y
Basic Information | |
---|---|
Species | Gossypium raimondii |
Cazyme ID | Gorai.013G260900.2 |
Family | GT35 |
Protein Properties | Length: 838 Molecular Weight: 95287.4 Isoelectric Point: 6.4792 |
Chromosome | Chromosome/Scaffold: 13 Start: 57536513 End: 57542743 |
Description | alpha-glucan phosphorylase 2 |
View CDS |
External Links |
---|
NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
---|---|---|---|
Family | Start | End | Evalue |
GT35 | 110 | 832 | 0 |
ALNKLGHELEEIAEQEKDAALGNGGLGRLASCFLDSMATLNLPAWGYGLRYKYGLFKQLITKQGQEEIAEDWLEKFSPWEVVRHDIVFPVRFFGSIEINP DGSRKWVGGEVVQALAYDVPIPGYKTKNTISLRLWEAKGRAEDFNLFQFNDGQYESAAQLHSRAQQICAVLYPGDATEDGKLLRLKQQFFLCSASLQDII LRFKERRSGKGSWKWSEFPSKVAVQLNDTHPTLAIPELMRLLMDDERLGWDEAWDVTTRTIAYTNHTVLPEALEKWSQPVMWKLLPRHMEIIEEIDKRFL AMINATRPDLEHKLPTMRVLDHNPQKPVVRMANLCVVSAHTVNGVAQLHSDILKAELFADYVSIWPTKFQNKTNGITPRRWLRFCSPELSNIITKWLKTD QWVTNLDLLSGLREFADNADFQDEWASAKMANKQRLAQYILRVTGVSIDPNSLFDIQVKRIHEYKRQLLNILGAIYRYKKLKEMSPELRKNTTSRTIMIG GKAFATYTNAKRIVKLVNDVGAVVNNDPEVNSYLKVVFVPNYNVSVAEMLIPGSELSQHISTAGMEASGTSNMKFALNGCLIIGTLDGANVEIREEIGEE NFFLFGARADEVPQLRKDRENGLFKPDPRFEEAKQFIRSGAFGSYDYNPLLDSLEGNSGYGRGDYFLVGHDFPDYMDAQARVDEAYKDRKKWLKMSILST AGSGKFSSDRTIAQYAKEIWNIE |
Full Sequence |
---|
Protein Sequence Length: 838 Download |
MAENGKSATE KVPAVANPLS EQPSEIASNI NYHAQFSPHF SPFKFEPEQA FFATAESVRD 60 RLVKQWNETF LHYHKVDPKQ TYYLSMEYLQ GRALTNAIGN LDIQNAYAEA LNKLGHELEE 120 IAEQEKDAAL GNGGLGRLAS CFLDSMATLN LPAWGYGLRY KYGLFKQLIT KQGQEEIAED 180 WLEKFSPWEV VRHDIVFPVR FFGSIEINPD GSRKWVGGEV VQALAYDVPI PGYKTKNTIS 240 LRLWEAKGRA EDFNLFQFND GQYESAAQLH SRAQQICAVL YPGDATEDGK LLRLKQQFFL 300 CSASLQDIIL RFKERRSGKG SWKWSEFPSK VAVQLNDTHP TLAIPELMRL LMDDERLGWD 360 EAWDVTTRTI AYTNHTVLPE ALEKWSQPVM WKLLPRHMEI IEEIDKRFLA MINATRPDLE 420 HKLPTMRVLD HNPQKPVVRM ANLCVVSAHT VNGVAQLHSD ILKAELFADY VSIWPTKFQN 480 KTNGITPRRW LRFCSPELSN IITKWLKTDQ WVTNLDLLSG LREFADNADF QDEWASAKMA 540 NKQRLAQYIL RVTGVSIDPN SLFDIQVKRI HEYKRQLLNI LGAIYRYKKL KEMSPELRKN 600 TTSRTIMIGG KAFATYTNAK RIVKLVNDVG AVVNNDPEVN SYLKVVFVPN YNVSVAEMLI 660 PGSELSQHIS TAGMEASGTS NMKFALNGCL IIGTLDGANV EIREEIGEEN FFLFGARADE 720 VPQLRKDREN GLFKPDPRFE EAKQFIRSGA FGSYDYNPLL DSLEGNSGYG RGDYFLVGHD 780 FPDYMDAQAR VDEAYKDRKK WLKMSILSTA GSGKFSSDRT IAQYAKEIWN IEECQVP* 840 |
Functional Domains Download unfiltered results here | ||||||||
---|---|---|---|---|---|---|---|---|
Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd04300 | GT1_Glycogen_Phosphorylase | 0 | 27 | 831 | 813 | + 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 | 30 | 831 | 810 | + 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 | 110 | 833 | 729 | + 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. | ||
PRK14985 | PRK14985 | 0 | 83 | 829 | 753 | + maltodextrin phosphorylase; Provisional | ||
COG0058 | GlgP | 0 | 20 | 832 | 819 | + Glucan phosphorylase [Carbohydrate transport and metabolism] |
Gene Ontology | |
---|---|
GO Term | Description |
GO:0004645 | phosphorylase activity |
GO:0005975 | carbohydrate metabolic process |
Annotations - NR Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
GenBank | AAM29154.1 | 0 | 2 | 836 | 8 | 839 | starch phosphorylase type H [Citrus hybrid cultivar] |
DDBJ | BAG31926.1 | 0 | 7 | 837 | 13 | 843 | alpha-1,4-glucan phosphorylase H isozyme [Cucurbita maxima] |
RefSeq | XP_002280732.1 | 0 | 2 | 837 | 6 | 843 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002313399.1 | 0 | 8 | 837 | 24 | 853 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002520435.1 | 0 | 9 | 837 | 21 | 849 | glycogen phosphorylase, putative [Ricinus communis] |
Annotations - PDB Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 1z8d_A | 0 | 21 | 832 | 23 | 829 | A Chain A, Crystal Structure Of Human Muscle Glycogen Phosphorylase A With Amp And Glucose |
PDB | 2ffr_A | 0 | 21 | 832 | 11 | 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 | 21 | 832 | 11 | 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 | 21 | 832 | 11 | 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 | 21 | 832 | 11 | 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 | ||||
---|---|---|---|---|
Hit | Length | Start | End | EValue |
HO782200 | 412 | 166 | 577 | 0 |
HO418036 | 539 | 236 | 753 | 0 |
HO586252 | 552 | 284 | 834 | 0 |
CO082104 | 295 | 314 | 608 | 0 |
HO613954 | 499 | 389 | 838 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
---|