | Phosphorylase | 1.0e-135 | 170 | 474 | 306 | + 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 | 407 | + 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 | 91 | 474 | 388 | + 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 | 583 | 981 | 404 | + 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 |
GenBank | AAK15695.1 | 0 | 56 | 985 | 1 | 928 | AF327055_1 alpha 1,4-glucan phosphorylase L isozyme [Oryza sativa] |
GenBank | ACC59201.1 | 0 | 4 | 985 | 3 | 971 | plastid alpha-1,4-glucan phosphorylase [Triticum aestivum] |
DDBJ | BAG49328.1 | 0 | 4 | 985 | 3 | 978 | plastidial starch phosphorylase 1 [Oryza sativa Japonica Group] |
GenBank | EEC76210.1 | 0 | 4 | 985 | 3 | 964 | hypothetical protein OsI_13605 [Oryza sativa Indica Group] |
GenBank | EEE59962.1 | 0 | 4 | 985 | 3 | 977 | hypothetical protein OsJ_12655 [Oryza sativa Japonica Group] |
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 | 1qm5_B | 0 | 585 | 977 | 404 | 792 | A Chain A, Phosphorylase Recognition And Phosphorylysis Of Its Oligosaccharide Substrate: Answers To A Long Outstanding Question |
PDB | 1qm5_B | 0 | 137 | 463 | 57 | 375 | A Chain A, Phosphorylase Recognition And Phosphorylysis Of Its Oligosaccharide Substrate: Answers To A Long Outstanding Question |
PDB | 1qm5_A | 0 | 585 | 977 | 404 | 792 | A Chain A, Phosphorylase Recognition And Phosphorylysis Of Its Oligosaccharide Substrate: Answers To A Long Outstanding Question |
PDB | 1qm5_A | 0 | 137 | 463 | 57 | 375 | A Chain A, Phosphorylase Recognition And Phosphorylysis Of Its Oligosaccharide Substrate: Answers To A Long Outstanding Question |
PDB | 1e4o_B | 0 | 585 | 977 | 404 | 792 | A Chain A, Phosphorylase Recognition And Phosphorylysis Of Its Oligosaccharide Substrate: Answers To A Long Outstanding Question |
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 | 401 | 586 | 986 | 0 |
HO778303 | 401 | 586 | 986 | 0 |
HO778303 | 408 | 110 | 517 | 0 |
HO620767 | 403 | 584 | 986 | 0 |
HO613954 | 403 | 584 | 986 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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