GER3_WHEAT
ID GER3_WHEAT Reviewed; 224 AA.
AC P26759;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Oxalate oxidase GF-3.8;
DE EC=1.2.3.4;
DE AltName: Full=Germin GF-3.8;
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 CHARACTERIZATION.
RX PubMed=8509360; DOI=10.1016/s0021-9258(18)31377-2;
RA Lane B.G., Dunwell J.M., Ray J.A., Schmitt M.R., Cuming A.C.;
RT "Germin, a protein marker of early plant development, is an oxalate
RT oxidase.";
RL J. Biol. Chem. 268:12239-12242(1993).
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 {ECO:0000250}.
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 -!- 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; M63224; AAA34271.1; -; Genomic_DNA.
DR AlphaFoldDB; P26759; -.
DR SMR; P26759; -.
DR PRIDE; P26759; -.
DR EnsemblPlants; TraesCLE_scaffold_039871_01G000100.1; TraesCLE_scaffold_039871_01G000100.1; TraesCLE_scaffold_039871_01G000100.
DR EnsemblPlants; TraesCS4B02G033200.1; TraesCS4B02G033200.1.cds1; TraesCS4B02G033200.
DR EnsemblPlants; TraesPAR_scaffold_019561_01G000100.1; TraesPAR_scaffold_019561_01G000100.1; TraesPAR_scaffold_019561_01G000100.
DR EnsemblPlants; TraesROB_scaffold_092809_01G000200.1; TraesROB_scaffold_092809_01G000200.1; TraesROB_scaffold_092809_01G000200.
DR EnsemblPlants; TraesWEE_scaffold_033334_01G000100.1; TraesWEE_scaffold_033334_01G000100.1; TraesWEE_scaffold_033334_01G000100.
DR Gramene; TraesCLE_scaffold_039871_01G000100.1; TraesCLE_scaffold_039871_01G000100.1; TraesCLE_scaffold_039871_01G000100.
DR Gramene; TraesCS4B02G033200.1; TraesCS4B02G033200.1.cds1; TraesCS4B02G033200.
DR Gramene; TraesPAR_scaffold_019561_01G000100.1; TraesPAR_scaffold_019561_01G000100.1; TraesPAR_scaffold_019561_01G000100.
DR Gramene; TraesROB_scaffold_092809_01G000200.1; TraesROB_scaffold_092809_01G000200.1; TraesROB_scaffold_092809_01G000200.
DR Gramene; TraesWEE_scaffold_033334_01G000100.1; TraesWEE_scaffold_033334_01G000100.1; TraesWEE_scaffold_033334_01G000100.
DR OMA; DESPWGA; -.
DR Proteomes; UP000019116; Unplaced.
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 /evidence="ECO:0000255"
FT CHAIN 24..224
FT /note="Oxalate oxidase GF-3.8"
FT /id="PRO_0000010835"
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; 23562 MW; E18A10435FA8BE80 CRC64;
MGYSKNIASG MFAMLLLASA VLSSNPHPLQ DFCVADLDGK AVSVNGHMCK PMSEAGDDFL
FSSKLAKAGN TSTPNGSAVT DLNVAEWPGT NTLGVSMNRV DFAPGGTNPP HIHPRATEIG
IVMKGELLVG ILGSLDSGNK LYSRVVRAGE TFLIPRGLMH FQFNVGKTEA SMVVFFNSQS
PSVVFVPLTL FGSNPPIPKP VLTKALRVEA GVVELLKSKF AGGS
