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Basic Information | |
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Species | Physcomitrella patens |
Cazyme ID | Pp1s30_182V6.1 |
Family | GT35 |
Protein Properties | Length: 1027 Molecular Weight: 117003 Isoelectric Point: 6.3218 |
Chromosome | Chromosome/Scaffold: 30 Start: 1219128 End: 1227144 |
Description | alpha-glucan phosphorylase 2 |
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 | 309 | 1021 | 0 |
ALSELGYDLEVIVEQERDAALGNGGLGRLAACFMDSLATMNYSAWGYGLRYQYGLFRQQLQDGYQHEQPDYWLNFGNPWEIERVHVTYPVKFFGKVEEDW VDGRKLIKWVPDELVEAVAYDNPIPGYKTSNTINLRLWAAKPSGEFDLQSFNTGDYVNAILSKQRAETISSVLYPDDRTYQGKELRLKQQYFFVSATLQD IIRRFKDNHSSFDDFPEKVAIQLNDTHPTIGVPEMMRLLVDVESLEWGKAWDITTRVFSVTIHSVLPEMLEKWPIELIQALLPRHIQIIYKINTIFLEEV KSKFGNDYDRLARMSIVDDGEKKVIKMASLALVASHTVNGVAWSHTELLKGSVFKDFYDLWPHKFRNKTNGVTQRRWLAFSNPGLREVLTKWLGTESWIT NLELLTGLRQYASDTTLHKEWNLVRRHNKARLALYIEAISGVKVSIDAMFDVQVKRIHEYKRQLLNVLSIIHRYDCIKNMTPEEKKKVVPRVCIIGGKAA PGYEIAKKIIKLVTTIGERINDDSDIGNLLKVIFIPDYNVSLAELVIPASDLSQHISTVGNEASGTSNMKFAMNGCLLLAARGGSNDEIQQEIGDENIFM FGAKADELGRLRAERRNFIPPRDFHRVTGMIRSGEFGHKEYFQELCDTVDGGDDFYLVGNDFASYLEAQARVDKTFVDRARWTQMSIMSTAGSGKFSSDR TIQEYAQDIWGIQ |
Full Sequence |
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Protein Sequence Length: 1027 Download |
MANALCQRSA SNSLLPIFTI TKPLTSPSYF PQLACRATLE SFSSAYTQRA LENDLTNSFC 60 SLKLQRRSPH LYGRDSVTTI HAQSVSAEAI DEASEDSIKI IVDTSTDQKA TTIEIVAPNW 120 PGLLASITDK FKALELQVAK ASVDLKDGNV FYKFSIQDQD GNAIVDAEYL GNVEKVLRRV 180 LNPALWSDLG KNVNLSPNVG DPETQRRRRL LWLMDQYLKN DVPSIQKSIV DHVEYTIARS 240 RFKFDDFEAY KATANSVRDR LLESWNDNQQ YYRDNDSKRV YYLSMEFLMG RSLLNSIFNL 300 GIKGEYAQAL SELGYDLEVI VEQERDAALG NGGLGRLAAC FMDSLATMNY SAWGYGLRYQ 360 YGLFRQQLQD GYQHEQPDYW LNFGNPWEIE RVHVTYPVKF FGKVEEDWVD GRKLIKWVPD 420 ELVEAVAYDN PIPGYKTSNT INLRLWAAKP SGEFDLQSFN TGDYVNAILS KQRAETISSV 480 LYPDDRTYQG KELRLKQQYF FVSATLQDII RRFKDNHSSF DDFPEKVAIQ LNDTHPTIGV 540 PEMMRLLVDV ESLEWGKAWD ITTRVFSVTI HSVLPEMLEK WPIELIQALL PRHIQIIYKI 600 NTIFLEEVKS KFGNDYDRLA RMSIVDDGEK KVIKMASLAL VASHTVNGVA WSHTELLKGS 660 VFKDFYDLWP HKFRNKTNGV TQRRWLAFSN PGLREVLTKW LGTESWITNL ELLTGLRQYA 720 SDTTLHKEWN LVRRHNKARL ALYIEAISGV KVSIDAMFDV QVKRIHEYKR QLLNVLSIIH 780 RYDCIKNMTP EEKKKVVPRV CIIGGKAAPG YEIAKKIIKL VTTIGERIND DSDIGNLLKV 840 IFIPDYNVSL AELVIPASDL SQHISTVGNE ASGTSNMKFA MNGCLLLAAR GGSNDEIQQE 900 IGDENIFMFG AKADELGRLR AERRNFIPPR DFHRVTGMIR SGEFGHKEYF QELCDTVDGG 960 DDFYLVGNDF ASYLEAQARV DKTFVDRARW TQMSIMSTAG SGKFSSDRTI QEYAQDIWGI 1020 QPVERF* 1080 |
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 | 226 | 1020 | 804 | + 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 | 229 | 1020 | 801 | + 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 | 309 | 1022 | 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 | 222 | 1023 | 811 | + glycogen phosphorylase; Provisional | ||
COG0058 | GlgP | 0 | 217 | 1022 | 820 | + 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 | 214 | 1024 | 1 | 811 | unnamed protein product [Vitis vinifera] |
GenBank | EEH55145.1 | 0 | 82 | 1025 | 60 | 1009 | glycosyltransferase family 35 protein [Micromonas pusilla CCMP1545] |
RefSeq | XP_001757919.1 | 0 | 214 | 1026 | 1 | 813 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_002273615.1 | 0 | 213 | 1024 | 4 | 815 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002305114.1 | 0 | 210 | 1023 | 1 | 814 | predicted protein [Populus trichocarpa] |
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 | 209 | 1023 | 27 | 878 | A Chain A, Phosphorylated Form Of Yeast Glycogen Phosphorylase With Phosphate Bound In The Active Site. |
PDB | 1ygp_A | 0 | 209 | 1023 | 27 | 878 | A Chain A, Phosphorylated Form Of Yeast Glycogen Phosphorylase With Phosphate Bound In The Active Site. |
PDB | 3nc4_A | 0 | 221 | 1022 | 22 | 828 | A Chain A, The Binding Of Beta-D-Glucopyranosyl-Thiosemicarbazone Derivatives To Glycogen Phosphorylase: A New Class Of Inhibit |
PDB | 3t3i_A | 0 | 221 | 1022 | 23 | 829 | A Chain A, The Binding Of Beta-D-Glucopyranosyl-Thiosemicarbazone Derivatives To Glycogen Phosphorylase: A New Class Of Inhibit |
PDB | 3t3h_A | 0 | 221 | 1022 | 23 | 829 | A Chain A, The Binding Of Beta-D-Glucopyranosyl-Thiosemicarbazone Derivatives To Glycogen Phosphorylase: A New Class Of Inhibit |
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 |
HO586252 | 541 | 485 | 1023 | 0 |
HO779924 | 620 | 131 | 734 | 0 |
HO376977 | 445 | 582 | 1025 | 0 |
FC368718 | 295 | 490 | 784 | 0 |
FC427628 | 283 | 570 | 852 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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