GER2_WHEAT
ID GER2_WHEAT Reviewed; 224 AA.
AC P15290;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Oxalate oxidase GF-2.8;
DE EC=1.2.3.4;
DE AltName: Full=Germin GF-2.8;
DE Flags: Precursor;
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2037593; DOI=10.1016/s0021-9258(18)99247-1;
RA Lane B.G., Bernier F., Dratewka-Kos E., Shafai R., Kennedy T.D., Pyne C.,
RA Munro J.R., Vaughan T., Walters D., Altomare F.;
RT "Homologies between members of the germin gene family in hexaploid wheat
RT and similarities between these wheat germins and certain Physarum
RT spherulins.";
RL J. Biol. Chem. 266:10461-10469(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2925674; DOI=10.1016/s0021-9258(18)83675-4;
RA Dratewka-Kos E., Rahman S., Grzekzak Z.F., Kennedy T.D., Murray R.K.,
RA Lane B.G.;
RT "Polypeptide structure of germin as deduced from cDNA sequencing.";
RL J. Biol. Chem. 264:4896-4900(1989).
RN [3]
RP CHARACTERIZATION.
RX PubMed=10092181; DOI=10.1023/a:1006123432157;
RA Berna A., Bernier F.;
RT "Regulation by biotic and abiotic stress of a wheat germin gene encoding
RT oxalate oxidase, a H2O2-producing enzyme.";
RL Plant Mol. Biol. 39:539-549(1999).
CC -!- FUNCTION: Produces developmental and stress-related release of hydrogen
CC peroxide in the apoplast. May play an important role in several aspects
CC of plant growth and defense mechanisms.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + O2 + oxalate = 2 CO2 + H2O2; Xref=Rhea:RHEA:21880,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:30623; EC=1.2.3.4;
CC -!- SUBUNIT: Oligomer (believed to be a pentamer but probably hexamer).
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast.
CC Cytoplasm. Secreted, cell wall. Note=Found in the apoplast and the
CC cytoplasm of germinating embryo cells. Associated with the cell wall.
CC -!- INDUCTION: By auxin, pathogens and heavy metal ions.
CC -!- MISCELLANEOUS: Associated mostly with highly substituted forms of
CC glucuronogalactoarabinoxylans.
CC -!- SIMILARITY: Belongs to the germin family. {ECO:0000305}.
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DR EMBL; M21962; AAA34268.1; -; mRNA.
DR EMBL; M63223; AAA34270.1; -; Genomic_DNA.
DR PIR; A40391; A33268.
DR AlphaFoldDB; P15290; -.
DR SMR; P15290; -.
DR STRING; 4565.Traes_4BS_7AE61936D.1; -.
DR PRIDE; P15290; -.
DR EnsemblPlants; TraesCAD_scaffold_071769_01G000600.1; TraesCAD_scaffold_071769_01G000600.1; TraesCAD_scaffold_071769_01G000600.
DR EnsemblPlants; TraesCLE_scaffold_067550_01G000100.1; TraesCLE_scaffold_067550_01G000100.1; TraesCLE_scaffold_067550_01G000100.
DR EnsemblPlants; TraesCS4D02G032000.1; TraesCS4D02G032000.1.cds1; TraesCS4D02G032000.
DR EnsemblPlants; TraesPAR_scaffold_065607_01G000100.1; TraesPAR_scaffold_065607_01G000100.1; TraesPAR_scaffold_065607_01G000100.
DR EnsemblPlants; TraesROB_scaffold_072937_01G000100.1; TraesROB_scaffold_072937_01G000100.1; TraesROB_scaffold_072937_01G000100.
DR EnsemblPlants; TraesWEE_scaffold_072014_01G000100.1; TraesWEE_scaffold_072014_01G000100.1; TraesWEE_scaffold_072014_01G000100.
DR Gramene; TraesCAD_scaffold_071769_01G000600.1; TraesCAD_scaffold_071769_01G000600.1; TraesCAD_scaffold_071769_01G000600.
DR Gramene; TraesCLE_scaffold_067550_01G000100.1; TraesCLE_scaffold_067550_01G000100.1; TraesCLE_scaffold_067550_01G000100.
DR Gramene; TraesCS4D02G032000.1; TraesCS4D02G032000.1.cds1; TraesCS4D02G032000.
DR Gramene; TraesPAR_scaffold_065607_01G000100.1; TraesPAR_scaffold_065607_01G000100.1; TraesPAR_scaffold_065607_01G000100.
DR Gramene; TraesROB_scaffold_072937_01G000100.1; TraesROB_scaffold_072937_01G000100.1; TraesROB_scaffold_072937_01G000100.
DR Gramene; TraesWEE_scaffold_072014_01G000100.1; TraesWEE_scaffold_072014_01G000100.1; TraesWEE_scaffold_072014_01G000100.
DR eggNOG; ENOG502QSRM; Eukaryota.
DR OMA; WINCERN; -.
DR BRENDA; 1.2.3.4; 6500.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; P15290; differential.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0050162; F:oxalate oxidase activity; IEA:UniProtKB-EC.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR006045; Cupin_1.
DR InterPro; IPR001929; Germin.
DR InterPro; IPR019780; Germin_Mn-BS.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR Pfam; PF00190; Cupin_1; 1.
DR PRINTS; PR00325; GERMIN.
DR SMART; SM00835; Cupin_1; 1.
DR SUPFAM; SSF51182; SSF51182; 1.
DR PROSITE; PS00725; GERMIN; 1.
PE 1: Evidence at protein level;
KW Apoplast; Cell wall; Cytoplasm; Disulfide bond; Glycoprotein; Manganese;
KW Metal-binding; Oxidoreductase; Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT CHAIN 24..224
FT /note="Oxalate oxidase GF-2.8"
FT /id="PRO_0000010834"
FT DOMAIN 63..214
FT /note="Cupin type-1"
FT /evidence="ECO:0000255"
FT BINDING 111
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 118
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 160
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 33..49
FT /evidence="ECO:0000250"
SQ SEQUENCE 224 AA; 23612 MW; 2D6DCAC3362CE962 CRC64;
MGYSKTLVAG LFAMLLLAPA VLATDPDPLQ DFCVADLDGK AVSVNGHTCK PMSEAGDDFL
FSSKLAKAGN TSTPNGSAVT ELDVAEWPGT NTLGVSMNRV DFAPGGTNPP HIHPRATEIG
IVMKGELLVG ILGSLDSGNK LYSRVVRAGE TFLIPRGLMH FQFNVGKTEA SMVVSFNSQN
PGIVFVPLTL FGSNPPIPTP VLTKALRVEA RVVELLKSKF AAGF
