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Basic Information | |
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Species | Picea abies |
Cazyme ID | MA_14581g0010 |
Family | GT35 |
Protein Properties | Length: 961 Molecular Weight: 109293 Isoelectric Point: 7.2436 |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GT35 | 154 | 956 | 0 |
ALSKLGSNLESVAEQEPDAALGNGGLGRLASCFLDSLATLDYPAWGYGLRYKYGLFHQNITKDGQQEVAENWLEMGNPWEIARHDVSYPIKFFGKVESRP DGTKRWVGGEDVKAIAYDVPIPGYKTKTTLNLRLWSTEVQAEDFDLQAFTAGEHNKAMEAQINAAKICYVLYPGDDSTEGKVLRLKQQYTLCSASLQDII SRFKGRSGHSLNWDEFPEKVAIQMNDTHPTLSVPELMRTLIDVEGLPWEKAWNITQRTVAYTNHTVLPEALEKWPFEVMQKLLPRHMEIIRTIDEEFIKE VIAKSNTMDLKELENKIRGMRILENDDFPESVVPVFSDLWKEEEAAKEAKVKAAKEAEAKAKAAKEAKAKAAKEVEASKEAVKDKSEAVEPEPKAQVKSQ DKKESKSNSNDTVFKPAKLVRMANICVIAGHSVNGVAEIHSEIVKKEVFSDFYEMWPEKFQNKTNGVTPRRWIRFCNPELSKVITKWLGTEDWVLKTELL AELRKFADNVDLQEEWRAAKRANKLKLVSYIREKTGYIISPDAMFDVQVKRIHEYKRQLLNILGVIYRYKKMKAKRIVKLITDVGVTINHDTEIGDLLKI VFIPDYNVSVAETLIPASELSQHISTAGMEASGTSNMKFSMNGCVLIGTLDGANVEIREEVGEENFFLFGARAHEIAGLRKERAEGKFKPDPRFEEAKDY IKSGVFGKYNYRPLLDSLEGNEGYKTERGVKRSLEGNEGYGRGDYFLVGKDFPAYVECQERVDAAYGDQEKWTRMSILNTAGSYKFSSDRTIHEYAKDIW GVK |
Full Sequence |
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Protein Sequence Length: 961 Download |
MRFSFTLSAT EDPFLIDRVL LERSSGRGWE NFFALAVRVH SCPFAVSPAN RKQNIPSAKK 60 FLLLLSLRRP ILRLLHRTLN IMQSSRLVSR LPQAYVATAE SVRDSLIRRW NEITEYYDEI 120 NPKQTYYLSM EFLQGRALLN AIGNLELTDA YAEALSKLGS NLESVAEQEP DAALGNGGLG 180 RLASCFLDSL ATLDYPAWGY GLRYKYGLFH QNITKDGQQE VAENWLEMGN PWEIARHDVS 240 YPIKFFGKVE SRPDGTKRWV GGEDVKAIAY DVPIPGYKTK TTLNLRLWST EVQAEDFDLQ 300 AFTAGEHNKA MEAQINAAKI CYVLYPGDDS TEGKVLRLKQ QYTLCSASLQ DIISRFKGRS 360 GHSLNWDEFP EKVAIQMNDT HPTLSVPELM RTLIDVEGLP WEKAWNITQR TVAYTNHTVL 420 PEALEKWPFE VMQKLLPRHM EIIRTIDEEF IKEVIAKSNT MDLKELENKI RGMRILENDD 480 FPESVVPVFS DLWKEEEAAK EAKVKAAKEA EAKAKAAKEA KAKAAKEVEA SKEAVKDKSE 540 AVEPEPKAQV KSQDKKESKS NSNDTVFKPA KLVRMANICV IAGHSVNGVA EIHSEIVKKE 600 VFSDFYEMWP EKFQNKTNGV TPRRWIRFCN PELSKVITKW LGTEDWVLKT ELLAELRKFA 660 DNVDLQEEWR AAKRANKLKL VSYIREKTGY IISPDAMFDV QVKRIHEYKR QLLNILGVIY 720 RYKKMKAKRI VKLITDVGVT INHDTEIGDL LKIVFIPDYN VSVAETLIPA SELSQHISTA 780 GMEASGTSNM KFSMNGCVLI GTLDGANVEI REEVGEENFF LFGARAHEIA GLRKERAEGK 840 FKPDPRFEEA KDYIKSGVFG KYNYRPLLDS LEGNEGYKTE RGVKRSLEGN EGYGRGDYFL 900 VGKDFPAYVE CQERVDAAYG DQEKWTRMSI LNTAGSYKFS SDRTIHEYAK DIWGVKQVKL 960 P 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-138 | 154 | 480 | 327 | + 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 | 569 | 955 | 416 | + 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 | 93 | 480 | 392 | + 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 | 571 | 956 | 415 | + 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 | 571 | 955 | 414 | + 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]. |
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 | CAA36612.1 | 0 | 91 | 960 | 100 | 965 | unnamed protein product [Solanum tuberosum] |
EMBL | CBI22291.1 | 0 | 91 | 961 | 114 | 982 | unnamed protein product [Vitis vinifera] |
Swiss-Prot | P04045 | 0 | 91 | 960 | 100 | 965 | PHSL1_SOLTU RecName: Full=Alpha-1,4 glucan phosphorylase L-1 isozyme, chloroplastic/amyloplastic; AltName: Full=Starch phosphorylase L-1; Flags: Precursor |
Swiss-Prot | P27598 | 0 | 91 | 961 | 93 | 955 | PHSL_IPOBA RecName: Full=Alpha-1,4 glucan phosphorylase L isozyme, chloroplastic/amyloplastic; AltName: Full=Starch phosphorylase L; Flags: Precursor |
RefSeq | XP_002279075.1 | 0 | 91 | 961 | 114 | 958 | PREDICTED: similar to Alpha-1,4 glucan phosphorylase L-1 isozyme, chloroplastic/amyloplastic [Vitis vinifera] |
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 | 2ffr_A | 0 | 67 | 956 | 16 | 817 | A Chain A, Crystallographic Studies On N-Azido-Beta-D-Glucopyranosylamine, An Inhibitor Of Glycogen Phosphorylase: Comparison With N-Acetyl-Beta-D- Glucopyranosylam |
PDB | 4el5_A | 0 | 67 | 956 | 16 | 817 | A Chain A, Crystallographic Studies On N-Azido-Beta-D-Glucopyranosylamine, An Inhibitor Of Glycogen Phosphorylase: Comparison With N-Acetyl-Beta-D- Glucopyranosylam |
PDB | 4el0_A | 0 | 67 | 956 | 16 | 817 | A Chain A, Crystallographic Studies On N-Azido-Beta-D-Glucopyranosylamine, An Inhibitor Of Glycogen Phosphorylase: Comparison With N-Acetyl-Beta-D- Glucopyranosylam |
PDB | 4eky_A | 0 | 67 | 956 | 16 | 817 | A Chain A, Crystallographic Studies On N-Azido-Beta-D-Glucopyranosylamine, An Inhibitor Of Glycogen Phosphorylase: Comparison With N-Acetyl-Beta-D- Glucopyranosylam |
PDB | 4eke_A | 0 | 67 | 956 | 16 | 817 | A Chain A, Crystallographic Studies On N-Azido-Beta-D-Glucopyranosylamine, An Inhibitor Of Glycogen Phosphorylase: Comparison With N-Acetyl-Beta-D- Glucopyranosylam |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO797178 | 416 | 574 | 961 | 0 |
HO778303 | 416 | 574 | 961 | 0 |
HO778303 | 396 | 94 | 489 | 0 |
HO613954 | 418 | 572 | 961 | 0 |
HO613954 | 58 | 431 | 488 | 0.000001 |
Sequence Alignments (This image is cropped. Click for full image.) |
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