Protein : Qrob_P0248750.2 Q. robur
Protein Identifier  ? Qrob_P0248750.2 Organism . Name  Quercus robur
Score  100.0 Score Type  egn
Protein Description  (M=5) 5.1.3.15 - Glucose-6-phosphate 1-epimerase. Code Enzyme  EC:5.1.3.15
Gene Prediction Quality  validated Protein length 

Sequence

Length: 319  
Kegg Orthology  K01792
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0 Synonyms

4 GO Terms

Identifier Name Description
GO:0003824 catalytic activity Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
GO:0005975 carbohydrate metabolic process The chemical reactions and pathways involving carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y. Includes the formation of carbohydrate derivatives by the addition of a carbohydrate residue to another molecule.
GO:0030246 carbohydrate binding Interacting selectively and non-covalently with any carbohydrate, which includes monosaccharides, oligosaccharides and polysaccharides as well as substances derived from monosaccharides by reduction of the carbonyl group (alditols), by oxidation of one or more hydroxy groups to afford the corresponding aldehydes, ketones, or carboxylic acids, or by replacement of one or more hydroxy group(s) by a hydrogen atom. Cyclitols are generally not regarded as carbohydrates.
GO:0016853 isomerase activity Catalysis of the geometric or structural changes within one molecule. Isomerase is the systematic name for any enzyme of EC class 5.

31 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|pmum:103329791 56 311 + 256 none 83.66 306 87.50 3e-163 putative glucose-6-phosphate 1-epimerase
blastp_kegg lcl|pper:PRUPE_ppa009111mg 56 311 + 256 none 83.66 306 87.50 4e-163 hypothetical protein
blastp_kegg lcl|pop:POPTR_0001s35450g 56 311 + 256 none 83.66 306 85.16 3e-161 POPTRDRAFT_797872 aldose 1-epimerase family protein
blastp_kegg lcl|rcu:RCOM_1064680 56 309 + 254 none 83.28 305 87.01 2e-159 aldose 1-epimerase putative
blastp_kegg lcl|tcc:TCM_016980 56 311 + 256 none 72.93 351 85.55 2e-159 Aldose 1-epimerase family protein isoform 1
blastp_kegg lcl|rcu:RCOM_1064700 56 311 + 256 none 83.66 306 85.55 5e-159 aldose 1-epimerase putative
blastp_kegg lcl|vvi:100266308 56 309 + 254 none 83.01 306 84.25 4e-156 putative glucose-6-phosphate 1-epimerase-like
blastp_kegg lcl|cit:102615193 56 311 + 256 none 83.66 306 83.59 1e-155 putative glucose-6-phosphate 1-epimerase-like
blastp_kegg lcl|mdm:103404264 56 311 + 256 none 83.66 306 83.59 3e-154 putative glucose-6-phosphate 1-epimerase
blastp_kegg lcl|pxb:103959720 56 311 + 256 none 83.66 306 83.20 3e-154 putative glucose-6-phosphate 1-epimerase
blastp_pdb 2cis_A 63 300 + 238 Gaps:18 82.15 297 32.38 8e-32 mol:protein length:297 GLUCOSE-6-PHOSPHATE 1-EPIMERASE
blastp_pdb 2cir_A 63 300 + 238 Gaps:18 82.15 297 32.38 8e-32 mol:protein length:297 HEXOSE-6-PHOSPHATE MUTAROTASE
blastp_pdb 2ciq_A 63 300 + 238 Gaps:18 82.15 297 32.38 8e-32 mol:protein length:297 HEXOSE-6-PHOSPHATE MUTAROTASE
blastp_pdb 2htb_D 64 274 + 211 Gaps:12 65.70 309 33.00 5e-21 mol:protein length:309 Putative enzyme related to aldose 1-epimerase
blastp_pdb 2htb_C 64 274 + 211 Gaps:12 65.70 309 33.00 5e-21 mol:protein length:309 Putative enzyme related to aldose 1-epimerase
blastp_pdb 2htb_B 64 274 + 211 Gaps:12 65.70 309 33.00 5e-21 mol:protein length:309 Putative enzyme related to aldose 1-epimerase
blastp_pdb 2htb_A 64 274 + 211 Gaps:12 65.70 309 33.00 5e-21 mol:protein length:309 Putative enzyme related to aldose 1-epimerase
blastp_pdb 2hta_B 64 274 + 211 Gaps:12 65.70 309 33.00 5e-21 mol:protein length:309 Putative enzyme related to aldose 1-epimerase
blastp_pdb 2hta_A 64 274 + 211 Gaps:12 65.70 309 33.00 5e-21 mol:protein length:309 Putative enzyme related to aldose 1-epimerase
blastp_pdb 1jov_A 59 272 + 214 Gaps:41 70.74 270 30.89 2e-16 mol:protein length:270 HI1317
blastp_uniprot_sprot sp|Q40784|AAPC_CENCI 56 309 + 254 Gaps:6 78.42 329 67.83 6e-122 Putative glucose-6-phosphate 1-epimerase OS Cenchrus ciliaris PE 2 SV 1
blastp_uniprot_sprot sp|Q03161|YMY9_YEAST 63 300 + 238 Gaps:18 82.15 297 32.38 3e-31 Glucose-6-phosphate 1-epimerase OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN YMR099C PE 1 SV 1
blastp_uniprot_sprot sp|P39173|YEAD_ECOLI 64 278 + 215 Gaps:13 70.75 294 33.65 2e-20 Putative glucose-6-phosphate 1-epimerase OS Escherichia coli (strain K12) GN yeaD PE 1 SV 2
blastp_uniprot_sprot sp|P44160|Y1317_HAEIN 59 272 + 214 Gaps:41 70.48 271 31.94 8e-16 Putative glucose-6-phosphate 1-epimerase OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) GN HI_1317 PE 3 SV 1
rpsblast_cdd gnl|CDD|185697 56 290 + 235 Gaps:8 86.62 269 46.35 5e-85 cd09020 D-hex-6-P-epi_like D-hexose-6-phosphate epimerase-like. D-Hexose-6-phosphate epimerase Ymr099c from Saccharomyces cerevisiae belongs to the large superfamily of aldose-1-epimerases. Its active site is very similar to the catalytic site of galactose mutarotase the best studied member of the superfamily. It also contains the conserved glutamate and histidine residues that have been shown in galactose mutarotase to be critical for catalysis the glutamate serving as the active site base to initiate the reaction by removing the proton from the C-1 hydroxyl group of the sugar substrate and the histidine as the active site acid to protonate the C-5 ring oxygen. In addition Ymr099c contains 2 conserved arginine residues which are involved in phosphate binding and exhibits hexose-6-phosphate mutarotase activity on glucose-6-P galactose-6-P and mannose-6-P.
rpsblast_cdd gnl|CDD|201693 32 290 + 259 Gaps:41 89.04 301 27.24 1e-42 pfam01263 Aldose_epim Aldose 1-epimerase.
rpsblast_cdd gnl|CDD|31020 4 279 + 276 Gaps:31 89.55 287 32.68 7e-39 COG0676 COG0676 Uncharacterized enzymes related to aldose 1-epimerase [Carbohydrate transport and metabolism].
rpsblast_cdd gnl|CDD|185702 59 242 + 184 Gaps:34 68.63 271 27.96 5e-21 cd09025 Aldose_epim_Slr1438 Aldose 1-epimerase similar to Synechocystis Slr1438. Proteins similar to Synechocystis Slr1438 are uncharacterized members of aldose-1-epimerase superfamily. Aldose 1-epimerases or mutarotases are key enzymes of carbohydrate metabolism catalyzing the interconversion of the alpha- and beta-anomers of hexose sugars such as glucose and galactose. This interconversion is an important step that allows anomer specific metabolic conversion of sugars. Studies of the catalytic mechanism of the best known member of the family galactose mutarotase have shown a glutamate and a histidine residue to be critical for catalysis the glutamate serves as the active site base to initiate the reaction by removing the proton from the C-1 hydroxyl group of the sugar substrate and the histidine as the active site acid to protonate the C-5 ring oxygen.
rpsblast_cdd gnl|CDD|185701 70 217 + 148 Gaps:45 61.46 288 25.99 1e-09 cd09024 Aldose_epim_lacX Aldose 1-epimerase similar to Lactococcus lactis lacX. Proteins similar to Lactococcus lactis lacX are uncharacterized members of aldose-1-epimerase superfamily. Aldose 1-epimerases or mutarotases are key enzymes of carbohydrate metabolism catalyzing the interconversion of the alpha- and beta-anomers of hexose sugars such as glucose and galactose. This interconversion is an important step that allows anomer specific metabolic conversion of sugars. Studies of the catalytic mechanism of the best known member of the family galactose mutarotase have shown a glutamate and a histidine residue to be critical for catalysis the glutamate serves as the active site base to initiate the reaction by removing the proton from the C-1 hydroxyl group of the sugar substrate and the histidine as the active site acid to protonate the C-5 ring oxygen.
rpsblast_cdd gnl|CDD|185695 60 252 + 193 Gaps:39 76.76 284 18.81 1e-07 cd01081 Aldose_epim aldose 1-epimerase superfamily. Aldose 1-epimerases or mutarotases are key enzymes of carbohydrate metabolism they catalyze the interconversion of the alpha- and beta-anomers of hexose sugars such as glucose and galactose. This interconversion is an important step that allows anomer specific metabolic conversion of sugars. Studies of the catalytic mechanism of the best known member of the family galactose mutarotase have shown a glutamate and a histidine residue to be critical for catalysis the glutamate serves as the active site base to initiate the reaction by removing the proton from the C-1 hydroxyl group of the sugar substrate and the histidine as the active site acid to protonate the C-5 ring oxygen.

8 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
Pfam 57 289 233 PF01263 none Aldose 1-epimerase IPR008183
Phobius 42 59 18 TRANSMEMBRANE none Region of a membrane-bound protein predicted to be embedded in the membrane. none
PANTHER 56 297 242 PTHR11122:SF11 none none none
Gene3D 56 290 235 G3DSA:2.70.98.10 none none IPR014718
Phobius 60 318 259 CYTOPLASMIC_DOMAIN none Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm. none
SUPERFAMILY 56 289 234 SSF74650 none none IPR011013
PANTHER 56 297 242 PTHR11122 none none none
Phobius 1 41 41 NON_CYTOPLASMIC_DOMAIN none Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. none

0 Localization

10 Qtllist

Qtl Name Chromosome Name Linkage Group Prox Marker Dist Marker Position QTL Pos One Pos Two Test Type Test Value R 2
Bourran2_2014_nLBD*_A4 Qrob_Chr08 8 v_12498_318 v_12364_308 34,91 16,12 53,62 lod 2,4961 5,2
Bourran2_2014_nSecLBD_3P Qrob_Chr08 8 s_1BN2OD_551 s_1B5AYF_599 17,17 0 43,51 lod 1,9229 4,4
Bourran2_2014_rEpiBC*_A4 Qrob_Chr08 8 v_12498_318 v_12364_308 35,77 14,11 55,31 lod 2,9413 6,2
Bourran2_2015_nEpiBC_3P Qrob_Chr12 12 s_1B73S5_217 v_7050_211 28,31 26,37 28,45 lod 4.5 11.6
Bourran2_2014_aSeqBC_A4 Qrob_Chr08 8 v_15999_278 v_AP13YL15_395 32,52 4,22 57,22 lod 2,7561 6,7
Bourran2_2014_nFork*_A4 Qrob_Chr08 8 PIE175 s_1CD7GJ_1398 31,22 5,24 57,24 lod 2,6724 6,8
Bourran2_2014_nPriLBD_A4 Qrob_Chr08 8 PIE175 v_9164_159 31,85 15,39 48,29 lod 2,8308 6,8
Bourran2_2015_rEpiBC_3P Qrob_Chr08 8 s_A9TNV_543 v_11837_70 9,93 9,83 11,15 lod 3.3 7.3
Champenoux_2015_nSeqBC_A4 Qrob_Chr08 8 v_AD7YD13_501 s_1A7IED_780 43,44 43,42 43,99 lod 3.7 8.9
NancyGreenhouseCO2_2001_ambient_elevated_leaf_cellulose_QTL3_d13Cf Qrob_Chr08 8 v_5216_549 v_11625_20 37.08 12,26 54,9 lod 6.5888 0.04

1 Targeting

Analysis Start End Length Location Reliability Signal Peptide Cut Off Mitochondrion Cut Off Network Signal Peptide Length
TargetP 1 12   Secretory pathway 5 0.739 0.034 NON-PLANT 12