Basic Information | |
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Species | Gossypium raimondii |
Cazyme ID | Gorai.011G147600.1 |
Family | CBM20 |
Protein Properties | Length: 1187 Molecular Weight: 130500 Isoelectric Point: 6.1961 |
Chromosome | Chromosome/Scaffold: 11 Start: 24011599 End: 24023751 |
Description | catalytics;carbohydrate kinases;phosphoglucan, water dikinases |
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 |
CBM20 | 85 | 164 | 2.4e-21 |
NICLDHQVQFGEHVVILGSTKELGSWKKQVPMNWSEDGWICDLELKGGESVEFKFVVVSKDKSVAWEGGNNRVLKLPQGG |
Full Sequence |
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Protein Sequence Length: 1187 Download |
MDSISLRSLH FQIPARKQLK FLPDAAIFSP RISFPFPFPP RINRHHKHSH SLVFAVSSTP 60 TREEEKKKKR TKVKPKSGSG KVGLNICLDH QVQFGEHVVI LGSTKELGSW KKQVPMNWSE 120 DGWICDLELK GGESVEFKFV VVSKDKSVAW EGGNNRVLKL PQGGSFGMIC HWNSTEETLE 180 LLPLSSEEYD DSVDDAGHSE STSTTDALEV EASPFVGQWQ GRPASFMRSN EHHNRELERR 240 WDTTGLEGLA LKLVEGDKSA RNWWRKLEVV RELLVGSLQS EERLEALICS AIYLKWINTG 300 QIPCFEDGGH HRPNRHAEIS RLIFRELERI SSRKDSSPQE LLVIRKIHPC LPSFKAEFTA 360 SVPLTRIRDI AHRNDIPHDL KQEIKHTIQN KLHRNAGPED LVATEAMLAR ITRDPGQYSE 420 AFVEQFKIFH LELKDFFNAG SLTEQLESIR ESLDERGIAA LVMFLECKKS LDAAEGSSSI 480 LDLIKTMRSL GALREVIVRG LESGLRNDAP DAAIAMRQKW RLCEIGLEDY SFVLLSRLLN 540 MLEAVGGANW FADNLESKNI SSWNDPLGAL IVGVHQLSLS GWKPEECAAI QNELTAWQEK 600 GLFAKEGSED GKRIWALRLK ATLDRSRRLT EEYSEVLLQL FPQKVQMLGK ALGIPENSIR 660 TYAEAEIRAG VIFQVSKLCS LLLKAVRTAL GSEGWDVLVP GVVSGTLVQV ENIVPGSLPS 720 SLEGPVILVV NKADGDEEVT AAGSNIAGVV LLQELPHLSH LGVRARQEKV IFVTCEDEEK 780 VSYIQKLEGK CVRLEASSSG VSISPSSLDD RDADSVAKNL STNGSSAVYM RGPPDLTGLS 840 PKASYSNKGS SSAGLILLAD ADAQTSGAKA AACGRLASLA AVSDKVYSDL GVPASFRVPA 900 GVVIPFGSME WALEQNKSME TFMSLREKIE TARLEDGELD NLCHQLQQLV SSVQPPQDLI 960 DSIMRVFPGN VRLIVRSSAN VEDLAGMSAA GLYESIPNVS PSNPTVFASA VSQVWASLYT 1020 RRAVLSRRAA GVSQKDATMA VLVQEMLAPD LSFVLHTLSP TDHDHNYVEA EIAPGLGETL 1080 ASGTRGTPWR LSSGKFDGLV KTVAFANFSE EMVVSGASPA DGEVIRLTVD YSKKPLTVDP 1140 VFRQQLSQRL SAVGFFLERK FGCPQDVEGC VLGKDIYVVQ TRPQPL* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
COG0574 | PpsA | 2.0e-16 | 894 | 1183 | 306 | + Phosphoenolpyruvate synthase/pyruvate phosphate dikinase [Carbohydrate transport and metabolism] | ||
TIGR01418 | PEP_synth | 2.0e-21 | 892 | 1184 | 312 | + phosphoenolpyruvate synthase. Also called pyruvate,water dikinase and PEP synthase. The member from Methanococcus jannaschii contains a large intein. This enzyme generates phosphoenolpyruvate (PEP) from pyruvate, hydrolyzing ATP to AMP and releasing inorganic phosphate in the process. The enzyme shows extensive homology to other enzymes that use PEP as substrate or product. This enzyme may provide PEP for gluconeogenesis, for PTS-type carbohydrate transport systems, or for other processes [Energy metabolism, Glycolysis/gluconeogenesis]. | ||
PRK06241 | PRK06241 | 5.0e-34 | 894 | 1183 | 299 | + phosphoenolpyruvate synthase; Validated | ||
cd05818 | CBM20_water_dikinase | 1.0e-39 | 84 | 172 | 89 | + Phosphoglucan water dikinase (also known as alpha-glucan water dikinase), N-terminal CBM20 (carbohydrate-binding module, family 20) domain. This domain is found in the chloroplast-encoded phosphoglucan water dikinase, one of two enzymes involved in the phosphorylation of plant starches. In addition to the CBM20 domain, phosphoglucan water dikinase contains a C-terminal pyruvate binding domain. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch. | ||
pfam01326 | PPDK_N | 6.0e-52 | 894 | 1184 | 294 | + Pyruvate phosphate dikinase, PEP/pyruvate binding domain. This enzyme catalyzes the reversible conversion of ATP to AMP, pyrophosphate and phosphoenolpyruvate (PEP). |
Gene Ontology | |
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GO Term | Description |
GO:0003824 | catalytic activity |
GO:0005524 | ATP binding |
GO:0005975 | carbohydrate metabolic process |
GO:0016301 | kinase activity |
GO:0016310 | phosphorylation |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
GenBank | AAU93516.1 | 0 | 41 | 1186 | 33 | 1196 | chloroplast alpha-glucan water dikinase isoform 3 [Arabidopsis thaliana] |
EMBL | CBI39424.1 | 0 | 1 | 1185 | 1 | 1148 | unnamed protein product [Vitis vinifera] |
RefSeq | NP_198009.3 | 0 | 41 | 1186 | 33 | 1196 | ATGWD3; carbohydrate kinase/ catalytic/ phosphoglucan, water dikinase [Arabidopsis thaliana] |
RefSeq | XP_002265211.1 | 0 | 1 | 1185 | 1 | 1187 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002518612.1 | 0 | 5 | 1185 | 3 | 1174 | chloroplast alpha-glucan water dikinase, 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 | 1kum_A | 0.0000002 | 82 | 163 | 7 | 95 | A Chain A, The Crystal Structure Of The Phosphoenolpyruvate Synthase From Neisseria Meningitidis |
PDB | 1kul_A | 0.0000002 | 82 | 163 | 7 | 95 | A Chain A, The Crystal Structure Of The Phosphoenolpyruvate Synthase From Neisseria Meningitidis |
PDB | 1acz_A | 0.0000002 | 82 | 163 | 7 | 95 | A Chain A, Glucoamylase, Granular Starch-Binding Domain Complex With Cyclodextrin, Nmr, 5 Structures |
PDB | 1ac0_A | 0.0000002 | 82 | 163 | 7 | 95 | A Chain A, Glucoamylase, Granular Starch-Binding Domain Complex With Cyclodextrin, Nmr, Minimized Average Structure |
PDB | 2ols_A | 0.0000004 | 862 | 1186 | 16 | 338 | A Chain A, The Crystal Structure Of The Phosphoenolpyruvate Synthase From Neisseria Meningitidis |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO778000 | 888 | 318 | 1187 | 0 |
HO794745 | 735 | 463 | 1187 | 0 |
CO076712 | 297 | 855 | 1151 | 0 |
ES796736 | 317 | 780 | 1096 | 0 |
HO794745 | 45 | 425 | 469 | 0.0000000000005 |
Sequence Alignments (This image is cropped. Click for full image.) |
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