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Basic Information | |
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Species | Sorghum bicolor |
Cazyme ID | Sb01g007560.2 |
Family | GT35 |
Protein Properties | Length: 956 Molecular Weight: 106839 Isoelectric Point: 5.1636 |
Chromosome | Chromosome/Scaffold: 1 Start: 6509017 End: 6515206 |
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 | 140 | 492 | 0 |
ALKQLGQNLEDVASQEPDAALGNGGLGRLASCFLDSLATLNYPAWGYGLRYKYGLFKQIITKDGQEEIAENWLEMGYPWEVVRNDVSYPVKFYGKVVEGT DGRKHWIGGENIKAVAHDVPIPGYKTRTTNNLRLWSTTVPAQDFDLAAFNSGDHTKAYEAHLNAEKICHILYPGDESLEGKVLRLKQQYTLCSASLQDII GRFESRAGESLNWEDFPSKVAVQMNDTHPTLCIPELMRILIDVKGLSWSEAWSITERTVAYTNHTVLPEALEKWSLDIMQKLLPRHVEIIETIDEELIND IVSKYGTTDTGLLKKKLKEMRILDNVDLPASISQLFVKPKDKKESPAKSKQKL | |||
GT35 | 550 | 949 | 0 |
KLPRVVRMANLCVVGGHSVNGVAEIHSEIVKQDVFNSFYEMWPTKFQNKTNGVTPRRWIRFCNPELSALISKWIGSDDWVLNTDKLAELKKFADNEDLHS EWRAAKRANKMKVVSLIREKTGYIVSPDAMFDVQVKRIHEYKRQLLNILGIVYRYKKMKEMSAEERAKSFVPRVCIFGGKAFATYIQAKRIVKFITDVAA TVNHDSDVGDLLKVVFVPDYNVSVAEALIPASELSQHISTAGMEASGTSNMKFAMNGCILIGTLDGANVEIREEVGEENFFLFGAEAHEIAGLRKERAEG KFVPDPRFEEVKEFVRSGVFGTYNYDELMGSLEGNEGYGRADYFLVGKDFPSYIECQEKVDKAYRDQKLWTRMSILNTAGSSKFSSDRTIHEYAKDIWDI |
Full Sequence |
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Protein Sequence Length: 956 Download |
MATTASPPLQ LATASRPHAS ASGGGGVGGV LLAGGCGGGV VPGRGRGRMQ RRVSARSVAS 60 DRDVQGPVSP AEEHFSPLKA YHATAKSVLD ALLINWNATY DYYNKMNVKQ AYYLSMEFLQ 120 GRALTNAIGN LEITGEYAEA LKQLGQNLED VASQEPDAAL GNGGLGRLAS CFLDSLATLN 180 YPAWGYGLRY KYGLFKQIIT KDGQEEIAEN WLEMGYPWEV VRNDVSYPVK FYGKVVEGTD 240 GRKHWIGGEN IKAVAHDVPI PGYKTRTTNN LRLWSTTVPA QDFDLAAFNS GDHTKAYEAH 300 LNAEKICHIL YPGDESLEGK VLRLKQQYTL CSASLQDIIG RFESRAGESL NWEDFPSKVA 360 VQMNDTHPTL CIPELMRILI DVKGLSWSEA WSITERTVAY TNHTVLPEAL EKWSLDIMQK 420 LLPRHVEIIE TIDEELINDI VSKYGTTDTG LLKKKLKEMR ILDNVDLPAS ISQLFVKPKD 480 KKESPAKSKQ KLLVKSLETI AEDEEKTELE EEEAEVLSEI EEEKLEPEEV EAEEEGSEDE 540 LDPFVKSDPK LPRVVRMANL CVVGGHSVNG VAEIHSEIVK QDVFNSFYEM WPTKFQNKTN 600 GVTPRRWIRF CNPELSALIS KWIGSDDWVL NTDKLAELKK FADNEDLHSE WRAAKRANKM 660 KVVSLIREKT GYIVSPDAMF DVQVKRIHEY KRQLLNILGI VYRYKKMKEM SAEERAKSFV 720 PRVCIFGGKA FATYIQAKRI VKFITDVAAT VNHDSDVGDL LKVVFVPDYN VSVAEALIPA 780 SELSQHISTA GMEASGTSNM KFAMNGCILI GTLDGANVEI REEVGEENFF LFGAEAHEIA 840 GLRKERAEGK FVPDPRFEEV KEFVRSGVFG TYNYDELMGS LEGNEGYGRA DYFLVGKDFP 900 SYIECQEKVD KAYRDQKLWT RMSILNTAGS SKFSSDRTIH EYAKDIWDIS PVILP* 960 |
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 | 140 | 444 | 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 | 552 | 949 | 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 | 73 | 444 | 376 | + 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 | 553 | 951 | 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 | 553 | 949 | 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 | 955 | 1 | 928 | AF327055_1 alpha 1,4-glucan phosphorylase L isozyme [Oryza sativa] |
GenBank | ACC59201.1 | 0 | 4 | 955 | 3 | 971 | plastid alpha-1,4-glucan phosphorylase [Triticum aestivum] |
GenBank | ACF94692.1 | 0 | 106 | 955 | 1 | 849 | starch phosphorylase 1 precursor [Zea mays] |
DDBJ | BAG49328.1 | 0 | 4 | 955 | 3 | 978 | plastidial starch phosphorylase 1 [Oryza sativa Japonica Group] |
GenBank | EEC76210.1 | 0 | 4 | 955 | 3 | 964 | hypothetical protein OsI_13605 [Oryza sativa Indica 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 | 555 | 947 | 404 | 792 | A Chain A, Phosphorylase Recognition And Phosphorylysis Of Its Oligosaccharide Substrate: Answers To A Long Outstanding Question |
PDB | 1qm5_B | 0 | 107 | 433 | 57 | 375 | A Chain A, Phosphorylase Recognition And Phosphorylysis Of Its Oligosaccharide Substrate: Answers To A Long Outstanding Question |
PDB | 1qm5_A | 0 | 555 | 947 | 404 | 792 | A Chain A, Phosphorylase Recognition And Phosphorylysis Of Its Oligosaccharide Substrate: Answers To A Long Outstanding Question |
PDB | 1qm5_A | 0 | 107 | 433 | 57 | 375 | A Chain A, Phosphorylase Recognition And Phosphorylysis Of Its Oligosaccharide Substrate: Answers To A Long Outstanding Question |
PDB | 1e4o_B | 0 | 555 | 947 | 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 | 556 | 956 | 0 |
HO778303 | 401 | 556 | 956 | 0 |
HO778303 | 408 | 80 | 487 | 0 |
HO620767 | 403 | 554 | 956 | 0 |
HO613954 | 403 | 554 | 956 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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