y
Basic Information | |
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Species | Mimulus guttatus |
Cazyme ID | mgv1a000698m |
Family | GT35 |
Protein Properties | Length: 1015 Molecular Weight: 115082 Isoelectric Point: 6.6255 |
Chromosome | Chromosome/Scaffold: 4 Start: 3247379 End: 3257211 |
Description | Glycosyl transferase, family 35 |
View CDS |
External Links |
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CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GT35 | 297 | 1007 | 0 |
ALAQLGFEFEVLAEQEGDAALGNGGLARLSACQMDSLATLDYPAMGYGLRYQYGLFRQIIVDGYQHEQPDFWLNFGNPWEIERVQVSYSVKFYGTVEEKA SNGVKYHVWVPGETVEAVAYDNPIPGYGTRNAINLRLWAAKPSGQYDLESYNTGDYINAVVNRQKAEIISNVLYPDDRSYQGKELRLKQQYFFVSASTQD IIRRFKDDHDNFDEFPDKVAFQINETQPSLAIVEVMRVLIDEERLAWKRAWEIVCKLFSFTSHSVNPEGLEKIPVDLLGSLLPRHLQIIYDINHNFMEEL KKKIGQDYRRLDQMSIVAEGTVKTIRMANLSIICSHTVNGVSRLHYELLKTRVFKEFYDLWPQKFQYKTNGVTQRRWIVVSNPSLCSLISKWLGTEEWIR NVDLLVGLREHASNPVLQQEWRMVKKINKIRLAEYIETLTGVEVSLDAMFDVQVKRIHEYKRQLLNILGIIHRYYCIKNMNESDRKKVVPRVCIIGGKAA PGYEIAKKIIKLCHAVAEKVNNDADVGDLLKLIFIPDYNVSVAEMVIPGSDLSQHISTAGHEASGTSSMKFLMNGCLLLATADGSTVEIAEEVGSENMFL FGAKVHEVPQLREKATSEVPIQFVRVVRMVRDGYFGFKDYFKSLCDTVEDGKDFYLLGSDFSSYLEAQAMADREFVNEEKWTRMSILSTAGSGRFSSDRT MDEYSKLSWGI |
Full Sequence |
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Protein Sequence Length: 1015 Download |
MSAISASRFS FAVGSSRPAA SSTRSTPDLH LPFATSLNLQ TNRFNPGLRS LNFFSNPPQA 60 STANGNVDIS AEGSSAAVTF LNDDAADATV FIIQARNRLG LLQVITRVFK VLGLTIERAT 120 IEFEADFFIK KFYVTNSEGK RIENPENLER IQHALIEAID GGDDTRGQVQ AGGRGVVVKK 180 LGLGLESSGQ SRGKAERMFR LMDEFLKNDP MSLQKDIIHH VEFTVARSRF SFDDFEAYQA 240 LSHSVRDRLI ERWHDTHQHF KKKDPKRLYF LSLEFLMGRS LSNSVINLGI RDEYADALAQ 300 LGFEFEVLAE QEGDAALGNG GLARLSACQM DSLATLDYPA MGYGLRYQYG LFRQIIVDGY 360 QHEQPDFWLN FGNPWEIERV QVSYSVKFYG TVEEKASNGV KYHVWVPGET VEAVAYDNPI 420 PGYGTRNAIN LRLWAAKPSG QYDLESYNTG DYINAVVNRQ KAEIISNVLY PDDRSYQGKE 480 LRLKQQYFFV SASTQDIIRR FKDDHDNFDE FPDKVAFQIN ETQPSLAIVE VMRVLIDEER 540 LAWKRAWEIV CKLFSFTSHS VNPEGLEKIP VDLLGSLLPR HLQIIYDINH NFMEELKKKI 600 GQDYRRLDQM SIVAEGTVKT IRMANLSIIC SHTVNGVSRL HYELLKTRVF KEFYDLWPQK 660 FQYKTNGVTQ RRWIVVSNPS LCSLISKWLG TEEWIRNVDL LVGLREHASN PVLQQEWRMV 720 KKINKIRLAE YIETLTGVEV SLDAMFDVQV KRIHEYKRQL LNILGIIHRY YCIKNMNESD 780 RKKVVPRVCI IGGKAAPGYE IAKKIIKLCH AVAEKVNNDA DVGDLLKLIF IPDYNVSVAE 840 MVIPGSDLSQ HISTAGHEAS GTSSMKFLMN GCLLLATADG STVEIAEEVG SENMFLFGAK 900 VHEVPQLREK ATSEVPIQFV RVVRMVRDGY FGFKDYFKSL CDTVEDGKDF YLLGSDFSSY 960 LEAQAMADRE FVNEEKWTRM SILSTAGSGR FSSDRTMDEY SKLSWGIQPC KCPF* 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 | 0 | 214 | 1007 | 801 | + 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 | 217 | 1007 | 798 | + 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]. | ||
pfam00343 | Phosphorylase | 0 | 297 | 1009 | 720 | + 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. | ||
PRK14986 | PRK14986 | 0 | 212 | 1011 | 807 | + glycogen phosphorylase; Provisional | ||
COG0058 | GlgP | 0 | 205 | 1009 | 819 | + Glucan phosphorylase [Carbohydrate transport and metabolism] |
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 | CBI30609.1 | 0 | 202 | 1013 | 1 | 813 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_001757919.1 | 0 | 202 | 1011 | 1 | 811 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_002273615.1 | 0 | 198 | 1013 | 1 | 817 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002305114.1 | 0 | 198 | 1014 | 1 | 818 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002509431.1 | 0 | 18 | 1014 | 7 | 949 | 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 | 1ygp_B | 0 | 208 | 1010 | 39 | 878 | A Chain A, Phosphorylated Form Of Yeast Glycogen Phosphorylase With Phosphate Bound In The Active Site. |
PDB | 1ygp_A | 0 | 208 | 1010 | 39 | 878 | A Chain A, Phosphorylated Form Of Yeast Glycogen Phosphorylase With Phosphate Bound In The Active Site. |
PDB | 1abb_D | 0 | 213 | 1011 | 18 | 822 | A Chain A, Control Of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies On R-State Glycogen Phosphorylase Reconstituted With Pyridoxal 5'-Diphosphate |
PDB | 1abb_C | 0 | 213 | 1011 | 18 | 822 | A Chain A, Control Of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies On R-State Glycogen Phosphorylase Reconstituted With Pyridoxal 5'-Diphosphate |
PDB | 1abb_B | 0 | 213 | 1011 | 18 | 822 | A Chain A, Control Of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies On R-State Glycogen Phosphorylase Reconstituted With Pyridoxal 5'-Diphosphate |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO779924 | 618 | 109 | 722 | 0 |
HO586252 | 541 | 473 | 1010 | 0 |
HO417459 | 293 | 624 | 916 | 0 |
HO417459 | 212 | 425 | 630 | 0 |
HO779924 | 54 | 55 | 108 | 0.0007 |
Sequence Alignments (This image is cropped. Click for full image.) |
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