Protein : Qrob_P0354520.2 Q. robur
Protein Identifier  ? Qrob_P0354520.2 Organism . Name  Quercus robur
Score  100.0 Score Type  egn
Protein Description  (M=1) 1.13.11.29 - Stizolobate synthase. Code Enzyme  EC:1.13.11.29
Gene Prediction Quality  validated Protein length 

Sequence

Length: 263  
Kegg Orthology  K15777
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0 Synonyms

6 GO Terms

Identifier Name Description
GO:0008270 zinc ion binding Interacting selectively and non-covalently with zinc (Zn) ions.
GO:0016491 oxidoreductase activity Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
GO:0055114 oxidation-reduction process A metabolic process that results in the removal or addition of one or more electrons to or from a substance, with or without the concomitant removal or addition of a proton or protons.
GO:0016701 oxidoreductase activity, acting on single donors with incorporation of molecular oxygen Catalysis of an oxidation-reduction (redox) reaction in which hydrogen or electrons are transferred from one donor, and molecular oxygen is incorporated into a donor.
GO:0006725 cellular aromatic compound metabolic process The chemical reactions and pathways involving aromatic compounds, any organic compound characterized by one or more planar rings, each of which contains conjugated double bonds and delocalized pi electrons, as carried out by individual cells.
GO:0008198 ferrous iron binding Interacting selectively and non-covalently with ferrous iron, Fe(II).

22 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|tcc:TCM_001659 2 261 + 260 Gaps:5 96.67 270 79.69 2e-151 Catalytic LigB subunit of aromatic ring-opening dioxygenase family isoform 1
blastp_kegg lcl|vvi:100262346 1 262 + 262 Gaps:3 100.00 263 77.95 3e-151 4 5-DOPA dioxygenase extradiol-like protein
blastp_kegg lcl|vvi:100244355 1 262 + 262 Gaps:6 100.00 266 76.69 9e-147 4 5-DOPA dioxygenase extradiol-like protein-like
blastp_kegg lcl|mtr:MTR_6g064960 2 262 + 261 Gaps:1 98.50 266 77.10 2e-145 4 5-DOPA dioxygenase extradiol-like protein
blastp_kegg lcl|gmx:100798236 2 262 + 261 Gaps:1 98.50 266 75.19 3e-145 extradiol ring-cleavage dioxygenase-like
blastp_kegg lcl|pop:POPTR_0004s14280g 1 260 + 260 Gaps:3 99.62 262 75.86 5e-145 POPTRDRAFT_818033 hypothetical protein
blastp_kegg lcl|cic:CICLE_v10026292mg 2 260 + 259 Gaps:3 97.74 266 75.00 1e-144 hypothetical protein
blastp_kegg lcl|pop:POPTR_0019s00350g 1 258 + 258 Gaps:4 91.49 282 77.52 1e-144 hypothetical protein
blastp_kegg lcl|cit:102612511 1 260 + 260 Gaps:3 83.39 313 76.63 2e-144 extradiol ring-cleavage dioxygenase-like
blastp_kegg lcl|cit:102612815 2 260 + 259 Gaps:3 97.74 266 75.00 5e-144 extradiol ring-cleavage dioxygenase-like
blastp_pdb 2pw6_A 1 257 + 257 Gaps:17 94.46 271 37.50 1e-48 mol:protein length:271 Uncharacterized protein ygiD
blastp_uniprot_sprot sp|Q949R4|DIOXL_ARATH 3 250 + 248 Gaps:8 93.68 269 70.24 2e-124 Extradiol ring-cleavage dioxygenase OS Arabidopsis thaliana GN LIGB PE 2 SV 1
blastp_uniprot_sprot sp|Q70FG7|DODA_BETVU 2 259 + 258 Gaps:3 96.64 268 64.86 2e-121 4 5-DOPA dioxygenase extradiol OS Beta vulgaris GN DODA PE 1 SV 1
blastp_uniprot_sprot sp|Q7XA48|DODA_PORGR 2 259 + 258 Gaps:4 95.94 271 55.00 2e-96 4 5-DOPA dioxygenase extradiol OS Portulaca grandiflora GN DODA PE 1 SV 1
blastp_uniprot_sprot sp|B6F0W8|DODA_MIRJA 3 262 + 260 Gaps:5 97.75 267 51.34 1e-91 4 5-DOPA dioxygenase extradiol OS Mirabilis jalapa GN DOD PE 1 SV 1
blastp_uniprot_sprot sp|P24197|YGID_ECOLI 1 257 + 257 Gaps:17 97.71 262 37.50 4e-48 Uncharacterized protein YgiD OS Escherichia coli (strain K12) GN ygiD PE 1 SV 3
blastp_uniprot_sprot sp|O74741|DIOXL_SCHPO 3 241 + 239 Gaps:27 86.87 297 29.46 1e-22 4 5-DOPA dioxygenase extradiol-like protein OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) GN SPBC1709.16c PE 3 SV 2
rpsblast_cdd gnl|CDD|153375 3 257 + 255 Gaps:9 99.60 253 53.97 7e-94 cd07363 45_DOPA_Dioxygenase The Class III extradiol dioxygenase 4 5-DOPA Dioxygenase catalyzes the incorporation of both atoms of molecular oxygen into 4 5-dihydroxy-phenylalanine. This subfamily is composed of plant 4 5-DOPA Dioxygenase the uncharacterized Escherichia coli protein Jw3007 and similar proteins. 4 5-DOPA Dioxygenase catalyzes the incorporation of both atoms of molecular oxygen into 4 5-dihydroxy-phenylalanine (4 5-DOPA). The reaction results in the opening of the cyclic ring between carbons 4 and 5 and producing an unstable seco-DOPA that rearranges to betalamic acid. 4 5-DOPA Dioxygenase is a key enzyme in the biosynthetic pathway of the plant pigment betalain. Homologs of DODA are present not only in betalain-producing plants but also in bacteria and archaea. This enzyme is a member of the class III extradiol dioxygenase family a group of enzymes which use a non-heme Fe(II) to cleave aromatic rings between a hydroxylated carbon and an adjacent non-hydroxylated carbon.
rpsblast_cdd gnl|CDD|202457 7 257 + 251 Gaps:20 99.61 258 40.08 5e-59 pfam02900 LigB Catalytic LigB subunit of aromatic ring-opening dioxygenase.
rpsblast_cdd gnl|CDD|33191 1 257 + 257 Gaps:7 96.27 268 40.70 2e-55 COG3384 COG3384 Uncharacterized conserved protein [Function unknown].
rpsblast_cdd gnl|CDD|182598 26 256 + 231 Gaps:15 95.12 246 39.32 7e-47 PRK10628 PRK10628 LigB family dioxygenase Provisional.
rpsblast_cdd gnl|CDD|153371 6 257 + 252 Gaps:22 98.46 260 24.22 3e-19 cd07320 Extradiol_Dioxygenase_3B_like Subunit B of Class III Extradiol ring-cleavage dioxygenases. Dioxygenases catalyze the incorporation of both atoms of molecular oxygen into substrates using a variety of reaction mechanisms resulting in the cleavage of aromatic rings. Two major groups of dioxygenases have been identified according to the cleavage site of the aromatic ring. Intradiol enzymes cleave the aromatic ring between two hydroxyl groups whereas extradiol enzymes cleave the aromatic ring between a hydroxylated carbon and an adjacent non-hydroxylated carbon. Extradiol dioxygenases can be further divided into three classes. Class I and II enzymes are evolutionary related and show sequence similarity with the two-domain class II enzymes evolving from the class I enzyme through gene duplication. Class III enzymes are different in sequence and structure and usually have two subunits designated A and B. This model represents the catalytic subunit B of extradiol dioxygenase class III enzymes. Enzymes belonging to this family include Protocatechuate 4 5-dioxygenase (LigAB) 2'-aminobiphenyl-2 3-diol 1 2-dioxygenase (CarB) 4 5-DOPA Dioxygenase 2 3-dihydroxyphenylpropionate 1 2-dioxygenase and 3 4-dihydroxyphenylacetate (homoprotocatechuate) 2 3-dioxygenase (HPCD). There are also some family members that do not show the typical dioxygenase activity.

6 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
PANTHER 1 262 262 PTHR30096 none none none
PIRSF 1 259 259 PIRSF006157 none none IPR014436
PANTHER 1 262 262 PTHR30096:SF2 none none none
Pfam 3 257 255 PF02900 none Catalytic LigB subunit of aromatic ring-opening dioxygenase IPR004183
SUPERFAMILY 3 257 255 SSF53213 none none IPR004183
Gene3D 1 257 257 G3DSA:3.40.830.10 none none IPR004183

0 Localization

3 Qtllist

Qtl Name Chromosome Name Linkage Group Prox Marker Dist Marker Position QTL Pos One Pos Two Test Type Test Value R 2
Bourran1_2004_QTL5_peak_Bud_burst_A4 Qrob_Chr10 10 s_1C8OKQ_688 v_12844_707 25,6 13,9 39,9 lod 2,7 6,1
Bourran2_2002_QTL13_peak_Bud_burst_3P Qrob_Chr10 10 s_1B1AG7_637 s_1A3A1N_709 19,44 0 49,44 lod 3 5,6
Champenoux_2015_nPriLBD_3P Qrob_Chr10 10 v_15000_157 v_15000_310 15,68 15,9 15,91 lod 2.4 5.5

0 Targeting