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Basic Information | |
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Species | Cucumis sativus |
Cazyme ID | Cucsa.273090.1 |
Family | GT35 |
Protein Properties | Length: 965 Molecular Weight: 108937 Isoelectric Point: 5.6611 |
Chromosome | Chromosome/Scaffold: 02511 Start: 81268 End: 88325 |
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 | 171 | 959 | 0 |
ALSKLGYELENVASQEPDAALGNGGLGRLASCFLDSLATLNYPAWGYGLRYKYGLFKQKITKDGQEEVAENWLEIGNPWEIVRNDIKYHIKFYGKVVIGS DGKKNWTGGEDIEAVAHDVPIPGYKTKNTINLRLWSTKAPTEDFDLAAFNAGEHSRASEALASAEKICHVLYPGDDSIEGKILRLKQQYTLCSASLQDIV ERFVRRSGANIKWEEFPEKVAVQMNDTHPTLCIPELMRILLDLKGLSWEEAWNVTQRTVAYTNHTVLPEALEKWNFELMQRLLPRHVEIIELIDEELIRT IISEYGTADLKLLREKLKELRILENVDLPAAYSDLFIEPEESSTIASTEVLKRSKEADSVDKDEFVEVDDELESKGIQDKKVEPTPPPPPPKMVRMANLS VVGGHAVNGVAEIHSEIVKDEVFNAFYKLWPGKFQNKTNGVTPRRWILFCNPDLSKLITNWIGSEDWVLNTEKLGGLKKFADDEDLQNQWRIAKRNNKLK AVSFLKEKTGYTVSPDAMFDIQVKRIHEYKRQLLNILGIVYRYKKMKEMSAKERKETYVPRVCIFGGKAFATYVQAKRIVKFITDVGATVNHDPEIGDLL KVIFVPDYNVSVAELLIPASELSQHISTAGMEASGTSNMKFAMNGCILIGTLDGANVEIRQEVGADNFFLFGAEAHEIAGLRKERAEGKFIPDPRFEEVK EYVRSGVFGSCDYEELIASLEGNEGFGRADYFLVGKDFPSYIECQEKVDEAYRDQKKWTRMSILNTAGSYKFSSDRTIHEYAKDIWSIK |
Full Sequence |
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Protein Sequence Length: 965 Download |
MAATSQFTLA LNPPHSFSHS YSFPSLIGLS SRYRQSKFLL LSTSSWRSPK RTFLVRNVSS 60 EPKLKDPVAD KESPTAATAF APDASSIASS IKYHAEFTPL FSPDRFDLPK AFFATAQSVR 120 DALIINWNET FELYERLNVK QAYYLSMEFL QGRALLNAIG NLELTGPYAE ALSKLGYELE 180 NVASQEPDAA LGNGGLGRLA SCFLDSLATL NYPAWGYGLR YKYGLFKQKI TKDGQEEVAE 240 NWLEIGNPWE IVRNDIKYHI KFYGKVVIGS DGKKNWTGGE DIEAVAHDVP IPGYKTKNTI 300 NLRLWSTKAP TEDFDLAAFN AGEHSRASEA LASAEKICHV LYPGDDSIEG KILRLKQQYT 360 LCSASLQDIV ERFVRRSGAN IKWEEFPEKV AVQMNDTHPT LCIPELMRIL LDLKGLSWEE 420 AWNVTQRTVA YTNHTVLPEA LEKWNFELMQ RLLPRHVEII ELIDEELIRT IISEYGTADL 480 KLLREKLKEL RILENVDLPA AYSDLFIEPE ESSTIASTEV LKRSKEADSV DKDEFVEVDD 540 ELESKGIQDK KVEPTPPPPP PKMVRMANLS VVGGHAVNGV AEIHSEIVKD EVFNAFYKLW 600 PGKFQNKTNG VTPRRWILFC NPDLSKLITN WIGSEDWVLN TEKLGGLKKF ADDEDLQNQW 660 RIAKRNNKLK AVSFLKEKTG YTVSPDAMFD IQVKRIHEYK RQLLNILGIV YRYKKMKEMS 720 AKERKETYVP RVCIFGGKAF ATYVQAKRIV KFITDVGATV NHDPEIGDLL KVIFVPDYNV 780 SVAELLIPAS ELSQHISTAG MEASGTSNMK FAMNGCILIG TLDGANVEIR QEVGADNFFL 840 FGAEAHEIAG LRKERAEGKF IPDPRFEEVK EYVRSGVFGS CDYEELIASL EGNEGFGRAD 900 YFLVGKDFPS YIECQEKVDE AYRDQKKWTR MSILNTAGSY KFSSDRTIHE YAKDIWSIKP 960 VELP* 1020 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam00343 | Phosphorylase | 2.0e-126 | 171 | 456 | 286 | + 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 | 1.0e-174 | 88 | 456 | 373 | + 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 | 562 | 958 | 402 | + 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 | 562 | 960 | 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 | 562 | 958 | 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 |
DDBJ | BAG31925.1 | 0 | 1 | 964 | 1 | 971 | alpha-1,4-glucan phosphorylase L isozyme [Cucurbita maxima] |
EMBL | CBI22291.1 | 0 | 14 | 964 | 13 | 982 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002279075.1 | 0 | 14 | 964 | 13 | 958 | PREDICTED: similar to Alpha-1,4 glucan phosphorylase L-1 isozyme, chloroplastic/amyloplastic [Vitis vinifera] |
RefSeq | XP_002305367.1 | 0 | 55 | 964 | 16 | 949 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002526085.1 | 0 | 30 | 964 | 31 | 977 | 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 | 3l7d_A | 0 | 64 | 960 | 5 | 830 | A Chain A, Crystal Structure Of Chondroitin Polymerase From Escherichia Coli Strain K4 (K4cp) Complexed With Udp-Glcua And Udp |
PDB | 3l7c_A | 0 | 64 | 960 | 5 | 830 | A Chain A, Crystal Structure Of Chondroitin Polymerase From Escherichia Coli Strain K4 (K4cp) Complexed With Udp-Glcua And Udp |
PDB | 3l7b_A | 0 | 64 | 960 | 5 | 830 | A Chain A, Crystal Structure Of Chondroitin Polymerase From Escherichia Coli Strain K4 (K4cp) Complexed With Udp-Glcua And Udp |
PDB | 3l7a_A | 0 | 64 | 960 | 5 | 830 | A Chain A, Crystal Structure Of Chondroitin Polymerase From Escherichia Coli Strain K4 (K4cp) Complexed With Udp-Glcua And Udp |
PDB | 3l79_A | 0 | 64 | 960 | 5 | 830 | A Chain A, Crystal Structure Of Chondroitin Polymerase From Escherichia Coli Strain K4 (K4cp) Complexed With Udp-Glcua And Udp |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO778303 | 864 | 111 | 965 | 0 |
HO797178 | 401 | 565 | 965 | 0 |
HO620767 | 403 | 563 | 965 | 0 |
HO613954 | 403 | 563 | 965 | 0 |
HO778303 | 51 | 64 | 113 | 0.0000000002 |
Sequence Alignments (This image is cropped. Click for full image.) |
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